annotate test-data/str.pdb @ 0:acce5039ece7 draft

planemo upload for repository https://github.com/galaxycomputationalchemistry/galaxy-tools-compchem/tools/mdfileconverter commit 8aeaf3f199cccb1bbb26a29628e7bb75abaf189d

HEADER    STRUCTURAL PROTEIN                      03-FEB-05   1YRF              
TITLE     CHICKEN VILLIN SUBDOMAIN HP-35, N68H, PH6.7                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: VILLIN;                                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: VHP;                                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 OTHER_DETAILS: SEQUENCE CORRESPONDS TO CHICKEN VILLIN RESIDUES 792-  
SOURCE   4 826                                                                  
KEYWDS    VILLIN HEADPIECE SUBDOMAIN, STRUCTURAL PROTEIN                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.K.CHIU,J.KUBELKA,R.HERBST-IRMER,W.A.EATON,J.HOFRICHTER,D.R.DAVIES   
REVDAT   5   11-OCT-17 1YRF    1       REMARK                                   
REVDAT   4   24-FEB-09 1YRF    1       VERSN                                    
REVDAT   3   21-JUN-05 1YRF    1       JRNL                                     
REVDAT   2   31-MAY-05 1YRF    1       JRNL                                     
REVDAT   1   03-MAY-05 1YRF    0                                                
JRNL        AUTH   T.K.CHIU,J.KUBELKA,R.HERBST-IRMER,W.A.EATON,J.HOFRICHTER,    
JRNL        AUTH 2 D.R.DAVIES                                                   
JRNL        TITL   HIGH-RESOLUTION X-RAY CRYSTAL STRUCTURES OF THE VILLIN       
JRNL        TITL 2 HEADPIECE SUBDOMAIN, AN ULTRAFAST FOLDING PROTEIN.           
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 102  7517 2005              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   15894611                                                     
JRNL        DOI    10.1073/PNAS.0502495102                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.07 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.07                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.155                  
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.161                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 622                    
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 15534                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : NULL                   
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.150                  
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.156                  
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 551                    
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 13866                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 289                                           
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 9                                             
REMARK   3   SOLVENT ATOMS      : 60                                            
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : NULL                    
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL                    
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : NULL                    
REMARK   3   NUMBER OF RESTRAINTS                     : NULL                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.020                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.020                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.020                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.100                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.100                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : NULL                    
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : NULL                    
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : NULL                    
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : NULL                    
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : NULL                    
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH & HUBER                        
REMARK   3   SPECIAL CASE: NULL                                                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS:                                           
REMARK   3  INDIVIDUAL ANISOTROPIC B FOR ALL NONHYDROGENS, HYDROGEN ADDED AS '  
REMARK   3  RIDING HYDROGENS' SHELX: DEFS 0.02 0.1 0.02, SIMU 0.1, ISOR 0.03,   
REMARK   3  WGHT 0.2, SWAT.  THE SIDE-CHAIN OF TRP64                            
REMARK   3  IS IN 2 CONFORMATIONS, THE FIRST CONFORMATION                       
REMARK   3  PARTIALLY OVERLAP EACH OTHER ON A 2-FOLD AXIS.                      
REMARK   4                                                                      
REMARK   4 1YRF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-FEB-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000031845.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-OCT-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 95.0                               
REMARK 200  PH                             : 6.70                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.90                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15545                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.070                              
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     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 19.80                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 50.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.07                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.42300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.26                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1UL 100MG/ML PEPTIDE PLUS 1UL (200MM     
REMARK 280  NAOAC, 2.2M AMSO4), PH 6.7, VAPOR DIFFUSION, SITTING DROP,          
REMARK 280  TEMPERATURE 293K, PH 6.70                                           
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       18.95433            
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       37.90867            
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       37.90867            
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       18.95433            
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 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 A1049  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A1060  LIES ON A SPECIAL POSITION.                          
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   H    TRP A    64     H3   ACT A    80              1.34            
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    ARG A  55   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    HIS A  68   CA  -  CB  -  CG  ANGL. DEV. = -11.7 DEGREES          
REMARK 500    PHE A  76   CA  -  CB  -  CG  ANGL. DEV. =  14.4 DEGREES          
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 SO4 A 77                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 80                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1YRI   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1WY3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1WY4   RELATED DB: PDB                                   
DBREF  1YRF A   42    76  UNP    P02640   VILI_CHICK     792    826             
SEQADV 1YRF HIS A   68  UNP  P02640    ASN   818 ENGINEERED                     
SEQRES   1 A   35  LEU SER ASP GLU ASP PHE LYS ALA VAL PHE GLY MET THR          
SEQRES   2 A   35  ARG SER ALA PHE ALA ASN LEU PRO LEU TRP LYS GLN GLN          
SEQRES   3 A   35  HIS LEU LYS LYS GLU LYS GLY LEU PHE                          
HET    SO4  A  77      10                                                       
HET    ACT  A  80      21                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ACT ACETATE ION                                                      
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3  ACT    C2 H3 O2 1-                                                  
FORMUL   4  HOH   *60(H2 O)                                                     
HELIX    1   1 SER A   43  GLY A   52  1                                  10    
HELIX    2   2 THR A   54  ALA A   59  1                                   6    
HELIX    3   3 PRO A   62  LYS A   73  1                                  12    
SITE     1 AC1  6 LEU A  42  PHE A  47  ARG A  55  LYS A  70                    
SITE     2 AC1  6 PHE A  76  HOH A1059                                          
SITE     1 AC2 10 SER A  43  GLU A  45  PRO A  62  LEU A  63                    
SITE     2 AC2 10 TRP A  64  LYS A  65  HOH A1001  HOH A1002                    
SITE     3 AC2 10 HOH A1049  HOH A1056                                          
CRYST1   32.155   32.155   56.863  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      0.031099  0.017955  0.000000        0.00000                         
SCALE2      0.000000  0.035910  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017586        0.00000                         
ATOM      1  N   LEU A  42      -7.397   9.811   7.912  1.00 18.08           N  
ANISOU    1  N   LEU A  42     1739   3554   1576   -927    -23     49       N  
ATOM      2  CA  LEU A  42      -6.429   9.299   6.989  1.00 17.02           C  
ANISOU    2  CA  LEU A  42     1521   3238   1708   -704   -244    459       C  
ATOM      3  C   LEU A  42      -4.999   9.526   7.461  1.00 14.52           C  
ANISOU    3  C   LEU A  42     1630   2164   1724   -513   -443    377       C  
ATOM      4  O   LEU A  42      -4.812  10.441   8.271  1.00 16.43           O  
ANISOU    4  O   LEU A  42     1544   3124   1575   -476   -234     83       O  
ATOM      5  CB  LEU A  42      -6.594  10.066   5.641  1.00 14.42           C  
ANISOU    5  CB  LEU A  42     1533   2331   1615    -38   -169    -43       C  
ATOM      6  CG  LEU A  42      -7.882   9.861   4.870  1.00 16.47           C  
ANISOU    6  CG  LEU A  42     1467   3208   1582    307   -132   -445       C  
ATOM      7  CD1 LEU A  42      -7.952  10.791   3.653  1.00 19.76           C  
ANISOU    7  CD1 LEU A  42     1696   3634   2177    693   -319   -103       C  
ATOM      8  CD2 LEU A  42      -7.970   8.419   4.423  1.00 21.37           C  
ANISOU    8  CD2 LEU A  42     2664   3364   2093   -595   -989   -465       C  
ATOM      9  H1  LEU A  42      -8.216   9.663   7.596  1.00 27.12           H  
ATOM     10  H2  LEU A  42      -7.273  10.686   8.018  1.00 27.12           H  
ATOM     11  H3  LEU A  42      -7.304   9.401   8.697  1.00 27.12           H  
ATOM     12  HA  LEU A  42      -6.581   8.341   6.846  1.00 20.42           H  
ATOM     13  HB2 LEU A  42      -6.503  11.014   5.824  1.00 17.31           H  
ATOM     14  HB3 LEU A  42      -5.857   9.814   5.062  1.00 17.31           H  
ATOM     15  HG  LEU A  42      -8.639  10.056   5.461  1.00 19.76           H  
ATOM     16 HD11 LEU A  42      -7.898  11.704   3.944  1.00 29.63           H  
ATOM     17 HD12 LEU A  42      -8.781  10.651   3.191  1.00 29.63           H  
ATOM     18 HD13 LEU A  42      -7.220  10.599   3.062  1.00 29.63           H  
ATOM     19 HD21 LEU A  42      -8.788   8.283   3.940  1.00 32.06           H  
ATOM     20 HD22 LEU A  42      -7.952   7.844   5.192  1.00 32.06           H  
ATOM     21 HD23 LEU A  42      -7.225   8.215   3.853  1.00 32.06           H  
ATOM     22  N   SER A  43      -4.031   8.813   6.991  1.00 16.48           N  
ANISOU   22  N   SER A  43     1830   1658   2773   -317   -939    397       N  
ATOM     23  CA  SER A  43      -2.633   9.119   7.222  1.00 15.70           C  
ANISOU   23  CA  SER A  43     1773   1334   2860    -99   -526    213       C  
ATOM     24  C   SER A  43      -2.326  10.449   6.544  1.00 13.37           C  
ANISOU   24  C   SER A  43     1300   1364   2418     92   -369    162       C  
ATOM     25  O   SER A  43      -3.048  10.929   5.652  1.00 12.46           O  
ANISOU   25  O   SER A  43     1395   1271   2069    201   -415    -80       O  
ATOM     26  CB  SER A  43      -1.729   8.019   6.644  1.00 18.18           C  
ANISOU   26  CB  SER A  43     2399   1518   2990    518  -1191    -53       C  
ATOM     27  OG  SER A  43      -1.809   8.072   5.255  1.00 16.83           O  
ANISOU   27  OG  SER A  43     2125   1394   2877    610   -724    -26       O  
ATOM     28  H   SER A  43      -4.225   8.123   6.516  1.00 19.78           H  
ATOM     29  HA  SER A  43      -2.473   9.200   8.185  1.00 18.84           H  
ATOM     30  HB2 SER A  43      -0.812   8.158   6.930  1.00 21.82           H  
ATOM     31  HB3 SER A  43      -2.019   7.149   6.961  1.00 21.82           H  
ATOM     32  HG  SER A  43      -1.329   7.491   4.932  1.00 25.25           H  
ATOM     33  N   ASP A  44      -1.212  11.029   6.951  1.00 15.05           N  
ANISOU   33  N   ASP A  44     1395   1389   2935     85   -441    113       N  
ATOM     34  CA  ASP A  44      -0.814  12.312   6.401  1.00 13.97           C  
ANISOU   34  CA  ASP A  44     1728   1333   2248    -61   -395   -148       C  
ATOM     35  C   ASP A  44      -0.478  12.119   4.919  1.00 13.08           C  
ANISOU   35  C   ASP A  44     1287   1304   2379    227   -545   -231       C  
ATOM     36  O   ASP A  44      -0.730  12.992   4.101  1.00 12.72           O  
ANISOU   36  O   ASP A  44     1119   1552   2162     58   -184    -37       O  
ATOM     37  CB  ASP A  44       0.294  13.000   7.193  1.00 16.52           C  
ANISOU   37  CB  ASP A  44     2059   2009   2210   -310   -847    345       C  
ATOM     38  CG  ASP A  44      -0.160  13.580   8.532  1.00 23.56           C  
ANISOU   38  CG  ASP A  44     2954   3156   2841   -661   -674   -879       C  
ATOM     39  OD1 ASP A  44      -1.380  13.541   8.740  1.00 25.79           O  
ANISOU   39  OD1 ASP A  44     3282   3917   2602  -1026     24   -926       O  
ATOM     40  OD2 ASP A  44       0.736  14.012   9.280  1.00 30.03           O  
ANISOU   40  OD2 ASP A  44     3400   5500   2511  -1216   -687   -738       O  
ATOM     41  H   ASP A  44      -0.721  10.645   7.543  1.00 18.06           H  
ATOM     42  HA  ASP A  44      -1.600  12.896   6.442  1.00 16.77           H  
ATOM     43  HB2 ASP A  44       1.004  12.360   7.356  1.00 19.83           H  
ATOM     44  HB3 ASP A  44       0.664  13.716   6.653  1.00 19.83           H  
ATOM     45  N   GLU A  45       0.100  10.944   4.606  1.00 14.19           N  
ANISOU   45  N   GLU A  45     1292   1357   2744    173   -515   -394       N  
ATOM     46  CA  GLU A  45       0.379  10.649   3.217  1.00 14.68           C  
ANISOU   46  CA  GLU A  45     1139   1603   2835    218    -38   -285       C  
ATOM     47  C   GLU A  45      -0.889  10.535   2.384  1.00 13.23           C  
ANISOU   47  C   GLU A  45     1291   1393   2341    356     16   -378       C  
ATOM     48  O   GLU A  45      -0.969  11.056   1.260  1.00 13.60           O  
ANISOU   48  O   GLU A  45     1402   1621   2144    242    141   -317       O  
ATOM     49  CB AGLU A  45       1.251   9.378   3.099  0.32 17.55           C  
ANISOU   49  CB AGLU A  45     1518   1768   3381    561   -353   -359       C  
ATOM     50  CB BGLU A  45       1.176   9.315   3.162  0.68 18.64           C  
ANISOU   50  CB BGLU A  45     1624   1733   3725    609   -404   -391       C  
ATOM     51  CG AGLU A  45       2.733   9.687   3.270  0.32 22.12           C  
ANISOU   51  CG AGLU A  45     1515   2303   4588    862   -624   -722       C  
ATOM     52  CG BGLU A  45       2.481   9.337   3.885  0.68 22.98           C  
ANISOU   52  CG BGLU A  45     2005   2152   4573    623   -974   -198       C  
ATOM     53  CD AGLU A  45       3.283  10.601   2.197  0.32 24.22           C  
ANISOU   53  CD AGLU A  45      822   3188   5192    721    478   -856       C  
ATOM     54  CD BGLU A  45       2.602   9.189   5.371  0.68 24.63           C  
ANISOU   54  CD BGLU A  45     1880   3125   4355    -20   -859   -632       C  
ATOM     55  OE1AGLU A  45       3.359  10.202   1.014  0.32 26.48           O  
ANISOU   55  OE1AGLU A  45     1694   3178   5189    527    429   -783       O  
ATOM     56  OE1BGLU A  45       3.806   9.109   5.768  0.68 34.43           O  
ANISOU   56  OE1BGLU A  45     1677   6793   4611   -244   -703    427       O  
ATOM     57  OE2AGLU A  45       3.672  11.747   2.509  0.32 37.15           O  
ANISOU   57  OE2AGLU A  45     4226   4450   5439  -1644   2631  -1597       O  
ATOM     58  OE2BGLU A  45       1.631   9.146   6.155  0.68 25.44           O  
ANISOU   58  OE2BGLU A  45     1485   2812   5368    483   -697   1865       O  
ATOM     59  H   GLU A  45       0.299  10.377   5.221  1.00 17.03           H  
ATOM     60  HA  GLU A  45       0.900  11.397   2.858  1.00 17.61           H  
ATOM     61  HB2AGLU A  45       0.978   8.739   3.775  0.32 21.06           H  
ATOM     62  HB2BGLU A  45       0.626   8.611   3.538  0.68 22.37           H  
ATOM     63  HB3AGLU A  45       1.108   8.972   2.229  0.32 21.06           H  
ATOM     64  HB3BGLU A  45       1.342   9.093   2.232  0.68 22.37           H  
ATOM     65  HG2AGLU A  45       2.869  10.102   4.136  0.32 26.55           H  
ATOM     66  HG2BGLU A  45       3.024   8.635   3.493  0.68 27.57           H  
ATOM     67  HG3AGLU A  45       3.231   8.855   3.260  0.32 26.55           H  
ATOM     68  HG3BGLU A  45       2.908  10.177   3.656  0.68 27.57           H  
ATOM     69  N   ASP A  46      -1.896   9.799   2.874  1.00 12.11           N  
ANISOU   69  N   ASP A  46     1279   1243   2082    341   -211   -296       N  
ATOM     70  CA  ASP A  46      -3.141   9.714   2.166  1.00 10.88           C  
ANISOU   70  CA  ASP A  46     1305   1239   1589    298   -223   -329       C  
ATOM     71  C   ASP A  46      -3.813  11.069   2.039  1.00 11.05           C  
ANISOU   71  C   ASP A  46     1186   1186   1827     75   -105   -300       C  
ATOM     72  O   ASP A  46      -4.427  11.338   1.008  1.00 11.12           O  
ANISOU   72  O   ASP A  46     1198   1316   1710    152   -117   -235       O  
ATOM     73  CB  ASP A  46      -4.089   8.712   2.784  1.00 13.77           C  
ANISOU   73  CB  ASP A  46     1616   1329   2287    -18   -161   -389       C  
ATOM     74  CG  ASP A  46      -3.756   7.247   2.650  1.00 17.09           C  
ANISOU   74  CG  ASP A  46     1975   1462   3057    -57   -621   -183       C  
ATOM     75  OD1 ASP A  46      -2.756   6.956   1.954  1.00 17.71           O  
ANISOU   75  OD1 ASP A  46     2411   1369   2951    249   -446   -571       O  
ATOM     76  OD2 ASP A  46      -4.457   6.356   3.206  1.00 18.74           O  
ANISOU   76  OD2 ASP A  46     2465   1417   3238    129   -493    278       O  
ATOM     77  H   ASP A  46      -1.796   9.377   3.616  1.00 14.54           H  
ATOM     78  HA  ASP A  46      -2.939   9.403   1.258  1.00 13.06           H  
ATOM     79  HB2 ASP A  46      -4.160   8.914   3.730  1.00 16.52           H  
ATOM     80  HB3 ASP A  46      -4.966   8.853   2.395  1.00 16.52           H  
ATOM     81  N   PHE A  47      -3.781  11.874   3.069  1.00 10.47           N  
ANISOU   81  N   PHE A  47     1192   1109   1676    302   -163   -203       N  
ATOM     82  CA  PHE A  47      -4.405  13.193   2.985  1.00 10.68           C  
ANISOU   82  CA  PHE A  47     1221   1232   1606    148    -25   -292       C  
ATOM     83  C   PHE A  47      -3.816  14.004   1.865  1.00  9.99           C  
ANISOU   83  C   PHE A  47     1176   1089   1530    152     16   -341       C  
ATOM     84  O   PHE A  47      -4.518  14.627   1.083  1.00 10.21           O  
ANISOU   84  O   PHE A  47     1218   1230   1430    224    -26   -160       O  
ATOM     85  CB  PHE A  47      -4.194  13.907   4.356  1.00 10.38           C  
ANISOU   85  CB  PHE A  47     1316   1266   1362    160    -59   -191       C  
ATOM     86  CG  PHE A  47      -4.893  15.269   4.429  1.00  9.06           C  
ANISOU   86  CG  PHE A  47     1185    991   1265    104     32    -69       C  
ATOM     87  CD1 PHE A  47      -4.378  16.375   3.845  1.00  9.66           C  
ANISOU   87  CD1 PHE A  47      984   1352   1333    114    128    -24       C  
ATOM     88  CD2 PHE A  47      -6.105  15.353   5.092  1.00  9.96           C  
ANISOU   88  CD2 PHE A  47     1196   1108   1481    -21     56     16       C  
ATOM     89  CE1 PHE A  47      -5.007  17.581   3.856  1.00 11.14           C  
ANISOU   89  CE1 PHE A  47     1523    929   1782     33    191   -210       C  
ATOM     90  CE2 PHE A  47      -6.762  16.537   5.120  1.00 11.60           C  
ANISOU   90  CE2 PHE A  47     1407   1263   1737    193    355   -166       C  
ATOM     91  CZ  PHE A  47      -6.244  17.653   4.497  1.00 11.82           C  
ANISOU   91  CZ  PHE A  47     1459   1052   1980    199    207   -135       C  
ATOM     92  H   PHE A  47      -3.393  11.628   3.796  1.00 12.56           H  
ATOM     93  HA  PHE A  47      -5.366  13.082   2.827  1.00 12.82           H  
ATOM     94  HB2 PHE A  47      -4.534  13.339   5.064  1.00 12.45           H  
ATOM     95  HB3 PHE A  47      -3.244  14.031   4.505  1.00 12.45           H  
ATOM     96  HD1 PHE A  47      -3.556  16.308   3.416  1.00 11.59           H  
ATOM     97  HD2 PHE A  47      -6.464  14.606   5.512  1.00 11.96           H  
ATOM     98  HE1 PHE A  47      -4.627  18.328   3.453  1.00 13.37           H  
ATOM     99  HE2 PHE A  47      -7.575  16.599   5.568  1.00 13.92           H  
ATOM    100  HZ  PHE A  47      -6.719  18.453   4.503  1.00 14.18           H  
ATOM    101  N   LYS A  48      -2.443  14.021   1.810  1.00 11.01           N  
ANISOU  101  N   LYS A  48     1071   1214   1899    144     -2   -219       N  
ATOM    102  CA  LYS A  48      -1.810  14.768   0.755  1.00 11.52           C  
ANISOU  102  CA  LYS A  48     1216   1187   1975    164     20   -376       C  
ATOM    103  C   LYS A  48      -2.187  14.234  -0.636  1.00 12.18           C  
ANISOU  103  C   LYS A  48     1159   1342   2128     26    179   -259       C  
ATOM    104  O   LYS A  48      -2.343  15.008  -1.562  1.00 13.18           O  
ANISOU  104  O   LYS A  48     1609   1632   1769    139    187   -307       O  
ATOM    105  CB  LYS A  48      -0.294  14.743   0.906  1.00 16.55           C  
ANISOU  105  CB  LYS A  48     1325   2425   2539   -177    136   -568       C  
ATOM    106  CG  LYS A  48       0.503  15.489  -0.165  1.00 18.60           C  
ANISOU  106  CG  LYS A  48     1658   2749   2659   -491    -47   -240       C  
ATOM    107  CD  LYS A  48       2.005  15.460   0.014  1.00 28.97           C  
ANISOU  107  CD  LYS A  48     1553   3467   5986   -691    572  -1112       C  
ATOM    108  CE  LYS A  48       2.641  15.546  -1.374  1.00 42.35           C  
ANISOU  108  CE  LYS A  48     3407   4894   7792  -1097   2707     81       C  
ATOM    109  NZ  LYS A  48       4.124  15.435  -1.322  1.00 60.82           N  
ANISOU  109  NZ  LYS A  48     3511   7063  12535    278   3946   1307       N  
ATOM    110  H   LYS A  48      -1.973  13.597   2.392  1.00 13.22           H  
ATOM    111  HA  LYS A  48      -2.109  15.699   0.816  1.00 13.83           H  
ATOM    112  HB2 LYS A  48      -0.069  15.122   1.771  1.00 19.86           H  
ATOM    113  HB3 LYS A  48      -0.004  13.818   0.911  1.00 19.86           H  
ATOM    114  HG2 LYS A  48       0.289  15.105  -1.030  1.00 22.32           H  
ATOM    115  HG3 LYS A  48       0.212  16.414  -0.176  1.00 22.32           H  
ATOM    116  HD2 LYS A  48       2.291  16.209   0.560  1.00 34.76           H  
ATOM    117  HD3 LYS A  48       2.274  14.639   0.454  1.00 34.76           H  
ATOM    118  HE2 LYS A  48       2.287  14.835  -1.930  1.00 50.82           H  
ATOM    119  HE3 LYS A  48       2.399  16.392  -1.783  1.00 50.82           H  
ATOM    120  HZ1 LYS A  48       4.452  15.449  -2.150  1.00 91.23           H  
ATOM    121  HZ2 LYS A  48       4.351  14.671  -0.926  1.00 91.23           H  
ATOM    122  HZ3 LYS A  48       4.457  16.119  -0.860  1.00 91.23           H  
ATOM    123  N   ALA A  49      -2.299  12.934  -0.784  1.00 11.63           N  
ANISOU  123  N   ALA A  49     1182   1336   1902    165     70   -489       N  
ATOM    124  CA  ALA A  49      -2.705  12.344  -2.049  1.00 12.53           C  
ANISOU  124  CA  ALA A  49     1367   1561   1831    235    258   -435       C  
ATOM    125  C   ALA A  49      -4.124  12.789  -2.416  1.00 12.02           C  
ANISOU  125  C   ALA A  49     1309   1523   1734    -98    213   -405       C  
ATOM    126  O   ALA A  49      -4.398  13.175  -3.567  1.00 12.87           O  
ANISOU  126  O   ALA A  49     1754   1436   1698    -39    -15   -130       O  
ATOM    127  CB  ALA A  49      -2.644  10.832  -1.966  1.00 14.66           C  
ANISOU  127  CB  ALA A  49     1590   1625   2353    327      1   -794       C  
ATOM    128  H   ALA A  49      -2.128  12.420  -0.116  1.00 13.96           H  
ATOM    129  HA  ALA A  49      -2.090  12.646  -2.749  1.00 15.03           H  
ATOM    130  HB1 ALA A  49      -1.751  10.560  -1.742  1.00 21.98           H  
ATOM    131  HB2 ALA A  49      -2.890  10.455  -2.814  1.00 21.98           H  
ATOM    132  HB3 ALA A  49      -3.251  10.524  -1.290  1.00 21.98           H  
ATOM    133  N   VAL A  50      -5.037  12.699  -1.455  1.00 11.41           N  
ANISOU  133  N   VAL A  50     1156   1375   1806     14    141   -405       N  
ATOM    134  CA  VAL A  50      -6.464  13.034  -1.752  1.00 10.98           C  
ANISOU  134  CA  VAL A  50     1212   1545   1415    101    -63   -341       C  
ATOM    135  C   VAL A  50      -6.650  14.522  -2.043  1.00 11.31           C  
ANISOU  135  C   VAL A  50     1205   1411   1682     60    -22   -314       C  
ATOM    136  O   VAL A  50      -7.310  14.909  -3.025  1.00 13.19           O  
ANISOU  136  O   VAL A  50     1591   1816   1603    245   -246   -317       O  
ATOM    137  CB  VAL A  50      -7.374  12.556  -0.622  1.00 10.98           C  
ANISOU  137  CB  VAL A  50     1188   1320   1664    -60    -67   -294       C  
ATOM    138  CG1 VAL A  50      -8.787  13.095  -0.797  1.00 12.38           C  
ANISOU  138  CG1 VAL A  50     1141   1710   1854     -6    -51   -316       C  
ATOM    139  CG2 VAL A  50      -7.406  11.011  -0.553  1.00 12.33           C  
ANISOU  139  CG2 VAL A  50     1343   1503   1841    -36     -7   -257       C  
ATOM    140  H   VAL A  50      -4.808  12.448  -0.664  1.00 13.70           H  
ATOM    141  HA  VAL A  50      -6.719  12.543  -2.561  1.00 13.17           H  
ATOM    142  HB  VAL A  50      -7.017  12.895   0.225  1.00 13.18           H  
ATOM    143 HG11 VAL A  50      -9.339  12.786  -0.074  1.00 18.57           H  
ATOM    144 HG12 VAL A  50      -9.148  12.783  -1.630  1.00 18.57           H  
ATOM    145 HG13 VAL A  50      -8.766  14.054  -0.797  1.00 18.57           H  
ATOM    146 HG21 VAL A  50      -6.513  10.677  -0.441  1.00 18.50           H  
ATOM    147 HG22 VAL A  50      -7.779  10.662  -1.366  1.00 18.50           H  
ATOM    148 HG23 VAL A  50      -7.946  10.735   0.191  1.00 18.50           H  
ATOM    149  N   PHE A  51      -6.049  15.385  -1.223  1.00 10.46           N  
ANISOU  149  N   PHE A  51      997   1452   1526     85     69   -209       N  
ATOM    150  CA  PHE A  51      -6.345  16.806  -1.316  1.00 11.37           C  
ANISOU  150  CA  PHE A  51     1317   1400   1600    229    100   -253       C  
ATOM    151  C   PHE A  51      -5.283  17.627  -2.045  1.00 12.04           C  
ANISOU  151  C   PHE A  51     1356   1544   1674     94     43    -38       C  
ATOM    152  O   PHE A  51      -5.519  18.825  -2.256  1.00 13.30           O  
ANISOU  152  O   PHE A  51     1494   1848   1710    379    159    222       O  
ATOM    153  CB  PHE A  51      -6.535  17.397   0.137  1.00 10.44           C  
ANISOU  153  CB  PHE A  51     1416   1200   1350    313     -8    -91       C  
ATOM    154  CG  PHE A  51      -7.796  16.781   0.760  1.00 10.73           C  
ANISOU  154  CG  PHE A  51     1122   1584   1370    421      0   -110       C  
ATOM    155  CD1 PHE A  51      -9.033  17.184   0.302  1.00 11.39           C  
ANISOU  155  CD1 PHE A  51     1289   1350   1689    259    -58   -202       C  
ATOM    156  CD2 PHE A  51      -7.755  15.829   1.743  1.00 11.23           C  
ANISOU  156  CD2 PHE A  51     1196   1399   1670    141     85    -74       C  
ATOM    157  CE1 PHE A  51     -10.197  16.642   0.792  1.00 12.07           C  
ANISOU  157  CE1 PHE A  51     1155   1356   2073    311    -87   -247       C  
ATOM    158  CE2 PHE A  51      -8.921  15.248   2.276  1.00 11.64           C  
ANISOU  158  CE2 PHE A  51     1224   1318   1881    262    104   -150       C  
ATOM    159  CZ  PHE A  51     -10.154  15.674   1.810  1.00 12.62           C  
ANISOU  159  CZ  PHE A  51     1150   1584   2062    223    214   -144       C  
ATOM    160  H   PHE A  51      -5.485  15.101  -0.639  1.00 12.55           H  
ATOM    161  HA  PHE A  51      -7.192  16.908  -1.798  1.00 13.64           H  
ATOM    162  HB2 PHE A  51      -5.760  17.189   0.683  1.00 12.53           H  
ATOM    163  HB3 PHE A  51      -6.625  18.362   0.092  1.00 12.53           H  
ATOM    164  HD1 PHE A  51      -9.080  17.841  -0.355  1.00 13.67           H  
ATOM    165  HD2 PHE A  51      -6.928  15.557   2.070  1.00 13.47           H  
ATOM    166  HE1 PHE A  51     -11.017  16.916   0.448  1.00 14.48           H  
ATOM    167  HE2 PHE A  51      -8.864  14.590   2.930  1.00 13.97           H  
ATOM    168  HZ  PHE A  51     -10.940  15.325   2.165  1.00 15.15           H  
ATOM    169  N   GLY A  52      -4.160  17.020  -2.398  1.00 12.05           N  
ANISOU  169  N   GLY A  52     1549   1541   1490    253    293    -22       N  
ATOM    170  CA  GLY A  52      -3.152  17.734  -3.159  1.00 13.16           C  
ANISOU  170  CA  GLY A  52     1624   1798   1576    184    258    -44       C  
ATOM    171  C   GLY A  52      -2.336  18.749  -2.441  1.00 13.45           C  
ANISOU  171  C   GLY A  52     1729   1631   1751    166    751    -38       C  
ATOM    172  O   GLY A  52      -1.709  19.617  -3.072  1.00 15.73           O  
ANISOU  172  O   GLY A  52     2172   1921   1885   -104    923    231       O  
ATOM    173  H   GLY A  52      -4.028  16.200  -2.176  1.00 14.46           H  
ATOM    174  HA2 GLY A  52      -2.545  17.079  -3.539  1.00 15.79           H  
ATOM    175  HA3 GLY A  52      -3.595  18.177  -3.899  1.00 15.79           H  
ATOM    176  N   MET A  53      -2.324  18.667  -1.103  1.00 11.69           N  
ANISOU  176  N   MET A  53     1502   1297   1641     38    428     88       N  
ATOM    177  CA  MET A  53      -1.538  19.556  -0.264  1.00 11.76           C  
ANISOU  177  CA  MET A  53     1346   1415   1709     12    507    101       C  
ATOM    178  C   MET A  53      -1.479  18.929   1.119  1.00 10.80           C  
ANISOU  178  C   MET A  53     1181   1187   1735    123    431     39       C  
ATOM    179  O   MET A  53      -2.277  18.005   1.409  1.00 11.15           O  
ANISOU  179  O   MET A  53     1313   1267   1656    -11    305     43       O  
ATOM    180  CB  MET A  53      -2.109  20.972  -0.233  1.00 11.87           C  
ANISOU  180  CB  MET A  53     1486   1483   1539    122    375    106       C  
ATOM    181  CG  MET A  53      -3.419  21.070   0.538  1.00 11.04           C  
ANISOU  181  CG  MET A  53     1132   1344   1721    117    282    199       C  
ATOM    182  SD  MET A  53      -4.172  22.713   0.458  1.00 13.43           S  
ANISOU  182  SD  MET A  53     1755   1597   1749    462    508    327       S  
ATOM    183  CE  MET A  53      -4.809  22.707  -1.193  1.00 22.18           C  
ANISOU  183  CE  MET A  53     3005   3879   1544   1957    415    581       C  
ATOM    184  H   MET A  53      -2.803  18.061  -0.725  1.00 14.02           H  
ATOM    185  HA  MET A  53      -0.627  19.598  -0.625  1.00 14.12           H  
ATOM    186  HB2 MET A  53      -1.459  21.566   0.174  1.00 14.24           H  
ATOM    187  HB3 MET A  53      -2.257  21.273  -1.143  1.00 14.24           H  
ATOM    188  HG2 MET A  53      -4.043  20.420   0.182  1.00 13.25           H  
ATOM    189  HG3 MET A  53      -3.254  20.844   1.467  1.00 13.25           H  
ATOM    190  HE1 MET A  53      -5.244  23.544  -1.371  1.00 33.27           H  
ATOM    191  HE2 MET A  53      -5.442  21.991  -1.289  1.00 33.27           H  
ATOM    192  HE3 MET A  53      -4.088  22.581  -1.814  1.00 33.27           H  
ATOM    193  N   THR A  54      -0.583  19.399   1.951  1.00 11.37           N  
ANISOU  193  N   THR A  54     1064   1194   2064    -14    342    102       N  
ATOM    194  CA  THR A  54      -0.515  18.886   3.302  1.00 11.16           C  
ANISOU  194  CA  THR A  54      967   1224   2050     18    108    135       C  
ATOM    195  C   THR A  54      -1.711  19.353   4.167  1.00 10.61           C  
ANISOU  195  C   THR A  54      984   1376   1670    -71     19    170       C  
ATOM    196  O   THR A  54      -2.378  20.346   3.858  1.00 10.26           O  
ANISOU  196  O   THR A  54     1059   1197   1643     60    105    193       O  
ATOM    197  CB  THR A  54       0.792  19.274   4.007  1.00 12.09           C  
ANISOU  197  CB  THR A  54     1018   1341   2237    -55    100    206       C  
ATOM    198  OG1 THR A  54       0.813  20.708   4.039  1.00 12.97           O  
ANISOU  198  OG1 THR A  54     1185   1312   2432   -138    -70    -65       O  
ATOM    199  CG2 THR A  54       2.066  18.800   3.285  1.00 12.71           C  
ANISOU  199  CG2 THR A  54     1036   1477   2315    141     86    245       C  
ATOM    200  H   THR A  54      -0.036  20.011   1.694  1.00 13.65           H  
ATOM    201  HA  THR A  54      -0.548  17.908   3.252  1.00 13.40           H  
ATOM    202  HB  THR A  54       0.787  18.925   4.923  1.00 14.51           H  
ATOM    203  HG1 THR A  54       1.494  20.963   4.419  1.00 19.46           H  
ATOM    204 HG21 THR A  54       2.838  19.071   3.787  1.00 19.06           H  
ATOM    205 HG22 THR A  54       2.101  19.191   2.409  1.00 19.06           H  
ATOM    206 HG23 THR A  54       2.053  17.843   3.208  1.00 19.06           H  
ATOM    207  N   ARG A  55      -1.894  18.683   5.279  1.00 12.21           N  
ANISOU  207  N   ARG A  55     1125   1464   2052     75    171    430       N  
ATOM    208  CA  ARG A  55      -2.838  19.161   6.294  1.00 12.16           C  
ANISOU  208  CA  ARG A  55     1029   1902   1690     51     35    338       C  
ATOM    209  C   ARG A  55      -2.564  20.589   6.726  1.00 13.13           C  
ANISOU  209  C   ARG A  55     1384   1652   1954    128   -134    371       C  
ATOM    210  O   ARG A  55      -3.492  21.364   6.897  1.00 13.08           O  
ANISOU  210  O   ARG A  55     1478   1965   1526    281    140    359       O  
ATOM    211  CB  ARG A  55      -2.783  18.306   7.535  1.00 14.52           C  
ANISOU  211  CB  ARG A  55     1645   1971   1899    119     18    623       C  
ATOM    212  CG  ARG A  55      -3.222  16.899   7.414  1.00 15.30           C  
ANISOU  212  CG  ARG A  55     1641   1802   2368    268    212    -95       C  
ATOM    213  CD  ARG A  55      -3.404  16.378   8.873  1.00 23.96           C  
ANISOU  213  CD  ARG A  55     3099   2824   3180   -841  -1322   1593       C  
ATOM    214  NE  ARG A  55      -3.607  14.954   8.600  1.00 19.70           N  
ANISOU  214  NE  ARG A  55     1829   3095   2562   -378   -343   1251       N  
ATOM    215  CZ  ARG A  55      -4.843  14.466   8.471  1.00 15.14           C  
ANISOU  215  CZ  ARG A  55     1734   2531   1486   -395    224    717       C  
ATOM    216  NH1 ARG A  55      -5.934  15.224   8.609  1.00 16.45           N  
ANISOU  216  NH1 ARG A  55     1916   2931   1403   -298    140    492       N  
ATOM    217  NH2 ARG A  55      -4.926  13.186   8.190  1.00 19.85           N  
ANISOU  217  NH2 ARG A  55     2931   2544   2066   -294    370    658       N  
ATOM    218  H   ARG A  55      -1.455  17.957   5.415  1.00 14.66           H  
ATOM    219  HA  ARG A  55      -3.744  19.115   5.924  1.00 14.60           H  
ATOM    220  HB2 ARG A  55      -1.869  18.306   7.858  1.00 17.42           H  
ATOM    221  HB3 ARG A  55      -3.328  18.731   8.216  1.00 17.42           H  
ATOM    222  HG2 ARG A  55      -4.059  16.844   6.927  1.00 18.35           H  
ATOM    223  HG3 ARG A  55      -2.555  16.373   6.946  1.00 18.35           H  
ATOM    224  HD2 ARG A  55      -2.614  16.533   9.414  1.00 28.75           H  
ATOM    225  HD3 ARG A  55      -4.176  16.776   9.305  1.00 28.75           H  
ATOM    226  HE  ARG A  55      -2.929  14.431   8.523  1.00 23.64           H  
ATOM    227 HH11 ARG A  55      -6.714  14.876   8.514  1.00 19.74           H  
ATOM    228 HH12 ARG A  55      -5.855  16.060   8.793  1.00 19.74           H  
ATOM    229 HH21 ARG A  55      -5.696  12.816   8.091  1.00 23.82           H  
ATOM    230 HH22 ARG A  55      -4.210  12.717   8.106  1.00 23.82           H  
ATOM    231  N   SER A  56      -1.281  20.890   6.924  1.00 14.12           N  
ANISOU  231  N   SER A  56     1280   2027   2058     19   -187    305       N  
ATOM    232  CA  SER A  56      -0.951  22.229   7.342  1.00 15.49           C  
ANISOU  232  CA  SER A  56     1477   2173   2236    -77   -474    145       C  
ATOM    233  C   SER A  56      -1.420  23.252   6.311  1.00 13.79           C  
ANISOU  233  C   SER A  56     1211   1811   2216    -27    197     14       C  
ATOM    234  O   SER A  56      -1.889  24.324   6.667  1.00 14.90           O  
ANISOU  234  O   SER A  56     1715   2086   1860    127   -182   -301       O  
ATOM    235  CB ASER A  56       0.571  22.309   7.531  0.50 17.74           C  
ANISOU  235  CB ASER A  56     1648   2419   2673   -334   -456    455       C  
ATOM    236  CB BSER A  56       0.557  22.369   7.583  0.50 18.13           C  
ANISOU  236  CB BSER A  56     1752   2435   2703   -378   -607    457       C  
ATOM    237  OG ASER A  56       0.810  23.598   8.048  0.50 21.38           O  
ANISOU  237  OG ASER A  56     1784   2251   4087   -349  -1152    524       O  
ATOM    238  OG BSER A  56       1.327  22.445   6.402  0.50 23.31           O  
ANISOU  238  OG BSER A  56     1776   3456   3623   -511     24    840       O  
ATOM    239  H   SER A  56      -0.666  20.301   6.805  1.00 16.95           H  
ATOM    240  HA  SER A  56      -1.390  22.414   8.198  1.00 18.59           H  
ATOM    241  HB2ASER A  56       0.876  21.629   8.151  0.50 21.29           H  
ATOM    242  HB2BSER A  56       0.716  23.168   8.110  0.50 21.76           H  
ATOM    243  HB3ASER A  56       1.029  22.189   6.685  0.50 21.29           H  
ATOM    244  HB3BSER A  56       0.861  21.609   8.104  0.50 21.76           H  
ATOM    245  HG ASER A  56       0.568  24.161   7.503  0.50 32.07           H  
ATOM    246  HG BSER A  56       1.212  21.767   5.957  0.50 34.96           H  
ATOM    247  N   ALA A  57      -1.183  22.971   5.033  1.00 12.87           N  
ANISOU  247  N   ALA A  57     1140   1549   2202   -102    120    -73       N  
ATOM    248  CA  ALA A  57      -1.605  23.886   3.988  1.00 12.33           C  
ANISOU  248  CA  ALA A  57     1161   1248   2276   -213    371     24       C  
ATOM    249  C   ALA A  57      -3.105  24.061   3.975  1.00 10.61           C  
ANISOU  249  C   ALA A  57     1191   1223   1618    -76    288     99       C  
ATOM    250  O   ALA A  57      -3.673  25.164   3.848  1.00 10.92           O  
ANISOU  250  O   ALA A  57     1465   1227   1457    -54    265    -12       O  
ATOM    251  CB  ALA A  57      -1.084  23.336   2.652  1.00 14.05           C  
ANISOU  251  CB  ALA A  57     1523   1350   2467     37   1033     93       C  
ATOM    252  H   ALA A  57      -0.776  22.242   4.825  1.00 15.45           H  
ATOM    253  HA  ALA A  57      -1.189  24.758   4.150  1.00 14.80           H  
ATOM    254  HB1 ALA A  57      -0.130  23.238   2.695  1.00 21.08           H  
ATOM    255  HB2 ALA A  57      -1.311  23.944   1.945  1.00 21.08           H  
ATOM    256  HB3 ALA A  57      -1.485  22.481   2.479  1.00 21.08           H  
ATOM    257  N   PHE A  58      -3.776  22.887   4.030  1.00  9.79           N  
ANISOU  257  N   PHE A  58     1043   1215   1459      5    340     37       N  
ATOM    258  CA  PHE A  58      -5.252  22.895   3.948  1.00  9.13           C  
ANISOU  258  CA  PHE A  58     1044   1113   1313     54     84    159       C  
ATOM    259  C   PHE A  58      -5.890  23.701   5.055  1.00  9.25           C  
ANISOU  259  C   PHE A  58      985   1245   1284    -48    109    160       C  
ATOM    260  O   PHE A  58      -6.925  24.356   4.880  1.00  9.85           O  
ANISOU  260  O   PHE A  58     1071   1258   1412     30    134     67       O  
ATOM    261  CB  PHE A  58      -5.666  21.411   3.942  1.00 10.06           C  
ANISOU  261  CB  PHE A  58     1076   1215   1531     -5    234    122       C  
ATOM    262  CG  PHE A  58      -7.107  21.102   3.609  1.00  9.27           C  
ANISOU  262  CG  PHE A  58     1040    963   1518    118    -15     40       C  
ATOM    263  CD1 PHE A  58      -8.105  20.966   4.543  1.00 10.72           C  
ANISOU  263  CD1 PHE A  58     1153   1108   1813    117    148     78       C  
ATOM    264  CD2 PHE A  58      -7.464  20.905   2.291  1.00 11.09           C  
ANISOU  264  CD2 PHE A  58     1255   1272   1686    151    219    -44       C  
ATOM    265  CE1 PHE A  58      -9.381  20.583   4.185  1.00 10.92           C  
ANISOU  265  CE1 PHE A  58     1121   1007   2019    164     54     75       C  
ATOM    266  CE2 PHE A  58      -8.704  20.536   1.877  1.00 12.03           C  
ANISOU  266  CE2 PHE A  58     1452   1313   1806    184   -294    -97       C  
ATOM    267  CZ  PHE A  58      -9.678  20.381   2.859  1.00 11.52           C  
ANISOU  267  CZ  PHE A  58     1238   1060   2081    139    -52    -75       C  
ATOM    268  H   PHE A  58      -3.349  22.146   4.112  1.00 11.74           H  
ATOM    269  HA  PHE A  58      -5.511  23.290   3.090  1.00 10.96           H  
ATOM    270  HB2 PHE A  58      -5.104  20.944   3.304  1.00 12.07           H  
ATOM    271  HB3 PHE A  58      -5.475  21.042   4.819  1.00 12.07           H  
ATOM    272  HD1 PHE A  58      -7.916  21.136   5.438  1.00 12.87           H  
ATOM    273  HD2 PHE A  58      -6.811  21.034   1.641  1.00 13.31           H  
ATOM    274  HE1 PHE A  58     -10.034  20.463   4.836  1.00 13.10           H  
ATOM    275  HE2 PHE A  58      -8.894  20.393   0.978  1.00 14.44           H  
ATOM    276  HZ  PHE A  58     -10.542  20.138   2.615  1.00 13.83           H  
ATOM    277  N   ALA A  59      -5.244  23.656   6.240  1.00 10.04           N  
ANISOU  277  N   ALA A  59     1149   1337   1331      0    -13    195       N  
ATOM    278  CA  ALA A  59      -5.744  24.329   7.395  1.00 10.25           C  
ANISOU  278  CA  ALA A  59     1247   1431   1215    -10    217    122       C  
ATOM    279  C   ALA A  59      -5.723  25.861   7.251  1.00 11.01           C  
ANISOU  279  C   ALA A  59     1270   1585   1328    -62     37    -16       C  
ATOM    280  O   ALA A  59      -6.357  26.577   8.032  1.00 12.39           O  
ANISOU  280  O   ALA A  59     1795   1582   1332    -71    201   -168       O  
ATOM    281  CB  ALA A  59      -4.972  23.872   8.630  1.00 13.23           C  
ANISOU  281  CB  ALA A  59     1727   1838   1461    116      3     53       C  
ATOM    282  H   ALA A  59      -4.511  23.211   6.300  1.00 12.05           H  
ATOM    283  HA  ALA A  59      -6.678  24.057   7.514  1.00 12.30           H  
ATOM    284  HB1 ALA A  59      -5.005  22.914   8.692  1.00 19.84           H  
ATOM    285  HB2 ALA A  59      -5.367  24.257   9.416  1.00 19.84           H  
ATOM    286  HB3 ALA A  59      -4.057  24.156   8.559  1.00 19.84           H  
ATOM    287  N   ASN A  60      -4.988  26.375   6.256  1.00 10.39           N  
ANISOU  287  N   ASN A  60     1158   1370   1421   -125      1    -64       N  
ATOM    288  CA  ASN A  60      -4.994  27.808   5.959  1.00 10.37           C  
ANISOU  288  CA  ASN A  60     1303   1213   1423    -46     82    -59       C  
ATOM    289  C   ASN A  60      -6.159  28.264   5.073  1.00 10.26           C  
ANISOU  289  C   ASN A  60     1287   1208   1404   -162    198    -65       C  
ATOM    290  O   ASN A  60      -6.373  29.467   4.960  1.00 11.80           O  
ANISOU  290  O   ASN A  60     1419   1175   1888    -94    -80   -110       O  
ATOM    291  CB  ASN A  60      -3.666  28.243   5.304  1.00 12.22           C  
ANISOU  291  CB  ASN A  60     1397   1597   1649   -360    -46     -7       C  
ATOM    292  CG  ASN A  60      -2.454  28.172   6.214  1.00 13.56           C  
ANISOU  292  CG  ASN A  60     1490   2031   1632   -382    -57    491       C  
ATOM    293  OD1 ASN A  60      -2.585  28.077   7.426  1.00 15.90           O  
ANISOU  293  OD1 ASN A  60     1960   2319   1763   -584   -318     34       O  
ATOM    294  ND2 ASN A  60      -1.230  28.311   5.673  1.00 18.68           N  
ANISOU  294  ND2 ASN A  60     1714   3606   1779   -654   -222   -148       N  
ATOM    295  H   ASN A  60      -4.501  25.850   5.781  1.00 12.47           H  
ATOM    296  HA  ASN A  60      -5.071  28.284   6.812  1.00 12.44           H  
ATOM    297  HB2 ASN A  60      -3.504  27.681   4.531  1.00 14.66           H  
ATOM    298  HB3 ASN A  60      -3.761  29.155   4.989  1.00 14.66           H  
ATOM    299 HD21 ASN A  60      -0.536  28.333   6.180  1.00 22.42           H  
ATOM    300 HD22 ASN A  60      -1.142  28.377   4.820  1.00 22.42           H  
ATOM    301  N   LEU A  61      -6.887  27.345   4.495  1.00  9.60           N  
ANISOU  301  N   LEU A  61     1116   1023   1510     92     99     16       N  
ATOM    302  CA  LEU A  61      -8.007  27.710   3.663  1.00  9.74           C  
ANISOU  302  CA  LEU A  61     1120   1127   1454    -90     74    153       C  
ATOM    303  C   LEU A  61      -9.164  28.163   4.527  1.00  9.32           C  
ANISOU  303  C   LEU A  61     1153   1143   1247    -84     63      8       C  
ATOM    304  O   LEU A  61      -9.261  27.805   5.720  1.00  9.59           O  
ANISOU  304  O   LEU A  61     1189   1218   1237    -36     45    -46       O  
ATOM    305  CB  LEU A  61      -8.413  26.529   2.780  1.00  9.79           C  
ANISOU  305  CB  LEU A  61     1199   1110   1411     60    104     82       C  
ATOM    306  CG  LEU A  61      -7.357  25.989   1.846  1.00 10.35           C  
ANISOU  306  CG  LEU A  61     1164   1396   1372     47    111    -70       C  
ATOM    307  CD1 LEU A  61      -7.851  24.720   1.202  1.00 12.71           C  
ANISOU  307  CD1 LEU A  61     1557   1379   1894     71    280   -278       C  
ATOM    308  CD2 LEU A  61      -6.996  27.006   0.785  1.00 12.89           C  
ANISOU  308  CD2 LEU A  61     1643   1696   1558    -42    420    308       C  
ATOM    309  H   LEU A  61      -6.696  26.515   4.612  1.00 11.53           H  
ATOM    310  HA  LEU A  61      -7.737  28.454   3.086  1.00 11.69           H  
ATOM    311  HB2 LEU A  61      -8.704  25.806   3.358  1.00 11.75           H  
ATOM    312  HB3 LEU A  61      -9.178  26.799   2.248  1.00 11.75           H  
ATOM    313  HG  LEU A  61      -6.554  25.782   2.368  1.00 12.42           H  
ATOM    314 HD11 LEU A  61      -7.178  24.381   0.607  1.00 19.07           H  
ATOM    315 HD12 LEU A  61      -8.652  24.904   0.707  1.00 19.07           H  
ATOM    316 HD13 LEU A  61      -8.036  24.067   1.881  1.00 19.07           H  
ATOM    317 HD21 LEU A  61      -6.323  26.640   0.207  1.00 19.34           H  
ATOM    318 HD22 LEU A  61      -6.659  27.801   1.206  1.00 19.34           H  
ATOM    319 HD23 LEU A  61      -7.777  27.223   0.271  1.00 19.34           H  
ATOM    320  N   PRO A  62     -10.115  28.916   3.990  1.00  9.74           N  
ANISOU  320  N   PRO A  62     1322   1080   1300     19    143     29       N  
ATOM    321  CA  PRO A  62     -11.336  29.283   4.776  1.00 10.34           C  
ANISOU  321  CA  PRO A  62     1318   1057   1553     61     12    -51       C  
ATOM    322  C   PRO A  62     -12.003  28.053   5.327  1.00  9.20           C  
ANISOU  322  C   PRO A  62     1122   1027   1346     28      0    -71       C  
ATOM    323  O   PRO A  62     -12.008  26.973   4.692  1.00  9.21           O  
ANISOU  323  O   PRO A  62     1202    996   1302     58     66    -72       O  
ATOM    324  CB  PRO A  62     -12.232  30.000   3.749  1.00 11.24           C  
ANISOU  324  CB  PRO A  62     1419   1141   1710    144   -166     83       C  
ATOM    325  CG  PRO A  62     -11.268  30.542   2.728  1.00 12.26           C  
ANISOU  325  CG  PRO A  62     1655   1333   1669    107   -169     53       C  
ATOM    326  CD  PRO A  62     -10.183  29.493   2.629  1.00 11.33           C  
ANISOU  326  CD  PRO A  62     1815   1061   1430     35     77     81       C  
ATOM    327  HA  PRO A  62     -11.099  29.895   5.504  1.00 12.41           H  
ATOM    328  HB2 PRO A  62     -12.855  29.379   3.340  1.00 13.49           H  
ATOM    329  HB3 PRO A  62     -12.732  30.718   4.168  1.00 13.49           H  
ATOM    330  HG2 PRO A  62     -11.707  30.666   1.872  1.00 14.71           H  
ATOM    331  HG3 PRO A  62     -10.901  31.392   3.018  1.00 14.71           H  
ATOM    332  HD2 PRO A  62     -10.415  28.815   1.976  1.00 13.60           H  
ATOM    333  HD3 PRO A  62      -9.335  29.894   2.380  1.00 13.60           H  
ATOM    334  N   LEU A  63     -12.592  28.155   6.489  1.00  9.50           N  
ANISOU  334  N   LEU A  63     1233   1016   1360      7     23   -171       N  
ATOM    335  CA  LEU A  63     -13.206  26.991   7.099  1.00  9.47           C  
ANISOU  335  CA  LEU A  63     1162   1123   1311     39     33   -145       C  
ATOM    336  C   LEU A  63     -14.300  26.401   6.233  1.00  8.79           C  
ANISOU  336  C   LEU A  63     1197    925   1217     94      5   -109       C  
ATOM    337  O   LEU A  63     -14.426  25.176   6.137  1.00  9.47           O  
ANISOU  337  O   LEU A  63     1129   1183   1288     63     27    -83       O  
ATOM    338  CB  LEU A  63     -13.751  27.296   8.492  1.00 10.54           C  
ANISOU  338  CB  LEU A  63     1224   1403   1379   -116    188   -245       C  
ATOM    339  CG  LEU A  63     -12.724  27.848   9.475  1.00 12.34           C  
ANISOU  339  CG  LEU A  63     1553   1831   1304   -257     87   -227       C  
ATOM    340  CD1 LEU A  63     -13.275  27.925  10.892  1.00 13.08           C  
ANISOU  340  CD1 LEU A  63     1836   1835   1300    -57    243   -254       C  
ATOM    341  CD2 LEU A  63     -11.427  27.034   9.480  1.00 16.11           C  
ANISOU  341  CD2 LEU A  63     1718   2739   1664    392   -125   -155       C  
ATOM    342  H   LEU A  63     -12.616  28.914   6.892  1.00 11.40           H  
ATOM    343  HA  LEU A  63     -12.509  26.308   7.199  1.00 11.36           H  
ATOM    344  HB2 LEU A  63     -14.473  27.938   8.406  1.00 12.65           H  
ATOM    345  HB3 LEU A  63     -14.126  26.482   8.862  1.00 12.65           H  
ATOM    346  HG  LEU A  63     -12.502  28.760   9.192  1.00 14.81           H  
ATOM    347 HD11 LEU A  63     -12.602  28.276  11.478  1.00 19.63           H  
ATOM    348 HD12 LEU A  63     -13.529  27.047  11.184  1.00 19.63           H  
ATOM    349 HD13 LEU A  63     -14.043  28.502  10.905  1.00 19.63           H  
ATOM    350 HD21 LEU A  63     -11.074  26.989   8.588  1.00 24.16           H  
ATOM    351 HD22 LEU A  63     -11.607  26.147   9.799  1.00 24.16           H  
ATOM    352 HD23 LEU A  63     -10.786  27.457  10.056  1.00 24.16           H  
ATOM    353  N   TRP A  64     -15.143  27.213   5.632  1.00  9.45           N  
ANISOU  353  N   TRP A  64     1157   1017   1415    281     19   -170       N  
ATOM    354  CA  TRP A  64     -16.208  26.687   4.791  1.00 10.50           C  
ANISOU  354  CA  TRP A  64     1251   1174   1565    337   -234   -281       C  
ATOM    355  C   TRP A  64     -15.626  25.944   3.609  1.00 10.21           C  
ANISOU  355  C   TRP A  64     1136   1250   1493    300   -270   -203       C  
ATOM    356  O   TRP A  64     -16.223  24.978   3.104  1.00 11.74           O  
ANISOU  356  O   TRP A  64     1237   1384   1841    263   -192   -567       O  
ATOM    357  CB ATRP A  64     -17.203  27.740   4.298  0.50 10.00           C  
ANISOU  357  CB ATRP A  64      758   1344   1697    216    177   -292       C  
ATOM    358  CB BTRP A  64     -17.069  27.881   4.303  0.50 12.24           C  
ANISOU  358  CB BTRP A  64     1423   1068   2159    304   -501   -381       C  
ATOM    359  CG ATRP A  64     -16.495  28.722   3.432  0.50 10.54           C  
ANISOU  359  CG ATRP A  64     1228    877   1902    267     66    -52       C  
ATOM    360  CG BTRP A  64     -18.028  28.187   5.428  0.50 15.02           C  
ANISOU  360  CG BTRP A  64     1235   1675   2798    614   -420   -576       C  
ATOM    361  CD1ATRP A  64     -15.961  29.930   3.767  0.50 12.24           C  
ANISOU  361  CD1ATRP A  64     1351   1154   2145    198   -288    -85       C  
ATOM    362  CD1BTRP A  64     -17.804  29.051   6.459  0.50 19.11           C  
ANISOU  362  CD1BTRP A  64     1224   3192   2846    464   -376  -1160       C  
ATOM    363  CD2ATRP A  64     -16.261  28.553   2.031  0.50 10.15           C  
ANISOU  363  CD2ATRP A  64      903   1134   1820    286   -114    184       C  
ATOM    364  CD2BTRP A  64     -19.325  27.637   5.647  0.50 16.49           C  
ANISOU  364  CD2BTRP A  64     1252   1686   3327    648   -190   -651       C  
ATOM    365  NE1ATRP A  64     -15.392  30.575   2.723  0.50 13.40           N  
ANISOU  365  NE1ATRP A  64     1472   1382   2237   -404  -1261    843       N  
ATOM    366  NE1BTRP A  64     -18.873  29.082   7.298  0.50 20.84           N  
ANISOU  366  NE1BTRP A  64     1764   3141   3013    204     35  -1154       N  
ATOM    367  CE2ATRP A  64     -15.569  29.707   1.620  0.50 10.95           C  
ANISOU  367  CE2ATRP A  64      625   1415   2123     44   -219    509       C  
ATOM    368  CE2BTRP A  64     -19.833  28.219   6.824  0.50 20.54           C  
ANISOU  368  CE2BTRP A  64     2323   2747   2733   -406    172   -581       C  
ATOM    369  CE3ATRP A  64     -16.576  27.519   1.130  0.50  9.52           C  
ANISOU  369  CE3ATRP A  64      884   1031   1703    323   -218    281       C  
ATOM    370  CE3BTRP A  64     -20.111  26.717   4.955  0.50 14.93           C  
ANISOU  370  CE3BTRP A  64     1620   1916   2135     92   -414    259       C  
ATOM    371  CZ2ATRP A  64     -15.175  29.851   0.272  0.50 12.61           C  
ANISOU  371  CZ2ATRP A  64      798   1673   2320    393    -54    593       C  
ATOM    372  CZ2BTRP A  64     -21.095  27.896   7.319  0.50 21.90           C  
ANISOU  372  CZ2BTRP A  64     2083   2571   3666     14    508  -1130       C  
ATOM    373  CZ3ATRP A  64     -16.177  27.684  -0.188  0.50 11.77           C  
ANISOU  373  CZ3ATRP A  64      935   1857   1678    315   -182    419       C  
ATOM    374  CZ3BTRP A  64     -21.357  26.393   5.442  0.50 18.44           C  
ANISOU  374  CZ3BTRP A  64     1860   2256   2890    -15    -22   -211       C  
ATOM    375  CH2ATRP A  64     -15.491  28.839  -0.591  0.50 12.90           C  
ANISOU  375  CH2ATRP A  64     1109   1921   1870    340   -155    626       C  
ATOM    376  CH2BTRP A  64     -21.840  26.983   6.613  0.50 21.77           C  
ANISOU  376  CH2BTRP A  64     2157   2201   3914   -136    552   -904       C  
ATOM    377  H   TRP A  64     -15.064  28.063   5.738  1.00 11.34           H  
ATOM    378  HA  TRP A  64     -16.710  26.038   5.327  1.00 12.60           H  
ATOM    379  HB2ATRP A  64     -17.914  27.311   3.796  0.50 12.00           H  
ATOM    380  HB2BTRP A  64     -16.509  28.650   4.114  0.50 14.69           H  
ATOM    381  HB3ATRP A  64     -17.600  28.198   5.056  0.50 12.00           H  
ATOM    382  HB3BTRP A  64     -17.555  27.643   3.498  0.50 14.69           H  
ATOM    383  HD1ATRP A  64     -15.985  30.277   4.629  0.50 14.69           H  
ATOM    384  HD1BTRP A  64     -17.027  29.549   6.573  0.50 22.94           H  
ATOM    385  HE1ATRP A  64     -15.007  31.344   2.728  0.50 16.08           H  
ATOM    386  HE1BTRP A  64     -18.939  29.562   8.009  0.50 25.01           H  
ATOM    387  HE3ATRP A  64     -17.008  26.808   1.338  0.50 11.42           H  
ATOM    388  HE3BTRP A  64     -19.794  26.323   4.170  0.50 17.92           H  
ATOM    389  HZ2ATRP A  64     -14.704  30.687   0.053  0.50 15.13           H  
ATOM    390  HZ2BTRP A  64     -21.376  28.311   8.114  0.50 26.28           H  
ATOM    391  HZ3ATRP A  64     -16.321  27.149  -0.891  0.50 14.09           H  
ATOM    392  HZ3BTRP A  64     -21.922  25.805   5.041  0.50 22.13           H  
ATOM    393  HH2ATRP A  64     -15.193  29.066  -1.491  0.50 15.48           H  
ATOM    394  HH2BTRP A  64     -22.669  26.795   6.981  0.50 26.12           H  
ATOM    395  N   LYS A  65     -14.485  26.386   3.133  1.00  9.91           N  
ANISOU  395  N   LYS A  65     1257   1031   1478    421   -278   -192       N  
ATOM    396  CA  LYS A  65     -13.841  25.745   1.965  1.00 10.39           C  
ANISOU  396  CA  LYS A  65     1422   1317   1207    397   -194    -36       C  
ATOM    397  C   LYS A  65     -13.236  24.415   2.342  1.00  9.37           C  
ANISOU  397  C   LYS A  65     1192   1070   1300    327    -54   -219       C  
ATOM    398  O   LYS A  65     -13.320  23.453   1.598  1.00 10.28           O  
ANISOU  398  O   LYS A  65     1259   1231   1415    230   -144   -317       O  
ATOM    399  CB  LYS A  65     -12.803  26.650   1.350  1.00 12.15           C  
ANISOU  399  CB  LYS A  65     2038   1167   1409    603     41     -6       C  
ATOM    400  CG  LYS A  65     -12.317  26.139   0.009  1.00 17.32           C  
ANISOU  400  CG  LYS A  65     3271   1407   1904   -199    788   -204       C  
ATOM    401  CD  LYS A  65     -11.808  27.209  -0.899  1.00 17.24           C  
ANISOU  401  CD  LYS A  65     2257   2202   2091   -137    403    238       C  
ATOM    402  CE  LYS A  65     -11.755  26.741  -2.342  1.00 16.79           C  
ANISOU  402  CE  LYS A  65     1676   2818   1886    351    176    450       C  
ATOM    403  NZ  LYS A  65     -11.214  27.823  -3.173  1.00 19.16           N  
ANISOU  403  NZ  LYS A  65     1601   3338   2339    124    118   1032       N  
ATOM    404  H   LYS A  65     -14.104  27.061   3.507  1.00 11.89           H  
ATOM    405  HA  LYS A  65     -14.534  25.581   1.292  1.00 12.46           H  
ATOM    406  HB2 LYS A  65     -13.181  27.536   1.235  1.00 14.58           H  
ATOM    407  HB3 LYS A  65     -12.048  26.725   1.954  1.00 14.58           H  
ATOM    408  HG2 LYS A  65     -11.609  25.493   0.159  1.00 20.79           H  
ATOM    409  HG3 LYS A  65     -13.048  25.677  -0.432  1.00 20.79           H  
ATOM    410  HD2 LYS A  65     -12.385  27.985  -0.835  1.00 20.69           H  
ATOM    411  HD3 LYS A  65     -10.919  27.473  -0.615  1.00 20.69           H  
ATOM    412  HE2 LYS A  65     -11.190  25.956  -2.414  1.00 20.15           H  
ATOM    413  HE3 LYS A  65     -12.646  26.506  -2.646  1.00 20.15           H  
ATOM    414  HZ1 LYS A  65     -11.185  27.558  -4.022  1.00 28.73           H  
ATOM    415  HZ2 LYS A  65     -10.393  28.026  -2.897  1.00 28.73           H  
ATOM    416  HZ3 LYS A  65     -11.737  28.540  -3.103  1.00 28.73           H  
ATOM    417  N   GLN A  66     -12.615  24.338   3.537  1.00  9.21           N  
ANISOU  417  N   GLN A  66     1172   1004   1324    142   -141    -91       N  
ATOM    418  CA  GLN A  66     -12.147  23.037   4.030  1.00  8.51           C  
ANISOU  418  CA  GLN A  66      902    991   1340    236    -36    -89       C  
ATOM    419  C   GLN A  66     -13.313  22.060   4.108  1.00  9.44           C  
ANISOU  419  C   GLN A  66      930   1113   1544     73     -3    -66       C  
ATOM    420  O   GLN A  66     -13.195  20.913   3.666  1.00 10.29           O  
ANISOU  420  O   GLN A  66     1113    956   1840    203   -153   -254       O  
ATOM    421  CB  GLN A  66     -11.539  23.190   5.397  1.00  8.91           C  
ANISOU  421  CB  GLN A  66      988    905   1492     81    -13    -70       C  
ATOM    422  CG  GLN A  66     -10.267  24.035   5.448  1.00  8.92           C  
ANISOU  422  CG  GLN A  66     1010   1091   1288    155    -10      0       C  
ATOM    423  CD  GLN A  66      -9.719  24.140   6.844  1.00 10.08           C  
ANISOU  423  CD  GLN A  66     1155   1269   1407    222   -131     36       C  
ATOM    424  OE1 GLN A  66      -9.660  23.152   7.574  1.00 11.52           O  
ANISOU  424  OE1 GLN A  66     1542   1347   1490    -44   -339     69       O  
ATOM    425  NE2 GLN A  66      -9.276  25.342   7.220  1.00 10.66           N  
ANISOU  425  NE2 GLN A  66     1355   1280   1417    148    -75    -95       N  
ATOM    426  H   GLN A  66     -12.493  25.048   4.007  1.00 11.06           H  
ATOM    427  HA  GLN A  66     -11.471  22.684   3.415  1.00 10.21           H  
ATOM    428  HB2 GLN A  66     -12.199  23.590   5.985  1.00 10.69           H  
ATOM    429  HB3 GLN A  66     -11.336  22.307   5.744  1.00 10.69           H  
ATOM    430  HG2 GLN A  66      -9.597  23.639   4.870  1.00 10.70           H  
ATOM    431  HG3 GLN A  66     -10.462  24.925   5.113  1.00 10.70           H  
ATOM    432 HE21 GLN A  66      -8.932  25.449   8.001  1.00 12.80           H  
ATOM    433 HE22 GLN A  66      -9.335  26.010   6.681  1.00 12.80           H  
ATOM    434  N   GLN A  67     -14.454  22.502   4.641  1.00  9.84           N  
ANISOU  434  N   GLN A  67     1092    951   1698     72    -12   -248       N  
ATOM    435  CA  GLN A  67     -15.624  21.639   4.734  1.00 11.02           C  
ANISOU  435  CA  GLN A  67     1153   1201   1832   -100     22   -298       C  
ATOM    436  C   GLN A  67     -16.060  21.194   3.342  1.00 11.50           C  
ANISOU  436  C   GLN A  67      977   1255   2139    287   -109   -448       C  
ATOM    437  O   GLN A  67     -16.327  20.021   3.104  1.00 13.37           O  
ANISOU  437  O   GLN A  67     1141   1391   2547     67     18   -781       O  
ATOM    438  CB  GLN A  67     -16.766  22.289   5.513  1.00 11.32           C  
ANISOU  438  CB  GLN A  67     1136   1338   1829   -113    143   -240       C  
ATOM    439  CG  GLN A  67     -17.964  21.373   5.639  1.00 12.17           C  
ANISOU  439  CG  GLN A  67     1260   1527   1838   -129     65    -54       C  
ATOM    440  CD  GLN A  67     -19.186  22.000   6.291  1.00 13.54           C  
ANISOU  440  CD  GLN A  67     1319   1648   2180    -49    253    127       C  
ATOM    441  OE1 GLN A  67     -19.611  23.084   5.886  1.00 14.64           O  
ANISOU  441  OE1 GLN A  67     1524   1811   2226    193    362    -86       O  
ATOM    442  NE2 GLN A  67     -19.738  21.339   7.291  1.00 18.34           N  
ANISOU  442  NE2 GLN A  67     1961   2772   2235    495    679    522       N  
ATOM    443  H   GLN A  67     -14.500  23.309   4.934  1.00 11.81           H  
ATOM    444  HA  GLN A  67     -15.355  20.835   5.226  1.00 13.22           H  
ATOM    445  HB2 GLN A  67     -16.453  22.527   6.399  1.00 13.59           H  
ATOM    446  HB3 GLN A  67     -17.035  23.105   5.063  1.00 13.59           H  
ATOM    447  HG2 GLN A  67     -18.211  21.065   4.753  1.00 14.61           H  
ATOM    448  HG3 GLN A  67     -17.704  20.595   6.156  1.00 14.61           H  
ATOM    449 HE21 GLN A  67     -20.427  21.662   7.692  1.00 22.01           H  
ATOM    450 HE22 GLN A  67     -19.409  20.585   7.542  1.00 22.01           H  
ATOM    451  N   HIS A  68     -16.173  22.129   2.419  1.00 11.54           N  
ANISOU  451  N   HIS A  68      987   1407   1992    288   -327   -488       N  
ATOM    452  CA  HIS A  68     -16.575  21.829   1.051  1.00 13.65           C  
ANISOU  452  CA  HIS A  68     1560   1374   2251    724   -785   -718       C  
ATOM    453  C   HIS A  68     -15.657  20.826   0.388  1.00 11.36           C  
ANISOU  453  C   HIS A  68     1363   1325   1628    374   -600   -348       C  
ATOM    454  O   HIS A  68     -16.107  19.875  -0.232  1.00 12.89           O  
ANISOU  454  O   HIS A  68     1389   1353   2157    511   -766   -602       O  
ATOM    455  CB AHIS A  68     -16.497  23.122   0.219  0.50 14.97           C  
ANISOU  455  CB AHIS A  68     1948   1673   2067   1022  -1107   -614       C  
ATOM    456  CB BHIS A  68     -16.707  23.133   0.264  0.50 16.44           C  
ANISOU  456  CB BHIS A  68     2442   1494   2311   1067  -1071   -689       C  
ATOM    457  CG AHIS A  68     -16.359  23.114  -1.272  0.50 13.66           C  
ANISOU  457  CG AHIS A  68     1432   1562   2197   1045   -705   -415       C  
ATOM    458  CG BHIS A  68     -17.493  22.690  -0.942  0.50 12.54           C  
ANISOU  458  CG BHIS A  68     1069   1816   1880    914   -450   -211       C  
ATOM    459  ND1AHIS A  68     -15.365  23.469  -2.137  0.50 15.94           N  
ANISOU  459  ND1AHIS A  68     2235   1424   2396    563   -716   -269       N  
ATOM    460  ND1BHIS A  68     -17.093  23.010  -2.214  0.50 13.78           N  
ANISOU  460  ND1BHIS A  68     1672   1535   2030    794     47   -116       N  
ATOM    461  CD2AHIS A  68     -17.324  22.633  -2.112  0.50 14.48           C  
ANISOU  461  CD2AHIS A  68     2129   1731   1642    544   -748     77       C  
ATOM    462  CD2BHIS A  68     -18.570  21.920  -1.103  0.50 12.31           C  
ANISOU  462  CD2BHIS A  68     1563   1684   1430    630   -174      6       C  
ATOM    463  CE1AHIS A  68     -15.662  23.286  -3.405  0.50 14.61           C  
ANISOU  463  CE1AHIS A  68     2053   1287   2209    660   -525   -192       C  
ATOM    464  CE1BHIS A  68     -17.963  22.488  -3.057  0.50 13.08           C  
ANISOU  464  CE1BHIS A  68     1673   1828   1468    745   -290    222       C  
ATOM    465  NE2AHIS A  68     -16.880  22.778  -3.393  0.50 15.16           N  
ANISOU  465  NE2AHIS A  68     2518   1492   1749    260   -544    -76       N  
ATOM    466  NE2BHIS A  68     -18.914  21.795  -2.396  0.50 15.49           N  
ANISOU  466  NE2BHIS A  68     2114   2086   1687    450   -305   -219       N  
ATOM    467  H   HIS A  68     -16.002  22.945   2.632  1.00 13.85           H  
ATOM    468  HA  HIS A  68     -17.494  21.489   1.045  1.00 16.37           H  
ATOM    469  HB2AHIS A  68     -17.296  23.633   0.422  0.50 17.96           H  
ATOM    470  HB2BHIS A  68     -17.188  23.805   0.772  0.50 19.73           H  
ATOM    471  HB3AHIS A  68     -15.747  23.631   0.565  0.50 17.96           H  
ATOM    472  HB3BHIS A  68     -15.839  23.483   0.011  0.50 19.73           H  
ATOM    473  HD1AHIS A  68     -14.609  23.785  -1.875  0.50 19.12           H  
ATOM    474  HD1BHIS A  68     -16.397  23.469  -2.425  0.50 16.54           H  
ATOM    475  HD2AHIS A  68     -18.141  22.270  -1.855  0.50 17.38           H  
ATOM    476  HD2BHIS A  68     -19.029  21.517  -0.402  0.50 14.77           H  
ATOM    477  HE1AHIS A  68     -15.132  23.473  -4.146  0.50 17.53           H  
ATOM    478  HE1BHIS A  68     -17.926  22.585  -3.981  0.50 15.70           H  
ATOM    479  N   LEU A  69     -14.352  21.051   0.488  1.00 10.74           N  
ANISOU  479  N   LEU A  69     1380   1100   1599    438   -412   -356       N  
ATOM    480  CA  LEU A  69     -13.421  20.190  -0.208  1.00 11.10           C  
ANISOU  480  CA  LEU A  69     1497   1113   1607    479   -336   -308       C  
ATOM    481  C   LEU A  69     -13.465  18.791   0.349  1.00 10.64           C  
ANISOU  481  C   LEU A  69     1198   1148   1697    380   -370   -260       C  
ATOM    482  O   LEU A  69     -13.356  17.799  -0.399  1.00 11.34           O  
ANISOU  482  O   LEU A  69     1473   1140   1694    359   -356   -380       O  
ATOM    483  CB  LEU A  69     -11.991  20.784  -0.171  1.00 11.79           C  
ANISOU  483  CB  LEU A  69     1590   1336   1554    225     12   -257       C  
ATOM    484  CG  LEU A  69     -11.766  22.081  -0.982  1.00 13.93           C  
ANISOU  484  CG  LEU A  69     2426   1371   1495    395     72   -172       C  
ATOM    485  CD1 LEU A  69     -10.417  22.707  -0.635  1.00 16.40           C  
ANISOU  485  CD1 LEU A  69     2296   1351   2584     24    679    -89       C  
ATOM    486  CD2 LEU A  69     -11.919  21.875  -2.459  1.00 19.45           C  
ANISOU  486  CD2 LEU A  69     4112   1824   1454    440    304      7       C  
ATOM    487  H   LEU A  69     -14.062  21.705   0.965  1.00 12.88           H  
ATOM    488  HA  LEU A  69     -13.700  20.146  -1.146  1.00 13.32           H  
ATOM    489  HB2 LEU A  69     -11.760  20.962   0.754  1.00 14.15           H  
ATOM    490  HB3 LEU A  69     -11.375  20.111  -0.499  1.00 14.15           H  
ATOM    491  HG  LEU A  69     -12.459  22.717  -0.707  1.00 16.71           H  
ATOM    492 HD11 LEU A  69     -10.351  22.819   0.316  1.00 24.60           H  
ATOM    493 HD12 LEU A  69     -10.341  23.563  -1.064  1.00 24.60           H  
ATOM    494 HD13 LEU A  69      -9.710  22.133  -0.939  1.00 24.60           H  
ATOM    495 HD21 LEU A  69     -12.777  21.484  -2.640  1.00 29.17           H  
ATOM    496 HD22 LEU A  69     -11.227  21.289  -2.773  1.00 29.17           H  
ATOM    497 HD23 LEU A  69     -11.851  22.720  -2.908  1.00 29.17           H  
ATOM    498  N   LYS A  70     -13.601  18.672   1.652  1.00 10.01           N  
ANISOU  498  N   LYS A  70      965   1097   1741    251   -367   -314       N  
ATOM    499  CA  LYS A  70     -13.729  17.362   2.262  1.00 10.62           C  
ANISOU  499  CA  LYS A  70     1109   1159   1765    224   -148   -232       C  
ATOM    500  C   LYS A  70     -15.025  16.662   1.829  1.00 10.96           C  
ANISOU  500  C   LYS A  70     1261   1123   1780    122   -189   -243       C  
ATOM    501  O   LYS A  70     -15.037  15.495   1.424  1.00 12.56           O  
ANISOU  501  O   LYS A  70     1325    967   2479    135   -193   -441       O  
ATOM    502  CB  LYS A  70     -13.639  17.415   3.777  1.00 12.59           C  
ANISOU  502  CB  LYS A  70     1975    962   1846   -168   -293   -109       C  
ATOM    503  CG  LYS A  70     -12.235  17.727   4.232  1.00 13.98           C  
ANISOU  503  CG  LYS A  70     1868   1529   1915      8   -230   -256       C  
ATOM    504  CD  LYS A  70     -12.073  17.606   5.705  1.00 17.69           C  
ANISOU  504  CD  LYS A  70     2492   2172   2057    111   -376   -365       C  
ATOM    505  CE  LYS A  70     -10.973  16.780   6.229  1.00 26.68           C  
ANISOU  505  CE  LYS A  70     2324   4636   3177    331   -639    927       C  
ATOM    506  NZ  LYS A  70     -10.787  17.210   7.642  1.00 52.52           N  
ANISOU  506  NZ  LYS A  70     8506   9051   2399  -4612  -2455   2598       N  
ATOM    507  H   LYS A  70     -13.615  19.375   2.146  1.00 12.01           H  
ATOM    508  HA  LYS A  70     -12.981  16.816   1.943  1.00 12.74           H  
ATOM    509  HB2 LYS A  70     -14.244  18.096   4.112  1.00 15.11           H  
ATOM    510  HB3 LYS A  70     -13.914  16.562   4.146  1.00 15.11           H  
ATOM    511  HG2 LYS A  70     -11.617  17.121   3.794  1.00 16.78           H  
ATOM    512  HG3 LYS A  70     -12.007  18.631   3.962  1.00 16.78           H  
ATOM    513  HD2 LYS A  70     -11.967  18.500   6.064  1.00 21.23           H  
ATOM    514  HD3 LYS A  70     -12.903  17.252   6.063  1.00 21.23           H  
ATOM    515  HE2 LYS A  70     -11.201  15.839   6.185  1.00 32.02           H  
ATOM    516  HE3 LYS A  70     -10.162  16.928   5.717  1.00 32.02           H  
ATOM    517  HZ1 LYS A  70     -10.127  16.739   8.010  1.00 78.78           H  
ATOM    518  HZ2 LYS A  70     -11.540  17.071   8.095  1.00 78.78           H  
ATOM    519  HZ3 LYS A  70     -10.582  18.075   7.664  1.00 78.78           H  
ATOM    520  N   LYS A  71     -16.152  17.368   1.871  1.00 12.18           N  
ANISOU  520  N   LYS A  71     1194   1163   2272    195   -105   -553       N  
ATOM    521  CA  LYS A  71     -17.421  16.759   1.466  1.00 14.09           C  
ANISOU  521  CA  LYS A  71     1272   1518   2565     80   -393   -760       C  
ATOM    522  C   LYS A  71     -17.394  16.353  -0.012  1.00 13.17           C  
ANISOU  522  C   LYS A  71     1215   1427   2359    205   -412   -585       C  
ATOM    523  O   LYS A  71     -17.958  15.323  -0.358  1.00 14.96           O  
ANISOU  523  O   LYS A  71     1479   1470   2733    188   -608   -664       O  
ATOM    524  CB  LYS A  71     -18.576  17.694   1.832  1.00 16.67           C  
ANISOU  524  CB  LYS A  71     1004   2014   3318     70   -139   -989       C  
ATOM    525  CG  LYS A  71     -18.752  17.719   3.380  1.00 20.57           C  
ANISOU  525  CG  LYS A  71     1847   2561   3409    223    -66  -1386       C  
ATOM    526  CD  LYS A  71     -19.956  18.416   3.933  1.00 24.81           C  
ANISOU  526  CD  LYS A  71     2155   2928   4345    192    511  -1444       C  
ATOM    527  CE  LYS A  71     -20.269  18.227   5.410  1.00 26.14           C  
ANISOU  527  CE  LYS A  71     2217   3367   4348   -105    564  -1706       C  
ATOM    528  NZ  LYS A  71     -21.650  18.772   5.665  1.00 24.54           N  
ANISOU  528  NZ  LYS A  71     1936   3432   3956    362    470   1306       N  
ATOM    529  H   LYS A  71     -16.135  18.185   2.137  1.00 14.62           H  
ATOM    530  HA  LYS A  71     -17.531  15.939   1.991  1.00 16.91           H  
ATOM    531  HB2 LYS A  71     -18.389  18.589   1.509  1.00 20.01           H  
ATOM    532  HB3 LYS A  71     -19.394  17.384   1.414  1.00 20.01           H  
ATOM    533  HG2 LYS A  71     -18.769  16.801   3.693  1.00 24.69           H  
ATOM    534  HG3 LYS A  71     -17.964  18.136   3.762  1.00 24.69           H  
ATOM    535  HD2 LYS A  71     -19.850  19.366   3.771  1.00 29.78           H  
ATOM    536  HD3 LYS A  71     -20.729  18.123   3.425  1.00 29.78           H  
ATOM    537  HE2 LYS A  71     -20.234  17.285   5.641  1.00 31.37           H  
ATOM    538  HE3 LYS A  71     -19.618  18.700   5.952  1.00 31.37           H  
ATOM    539  HZ1 LYS A  71     -21.853  18.674   6.526  1.00 36.81           H  
ATOM    540  HZ2 LYS A  71     -22.240  18.328   5.169  1.00 36.81           H  
ATOM    541  HZ3 LYS A  71     -21.672  19.635   5.452  1.00 36.81           H  
ATOM    542  N   GLU A  72     -16.796  17.159  -0.860  1.00 13.47           N  
ANISOU  542  N   GLU A  72     1455   1285   2377    427   -622   -583       N  
ATOM    543  CA  GLU A  72     -16.701  16.806  -2.262  1.00 14.94           C  
ANISOU  543  CA  GLU A  72     2084   1485   2106    355   -868   -515       C  
ATOM    544  C   GLU A  72     -15.959  15.495  -2.475  1.00 13.89           C  
ANISOU  544  C   GLU A  72     1839   1248   2190    208   -532   -510       C  
ATOM    545  O   GLU A  72     -16.239  14.825  -3.474  1.00 17.05           O  
ANISOU  545  O   GLU A  72     2630   1464   2385    290   -946   -652       O  
ATOM    546  CB  GLU A  72     -16.025  17.916  -3.064  1.00 16.23           C  
ANISOU  546  CB  GLU A  72     2047   1439   2681    139   -418   -537       C  
ATOM    547  CG  GLU A  72     -16.872  19.144  -3.377  1.00 21.33           C  
ANISOU  547  CG  GLU A  72     2861   1681   3562    301  -1494   -337       C  
ATOM    548  CD  GLU A  72     -18.054  18.817  -4.263  1.00 25.01           C  
ANISOU  548  CD  GLU A  72     3141   2525   3835    682  -1787  -1316       C  
ATOM    549  OE1 GLU A  72     -19.258  19.050  -3.887  1.00 29.61           O  
ANISOU  549  OE1 GLU A  72     2887   3908   4456   1140  -1911  -1749       O  
ATOM    550  OE2 GLU A  72     -17.820  18.304  -5.393  1.00 26.68           O  
ANISOU  550  OE2 GLU A  72     3574   3220   3344    726  -1449   -827       O  
ATOM    551  H   GLU A  72     -16.459  17.899  -0.581  1.00 16.16           H  
ATOM    552  HA  GLU A  72     -17.611  16.697  -2.607  1.00 17.92           H  
ATOM    553  HB2 GLU A  72     -15.240  18.208  -2.575  1.00 19.48           H  
ATOM    554  HB3 GLU A  72     -15.719  17.539  -3.904  1.00 19.48           H  
ATOM    555  HG2 GLU A  72     -17.193  19.528  -2.546  1.00 25.59           H  
ATOM    556  HG3 GLU A  72     -16.319  19.808  -3.817  1.00 25.59           H  
ATOM    557  N   LYS A  73     -15.043  15.139  -1.589  1.00 12.94           N  
ANISOU  557  N   LYS A  73     1785   1217   1915    255   -435   -465       N  
ATOM    558  CA  LYS A  73     -14.244  13.928  -1.666  1.00 13.02           C  
ANISOU  558  CA  LYS A  73     1802   1214   1931    341   -104   -559       C  
ATOM    559  C   LYS A  73     -14.885  12.823  -0.810  1.00 13.18           C  
ANISOU  559  C   LYS A  73     1502   1084   2423    188   -108   -591       C  
ATOM    560  O   LYS A  73     -14.334  11.732  -0.639  1.00 13.71           O  
ANISOU  560  O   LYS A  73     1578   1216   2415    168   -212   -546       O  
ATOM    561  CB  LYS A  73     -12.790  14.191  -1.279  1.00 13.44           C  
ANISOU  561  CB  LYS A  73     1739   1322   2046      0   -244   -409       C  
ATOM    562  CG  LYS A  73     -11.929  15.017  -2.210  1.00 15.18           C  
ANISOU  562  CG  LYS A  73     2010   1738   2018    333    130   -260       C  
ATOM    563  CD  LYS A  73     -11.554  14.311  -3.480  1.00 18.87           C  
ANISOU  563  CD  LYS A  73     2918   1798   2452     43    339   -523       C  
ATOM    564  CE  LYS A  73     -10.653  15.125  -4.414  1.00 17.92           C  
ANISOU  564  CE  LYS A  73     2511   2632   1665    710    147   -117       C  
ATOM    565  NZ  LYS A  73     -11.353  16.257  -5.013  1.00 21.98           N  
ANISOU  565  NZ  LYS A  73     3600   2230   2522    580   -276   -145       N  
ATOM    566  H   LYS A  73     -14.910  15.663  -0.919  1.00 15.53           H  
ATOM    567  HA  LYS A  73     -14.254  13.625  -2.598  1.00 15.62           H  
ATOM    568  HB2 LYS A  73     -12.790  14.628  -0.413  1.00 16.13           H  
ATOM    569  HB3 LYS A  73     -12.356  13.331  -1.163  1.00 16.13           H  
ATOM    570  HG2 LYS A  73     -12.406  15.831  -2.435  1.00 18.21           H  
ATOM    571  HG3 LYS A  73     -11.118  15.271  -1.742  1.00 18.21           H  
ATOM    572  HD2 LYS A  73     -11.099  13.485  -3.252  1.00 22.64           H  
ATOM    573  HD3 LYS A  73     -12.365  14.078  -3.957  1.00 22.64           H  
ATOM    574  HE2 LYS A  73      -9.889  15.452  -3.913  1.00 21.50           H  
ATOM    575  HE3 LYS A  73     -10.322  14.547  -5.119  1.00 21.50           H  
ATOM    576  HZ1 LYS A  73     -10.799  16.695  -5.555  1.00 32.97           H  
ATOM    577  HZ2 LYS A  73     -11.635  16.805  -4.371  1.00 32.97           H  
ATOM    578  HZ3 LYS A  73     -12.051  15.961  -5.479  1.00 32.97           H  
ATOM    579  N   GLY A  74     -16.077  13.044  -0.279  1.00 14.34           N  
ANISOU  579  N   GLY A  74     1384   1178   2887     12   -170   -629       N  
ATOM    580  CA  GLY A  74     -16.752  12.057   0.531  1.00 15.94           C  
ANISOU  580  CA  GLY A  74     1172   1435   3450     30    109   -587       C  
ATOM    581  C   GLY A  74     -16.220  11.817   1.937  1.00 16.82           C  
ANISOU  581  C   GLY A  74     1698   1408   3286    237    381   -363       C  
ATOM    582  O   GLY A  74     -16.577  10.749   2.485  1.00 19.51           O  
ANISOU  582  O   GLY A  74     2547   1627   3237   -208    955   -534       O  
ATOM    583  H   GLY A  74     -16.462  13.799  -0.422  1.00 17.21           H  
ATOM    584  HA2 GLY A  74     -17.683  12.317   0.605  1.00 19.13           H  
ATOM    585  HA3 GLY A  74     -16.728  11.212   0.054  1.00 19.13           H  
ATOM    586  N   LEU A  75     -15.494  12.793   2.472  1.00 15.06           N  
ANISOU  586  N   LEU A  75     1692   1566   2464     21    597   -389       N  
ATOM    587  CA  LEU A  75     -14.840  12.798   3.791  1.00 17.22           C  
ANISOU  587  CA  LEU A  75     2589   1876   2079    158    695    107       C  
ATOM    588  C   LEU A  75     -15.429  13.866   4.700  1.00 21.12           C  
ANISOU  588  C   LEU A  75     3802   2201   2023    441    624     -5       C  
ATOM    589  O   LEU A  75     -16.185  14.761   4.254  1.00 29.19           O  
ANISOU  589  O   LEU A  75     4912   3147   3030   1847    505    -78       O  
ATOM    590  CB  LEU A  75     -13.307  12.989   3.652  1.00 16.33           C  
ANISOU  590  CB  LEU A  75     2552   1625   2025   -305   -234    125       C  
ATOM    591  CG  LEU A  75     -12.603  11.879   2.875  1.00 18.34           C  
ANISOU  591  CG  LEU A  75     1390   1882   3695    -33   -170    -17       C  
ATOM    592  CD1 LEU A  75     -11.302  12.226   2.169  1.00 19.26           C  
ANISOU  592  CD1 LEU A  75     2536   2773   2011   -297    109    -83       C  
ATOM    593  CD2 LEU A  75     -12.235  10.754   3.868  1.00 19.94           C  
ANISOU  593  CD2 LEU A  75     2472   1659   3447    -40    560    -44       C  
ATOM    594  H   LEU A  75     -15.396  13.501   1.994  1.00 18.07           H  
ATOM    595  HA  LEU A  75     -14.998  11.926   4.209  1.00 20.67           H  
ATOM    596  HB2 LEU A  75     -13.138  13.834   3.208  1.00 19.59           H  
ATOM    597  HB3 LEU A  75     -12.919  13.041   4.540  1.00 19.59           H  
ATOM    598  HG  LEU A  75     -13.230  11.517   2.214  1.00 22.00           H  
ATOM    599 HD11 LEU A  75     -10.980  11.456   1.694  1.00 28.90           H  
ATOM    600 HD12 LEU A  75     -10.648  12.498   2.817  1.00 28.90           H  
ATOM    601 HD13 LEU A  75     -11.456  12.943   1.549  1.00 28.90           H  
ATOM    602 HD21 LEU A  75     -13.017  10.492   4.360  1.00 29.92           H  
ATOM    603 HD22 LEU A  75     -11.565  11.072   4.478  1.00 29.92           H  
ATOM    604 HD23 LEU A  75     -11.893   9.999   3.384  1.00 29.92           H  
ATOM    605  N   PHE A  76     -15.104  13.794   5.989  1.00 23.71           N  
ANISOU  605  N   PHE A  76     3139   3657   2213    815    336   -640       N  
ATOM    606  CA  PHE A  76     -15.675  14.558   7.079  1.00 27.04           C  
ANISOU  606  CA  PHE A  76     3559   4436   2279    349    659  -1209       C  
ATOM    607  C   PHE A  76     -14.598  15.451   7.691  1.00 25.07           C  
ANISOU  607  C   PHE A  76     3127   3416   2984   1248   -117   -971       C  
ATOM    608  O   PHE A  76     -13.476  14.934   7.600  1.00 28.87           O  
ANISOU  608  O   PHE A  76     3157   4601   3213   1160    471  -1205       O  
ATOM    609  CB APHE A  76     -16.178  13.661   8.210  0.68 29.30           C  
ANISOU  609  CB APHE A  76     3638   4568   2929    816   1343   -911       C  
ATOM    610  CB BPHE A  76     -16.210  13.722   8.218  0.32 30.91           C  
ANISOU  610  CB BPHE A  76     3656   5107   2980    543   1286   -792       C  
ATOM    611  CG APHE A  76     -17.354  12.794   7.799  0.68 31.85           C  
ANISOU  611  CG APHE A  76     3576   5439   3085    434   1149   -324       C  
ATOM    612  CG BPHE A  76     -17.230  12.626   8.167  0.32 28.96           C  
ANISOU  612  CG BPHE A  76     3336   5237   2430    617   1273   -612       C  
ATOM    613  CD1APHE A  76     -17.394  11.455   8.145  0.68 30.32           C  
ANISOU  613  CD1APHE A  76     3350   5738   2434   -175   1065     60       C  
ATOM    614  CD1BPHE A  76     -16.821  11.302   8.294  0.32 28.99           C  
ANISOU  614  CD1BPHE A  76     3459   5303   2253    385    516    243       C  
ATOM    615  CD2APHE A  76     -18.380  13.356   7.069  0.68 41.04           C  
ANISOU  615  CD2APHE A  76     5614   6177   3801   -645   -780    843       C  
ATOM    616  CD2BPHE A  76     -18.585  12.858   8.009  0.32 29.24           C  
ANISOU  616  CD2BPHE A  76     3412   5629   2069    688   1193   -300       C  
ATOM    617  CE1APHE A  76     -18.469  10.676   7.769  0.68 37.01           C  
ANISOU  617  CE1APHE A  76     4935   6240   2887   -610   -655     34       C  
ATOM    618  CE1BPHE A  76     -17.696  10.238   8.273  0.32 28.31           C  
ANISOU  618  CE1BPHE A  76     3754   5511   1492    177  -1151   1398       C  
ATOM    619  CE2APHE A  76     -19.460  12.579   6.673  0.68 38.95           C  
ANISOU  619  CE2APHE A  76     5066   6286   3446   -579   -144    487       C  
ATOM    620  CE2BPHE A  76     -19.479  11.803   7.999  0.32 31.57           C  
ANISOU  620  CE2BPHE A  76     3522   5884   2589    497   -499      4       C  
ATOM    621  CZ APHE A  76     -19.483  11.245   7.022  0.68 36.92           C  
ANISOU  621  CZ APHE A  76     4614   6053   3361   -236   -344     36       C  
ATOM    622  CZ BPHE A  76     -19.056  10.494   8.140  0.32 31.21           C  
ANISOU  622  CZ BPHE A  76     3584   5825   2451    276   -305    262       C  
ATOM    623  OXT PHE A  76     -14.897  16.487   8.302  1.00 32.53           O  
ANISOU  623  OXT PHE A  76     3505   2634   6223    305   1176  -1453       O  
ATOM    624  H   PHE A  76     -14.488  13.231   6.197  1.00 28.46           H  
ATOM    625  HA  PHE A  76     -16.411  15.111   6.744  1.00 32.45           H  
ATOM    626  HB2APHE A  76     -15.452  13.089   8.506  0.68 35.16           H  
ATOM    627  HB2BPHE A  76     -15.428  13.323   8.630  0.32 37.09           H  
ATOM    628  HB3APHE A  76     -16.442  14.216   8.960  0.68 35.16           H  
ATOM    629  HB3BPHE A  76     -16.555  14.360   8.862  0.32 37.09           H  
ATOM    630  HD1APHE A  76     -16.697  11.080   8.633  0.68 36.39           H  
ATOM    631  HD1BPHE A  76     -15.913  11.126   8.398  0.32 34.79           H  
ATOM    632  HD2APHE A  76     -18.348  14.257   6.841  0.68 49.24           H  
ATOM    633  HD2BPHE A  76     -18.896  13.729   7.908  0.32 35.09           H  
ATOM    634  HE1APHE A  76     -18.511   9.780   8.015  0.68 44.41           H  
ATOM    635  HE1BPHE A  76     -17.383   9.365   8.347  0.32 33.98           H  
ATOM    636  HE2APHE A  76     -20.156  12.952   6.182  0.68 46.74           H  
ATOM    637  HE2BPHE A  76     -20.387  11.978   7.895  0.32 37.88           H  
ATOM    638  HZ APHE A  76     -20.197  10.716   6.747  0.68 44.31           H  
ATOM    639  HZ BPHE A  76     -19.671   9.797   8.146  0.32 37.46           H  
TER     640      PHE A  76                                                      
HETATM  641  S  ASO4 A  77      -9.081  13.780   7.257  0.50 25.43           S  
ANISOU  641  S  ASO4 A  77     3170   3949   2544   -236    768    303       S  
HETATM  642  S  BSO4 A  77      -9.776  12.835   6.874  0.50 27.31           S  
ANISOU  642  S  BSO4 A  77     3754   4351   2271   -337    609   -894       S  
HETATM  643  O1 ASO4 A  77      -9.112  13.700   5.768  0.50 23.54           O  
ANISOU  643  O1 ASO4 A  77     3838   2873   2232   -775    560     30       O  
HETATM  644  O1 BSO4 A  77     -10.255  11.522   7.196  0.50 17.83           O  
ANISOU  644  O1 BSO4 A  77     1882   3783   1109    118     35   -739       O  
HETATM  645  O2 ASO4 A  77      -7.901  12.925   7.633  0.50 18.20           O  
ANISOU  645  O2 ASO4 A  77     2001   3259   1654  -1162    887   -835       O  
HETATM  646  O2 BSO4 A  77     -10.778  13.905   7.102  0.50 22.82           O  
ANISOU  646  O2 BSO4 A  77     4056   3557   1059   -425    571   -285       O  
HETATM  647  O3 ASO4 A  77     -10.525  13.790   7.474  0.50 22.93           O  
ANISOU  647  O3 ASO4 A  77     2974   2319   3421   -287    810   -620       O  
HETATM  648  O3 BSO4 A  77      -9.643  13.033   5.432  0.50 18.27           O  
ANISOU  648  O3 BSO4 A  77     2124   2776   2043   -836    224   -790       O  
HETATM  649  O4 ASO4 A  77      -8.651  15.091   7.688  0.50 19.18           O  
ANISOU  649  O4 ASO4 A  77     1217   4266   1805    150   -371   -208       O  
HETATM  650  O4 BSO4 A  77      -8.493  12.860   7.594  0.50 23.74           O  
ANISOU  650  O4 BSO4 A  77     4399   2403   2220  -1045   -127    505       O  
HETATM  651  C  AACT A  80     -14.897  33.444   4.737  0.33 27.92           C  
ANISOU  651  C  AACT A  80     2845   1206   6557   -875  -3161   1370       C  
HETATM  652  C  BACT A  80     -14.417  31.170   6.909  0.33  6.79           C  
ANISOU  652  C  BACT A  80     1237      9   1336    467   -143   -182       C  
HETATM  653  C  CACT A  80     -14.541  31.029   6.875  0.33 11.39           C  
ANISOU  653  C  CACT A  80     2231   1251    847   -286   -237   -785       C  
HETATM  654  O  AACT A  80     -16.133  33.900   4.732  0.33 27.91           O  
ANISOU  654  O  AACT A  80     4486   1296   4823   1218  -3311    -46       O  
HETATM  655  O  BACT A  80     -13.190  30.815   7.378  0.33 11.99           O  
ANISOU  655  O  BACT A  80     2215    616   1722    578   -967   -505       O  
HETATM  656  O  CACT A  80     -14.988  32.240   6.845  0.33 19.65           O  
ANISOU  656  O  CACT A  80     3544   1277   2645   -446  -1071    225       O  
HETATM  657  OXTAACT A  80     -14.133  33.893   3.875  0.33 35.31           O  
ANISOU  657  OXTAACT A  80     4672   2533   6213   -423  -2822   2593       O  
HETATM  658  OXTBACT A  80     -15.284  31.160   7.804  0.33 20.00           O  
ANISOU  658  OXTBACT A  80     2609   2804   2187   -335    723   -962       O  
HETATM  659  OXTCACT A  80     -13.343  30.791   7.070  0.33 19.82           O  
ANISOU  659  OXTCACT A  80     2090   2843   2597   -161    711   -681       O  
HETATM  660  CH3AACT A  80     -14.420  32.560   5.853  0.33 18.85           C  
ANISOU  660  CH3AACT A  80     1496    931   4734      5  -1333    605       C  
HETATM  661  CH3BACT A  80     -14.847  30.250   5.756  0.33  6.83           C  
ANISOU  661  CH3BACT A  80      897    450   1248    173   -221     70       C  
HETATM  662  CH3CACT A  80     -15.558  29.900   7.061  0.33 12.63           C  
ANISOU  662  CH3CACT A  80     2071    915   1811    192     53   -648       C  
HETATM  663  H1 AACT A  80     -15.162  32.329   6.417  0.33 28.27           H  
HETATM  664  H1 BACT A  80     -14.166  30.245   5.079  0.33 10.24           H  
HETATM  665  H1 CACT A  80     -16.439  30.228   6.866  0.33 18.94           H  
HETATM  666  H2 AACT A  80     -13.758  33.025   6.370  0.33 28.27           H  
HETATM  667  H2 BACT A  80     -15.670  30.571   5.380  0.33 10.24           H  
HETATM  668  H2 CACT A  80     -15.527  29.586   7.967  0.33 18.94           H  
HETATM  669  H3 AACT A  80     -14.036  31.760   5.486  0.33 28.27           H  
HETATM  670  H3 BACT A  80     -14.974  29.358   6.089  0.33 10.24           H  
HETATM  671  H3 CACT A  80     -15.347  29.177   6.465  0.33 18.94           H  
HETATM  672  O  BHOH A1001      -0.554   5.878   4.297  0.67 25.60           O  
ANISOU  672  O  BHOH A1001     3421   2666   3641    565    683  -1035       O  
HETATM  673  O  AHOH A1002     -11.596  30.458   7.935  0.33 21.00           O  
ANISOU  673  O  AHOH A1002     2769   2670   2540   -121    337   -366       O  
HETATM  674  O  BHOH A1002     -15.095  33.298   1.814  0.67 21.29           O  
ANISOU  674  O  BHOH A1002     2944   2360   2783    -87     85   -258       O  
HETATM  675  O   HOH A1003       0.820  18.873   7.485  1.00 17.94           O  
ANISOU  675  O   HOH A1003     1509   2574   2734    370   -267    379       O  
HETATM  676  O   HOH A1004     -14.093  23.273   8.266  1.00 15.23           O  
ANISOU  676  O   HOH A1004     2015   1884   1886    -11   -146    265       O  
HETATM  677  O   HOH A1005      -9.689  18.844  -3.488  1.00 19.88           O  
ANISOU  677  O   HOH A1005     2463   2498   2593    360     60   -236       O  
HETATM  678  O   HOH A1006      -6.006  20.263   7.552  1.00 21.40           O  
ANISOU  678  O   HOH A1006     2948   2606   2578   -232   -270    960       O  
HETATM  679  O   HOH A1007     -15.078  13.466  -5.431  1.00 17.52           O  
ANISOU  679  O   HOH A1007     2492   1727   2439    362   -343    129       O  
HETATM  680  O   HOH A1008      -0.433  15.884   4.974  1.00 20.70           O  
ANISOU  680  O   HOH A1008     2637   2258   2970    363   -246    515       O  
HETATM  681  O   HOH A1009     -12.235  18.323  -2.979  1.00 15.27           O  
ANISOU  681  O   HOH A1009     2325   1645   1831    286    104   -204       O  
HETATM  682  O   HOH A1010      -8.253  29.235   7.923  1.00 28.08           O  
ANISOU  682  O   HOH A1010     3955   3954   2760   -712     21   -608       O  
HETATM  683  O   HOH A1011     -19.849  13.736   1.275  1.00 28.25           O  
ANISOU  683  O   HOH A1011     3989   3067   3677    -63    152   -503       O  
HETATM  684  O   HOH A1012      -0.190  18.938  -5.282  1.00 18.83           O  
ANISOU  684  O   HOH A1012     2397   2451   2306   -291    494   -155       O  
HETATM  685  O   HOH A1013      -0.619   7.036   0.402  1.00 24.04           O  
ANISOU  685  O   HOH A1013     3424   3436   2276   -584    224   -762       O  
HETATM  686  O   HOH A1014     -16.483  18.569   7.437  1.00 25.28           O  
ANISOU  686  O   HOH A1014     3944   3175   2488   -456   -213   -109       O  
HETATM  687  O   HOH A1015      -8.112  31.592   4.198  1.00 17.76           O  
ANISOU  687  O   HOH A1015     2234   1897   2617     53    100    -22       O  
HETATM  688  O   HOH A1016      -4.949   6.419   5.632  1.00 19.74           O  
ANISOU  688  O   HOH A1016     2952   1868   2682   -160   -445     10       O  
HETATM  689  O   HOH A1017       1.070  11.301  -0.697  1.00 18.39           O  
ANISOU  689  O   HOH A1017     1850   2254   2882   -100    456   -768       O  
HETATM  690  O   HOH A1018      -7.876  20.182  -1.836  1.00 15.52           O  
ANISOU  690  O   HOH A1018     1820   1962   2116    452     -1   -117       O  
HETATM  691  O   HOH A1019      -8.786  32.546   1.606  1.00 18.57           O  
ANISOU  691  O   HOH A1019     2057   2121   2879   -316    438    369       O  
HETATM  692  O   HOH A1020      -7.959  25.728   9.960  1.00 19.16           O  
ANISOU  692  O   HOH A1020     2407   2705   2169   -277    421   -491       O  
HETATM  693  O   HOH A1021      -2.298  12.673  11.237  1.00 25.37           O  
ANISOU  693  O   HOH A1021     3301   3233   3106   -660   -364    284       O  
HETATM  694  O   HOH A1022      -1.682  25.950   8.828  1.00 22.66           O  
ANISOU  694  O   HOH A1022     3423   2665   2522    184   -194     22       O  
HETATM  695  O   HOH A1023      -2.999   4.311   5.855  1.00 25.00           O  
ANISOU  695  O   HOH A1023     3965   2531   3002    171     41   -327       O  
HETATM  696  O   HOH A1024     -19.078  13.502   3.996  1.00 35.65           O  
ANISOU  696  O   HOH A1024     4759   4522   4263   -108    127   -495       O  
HETATM  697  O   HOH A1025       0.281  10.142   9.221  1.00 27.12           O  
ANISOU  697  O   HOH A1025     3946   3207   3149   -215  -1451    687       O  
HETATM  698  O   HOH A1026     -12.423  14.451  10.060  1.00 26.06           O  
ANISOU  698  O   HOH A1026     2759   3627   3516    -62    890    -39       O  
HETATM  699  O   HOH A1027       1.249  28.289   7.090  1.00 34.60           O  
ANISOU  699  O   HOH A1027     3557   4740   4848    283   -990    303       O  
HETATM  700  O   HOH A1028     -13.588  15.291  -6.223  1.00 28.31           O  
ANISOU  700  O   HOH A1028     3479   3587   3690     43   -937    -33       O  
HETATM  701  O   HOH A1029      -7.846  22.403  -3.431  1.00 23.18           O  
ANISOU  701  O   HOH A1029     2823   3012   2971    132      6    921       O  
HETATM  702  O   HOH A1030     -13.403  19.391  -5.202  1.00 33.40           O  
ANISOU  702  O   HOH A1030     4550   4191   3947     15    -72    271       O  
HETATM  703  O   HOH A1031       0.254  17.096   9.432  1.00 24.02           O  
ANISOU  703  O   HOH A1031     3025   2684   3418   -123   -536    461       O  
HETATM  704  O   HOH A1032       1.040  12.761  -3.154  1.00 29.88           O  
ANISOU  704  O   HOH A1032     3386   3844   4124    394    752    157       O  
HETATM  705  O   HOH A1033       3.426  19.846   7.600  1.00 30.34           O  
ANISOU  705  O   HOH A1033     3547   4139   3841   -183   -173    667       O  
HETATM  706  O   HOH A1034     -14.763  20.659   8.326  1.00 23.70           O  
ANISOU  706  O   HOH A1034     3167   2417   3422    469   -638    377       O  
HETATM  707  O   HOH A1035       0.571  21.251  -6.829  1.00 25.38           O  
ANISOU  707  O   HOH A1035     3235   3445   2962    128    833   -360       O  
HETATM  708  O   HOH A1036      -0.527  14.954  -3.540  1.00 32.20           O  
ANISOU  708  O   HOH A1036     3968   4025   4239    364    838   -487       O  
HETATM  709  O   HOH A1037      -7.614  17.047  -4.661  1.00 24.44           O  
ANISOU  709  O   HOH A1037     3693   2945   2649    -54   -649    872       O  
HETATM  710  O   HOH A1038      -8.990  24.644  -3.148  1.00 26.65           O  
ANISOU  710  O   HOH A1038     3284   3307   3533    173    932     -4       O  
HETATM  711  O   HOH A1039     -21.418  24.474   7.455  1.00 35.05           O  
ANISOU  711  O   HOH A1039     4324   4503   4490    215   -299    -83       O  
HETATM  712  O   HOH A1040     -18.174   9.209   3.862  1.00 42.98           O  
ANISOU  712  O   HOH A1040     5347   5429   5556     -4     64    193       O  
HETATM  713  O   HOH A1041      -9.694  32.209   6.294  1.00 31.61           O  
ANISOU  713  O   HOH A1041     3908   4080   4024      3   1345   -732       O  
HETATM  714  O   HOH A1042     -11.100  20.706   7.995  1.00 26.89           O  
ANISOU  714  O   HOH A1042     4823   2803   2593   -359   -798    520       O  
HETATM  715  O   HOH A1043      -5.902   5.758   7.691  1.00 30.51           O  
ANISOU  715  O   HOH A1043     4562   3158   3873    -40    160    667       O  
HETATM  716  O   HOH A1044     -16.029  19.580  -6.124  1.00 52.02           O  
ANISOU  716  O   HOH A1044     6675   6434   6655     28   -306     90       O  
HETATM  717  O   HOH A1045     -19.869  18.204  -1.495  1.00 27.06           O  
ANISOU  717  O   HOH A1045     3337   3041   3905    528   -635   -187       O  
HETATM  718  O   HOH A1046      -5.494  21.039  -4.590  1.00 31.63           O  
ANISOU  718  O   HOH A1046     4463   3858   3697   -439    941   -137       O  
HETATM  719  O   HOH A1047     -20.195  13.314  -2.708  1.00 57.70           O  
ANISOU  719  O   HOH A1047     7033   7313   7575    254     60     22       O  
HETATM  720  O   HOH A1048      -9.445  20.708  -5.549  1.00 35.33           O  
ANISOU  720  O   HOH A1048     4853   4471   4098     84     40      4       O  
HETATM  721  O   HOH A1049     -16.751  29.013   9.477  0.50 36.87           O  
ANISOU  721  O   HOH A1049     4726   4797   4484    -61    306    177       O  
HETATM  722  O   HOH A1050      -1.376  29.655   9.483  1.00 45.50           O  
ANISOU  722  O   HOH A1050     6077   5824   5389   -250   -426    -20       O  
HETATM  723  O   HOH A1051     -21.245  18.272   8.364  1.00 36.21           O  
ANISOU  723  O   HOH A1051     4423   4527   4809   -142   -489    743       O  
HETATM  724  O   HOH A1052     -18.840  16.736  -6.797  1.00 33.47           O  
ANISOU  724  O   HOH A1052     3970   4272   4473    105   -941    135       O  
HETATM  725  O   HOH A1053     -11.018  34.254   1.994  1.00 31.47           O  
ANISOU  725  O   HOH A1053     3679   3661   4617    534   -509    912       O  
HETATM  726  O   HOH A1054     -11.454  25.194  -5.155  1.00 45.64           O  
ANISOU  726  O   HOH A1054     5771   5709   5860   -183   -290     89       O  
HETATM  727  O   HOH A1055     -18.538  14.850  -4.264  1.00 43.27           O  
ANISOU  727  O   HOH A1055     5026   5467   5948    406   -273    241       O  
HETATM  728  O   HOH A1056     -14.137  34.778   8.213  1.00 43.04           O  
ANISOU  728  O   HOH A1056     5010   5550   5794    -37   -415   -153       O  
HETATM  729  O   HOH A1057      -5.495  31.337   6.878  1.00 33.39           O  
ANISOU  729  O   HOH A1057     4755   3450   4483     13     64   -794       O  
HETATM  730  O   HOH A1058      -8.694  30.139   9.984  1.00 39.11           O  
ANISOU  730  O   HOH A1058     5749   4866   4244   -435    383   -267       O  
HETATM  731  O   HOH A1059      -1.857  22.585  -6.796  1.00 31.37           O  
ANISOU  731  O   HOH A1059     3530   4123   4264    364    738    -69       O  
HETATM  732  O   HOH A1060     -13.004  33.171   0.000  0.50 43.97           O  
ANISOU  732  O   HOH A1060     5472   5539   5694     58   -638    368       O  
CONECT  641  643  645  647  649                                                 
CONECT  642  644  646  648  650                                                 
CONECT  643  641                                                                
CONECT  644  642                                                                
CONECT  645  641                                                                
CONECT  646  642                                                                
CONECT  647  641                                                                
CONECT  648  642                                                                
CONECT  649  641                                                                
CONECT  650  642                                                                
CONECT  651  654  657  660                                                      
CONECT  652  655  658  661                                                      
CONECT  653  656  659  662                                                      
CONECT  654  651                                                                
CONECT  655  652                                                                
CONECT  656  653                                                                
CONECT  657  651                                                                
CONECT  658  652                                                                
CONECT  659  653                                                                
CONECT  660  651  663  666  669                                                 
CONECT  661  652  664  667  670                                                 
CONECT  662  653  665  668  671                                                 
CONECT  663  660                                                                
CONECT  664  661                                                                
CONECT  665  662                                                                
CONECT  666  660                                                                
CONECT  667  661                                                                
CONECT  668  662                                                                
CONECT  669  660                                                                
CONECT  670  661                                                                
CONECT  671  662                                                                
MASTER      243    0    2    3    0    0    5    6  358    1   31    3          
END