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Browse entries in the PDBbind-CN Database

HEADER    RNA-BINDING PROTEIN/RNA                 13-AUG-16   5SZE              
TITLE     CRYSTAL STRUCTURE OF AQUIFEX AEOLICUS HFQ-RNA COMPLEX AT 1.5A         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RNA-BINDING PROTEIN HFQ;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: RNA (5'-R(P*UP*UP*U)-3');                                  
COMPND   7 CHAIN: C;                                                            
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: AQUIFEX AEOLICUS (STRAIN VF5);                  
SOURCE   3 ORGANISM_TAXID: 224324;                                              
SOURCE   4 STRAIN: VF5;                                                         
SOURCE   5 GENE: HFQ, AQ_108, AQ_108B;                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: UNIDENTIFIED;                                   
SOURCE  11 ORGANISM_TAXID: 32644                                                
KEYWDS    HFQ, AQUIFEX, RNA-BINDING, RNA-BINDING PROTEIN-RNA COMPLEX            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.STANEK,J.PATTERSON,P.S.RANDOLPH,C.MURA                              
REVDAT   4   27-NOV-19 5SZE    1       REMARK                                   
REVDAT   3   20-SEP-17 5SZE    1       REMARK                                   
REVDAT   2   19-APR-17 5SZE    1       JRNL                                     
REVDAT   1   12-APR-17 5SZE    0                                                
JRNL        AUTH   K.A.STANEK,J.PATTERSON-WEST,P.S.RANDOLPH,C.MURA              
JRNL        TITL   CRYSTAL STRUCTURE AND RNA-BINDING PROPERTIES OF AN HFQ       
JRNL        TITL 2 HOMOLOG FROM THE DEEP-BRANCHING AQUIFICAE: CONSERVATION OF   
JRNL        TITL 3 THE LATERAL RNA-BINDING MODE.                                
JRNL        REF    ACTA CRYSTALLOGR D STRUCT     V.  73   294 2017              
JRNL        REF  2 BIOL                                                         
JRNL        REFN                   ISSN 2059-7983                               
JRNL        PMID   28375142                                                     
JRNL        DOI    10.1107/S2059798317000031                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10-2155_1309: ???)                         
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.21                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 13171                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.146                           
REMARK   3   R VALUE            (WORKING SET) : 0.144                           
REMARK   3   FREE R VALUE                     : 0.172                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 662                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 34.2189 -  2.5652    0.94     2540   117  0.1581 0.1706        
REMARK   3     2  2.5652 -  2.0362    0.97     2569   121  0.1409 0.1685        
REMARK   3     3  2.0362 -  1.7788    0.95     2474   157  0.1198 0.1549        
REMARK   3     4  1.7788 -  1.6162    0.95     2460   141  0.1219 0.1971        
REMARK   3     5  1.6162 -  1.5003    0.94     2466   126  0.1343 0.2095        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.150            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.860           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005            668                                  
REMARK   3   ANGLE     :  0.754            904                                  
REMARK   3   CHIRALITY :  0.050            107                                  
REMARK   3   PLANARITY :  0.004            104                                  
REMARK   3   DIHEDRAL  : 12.301            401                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5SZE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-AUG-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000223380.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-JUN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9195                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13177                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 34.210                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1U1S                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 35.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CACODYLATE, PEG 8000, MPD,        
REMARK 280  GUANIDINIUM, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 6                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z                                                
REMARK 290       6555   X-Y,X,Z                                                 
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
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        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: DODECAMERIC                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
REMARK 350   BIOMT1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14650 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 21440 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 211  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     PHE A    74                                                      
REMARK 465     GLU A    75                                                      
REMARK 465     GLU A    76                                                      
REMARK 465     ALA A    77                                                      
REMARK 465     GLY A    78                                                      
REMARK 465     VAL A    79                                                      
REMARK 465     PRO A    80                                                      
REMARK 465     GLY A    81                                                      
REMARK 465     GLN A    82                                                      
REMARK 465     GLY A    83                                                      
REMARK 465       U C     4                                                      
REMARK 465       U C     5                                                      
REMARK 465       U C     6                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470       U C   3    O5'  C5'  C4'  O4'  C3'  O3'  C2'                   
REMARK 470       U C   3    O2'  C1'  N1   C2   O2   N3   C4                    
REMARK 470       U C   3    O4   C5   C6                                        
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MRD A 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 102                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5SZD   RELATED DB: PDB                                   
DBREF  5SZE A    4    83  UNP    O66512   HFQ_AQUAE        1     80             
DBREF  5SZE C    1     6  PDB    5SZE     5SZE             1      6             
SEQADV 5SZE GLY A    1  UNP  O66512              EXPRESSION TAG                 
SEQADV 5SZE SER A    2  UNP  O66512              EXPRESSION TAG                 
SEQADV 5SZE HIS A    3  UNP  O66512              EXPRESSION TAG                 
SEQRES   1 A   83  GLY SER HIS MET PRO TYR LYS LEU GLN GLU SER PHE LEU          
SEQRES   2 A   83  ASN THR ALA ARG LYS LYS ARG VAL LYS VAL SER VAL TYR          
SEQRES   3 A   83  LEU VAL ASN GLY VAL ARG LEU GLN GLY ARG ILE ARG SER          
SEQRES   4 A   83  PHE ASP LEU PHE THR ILE LEU LEU GLU ASP GLY LYS GLN          
SEQRES   5 A   83  GLN THR LEU VAL TYR LYS HIS ALA ILE THR THR ILE VAL          
SEQRES   6 A   83  PRO HIS GLU ARG LEU GLU ILE GLU PHE GLU GLU ALA GLY          
SEQRES   7 A   83  VAL PRO GLY GLN GLY                                          
SEQRES   1 C    6    U   U   U   U   U   U                                      
HET    MRD  A 101       8                                                       
HET    PEG  A 102       7                                                       
HETNAM     MRD (4R)-2-METHYLPENTANE-2,4-DIOL                                    
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
FORMUL   3  MRD    C6 H14 O2                                                    
FORMUL   4  PEG    C4 H10 O3                                                    
FORMUL   5  HOH   *36(H2 O)                                                     
HELIX    1 AA1 LYS A    7  LYS A   19  1                                  13    
SHEET    1 AA1 5 GLN A  52  TYR A  57  0                                        
SHEET    2 AA1 5 THR A  44  ASP A  49 -1  N  ILE A  45   O  VAL A  56           
SHEET    3 AA1 5 ARG A  32  PHE A  40 -1  N  SER A  39   O  LEU A  46           
SHEET    4 AA1 5 LYS A  22  LEU A  27 -1  N  VAL A  25   O  LEU A  33           
SHEET    5 AA1 5 ILE A  61  PRO A  66 -1  O  THR A  62   N  TYR A  26           
SITE     1 AC1  6 GLN A   9  LEU A  42  PHE A  43  TYR A  57                    
SITE     2 AC1  6 HIS A  59  HOH A 212                                          
SITE     1 AC2  6 TYR A  26  LEU A  27  ASN A  29  THR A  62                    
SITE     2 AC2  6 THR A  63  HOH A 206                                          
CRYST1   66.190   66.190   34.210  90.00  90.00 120.00 P 6           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      0.015108  0.008723  0.000000        0.00000                         
SCALE2      0.000000  0.017445  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.029231        0.00000                         
ATOM      1  N   HIS A   3      -9.003  22.558   7.670  1.00 69.01           N  
ANISOU    1  N   HIS A   3     9036   9412   7773   3517  -1079   2310       N  
ATOM      2  CA  HIS A   3      -9.520  21.806   8.808  1.00 62.49           C  
ANISOU    2  CA  HIS A   3     8216   9083   6445   2537   -938   2242       C  
ATOM      3  C   HIS A   3      -8.661  20.585   9.102  1.00 54.08           C  
ANISOU    3  C   HIS A   3     7445   8446   4658   1987  -1140   1504       C  
ATOM      4  O   HIS A   3      -9.175  19.497   9.361  1.00 50.82           O  
ANISOU    4  O   HIS A   3     7264   8377   3668   1684  -1418   1134       O  
ATOM      5  CB  HIS A   3     -10.966  21.386   8.553  1.00 62.48           C  
ANISOU    5  CB  HIS A   3     8387   8774   6579   2414   -696   3183       C  
ATOM      6  CG  HIS A   3     -11.923  22.535   8.524  1.00 63.12           C  
ANISOU    6  CG  HIS A   3     8511   8601   6869   2060   -620   3813       C  
ATOM      7  ND1 HIS A   3     -12.600  22.967   9.644  1.00 63.08           N  
ANISOU    7  ND1 HIS A   3     8524   8484   6960   1916   -604   4065       N  
ATOM      8  CD2 HIS A   3     -12.301  23.354   7.515  1.00 63.69           C  
ANISOU    8  CD2 HIS A   3     8570   8533   7098   1980   -468   4056       C  
ATOM      9  CE1 HIS A   3     -13.362  23.997   9.324  1.00 63.40           C  
ANISOU    9  CE1 HIS A   3     8577   8371   7141   2003   -513   4095       C  
ATOM     10  NE2 HIS A   3     -13.199  24.252   8.038  1.00 63.96           N  
ANISOU   10  NE2 HIS A   3     8585   8395   7323   2035   -343   4135       N  
ATOM     11  N   MET A   4      -7.349  20.776   9.062  1.00 49.26           N  
ANISOU   11  N   MET A   4     6781   7700   4233   1031  -1080   1193       N  
ATOM     12  CA  MET A   4      -6.468  19.667   9.373  1.00 46.31           C  
ANISOU   12  CA  MET A   4     5997   7308   4290     49   -799    803       C  
ATOM     13  C   MET A   4      -6.032  19.725  10.831  1.00 40.55           C  
ANISOU   13  C   MET A   4     4924   6380   4102   -822   -580   1317       C  
ATOM     14  O   MET A   4      -5.918  20.811  11.409  1.00 37.80           O  
ANISOU   14  O   MET A   4     4525   5985   3850  -1333   -270   1492       O  
ATOM     15  CB  MET A   4      -5.237  19.686   8.464  1.00 49.36           C  
ANISOU   15  CB  MET A   4     6263   7679   4812    134   -824    155       C  
ATOM     16  CG  MET A   4      -5.591  19.589   6.992  1.00 52.79           C  
ANISOU   16  CG  MET A   4     6484   8029   5547    355   -890   -259       C  
ATOM     17  SD  MET A   4      -4.217  19.028   5.984  1.00 55.06           S  
ANISOU   17  SD  MET A   4     6800   8168   5951    553   -950   -865       S  
ATOM     18  CE  MET A   4      -3.799  17.501   6.826  1.00 57.47           C  
ANISOU   18  CE  MET A   4     6856   8255   6723    698   -855  -1032       C  
ATOM     19  N   PRO A   5      -5.801  18.570  11.453  1.00 37.67           N  
ANISOU   19  N   PRO A   5     4466   5619   4228   -907   -627   1204       N  
ATOM     20  CA  PRO A   5      -5.393  18.564  12.864  1.00 34.75           C  
ANISOU   20  CA  PRO A   5     4116   5132   3954   -996   -653   1147       C  
ATOM     21  C   PRO A   5      -3.968  19.075  13.020  1.00 33.32           C  
ANISOU   21  C   PRO A   5     3680   4883   4096   -951   -711    530       C  
ATOM     22  O   PRO A   5      -3.044  18.577  12.372  1.00 35.32           O  
ANISOU   22  O   PRO A   5     4104   5306   4011   -353   -862   -168       O  
ATOM     23  CB  PRO A   5      -5.510  17.087  13.260  1.00 35.22           C  
ANISOU   23  CB  PRO A   5     4360   5181   3842   -858   -475   1513       C  
ATOM     24  CG  PRO A   5      -5.350  16.340  11.976  1.00 36.65           C  
ANISOU   24  CG  PRO A   5     4519   5148   4258   -828   -592   1337       C  
ATOM     25  CD  PRO A   5      -5.967  17.207  10.915  1.00 36.73           C  
ANISOU   25  CD  PRO A   5     4439   5300   4216   -965   -722   1201       C  
ATOM     26  N   TYR A   6      -3.796  20.080  13.877  1.00 30.27           N  
ANISOU   26  N   TYR A   6     3278   4235   3987  -1015   -553    839       N  
ATOM     27  CA  TYR A   6      -2.458  20.564  14.189  1.00 28.77           C  
ANISOU   27  CA  TYR A   6     3214   3899   3818   -527   -427    911       C  
ATOM     28  C   TYR A   6      -1.693  19.516  14.990  1.00 24.54           C  
ANISOU   28  C   TYR A   6     2973   3317   3032   -338   -593    543       C  
ATOM     29  O   TYR A   6      -2.263  18.782  15.801  1.00 24.89           O  
ANISOU   29  O   TYR A   6     2908   3186   3363   -260   -752    269       O  
ATOM     30  CB  TYR A   6      -2.509  21.873  14.983  1.00 32.51           C  
ANISOU   30  CB  TYR A   6     3723   4059   4570   -275   -137   1474       C  
ATOM     31  CG  TYR A   6      -3.163  23.045  14.280  0.81 36.52           C  
ANISOU   31  CG  TYR A   6     4264   4268   5343     -6    421   1931       C  
ATOM     32  CD1 TYR A   6      -3.418  23.020  12.913  0.95 37.63           C  
ANISOU   32  CD1 TYR A   6     4540   4322   5434    215    609   2224       C  
ATOM     33  CD2 TYR A   6      -3.518  24.183  14.991  0.56 38.40           C  
ANISOU   33  CD2 TYR A   6     4568   4303   5719    134    583   2246       C  
ATOM     34  CE1 TYR A   6      -4.017  24.093  12.280  1.00 39.04           C  
ANISOU   34  CE1 TYR A   6     4784   4490   5561    463    527   2097       C  
ATOM     35  CE2 TYR A   6      -4.116  25.258  14.368  1.00 40.07           C  
ANISOU   35  CE2 TYR A   6     4791   4409   6025    411    572   2246       C  
ATOM     36  CZ  TYR A   6      -4.363  25.210  13.013  0.70 39.88           C  
ANISOU   36  CZ  TYR A   6     4914   4433   5808    554    492   2277       C  
ATOM     37  OH  TYR A   6      -4.958  26.284  12.392  0.49 40.67           O  
ANISOU   37  OH  TYR A   6     5098   4358   5996    613    511   2249       O  
ATOM     38  N   LYS A   7      -0.382  19.459  14.759  1.00 22.14           N  
ANISOU   38  N   LYS A   7     2720   3193   2498   -268   -452      0       N  
ATOM     39  CA  LYS A   7       0.502  18.501  15.427  1.00 21.10           C  
ANISOU   39  CA  LYS A   7     2698   3166   2153    300   -249     75       C  
ATOM     40  C   LYS A   7       0.867  19.027  16.817  1.00 18.04           C  
ANISOU   40  C   LYS A   7     2054   2181   2617   -181    -10    151       C  
ATOM     41  O   LYS A   7       1.947  19.578  17.051  1.00 18.63           O  
ANISOU   41  O   LYS A   7     1888   2357   2832   -358    -11     65       O  
ATOM     42  CB  LYS A   7       1.743  18.254  14.578  1.00 28.46           C  
ANISOU   42  CB  LYS A   7     3682   4347   2784   1167   -504   -567       C  
ATOM     43  CG  LYS A   7       1.453  17.724  13.177  1.00 36.66           C  
ANISOU   43  CG  LYS A   7     4513   5699   3716   2161   -231   -464       C  
ATOM     44  CD  LYS A   7       2.737  17.540  12.374  1.00 42.82           C  
ANISOU   44  CD  LYS A   7     5268   6651   4350   2904    161   -438       C  
ATOM     45  CE  LYS A   7       2.460  16.914  11.012  1.00 48.07           C  
ANISOU   45  CE  LYS A   7     5677   7302   5285   3125    -39   -415       C  
ATOM     46  NZ  LYS A   7       1.647  17.798  10.133  1.00 49.61           N  
ANISOU   46  NZ  LYS A   7     5735   7588   5528   3094   -292   -423       N  
ATOM     47  N   LEU A   8      -0.054  18.826  17.766  1.00 15.48           N  
ANISOU   47  N   LEU A   8     1864   1742   2274    -79   -373   -160       N  
ATOM     48  CA  LEU A   8       0.089  19.416  19.099  1.00 13.92           C  
ANISOU   48  CA  LEU A   8     1473   1377   2437    -99   -341    122       C  
ATOM     49  C   LEU A   8       1.314  18.880  19.827  1.00 13.12           C  
ANISOU   49  C   LEU A   8     1553   1368   2061     45    -93    217       C  
ATOM     50  O   LEU A   8       2.122  19.655  20.350  1.00 13.70           O  
ANISOU   50  O   LEU A   8     1546   1241   2416    -79    -99     10       O  
ATOM     51  CB  LEU A   8      -1.169  19.161  19.936  1.00 15.75           C  
ANISOU   51  CB  LEU A   8     1426   1749   2808    205     94   -137       C  
ATOM     52  CG  LEU A   8      -1.022  19.460  21.435  1.00 15.03           C  
ANISOU   52  CG  LEU A   8     1355   1371   2984     18    235   -196       C  
ATOM     53  CD1 LEU A   8      -0.765  20.958  21.704  1.00 15.53           C  
ANISOU   53  CD1 LEU A   8     1241   1285   3376    -82    233   -417       C  
ATOM     54  CD2 LEU A   8      -2.243  18.950  22.218  1.00 15.69           C  
ANISOU   54  CD2 LEU A   8     1299   1437   3223   -157     17    101       C  
ATOM     55  N   GLN A   9       1.456  17.554  19.903  1.00 14.54           N  
ANISOU   55  N   GLN A   9     1449   1567   2509    360   -238    116       N  
ATOM     56  CA  GLN A   9       2.549  16.990  20.689  1.00 12.93           C  
ANISOU   56  CA  GLN A   9     1311   1182   2420     37   -105    372       C  
ATOM     57  C   GLN A   9       3.901  17.453  20.162  1.00 13.56           C  
ANISOU   57  C   GLN A   9     1268   1410   2473   -373    -20    172       C  
ATOM     58  O   GLN A   9       4.759  17.901  20.931  1.00 13.76           O  
ANISOU   58  O   GLN A   9     1344   1420   2463   -387   -177     31       O  
ATOM     59  CB  GLN A   9       2.476  15.462  20.698  1.00 13.28           C  
ANISOU   59  CB  GLN A   9     1556   1040   2447    159    271    615       C  
ATOM     60  CG  GLN A   9       3.566  14.886  21.576  1.00 14.62           C  
ANISOU   60  CG  GLN A   9     1506   1373   2676    382     59    306       C  
ATOM     61  CD  GLN A   9       3.650  13.368  21.612  1.00 12.90           C  
ANISOU   61  CD  GLN A   9     1297   1183   2422    212   -206    -83       C  
ATOM     62  OE1 GLN A   9       4.555  12.837  22.235  1.00 15.21           O  
ANISOU   62  OE1 GLN A   9     1324   1272   3184     31    -69    202       O  
ATOM     63  NE2 GLN A   9       2.717  12.672  20.962  1.00 14.76           N  
ANISOU   63  NE2 GLN A   9     1349   1605   2656    283     78   -269       N  
ATOM     64  N   GLU A  10       4.104  17.355  18.849  1.00 14.07           N  
ANISOU   64  N   GLU A  10     1238   1657   2451   -285    274    329       N  
ATOM     65  CA  GLU A  10       5.386  17.735  18.268  1.00 15.90           C  
ANISOU   65  CA  GLU A  10     1665   1710   2666   -687      6   -447       C  
ATOM     66  C   GLU A  10       5.645  19.227  18.437  1.00 15.30           C  
ANISOU   66  C   GLU A  10     1563   1795   2455   -552   -126     98       C  
ATOM     67  O   GLU A  10       6.777  19.639  18.711  1.00 15.78           O  
ANISOU   67  O   GLU A  10     1789   1876   2329   -120    -56    109       O  
ATOM     68  CB  GLU A  10       5.419  17.331  16.795  1.00 21.76           C  
ANISOU   68  CB  GLU A  10     2616   2378   3272   -556    390   -925       C  
ATOM     69  CG  GLU A  10       5.186  15.824  16.561  1.00 31.57           C  
ANISOU   69  CG  GLU A  10     3917   3412   4666    214    276  -1170       C  
ATOM     70  CD  GLU A  10       3.714  15.434  16.303  1.00 35.93           C  
ANISOU   70  CD  GLU A  10     4758   4034   4860    717    -27  -1781       C  
ATOM     71  OE1 GLU A  10       2.786  16.047  16.877  1.00 33.91           O  
ANISOU   71  OE1 GLU A  10     4881   4077   3924    471    113  -1415       O  
ATOM     72  OE2 GLU A  10       3.492  14.490  15.512  1.00 39.85           O  
ANISOU   72  OE2 GLU A  10     5309   4527   5305   1416   -247  -2153       O  
ATOM     73  N   SER A  11       4.607  20.054  18.303  1.00 14.42           N  
ANISOU   73  N   SER A  11     1620   1548   2309   -195   -253    236       N  
ATOM     74  CA  SER A  11       4.818  21.491  18.437  1.00 15.84           C  
ANISOU   74  CA  SER A  11     1664   1832   2524   -183   -214    553       C  
ATOM     75  C   SER A  11       5.136  21.866  19.879  1.00 14.88           C  
ANISOU   75  C   SER A  11     1274   1650   2728   -495    124    479       C  
ATOM     76  O   SER A  11       5.999  22.719  20.133  1.00 15.89           O  
ANISOU   76  O   SER A  11     1473   1437   3127   -275    151    537       O  
ATOM     77  CB  SER A  11       3.588  22.236  17.934  1.00 19.40           C  
ANISOU   77  CB  SER A  11     2218   2249   2903   -176   -788    303       C  
ATOM     78  OG  SER A  11       3.334  21.908  16.577  1.00 25.48           O  
ANISOU   78  OG  SER A  11     2969   2681   4031     46   -902    468       O  
ATOM     79  N   PHE A  12       4.449  21.237  20.835  1.00 14.16           N  
ANISOU   79  N   PHE A  12     1151   1394   2837    -50     52    266       N  
ATOM     80  CA  PHE A  12       4.739  21.458  22.248  1.00 13.36           C  
ANISOU   80  CA  PHE A  12      940   1592   2546   -192    391    252       C  
ATOM     81  C   PHE A  12       6.173  21.054  22.578  1.00 12.45           C  
ANISOU   81  C   PHE A  12     1185   1028   2516   -255    175     73       C  
ATOM     82  O   PHE A  12       6.932  21.835  23.162  1.00 13.51           O  
ANISOU   82  O   PHE A  12     1378   1307   2448    -39   -151    154       O  
ATOM     83  CB  PHE A  12       3.723  20.675  23.094  1.00 13.01           C  
ANISOU   83  CB  PHE A  12     1175   1578   2188   -187     72    -62       C  
ATOM     84  CG  PHE A  12       3.903  20.820  24.580  1.00 13.53           C  
ANISOU   84  CG  PHE A  12     1358   1478   2302   -337     95    -62       C  
ATOM     85  CD1 PHE A  12       4.885  20.099  25.253  1.00 14.78           C  
ANISOU   85  CD1 PHE A  12     1587   1422   2608   -669    -65    374       C  
ATOM     86  CD2 PHE A  12       3.066  21.638  25.313  1.00 15.88           C  
ANISOU   86  CD2 PHE A  12     1616   1655   2764   -589    313   -521       C  
ATOM     87  CE1 PHE A  12       5.042  20.224  26.614  1.00 16.92           C  
ANISOU   87  CE1 PHE A  12     1953   1621   2857   -222    -57    230       C  
ATOM     88  CE2 PHE A  12       3.216  21.757  26.684  1.00 16.69           C  
ANISOU   88  CE2 PHE A  12     1598   1936   2807   -548     55   -404       C  
ATOM     89  CZ  PHE A  12       4.204  21.049  27.333  1.00 16.94           C  
ANISOU   89  CZ  PHE A  12     1746   1853   2837   -294    -36   -395       C  
ATOM     90  N   LEU A  13       6.558  19.829  22.212  1.00 12.72           N  
ANISOU   90  N   LEU A  13     1192   1053   2588      6    292     36       N  
ATOM     91  CA  LEU A  13       7.897  19.349  22.543  1.00 11.38           C  
ANISOU   91  CA  LEU A  13     1097    929   2298   -295     66    172       C  
ATOM     92  C   LEU A  13       8.970  20.172  21.847  1.00 12.50           C  
ANISOU   92  C   LEU A  13     1257   1083   2409   -289    -53    282       C  
ATOM     93  O   LEU A  13      10.009  20.483  22.451  1.00 12.89           O  
ANISOU   93  O   LEU A  13     1173   1110   2616   -114   -317    159       O  
ATOM     94  CB  LEU A  13       8.042  17.875  22.168  1.00 11.63           C  
ANISOU   94  CB  LEU A  13     1298    868   2251   -275    192    109       C  
ATOM     95  CG  LEU A  13       7.138  16.899  22.932  1.00 12.06           C  
ANISOU   95  CG  LEU A  13     1287   1060   2235   -458     29    -43       C  
ATOM     96  CD1 LEU A  13       7.283  15.484  22.378  1.00 12.73           C  
ANISOU   96  CD1 LEU A  13     1393    862   2580    -98    102    -15       C  
ATOM     97  CD2 LEU A  13       7.462  16.916  24.407  1.00 14.69           C  
ANISOU   97  CD2 LEU A  13     1823   1508   2250    111    267     63       C  
ATOM     98  N   ASN A  14       8.747  20.525  20.575  1.00 14.06           N  
ANISOU   98  N   ASN A  14     1540   1346   2458    110    359    597       N  
ATOM     99  CA  ASN A  14       9.775  21.250  19.833  1.00 13.94           C  
ANISOU   99  CA  ASN A  14     1728   1294   2276   -163    153    247       C  
ATOM    100  C   ASN A  14       9.904  22.680  20.337  1.00 13.86           C  
ANISOU  100  C   ASN A  14     1737   1227   2303   -263    -15    297       C  
ATOM    101  O   ASN A  14      11.010  23.239  20.362  1.00 14.94           O  
ANISOU  101  O   ASN A  14     1933   1352   2391   -434     25    190       O  
ATOM    102  CB  ASN A  14       9.475  21.238  18.331  1.00 14.53           C  
ANISOU  102  CB  ASN A  14     1570   1691   2259   -248    182    416       C  
ATOM    103  CG  ASN A  14      10.742  21.359  17.485  1.00 16.56           C  
ANISOU  103  CG  ASN A  14     1739   2118   2436    -59   -275    341       C  
ATOM    104  OD1 ASN A  14      11.821  20.940  17.907  1.00 16.63           O  
ANISOU  104  OD1 ASN A  14     1537   2267   2514   -154   -143    277       O  
ATOM    105  ND2 ASN A  14      10.611  21.914  16.291  1.00 20.39           N  
ANISOU  105  ND2 ASN A  14     2465   2525   2759     88    145    465       N  
ATOM    106  N   THR A  15       8.789  23.294  20.737  1.00 13.52           N  
ANISOU  106  N   THR A  15     1609   1315   2212    -73   -254    358       N  
ATOM    107  CA  THR A  15       8.868  24.643  21.292  1.00 13.98           C  
ANISOU  107  CA  THR A  15     1549   1294   2470     73    -38    418       C  
ATOM    108  C   THR A  15       9.598  24.636  22.625  1.00 12.81           C  
ANISOU  108  C   THR A  15     1544    778   2546   -153   -132    420       C  
ATOM    109  O   THR A  15      10.472  25.474  22.864  1.00 14.99           O  
ANISOU  109  O   THR A  15     1610   1137   2947   -351     96    273       O  
ATOM    110  CB  THR A  15       7.469  25.246  21.445  1.00 13.91           C  
ANISOU  110  CB  THR A  15     1526   1287   2471    -12   -347    280       C  
ATOM    111  OG1 THR A  15       6.850  25.319  20.156  1.00 16.46           O  
ANISOU  111  OG1 THR A  15     1852   1651   2752   -116   -525    118       O  
ATOM    112  CG2 THR A  15       7.548  26.645  22.044  1.00 15.76           C  
ANISOU  112  CG2 THR A  15     1839   1141   3007    -43   -200     30       C  
ATOM    113  N   ALA A  16       9.273  23.679  23.505  1.00 12.73           N  
ANISOU  113  N   ALA A  16     1395    999   2443   -125    -82    315       N  
ATOM    114  CA  ALA A  16      10.016  23.567  24.757  1.00 12.08           C  
ANISOU  114  CA  ALA A  16     1330   1256   2003     27    -41    216       C  
ATOM    115  C   ALA A  16      11.497  23.334  24.488  1.00 11.93           C  
ANISOU  115  C   ALA A  16     1181   1141   2211   -185    -33    250       C  
ATOM    116  O   ALA A  16      12.362  23.913  25.162  1.00 13.16           O  
ANISOU  116  O   ALA A  16     1281   1193   2528   -158    -52     -9       O  
ATOM    117  CB  ALA A  16       9.450  22.438  25.618  1.00 12.74           C  
ANISOU  117  CB  ALA A  16     1350   1491   2001   -209    271    245       C  
ATOM    118  N   ARG A  17      11.804  22.501  23.492  1.00 12.32           N  
ANISOU  118  N   ARG A  17     1171   1458   2050    -14     99     47       N  
ATOM    119  CA  ARG A  17      13.198  22.220  23.155  1.00 11.50           C  
ANISOU  119  CA  ARG A  17     1227   1111   2032   -199    216     -9       C  
ATOM    120  C   ARG A  17      13.911  23.474  22.658  1.00 13.43           C  
ANISOU  120  C   ARG A  17     1358   1066   2680   -429    279    258       C  
ATOM    121  O   ARG A  17      14.986  23.830  23.157  1.00 14.44           O  
ANISOU  121  O   ARG A  17     1743   1134   2610   -306     22     52       O  
ATOM    122  CB  ARG A  17      13.269  21.119  22.092  1.00 12.09           C  
ANISOU  122  CB  ARG A  17     1313   1006   2274   -397     31    -40       C  
ATOM    123  CG  ARG A  17      14.705  20.760  21.694  1.00 13.66           C  
ANISOU  123  CG  ARG A  17     1382   1621   2186   -248     95   -270       C  
ATOM    124  CD  ARG A  17      14.741  19.836  20.503  1.00 15.12           C  
ANISOU  124  CD  ARG A  17     1745   1545   2453    113    140    201       C  
ATOM    125  NE  ARG A  17      14.338  20.491  19.260  1.00 14.69           N  
ANISOU  125  NE  ARG A  17     1784   1567   2229    -89    204     69       N  
ATOM    126  CZ  ARG A  17      15.164  21.150  18.453  1.00 17.86           C  
ANISOU  126  CZ  ARG A  17     2031   2140   2614   -323    -56    447       C  
ATOM    127  NH1 ARG A  17      16.446  21.281  18.770  1.00 19.29           N  
ANISOU  127  NH1 ARG A  17     2186   2551   2593   -436      4    270       N  
ATOM    128  NH2 ARG A  17      14.704  21.697  17.339  1.00 21.48           N  
ANISOU  128  NH2 ARG A  17     2445   2682   3036   -344    303    423       N  
ATOM    129  N   LYS A  18      13.331  24.148  21.658  1.00 13.92           N  
ANISOU  129  N   LYS A  18     1886    934   2469   -118    257    186       N  
ATOM    130  CA  LYS A  18      14.007  25.280  21.028  1.00 14.64           C  
ANISOU  130  CA  LYS A  18     1990   1028   2545   -467    211    215       C  
ATOM    131  C   LYS A  18      14.160  26.447  21.994  1.00 13.82           C  
ANISOU  131  C   LYS A  18     1671   1055   2526   -319    419    513       C  
ATOM    132  O   LYS A  18      15.150  27.186  21.933  1.00 16.17           O  
ANISOU  132  O   LYS A  18     1702   1496   2948   -279    216    202       O  
ATOM    133  CB  LYS A  18      13.239  25.728  19.788  1.00 16.79           C  
ANISOU  133  CB  LYS A  18     2506   1256   2618   -258    294     23       C  
ATOM    134  CG  LYS A  18      13.285  24.774  18.613  1.00 24.28           C  
ANISOU  134  CG  LYS A  18     3153   2296   3774   -164    102    366       C  
ATOM    135  CD  LYS A  18      12.438  25.322  17.473  1.00 32.29           C  
ANISOU  135  CD  LYS A  18     3833   3497   4938    373     82    379       C  
ATOM    136  CE  LYS A  18      12.629  24.533  16.194  1.00 38.92           C  
ANISOU  136  CE  LYS A  18     4348   4192   6247    579    -29    783       C  
ATOM    137  NZ  LYS A  18      11.861  25.126  15.061  1.00 42.98           N  
ANISOU  137  NZ  LYS A  18     4737   4599   6993    884    -31   1228       N  
ATOM    138  N   LYS A  19      13.180  26.658  22.863  1.00 13.32           N  
ANISOU  138  N   LYS A  19     1560   1026   2476   -457     95    179       N  
ATOM    139  CA  LYS A  19      13.248  27.750  23.823  1.00 14.23           C  
ANISOU  139  CA  LYS A  19     1637    960   2810   -367    -97    158       C  
ATOM    140  C   LYS A  19      13.969  27.353  25.102  1.00 14.66           C  
ANISOU  140  C   LYS A  19     1705   1076   2791   -117    105    239       C  
ATOM    141  O   LYS A  19      14.119  28.189  26.000  1.00 14.86           O  
ANISOU  141  O   LYS A  19     1852    795   2998    -47    196    244       O  
ATOM    142  CB  LYS A  19      11.835  28.259  24.145  1.00 18.07           C  
ANISOU  142  CB  LYS A  19     1976   1783   3107    255   -290    179       C  
ATOM    143  CG  LYS A  19      11.065  28.755  22.932  1.00 21.09           C  
ANISOU  143  CG  LYS A  19     2336   1862   3814    -16   -357    396       C  
ATOM    144  CD  LYS A  19      11.700  29.986  22.326  1.00 27.84           C  
ANISOU  144  CD  LYS A  19     3155   2654   4770    620   -728    461       C  
ATOM    145  CE  LYS A  19      10.905  30.473  21.125  1.00 32.38           C  
ANISOU  145  CE  LYS A  19     3878   2740   5683    640  -1120    568       C  
ATOM    146  NZ  LYS A  19      11.294  31.850  20.697  1.00 37.61           N  
ANISOU  146  NZ  LYS A  19     4416   3334   6540    829   -871    588       N  
ATOM    147  N   ARG A  20      14.425  26.102  25.198  1.00 13.92           N  
ANISOU  147  N   ARG A  20     1621   1036   2632   -133     68    147       N  
ATOM    148  CA  ARG A  20      15.190  25.630  26.352  1.00 13.22           C  
ANISOU  148  CA  ARG A  20     1448   1083   2491   -275     28    222       C  
ATOM    149  C   ARG A  20      14.441  25.919  27.647  1.00 12.77           C  
ANISOU  149  C   ARG A  20     1546    769   2534   -248   -192   -193       C  
ATOM    150  O   ARG A  20      15.007  26.377  28.636  1.00 15.91           O  
ANISOU  150  O   ARG A  20     1797   1319   2929   -334   -129   -220       O  
ATOM    151  CB  ARG A  20      16.608  26.225  26.357  1.00 15.28           C  
ANISOU  151  CB  ARG A  20     1556   1207   3044   -219    120   -375       C  
ATOM    152  CG  ARG A  20      17.365  25.853  25.084  1.00 16.58           C  
ANISOU  152  CG  ARG A  20     1350   1502   3450   -125    370   -110       C  
ATOM    153  CD  ARG A  20      18.875  26.042  25.172  1.00 17.42           C  
ANISOU  153  CD  ARG A  20     1405   1512   3703    196    205     71       C  
ATOM    154  NE  ARG A  20      19.476  25.173  26.176  1.00 18.33           N  
ANISOU  154  NE  ARG A  20     1533   1389   4041    214     -1   -166       N  
ATOM    155  CZ  ARG A  20      20.020  25.597  27.314  1.00 19.19           C  
ANISOU  155  CZ  ARG A  20     1481   1416   4395   -208   -171    416       C  
ATOM    156  NH1 ARG A  20      20.049  26.893  27.600  1.00 18.71           N  
ANISOU  156  NH1 ARG A  20     1596   1353   4160   -316      1    550       N  
ATOM    157  NH2 ARG A  20      20.551  24.721  28.159  1.00 20.95           N  
ANISOU  157  NH2 ARG A  20     1613   1682   4665     27   -369    907       N  
ATOM    158  N   VAL A  21      13.144  25.626  27.634  1.00 13.91           N  
ANISOU  158  N   VAL A  21     1397    977   2909   -311     81     78       N  
ATOM    159  CA  VAL A  21      12.291  25.831  28.795  1.00 14.90           C  
ANISOU  159  CA  VAL A  21     1672   1532   2456    -80   -154     70       C  
ATOM    160  C   VAL A  21      12.400  24.620  29.708  1.00 15.48           C  
ANISOU  160  C   VAL A  21     1748   1481   2654   -263    -44    -77       C  
ATOM    161  O   VAL A  21      12.251  23.475  29.261  1.00 15.62           O  
ANISOU  161  O   VAL A  21     1966   1354   2614   -235    237   -134       O  
ATOM    162  CB  VAL A  21      10.836  26.062  28.355  1.00 15.38           C  
ANISOU  162  CB  VAL A  21     1674   1814   2355    -34     22    109       C  
ATOM    163  CG1 VAL A  21       9.916  26.162  29.554  1.00 16.89           C  
ANISOU  163  CG1 VAL A  21     1775   2068   2576     46    535      2       C  
ATOM    164  CG2 VAL A  21      10.742  27.321  27.501  1.00 16.44           C  
ANISOU  164  CG2 VAL A  21     1721   1672   2852    121     57    431       C  
ATOM    165  N   LYS A  22      12.642  24.861  30.990  1.00 14.94           N  
ANISOU  165  N   LYS A  22     1483   1607   2587   -575    212    166       N  
ATOM    166  CA  LYS A  22      12.643  23.767  31.951  1.00 14.20           C  
ANISOU  166  CA  LYS A  22     1555   1670   2172   -469     94   -120       C  
ATOM    167  C   LYS A  22      11.240  23.183  32.062  1.00 14.28           C  
ANISOU  167  C   LYS A  22     1221   1666   2539   -327     19     51       C  
ATOM    168  O   LYS A  22      10.246  23.915  32.030  1.00 14.97           O  
ANISOU  168  O   LYS A  22     1238   1465   2987    -97     63     -1       O  
ATOM    169  CB  LYS A  22      13.124  24.260  33.313  1.00 18.03           C  
ANISOU  169  CB  LYS A  22     2126   2526   2200   -197   -174     23       C  
ATOM    170  CG  LYS A  22      13.229  23.166  34.360  1.00 25.98           C  
ANISOU  170  CG  LYS A  22     2773   3758   3341    353   -782    -73       C  
ATOM    171  CD  LYS A  22      13.985  23.644  35.593  1.00 28.77           C  
ANISOU  171  CD  LYS A  22     3124   4571   3237    409  -1447    -70       C  
ATOM    172  CE  LYS A  22      14.275  22.489  36.551  1.00 33.93           C  
ANISOU  172  CE  LYS A  22     3691   5389   3811    782  -1629   -103       C  
ATOM    173  NZ  LYS A  22      15.113  22.913  37.702  1.00 37.93           N  
ANISOU  173  NZ  LYS A  22     4119   5937   4355   1019  -1273    106       N  
ATOM    174  N   VAL A  23      11.151  21.851  32.186  1.00 13.21           N  
ANISOU  174  N   VAL A  23     1113   1470   2434   -650    -37    130       N  
ATOM    175  CA  VAL A  23       9.858  21.190  32.305  1.00 13.68           C  
ANISOU  175  CA  VAL A  23     1494   1649   2055    -47   -173   -133       C  
ATOM    176  C   VAL A  23       9.872  20.238  33.489  1.00 14.25           C  
ANISOU  176  C   VAL A  23     1467   1599   2349   -223    -56    149       C  
ATOM    177  O   VAL A  23      10.921  19.753  33.923  1.00 14.45           O  
ANISOU  177  O   VAL A  23     1391   1804   2296   -182   -133   -152       O  
ATOM    178  CB  VAL A  23       9.450  20.415  31.027  1.00 12.31           C  
ANISOU  178  CB  VAL A  23     1554   1330   1792   -159   -172   -160       C  
ATOM    179  CG1 VAL A  23       9.376  21.335  29.843  1.00 13.47           C  
ANISOU  179  CG1 VAL A  23     1723   1411   1983   -141   -195    412       C  
ATOM    180  CG2 VAL A  23      10.406  19.250  30.748  1.00 13.05           C  
ANISOU  180  CG2 VAL A  23     1804   1063   2092     58   -137    -45       C  
ATOM    181  N   SER A  24       8.673  19.954  33.993  1.00 12.96           N  
ANISOU  181  N   SER A  24     1565   1540   1818   -224    -54    -10       N  
ATOM    182  CA  SER A  24       8.444  18.833  34.893  1.00 12.97           C  
ANISOU  182  CA  SER A  24     1493   1497   1939   -284    -28   -170       C  
ATOM    183  C   SER A  24       7.764  17.719  34.115  1.00 12.95           C  
ANISOU  183  C   SER A  24     1439   1345   2137   -252    -78    -22       C  
ATOM    184  O   SER A  24       6.737  17.946  33.468  1.00 13.23           O  
ANISOU  184  O   SER A  24     1624   1360   2041   -196   -322     26       O  
ATOM    185  CB  SER A  24       7.582  19.237  36.091  1.00 15.01           C  
ANISOU  185  CB  SER A  24     1635   1937   2131   -348    100   -440       C  
ATOM    186  OG  SER A  24       8.295  20.077  36.983  1.00 15.57           O  
ANISOU  186  OG  SER A  24     1885   1799   2230   -177    115    -89       O  
ATOM    187  N   VAL A  25       8.331  16.519  34.182  1.00 12.32           N  
ANISOU  187  N   VAL A  25     1411   1227   2042   -168   -168   -149       N  
ATOM    188  CA  VAL A  25       7.776  15.342  33.516  1.00 12.14           C  
ANISOU  188  CA  VAL A  25     1555   1154   1903   -378     16      3       C  
ATOM    189  C   VAL A  25       7.316  14.380  34.599  1.00 12.73           C  
ANISOU  189  C   VAL A  25     1469   1283   2085   -310   -456     18       C  
ATOM    190  O   VAL A  25       8.131  13.904  35.397  1.00 14.03           O  
ANISOU  190  O   VAL A  25     1448   1553   2331    -78   -345    301       O  
ATOM    191  CB  VAL A  25       8.809  14.681  32.589  1.00 12.77           C  
ANISOU  191  CB  VAL A  25     1589   1538   1724     31   -218   -162       C  
ATOM    192  CG1 VAL A  25       8.224  13.422  31.936  1.00 14.71           C  
ANISOU  192  CG1 VAL A  25     1613   1666   2311   -284   -361   -146       C  
ATOM    193  CG2 VAL A  25       9.297  15.671  31.537  1.00 13.66           C  
ANISOU  193  CG2 VAL A  25     1310   1788   2091     35     66    248       C  
ATOM    194  N   TYR A  26       6.014  14.105  34.646  1.00 13.07           N  
ANISOU  194  N   TYR A  26     1559   1368   2037   -454     57   -167       N  
ATOM    195  CA  TYR A  26       5.457  13.224  35.660  1.00 12.63           C  
ANISOU  195  CA  TYR A  26     1377   1326   2095   -443    257      3       C  
ATOM    196  C   TYR A  26       5.273  11.832  35.074  1.00 13.16           C  
ANISOU  196  C   TYR A  26     1555   1296   2149   -256     86    199       C  
ATOM    197  O   TYR A  26       4.807  11.686  33.941  1.00 14.64           O  
ANISOU  197  O   TYR A  26     1505   1744   2314   -182   -518    275       O  
ATOM    198  CB  TYR A  26       4.120  13.757  36.179  1.00 13.96           C  
ANISOU  198  CB  TYR A  26     1610   1362   2331   -184    336   -125       C  
ATOM    199  CG  TYR A  26       4.244  15.057  36.931  1.00 15.09           C  
ANISOU  199  CG  TYR A  26     1753   1636   2346   -365     -3   -550       C  
ATOM    200  CD1 TYR A  26       4.218  16.276  36.265  1.00 16.29           C  
ANISOU  200  CD1 TYR A  26     1918   1289   2982   -360    310   -632       C  
ATOM    201  CD2 TYR A  26       4.398  15.066  38.308  1.00 16.91           C  
ANISOU  201  CD2 TYR A  26     2310   1755   2360   -296    105   -522       C  
ATOM    202  CE1 TYR A  26       4.330  17.475  36.959  1.00 19.05           C  
ANISOU  202  CE1 TYR A  26     2264   1960   3014   -239    151   -776       C  
ATOM    203  CE2 TYR A  26       4.507  16.249  39.004  1.00 18.44           C  
ANISOU  203  CE2 TYR A  26     2729   1525   2752   -245   -106   -831       C  
ATOM    204  CZ  TYR A  26       4.474  17.448  38.326  1.00 21.04           C  
ANISOU  204  CZ  TYR A  26     2659   2127   3207    -48     65   -997       C  
ATOM    205  OH  TYR A  26       4.583  18.620  39.032  1.00 25.06           O  
ANISOU  205  OH  TYR A  26     2955   2674   3894     97    -94   -976       O  
ATOM    206  N   LEU A  27       5.643  10.818  35.848  1.00 14.40           N  
ANISOU  206  N   LEU A  27     1690   1364   2416    230     56    239       N  
ATOM    207  CA  LEU A  27       5.563   9.435  35.400  1.00 14.61           C  
ANISOU  207  CA  LEU A  27     1908   1364   2277    115   -143    193       C  
ATOM    208  C   LEU A  27       4.366   8.722  36.022  1.00 17.37           C  
ANISOU  208  C   LEU A  27     2054   1599   2949   -198     50    244       C  
ATOM    209  O   LEU A  27       3.832   9.136  37.052  1.00 18.41           O  
ANISOU  209  O   LEU A  27     2202   1851   2942   -401    182    381       O  
ATOM    210  CB  LEU A  27       6.849   8.681  35.736  1.00 14.97           C  
ANISOU  210  CB  LEU A  27     1749   1308   2633     91    -43     91       C  
ATOM    211  CG  LEU A  27       8.143   9.339  35.260  1.00 15.31           C  
ANISOU  211  CG  LEU A  27     1891   1414   2513     88   -304    284       C  
ATOM    212  CD1 LEU A  27       9.327   8.431  35.546  1.00 18.15           C  
ANISOU  212  CD1 LEU A  27     2253   1775   2870    665   -114    147       C  
ATOM    213  CD2 LEU A  27       8.072   9.673  33.782  1.00 17.62           C  
ANISOU  213  CD2 LEU A  27     2094   1664   2938    146    -76    224       C  
ATOM    214  N   VAL A  28       3.962   7.622  35.375  1.00 18.61           N  
ANISOU  214  N   VAL A  28     2278   1488   3303   -481     72    192       N  
ATOM    215  CA  VAL A  28       2.802   6.844  35.810  1.00 19.29           C  
ANISOU  215  CA  VAL A  28     2504   1714   3110   -584    154    355       C  
ATOM    216  C   VAL A  28       2.938   6.354  37.242  1.00 22.13           C  
ANISOU  216  C   VAL A  28     2527   2225   3654   -524    347    663       C  
ATOM    217  O   VAL A  28       1.926   6.103  37.903  1.00 26.32           O  
ANISOU  217  O   VAL A  28     2550   3116   4334   -113    207   1392       O  
ATOM    218  CB  VAL A  28       2.555   5.647  34.862  1.00 21.40           C  
ANISOU  218  CB  VAL A  28     2846   1982   3303   -598   -117    200       C  
ATOM    219  CG1 VAL A  28       2.055   6.127  33.515  1.00 24.94           C  
ANISOU  219  CG1 VAL A  28     3061   2277   4139   -543   -134   -301       C  
ATOM    220  CG2 VAL A  28       3.820   4.830  34.694  1.00 22.78           C  
ANISOU  220  CG2 VAL A  28     2995   2190   3471   -747    -32     38       C  
ATOM    221  N   ASN A  29       4.162   6.205  37.746  1.00 20.83           N  
ANISOU  221  N   ASN A  29     2623   1991   3300   -430    312    641       N  
ATOM    222  CA  ASN A  29       4.380   5.717  39.100  1.00 22.84           C  
ANISOU  222  CA  ASN A  29     2849   2517   3312   -163    354    996       C  
ATOM    223  C   ASN A  29       4.564   6.838  40.119  1.00 24.18           C  
ANISOU  223  C   ASN A  29     3141   2850   3199   -395    262    516       C  
ATOM    224  O   ASN A  29       4.953   6.563  41.258  1.00 27.14           O  
ANISOU  224  O   ASN A  29     3423   3259   3629   -490    213    327       O  
ATOM    225  CB  ASN A  29       5.585   4.769  39.135  1.00 23.70           C  
ANISOU  225  CB  ASN A  29     3000   2758   3249    389     71   1269       C  
ATOM    226  CG  ASN A  29       6.852   5.400  38.588  1.00 23.05           C  
ANISOU  226  CG  ASN A  29     3021   2446   3292    444    -57   1009       C  
ATOM    227  OD1 ASN A  29       6.953   6.626  38.453  1.00 22.73           O  
ANISOU  227  OD1 ASN A  29     2852   2369   3415    113    -18    695       O  
ATOM    228  ND2 ASN A  29       7.833   4.562  38.265  1.00 25.75           N  
ANISOU  228  ND2 ASN A  29     3254   2992   3540    828   -501    641       N  
ATOM    229  N   GLY A  30       4.298   8.088  39.744  1.00 24.11           N  
ANISOU  229  N   GLY A  30     2841   3157   3162   -696    388    278       N  
ATOM    230  CA  GLY A  30       4.382   9.192  40.675  1.00 23.30           C  
ANISOU  230  CA  GLY A  30     2633   3428   2791   -731    332    161       C  
ATOM    231  C   GLY A  30       5.716   9.914  40.721  1.00 23.38           C  
ANISOU  231  C   GLY A  30     2788   3335   2761   -682    281    303       C  
ATOM    232  O   GLY A  30       5.807  10.963  41.371  1.00 25.80           O  
ANISOU  232  O   GLY A  30     3019   3751   3033   -599    242   -118       O  
ATOM    233  N   VAL A  31       6.751   9.389  40.062  1.00 20.95           N  
ANISOU  233  N   VAL A  31     2651   2859   2448   -663    177    854       N  
ATOM    234  CA  VAL A  31       8.037  10.080  39.994  1.00 21.03           C  
ANISOU  234  CA  VAL A  31     2615   2910   2464   -378   -123    977       C  
ATOM    235  C   VAL A  31       7.902  11.343  39.150  1.00 19.50           C  
ANISOU  235  C   VAL A  31     2560   2383   2467   -376   -231    219       C  
ATOM    236  O   VAL A  31       7.220  11.352  38.117  1.00 18.43           O  
ANISOU  236  O   VAL A  31     2348   2199   2455   -379   -339    234       O  
ATOM    237  CB  VAL A  31       9.113   9.142  39.417  1.00 23.72           C  
ANISOU  237  CB  VAL A  31     2739   2954   3318   -188   -318   1373       C  
ATOM    238  CG1 VAL A  31      10.403   9.901  39.118  1.00 25.73           C  
ANISOU  238  CG1 VAL A  31     2649   2970   4158   -254   -271   1123       C  
ATOM    239  CG2 VAL A  31       9.390   7.989  40.365  1.00 26.15           C  
ANISOU  239  CG2 VAL A  31     2980   3246   3708    140   -635   1616       C  
ATOM    240  N   ARG A  32       8.553  12.424  39.584  1.00 18.18           N  
ANISOU  240  N   ARG A  32     2385   2520   2003   -440   -356    426       N  
ATOM    241  CA  ARG A  32       8.618  13.658  38.811  1.00 18.35           C  
ANISOU  241  CA  ARG A  32     2324   2601   2046   -450     65    328       C  
ATOM    242  C   ARG A  32      10.065  13.942  38.446  1.00 16.83           C  
ANISOU  242  C   ARG A  32     1956   2546   1892   -356   -340    214       C  
ATOM    243  O   ARG A  32      10.916  14.074  39.334  1.00 19.90           O  
ANISOU  243  O   ARG A  32     2196   3118   2248   -329    -96    384       O  
ATOM    244  CB  ARG A  32       8.037  14.846  39.580  1.00 19.48           C  
ANISOU  244  CB  ARG A  32     2741   2711   1949   -426    125    327       C  
ATOM    245  CG  ARG A  32       8.059  16.142  38.771  1.00 20.42           C  
ANISOU  245  CG  ARG A  32     3160   2788   1811   -188     19   -153       C  
ATOM    246  CD  ARG A  32       7.774  17.335  39.653  1.00 22.72           C  
ANISOU  246  CD  ARG A  32     3574   2933   2125   -485   -458   -342       C  
ATOM    247  NE  ARG A  32       8.906  17.631  40.521  1.00 23.85           N  
ANISOU  247  NE  ARG A  32     3928   2895   2240   -771   -814   -696       N  
ATOM    248  CZ  ARG A  32       8.814  18.311  41.655  1.00 31.08           C  
ANISOU  248  CZ  ARG A  32     4256   3870   3681   -199   -954   -614       C  
ATOM    249  NH1 ARG A  32       7.633  18.755  42.064  1.00 33.34           N  
ANISOU  249  NH1 ARG A  32     4300   4242   4124    116  -1050   -654       N  
ATOM    250  NH2 ARG A  32       9.900  18.533  42.385  1.00 34.55           N  
ANISOU  250  NH2 ARG A  32     4486   4353   4290    -11  -1100   -486       N  
ATOM    251  N   LEU A  33      10.334  14.044  37.150  1.00 14.35           N  
ANISOU  251  N   LEU A  33     1711   2054   1689   -191   -173    264       N  
ATOM    252  CA  LEU A  33      11.631  14.432  36.616  1.00 14.55           C  
ANISOU  252  CA  LEU A  33     1574   1961   1993   -238    -82    317       C  
ATOM    253  C   LEU A  33      11.613  15.907  36.233  1.00 14.97           C  
ANISOU  253  C   LEU A  33     1718   1707   2263   -225   -436    229       C  
ATOM    254  O   LEU A  33      10.568  16.456  35.888  1.00 15.95           O  
ANISOU  254  O   LEU A  33     1626   1900   2533   -297   -851   -165       O  
ATOM    255  CB  LEU A  33      11.977  13.593  35.388  1.00 15.60           C  
ANISOU  255  CB  LEU A  33     1624   1917   2387   -199   -174    298       C  
ATOM    256  CG  LEU A  33      11.743  12.097  35.521  1.00 18.83           C  
ANISOU  256  CG  LEU A  33     2005   2257   2893     67     52    409       C  
ATOM    257  CD1 LEU A  33      11.932  11.429  34.172  1.00 20.84           C  
ANISOU  257  CD1 LEU A  33     2475   2054   3391    -54    241    111       C  
ATOM    258  CD2 LEU A  33      12.692  11.519  36.550  1.00 21.19           C  
ANISOU  258  CD2 LEU A  33     1874   2573   3603    458     99    490       C  
ATOM    259  N   GLN A  34      12.782  16.543  36.275  1.00 14.48           N  
ANISOU  259  N   GLN A  34     1610   1687   2206    -36    -33    265       N  
ATOM    260  CA  GLN A  34      12.897  17.933  35.851  1.00 15.16           C  
ANISOU  260  CA  GLN A  34     1828   1704   2227   -127   -172     -1       C  
ATOM    261  C   GLN A  34      14.132  18.112  34.987  1.00 14.55           C  
ANISOU  261  C   GLN A  34     1568   1624   2335   -113   -612    308       C  
ATOM    262  O   GLN A  34      15.170  17.485  35.219  1.00 18.26           O  
ANISOU  262  O   GLN A  34     1627   2192   3119   -106   -315    480       O  
ATOM    263  CB  GLN A  34      12.953  18.901  37.041  1.00 17.91           C  
ANISOU  263  CB  GLN A  34     2279   2002   2525   -346     26   -457       C  
ATOM    264  CG  GLN A  34      11.657  18.981  37.827  1.00 20.57           C  
ANISOU  264  CG  GLN A  34     2556   2453   2804   -113     13   -611       C  
ATOM    265  CD  GLN A  34      11.616  20.150  38.781  1.00 24.96           C  
ANISOU  265  CD  GLN A  34     2805   3347   3331   -266     -4   -863       C  
ATOM    266  OE1 GLN A  34      12.591  20.873  38.925  1.00 29.08           O  
ANISOU  266  OE1 GLN A  34     3261   3692   4097   -227   -126  -1314       O  
ATOM    267  NE2 GLN A  34      10.471  20.353  39.425  1.00 27.82           N  
ANISOU  267  NE2 GLN A  34     2894   3946   3731     39     63   -433       N  
ATOM    268  N   GLY A  35      14.011  18.958  33.976  1.00 13.99           N  
ANISOU  268  N   GLY A  35     1332   1642   2341    -55   -282     40       N  
ATOM    269  CA  GLY A  35      15.136  19.242  33.114  1.00 14.85           C  
ANISOU  269  CA  GLY A  35     1259   1861   2524    -32   -294   -147       C  
ATOM    270  C   GLY A  35      14.661  19.954  31.868  1.00 13.63           C  
ANISOU  270  C   GLY A  35     1330   1517   2331   -145    -78   -201       C  
ATOM    271  O   GLY A  35      13.505  20.379  31.773  1.00 15.69           O  
ANISOU  271  O   GLY A  35     1154   1888   2919     11     89     25       O  
ATOM    272  N   ARG A  36      15.571  20.069  30.914  1.00 13.16           N  
ANISOU  272  N   ARG A  36     1477   1125   2396   -166     36   -104       N  
ATOM    273  CA  ARG A  36      15.228  20.571  29.596  1.00 12.29           C  
ANISOU  273  CA  ARG A  36     1487   1026   2155   -309      1   -136       C  
ATOM    274  C   ARG A  36      15.094  19.405  28.631  1.00 13.50           C  
ANISOU  274  C   ARG A  36     1507   1205   2417   -214   -131    -58       C  
ATOM    275  O   ARG A  36      15.769  18.379  28.766  1.00 13.91           O  
ANISOU  275  O   ARG A  36     1734   1219   2330     74   -286    -15       O  
ATOM    276  CB  ARG A  36      16.278  21.554  29.080  1.00 13.96           C  
ANISOU  276  CB  ARG A  36     1806   1006   2492   -647    -24    178       C  
ATOM    277  CG  ARG A  36      16.297  22.872  29.826  1.00 16.33           C  
ANISOU  277  CG  ARG A  36     2256   1089   2859   -714   -234     36       C  
ATOM    278  CD  ARG A  36      17.355  23.771  29.223  1.00 19.48           C  
ANISOU  278  CD  ARG A  36     2583   1331   3487   -863   -120    157       C  
ATOM    279  NE  ARG A  36      17.401  25.100  29.828  1.00 20.69           N  
ANISOU  279  NE  ARG A  36     2561   1619   3683  -1038   -245     72       N  
ATOM    280  CZ  ARG A  36      18.270  25.453  30.766  1.00 23.38           C  
ANISOU  280  CZ  ARG A  36     3051   1893   3938   -520   -503   -318       C  
ATOM    281  NH1 ARG A  36      19.161  24.575  31.206  1.00 24.66           N  
ANISOU  281  NH1 ARG A  36     2974   2274   4124   -324   -664   -141       N  
ATOM    282  NH2 ARG A  36      18.252  26.681  31.261  1.00 26.86           N  
ANISOU  282  NH2 ARG A  36     3536   2350   4320    -31   -532   -746       N  
ATOM    283  N   ILE A  37      14.199  19.567  27.660  1.00 12.83           N  
ANISOU  283  N   ILE A  37     1383   1385   2109   -409   -250    -58       N  
ATOM    284  CA  ILE A  37      14.059  18.604  26.575  1.00 13.08           C  
ANISOU  284  CA  ILE A  37     1651   1083   2237   -209   -371    -83       C  
ATOM    285  C   ILE A  37      15.170  18.901  25.574  1.00 12.92           C  
ANISOU  285  C   ILE A  37     1659   1003   2249   -260   -197    243       C  
ATOM    286  O   ILE A  37      15.122  19.898  24.848  1.00 14.45           O  
ANISOU  286  O   ILE A  37     1911   1311   2268     -9    -17    264       O  
ATOM    287  CB  ILE A  37      12.677  18.668  25.929  1.00 12.93           C  
ANISOU  287  CB  ILE A  37     1583    972   2357   -387   -333    -97       C  
ATOM    288  CG1 ILE A  37      11.610  18.282  26.961  1.00 15.47           C  
ANISOU  288  CG1 ILE A  37     1362   1281   3233   -466   -426    136       C  
ATOM    289  CG2 ILE A  37      12.616  17.763  24.704  1.00 14.58           C  
ANISOU  289  CG2 ILE A  37     2079   1263   2198   -285   -579   -551       C  
ATOM    290  CD1 ILE A  37      10.199  18.531  26.493  1.00 17.63           C  
ANISOU  290  CD1 ILE A  37     1375   1980   3344   -340   -812     47       C  
ATOM    291  N   ARG A  38      16.204  18.058  25.570  1.00 14.57           N  
ANISOU  291  N   ARG A  38     1809   1403   2323   -316   -365     94       N  
ATOM    292  CA  ARG A  38      17.289  18.223  24.614  1.00 14.13           C  
ANISOU  292  CA  ARG A  38     1449   1581   2340   -117   -349    143       C  
ATOM    293  C   ARG A  38      16.923  17.666  23.247  1.00 12.86           C  
ANISOU  293  C   ARG A  38     1337   1226   2324   -278   -276    282       C  
ATOM    294  O   ARG A  38      17.326  18.222  22.219  1.00 14.80           O  
ANISOU  294  O   ARG A  38     1690   1420   2515   -209     48     98       O  
ATOM    295  CB  ARG A  38      18.551  17.539  25.145  1.00 15.43           C  
ANISOU  295  CB  ARG A  38     1277   1929   2655   -274   -562    106       C  
ATOM    296  CG  ARG A  38      19.753  17.634  24.225  1.00 20.93           C  
ANISOU  296  CG  ARG A  38     1659   2743   3550      0    -19    272       C  
ATOM    297  CD  ARG A  38      20.280  19.067  24.159  1.00 25.81           C  
ANISOU  297  CD  ARG A  38     1867   3372   4568   -185    667    784       C  
ATOM    298  NE  ARG A  38      21.357  19.209  23.186  1.00 31.76           N  
ANISOU  298  NE  ARG A  38     2156   4379   5531   -174    520    796       N  
ATOM    299  CZ  ARG A  38      22.638  18.983  23.453  1.00 36.72           C  
ANISOU  299  CZ  ARG A  38     2704   4929   6317   -113    488    797       C  
ATOM    300  NH1 ARG A  38      23.006  18.600  24.670  1.00 38.87           N  
ANISOU  300  NH1 ARG A  38     3060   5104   6603    -56    526   1273       N  
ATOM    301  NH2 ARG A  38      23.553  19.137  22.503  1.00 38.11           N  
ANISOU  301  NH2 ARG A  38     2911   5212   6359    -18    763    580       N  
ATOM    302  N   SER A  39      16.145  16.591  23.218  1.00 13.88           N  
ANISOU  302  N   SER A  39     1607   1135   2531    -12    -79   -266       N  
ATOM    303  CA  SER A  39      15.811  15.902  21.984  1.00 12.44           C  
ANISOU  303  CA  SER A  39     1495   1158   2074   -176    260   -183       C  
ATOM    304  C   SER A  39      14.558  15.085  22.246  1.00 12.94           C  
ANISOU  304  C   SER A  39     1544   1164   2207   -107    -29      0       C  
ATOM    305  O   SER A  39      14.230  14.788  23.392  1.00 14.46           O  
ANISOU  305  O   SER A  39     1589   1618   2287   -221   -140   -185       O  
ATOM    306  CB  SER A  39      16.972  15.007  21.521  1.00 15.91           C  
ANISOU  306  CB  SER A  39     1715   1596   2735   -291    159   -488       C  
ATOM    307  OG  SER A  39      16.694  14.423  20.263  1.00 19.29           O  
ANISOU  307  OG  SER A  39     1878   2354   3099   -358     29   -669       O  
ATOM    308  N   PHE A  40      13.852  14.749  21.174  1.00 13.17           N  
ANISOU  308  N   PHE A  40     1347   1282   2374    -73    -61      8       N  
ATOM    309  CA  PHE A  40      12.727  13.832  21.286  1.00 12.27           C  
ANISOU  309  CA  PHE A  40     1255   1103   2306   -239   -169   -151       C  
ATOM    310  C   PHE A  40      12.552  13.119  19.955  1.00 12.57           C  
ANISOU  310  C   PHE A  40     1336   1291   2150     70    -53    125       C  
ATOM    311  O   PHE A  40      13.088  13.536  18.930  1.00 15.07           O  
ANISOU  311  O   PHE A  40     1498   1778   2449   -214    210   -202       O  
ATOM    312  CB  PHE A  40      11.431  14.557  21.696  1.00 14.03           C  
ANISOU  312  CB  PHE A  40     1462   1517   2350    101    235    107       C  
ATOM    313  CG  PHE A  40      10.937  15.544  20.673  1.00 13.89           C  
ANISOU  313  CG  PHE A  40     1471   1439   2369    121     78    -48       C  
ATOM    314  CD1 PHE A  40      11.423  16.843  20.654  1.00 13.85           C  
ANISOU  314  CD1 PHE A  40     1388   1261   2614    120     23     15       C  
ATOM    315  CD2 PHE A  40       9.978  15.173  19.738  1.00 16.05           C  
ANISOU  315  CD2 PHE A  40     1804   1823   2472    529     53   -132       C  
ATOM    316  CE1 PHE A  40      10.970  17.753  19.716  1.00 14.85           C  
ANISOU  316  CE1 PHE A  40     1490   1603   2550    324     21    -70       C  
ATOM    317  CE2 PHE A  40       9.524  16.072  18.800  1.00 16.88           C  
ANISOU  317  CE2 PHE A  40     1903   1837   2672    518    149      2       C  
ATOM    318  CZ  PHE A  40      10.026  17.371  18.789  1.00 15.20           C  
ANISOU  318  CZ  PHE A  40     1591   1623   2560    437    139   -104       C  
ATOM    319  N   ASP A  41      11.811  12.019  19.982  1.00 13.25           N  
ANISOU  319  N   ASP A  41     1496   1306   2232     71    239     92       N  
ATOM    320  CA  ASP A  41      11.386  11.372  18.748  1.00 13.24           C  
ANISOU  320  CA  ASP A  41     1514   1347   2168   -130     23   -231       C  
ATOM    321  C   ASP A  41      10.013  10.762  19.005  1.00 12.93           C  
ANISOU  321  C   ASP A  41     1462   1339   2112    -27   -349     -9       C  
ATOM    322  O   ASP A  41       9.330  11.141  19.960  1.00 14.41           O  
ANISOU  322  O   ASP A  41     1516   1562   2397   -136   -279   -200       O  
ATOM    323  CB  ASP A  41      12.459  10.381  18.248  1.00 13.73           C  
ANISOU  323  CB  ASP A  41     1550   1379   2288    430     29     27       C  
ATOM    324  CG  ASP A  41      12.637   9.160  19.138  1.00 14.19           C  
ANISOU  324  CG  ASP A  41     1281   1617   2493    266    -85     -7       C  
ATOM    325  OD1 ASP A  41      11.994   9.036  20.192  1.00 14.31           O  
ANISOU  325  OD1 ASP A  41     1351   1683   2402     92    110    157       O  
ATOM    326  OD2 ASP A  41      13.466   8.306  18.761  1.00 15.37           O  
ANISOU  326  OD2 ASP A  41     1428   1600   2810    327   -265   -130       O  
ATOM    327  N   LEU A  42       9.602   9.817  18.156  1.00 13.55           N  
ANISOU  327  N   LEU A  42     1357   1502   2289   -264   -414   -203       N  
ATOM    328  CA  LEU A  42       8.227   9.330  18.231  1.00 13.70           C  
ANISOU  328  CA  LEU A  42     1425   1599   2183   -431   -371    -77       C  
ATOM    329  C   LEU A  42       7.908   8.754  19.605  1.00 14.89           C  
ANISOU  329  C   LEU A  42     1420   1601   2636     10   -394   -197       C  
ATOM    330  O   LEU A  42       6.827   9.001  20.154  1.00 13.86           O  
ANISOU  330  O   LEU A  42     1492   1530   2244    220   -378   -202       O  
ATOM    331  CB  LEU A  42       7.978   8.300  17.131  1.00 16.17           C  
ANISOU  331  CB  LEU A  42     1724   1978   2441   -484   -479   -338       C  
ATOM    332  CG  LEU A  42       6.568   7.740  17.004  1.00 20.81           C  
ANISOU  332  CG  LEU A  42     2070   2952   2884   -144   -358   -330       C  
ATOM    333  CD1 LEU A  42       5.576   8.868  16.857  1.00 22.05           C  
ANISOU  333  CD1 LEU A  42     1602   3485   3290   -369   -305    230       C  
ATOM    334  CD2 LEU A  42       6.523   6.825  15.806  1.00 21.23           C  
ANISOU  334  CD2 LEU A  42     2610   3025   2430   -136   -348   -348       C  
ATOM    335  N   PHE A  43       8.838   8.012  20.205  1.00 13.48           N  
ANISOU  335  N   PHE A  43     1490   1578   2055    -75   -273     60       N  
ATOM    336  CA  PHE A  43       8.514   7.323  21.441  1.00 12.57           C  
ANISOU  336  CA  PHE A  43     1503   1040   2232   -141   -281   -437       C  
ATOM    337  C   PHE A  43       9.312   7.755  22.663  1.00 12.72           C  
ANISOU  337  C   PHE A  43     1071   1379   2383    -14   -204   -455       C  
ATOM    338  O   PHE A  43       8.994   7.295  23.764  1.00 12.75           O  
ANISOU  338  O   PHE A  43      900   1521   2422     86   -337    -64       O  
ATOM    339  CB  PHE A  43       8.668   5.807  21.247  1.00 14.51           C  
ANISOU  339  CB  PHE A  43     1819   1224   2470   -360   -189   -635       C  
ATOM    340  CG  PHE A  43       7.662   5.233  20.301  1.00 17.17           C  
ANISOU  340  CG  PHE A  43     2188   1509   2827   -248   -183   -528       C  
ATOM    341  CD1 PHE A  43       6.307   5.265  20.618  1.00 19.18           C  
ANISOU  341  CD1 PHE A  43     2224   1727   3335   -377   -574   -536       C  
ATOM    342  CD2 PHE A  43       8.053   4.670  19.095  1.00 18.89           C  
ANISOU  342  CD2 PHE A  43     2458   1908   2813    -35   -320   -211       C  
ATOM    343  CE1 PHE A  43       5.365   4.743  19.750  1.00 20.51           C  
ANISOU  343  CE1 PHE A  43     2428   2148   3217   -219   -586   -796       C  
ATOM    344  CE2 PHE A  43       7.112   4.130  18.226  1.00 18.99           C  
ANISOU  344  CE2 PHE A  43     2309   2017   2887   -109   -489   -659       C  
ATOM    345  CZ  PHE A  43       5.769   4.168  18.553  1.00 20.92           C  
ANISOU  345  CZ  PHE A  43     2573   2301   3074   -167   -482  -1010       C  
ATOM    346  N   THR A  44      10.326   8.612  22.525  1.00 10.91           N  
ANISOU  346  N   THR A  44     1183    843   2120   -243   -198   -296       N  
ATOM    347  CA  THR A  44      11.161   8.943  23.675  1.00 11.37           C  
ANISOU  347  CA  THR A  44     1256   1081   1983   -130   -367   -558       C  
ATOM    348  C   THR A  44      11.447  10.439  23.730  1.00 10.67           C  
ANISOU  348  C   THR A  44      968    892   2196   -178   -410   -301       C  
ATOM    349  O   THR A  44      11.276  11.173  22.754  1.00 12.57           O  
ANISOU  349  O   THR A  44     1305   1081   2390      4   -220    -38       O  
ATOM    350  CB  THR A  44      12.500   8.170  23.679  1.00 11.64           C  
ANISOU  350  CB  THR A  44     1246    980   2197    249    384    -21       C  
ATOM    351  OG1 THR A  44      13.285   8.533  22.533  1.00 13.19           O  
ANISOU  351  OG1 THR A  44     1295   1321   2396     37    191    128       O  
ATOM    352  CG2 THR A  44      12.263   6.649  23.705  1.00 12.87           C  
ANISOU  352  CG2 THR A  44     1204    984   2703     -8    -72   -301       C  
ATOM    353  N   ILE A  45      11.865  10.871  24.916  1.00 10.92           N  
ANISOU  353  N   ILE A  45      874   1024   2252    -77   -401   -484       N  
ATOM    354  CA  ILE A  45      12.295  12.240  25.194  1.00 11.18           C  
ANISOU  354  CA  ILE A  45      875   1009   2364   -134    -82   -503       C  
ATOM    355  C   ILE A  45      13.620  12.151  25.937  1.00 11.89           C  
ANISOU  355  C   ILE A  45      990   1025   2502    -69   -127     90       C  
ATOM    356  O   ILE A  45      13.747  11.373  26.887  1.00 14.04           O  
ANISOU  356  O   ILE A  45     1460   1168   2708   -165   -172    193       O  
ATOM    357  CB  ILE A  45      11.260  13.004  26.041  1.00 12.77           C  
ANISOU  357  CB  ILE A  45     1225   1207   2421     23   -149   -533       C  
ATOM    358  CG1 ILE A  45       9.968  13.183  25.251  1.00 12.81           C  
ANISOU  358  CG1 ILE A  45     1256   1310   2302    188    -32   -282       C  
ATOM    359  CG2 ILE A  45      11.809  14.357  26.485  1.00 15.18           C  
ANISOU  359  CG2 ILE A  45     1274   1634   2859    -16    177   -231       C  
ATOM    360  CD1 ILE A  45       8.805  13.631  26.083  1.00 13.61           C  
ANISOU  360  CD1 ILE A  45     1372   1384   2414    256     73     -2       C  
ATOM    361  N   LEU A  46      14.601  12.948  25.512  1.00 12.25           N  
ANISOU  361  N   LEU A  46     1055   1098   2502    -49   -114    -91       N  
ATOM    362  CA  LEU A  46      15.889  13.039  26.192  1.00 11.37           C  
ANISOU  362  CA  LEU A  46      688   1210   2422   -204   -139     -1       C  
ATOM    363  C   LEU A  46      15.865  14.273  27.077  1.00 12.53           C  
ANISOU  363  C   LEU A  46     1143   1245   2374   -259   -319   -165       C  
ATOM    364  O   LEU A  46      15.836  15.403  26.573  1.00 13.91           O  
ANISOU  364  O   LEU A  46     1588   1311   2385   -234   -157    217       O  
ATOM    365  CB  LEU A  46      17.051  13.117  25.202  1.00 12.53           C  
ANISOU  365  CB  LEU A  46      738   1403   2619   -102   -118    309       C  
ATOM    366  CG  LEU A  46      18.449  13.180  25.831  1.00 16.29           C  
ANISOU  366  CG  LEU A  46     1258   2013   2920    191   -102     61       C  
ATOM    367  CD1 LEU A  46      18.774  11.864  26.528  1.00 17.50           C  
ANISOU  367  CD1 LEU A  46     1216   2271   3162    367   -420    131       C  
ATOM    368  CD2 LEU A  46      19.507  13.527  24.787  1.00 18.37           C  
ANISOU  368  CD2 LEU A  46     1442   2610   2927    278   -102   -318       C  
ATOM    369  N  ALEU A  47      15.928  14.064  28.390  0.45 12.69           N  
ANISOU  369  N  ALEU A  47     1359   1261   2201    -80   -384   -272       N  
ATOM    370  N  BLEU A  47      15.802  14.053  28.382  0.55 11.83           N  
ANISOU  370  N  BLEU A  47     1215   1235   2043   -250   -332   -217       N  
ATOM    371  CA ALEU A  47      15.862  15.134  29.380  0.45 13.64           C  
ANISOU  371  CA ALEU A  47     1367   1474   2343     33   -381   -235       C  
ATOM    372  CA BLEU A  47      15.928  15.131  29.345  0.55 12.61           C  
ANISOU  372  CA BLEU A  47     1072   1390   2329   -484   -267   -241       C  
ATOM    373  C  ALEU A  47      17.239  15.364  29.996  0.45 13.75           C  
ANISOU  373  C  ALEU A  47     1385   1324   2515   -132   -264   -167       C  
ATOM    374  C  BLEU A  47      17.390  15.358  29.676  0.55 14.05           C  
ANISOU  374  C  BLEU A  47     1374   1337   2629   -495   -294   -187       C  
ATOM    375  O  ALEU A  47      17.850  14.426  30.521  0.45 14.25           O  
ANISOU  375  O  ALEU A  47     1502   1179   2733    229   -319   -278       O  
ATOM    376  O  BLEU A  47      18.202  14.430  29.692  0.55 16.69           O  
ANISOU  376  O  BLEU A  47     1841   1402   3097    -77     57   -274       O  
ATOM    377  CB ALEU A  47      14.846  14.778  30.468  0.45 15.31           C  
ANISOU  377  CB ALEU A  47     1799   1621   2399    283   -221     52       C  
ATOM    378  CB BLEU A  47      15.166  14.819  30.631  0.55 13.40           C  
ANISOU  378  CB BLEU A  47     1173   1563   2355   -453    238    253       C  
ATOM    379  CG ALEU A  47      14.317  15.865  31.400  0.45 15.68           C  
ANISOU  379  CG ALEU A  47     1831   1657   2469    160   -119   -134       C  
ATOM    380  CG BLEU A  47      13.646  14.880  30.552  0.55 13.26           C  
ANISOU  380  CG BLEU A  47     1070   1355   2612   -476    260    173       C  
ATOM    381  CD1ALEU A  47      13.455  16.833  30.625  0.45 15.47           C  
ANISOU  381  CD1ALEU A  47     1716   1517   2644    220   -250   -610       C  
ATOM    382  CD1BLEU A  47      13.038  14.582  31.910  0.55 13.22           C  
ANISOU  382  CD1BLEU A  47     1270   1179   2575   -453    167    421       C  
ATOM    383  CD2ALEU A  47      13.535  15.246  32.546  0.45 14.71           C  
ANISOU  383  CD2ALEU A  47     1793   1386   2411   -155   -320   -645       C  
ATOM    384  CD2BLEU A  47      13.197  16.239  30.049  0.55 14.34           C  
ANISOU  384  CD2BLEU A  47     1306   1286   2856   -109    455     99       C  
ATOM    385  N   GLU A  48      17.716  16.610  29.950  1.00 14.10           N  
ANISOU  385  N   GLU A  48     1527   1327   2502   -403   -350   -156       N  
ATOM    386  CA  GLU A  48      19.036  16.973  30.443  1.00 16.77           C  
ANISOU  386  CA  GLU A  48     1723   1662   2987   -426   -324      0       C  
ATOM    387  C   GLU A  48      18.886  17.940  31.604  1.00 17.69           C  
ANISOU  387  C   GLU A  48     1937   2043   2740   -429  -1206   -109       C  
ATOM    388  O   GLU A  48      18.169  18.941  31.502  1.00 19.64           O  
ANISOU  388  O   GLU A  48     2009   2178   3274    -30  -1020   -513       O  
ATOM    389  CB  GLU A  48      19.898  17.578  29.330  1.00 22.56           C  
ANISOU  389  CB  GLU A  48     2035   2633   3904   -151   -369   -421       C  
ATOM    390  CG  GLU A  48      20.527  16.523  28.417  1.00 28.65           C  
ANISOU  390  CG  GLU A  48     2322   3527   5038    -89   -565   -242       C  
ATOM    391  CD  GLU A  48      21.526  17.092  27.420  1.00 34.03           C  
ANISOU  391  CD  GLU A  48     2628   4487   5814    287      9    347       C  
ATOM    392  OE1 GLU A  48      21.460  18.305  27.123  1.00 31.96           O  
ANISOU  392  OE1 GLU A  48     2576   3832   5735   -369    143    557       O  
ATOM    393  OE2 GLU A  48      22.385  16.315  26.938  1.00 39.79           O  
ANISOU  393  OE2 GLU A  48     3152   5623   6343   1015    -34    431       O  
ATOM    394  N   ASP A  49      19.561  17.634  32.705  1.00 21.73           N  
ANISOU  394  N   ASP A  49     2545   2732   2980   -267  -1298   -882       N  
ATOM    395  CA  ASP A  49      19.587  18.481  33.888  1.00 29.54           C  
ANISOU  395  CA  ASP A  49     3466   4129   3629    -62  -1936   -912       C  
ATOM    396  C   ASP A  49      21.048  18.660  34.250  1.00 33.77           C  
ANISOU  396  C   ASP A  49     3996   4317   4519   -166  -1975   -902       C  
ATOM    397  O   ASP A  49      21.684  17.720  34.736  1.00 35.37           O  
ANISOU  397  O   ASP A  49     4286   4690   4461    283  -1455   -916       O  
ATOM    398  CB  ASP A  49      18.812  17.852  35.040  1.00 34.94           C  
ANISOU  398  CB  ASP A  49     4145   5214   3916    157  -1932  -1067       C  
ATOM    399  CG  ASP A  49      18.618  18.802  36.188  1.00 42.32           C  
ANISOU  399  CG  ASP A  49     4955   6635   4491    733  -1699   -978       C  
ATOM    400  OD1 ASP A  49      18.140  19.935  35.948  1.00 45.85           O  
ANISOU  400  OD1 ASP A  49     5560   7133   4727    829  -1545  -1031       O  
ATOM    401  OD2 ASP A  49      18.955  18.421  37.328  1.00 46.00           O  
ANISOU  401  OD2 ASP A  49     5284   7167   5026    921  -1326   -769       O  
ATOM    402  N   GLY A  50      21.580  19.854  34.006  1.00 38.09           N  
ANISOU  402  N   GLY A  50     4204   4213   6054   -533  -2058   -475       N  
ATOM    403  CA  GLY A  50      23.004  20.056  34.140  1.00 41.10           C  
ANISOU  403  CA  GLY A  50     4573   3726   7317   -857  -1757    -95       C  
ATOM    404  C   GLY A  50      23.761  19.044  33.309  1.00 44.16           C  
ANISOU  404  C   GLY A  50     4753   3736   8291  -1076  -1797    147       C  
ATOM    405  O   GLY A  50      23.698  19.063  32.077  1.00 44.81           O  
ANISOU  405  O   GLY A  50     4785   3656   8586  -1432  -1725    411       O  
ATOM    406  N   LYS A  51      24.446  18.125  33.979  1.00 47.01           N  
ANISOU  406  N   LYS A  51     5085   3796   8981  -1043  -1786   -126       N  
ATOM    407  CA  LYS A  51      25.276  17.145  33.297  1.00 48.71           C  
ANISOU  407  CA  LYS A  51     5046   4168   9292   -985  -1875   -288       C  
ATOM    408  C   LYS A  51      24.546  15.841  32.998  1.00 45.68           C  
ANISOU  408  C   LYS A  51     4512   3931   8914  -1268  -2048   -545       C  
ATOM    409  O   LYS A  51      24.964  15.108  32.093  1.00 47.32           O  
ANISOU  409  O   LYS A  51     4515   4069   9394  -1513  -1752   -238       O  
ATOM    410  CB  LYS A  51      26.523  16.858  34.139  1.00 52.18           C  
ANISOU  410  CB  LYS A  51     5584   4778   9466   -567  -1792   -253       C  
ATOM    411  CG  LYS A  51      26.476  17.485  35.528  1.00 54.58           C  
ANISOU  411  CG  LYS A  51     6048   5355   9334    -32  -1586    -94       C  
ATOM    412  CD  LYS A  51      27.647  18.433  35.762  1.00 57.01           C  
ANISOU  412  CD  LYS A  51     6390   5875   9396    308  -1283    160       C  
ATOM    413  CE  LYS A  51      27.209  19.895  35.795  1.00 59.27           C  
ANISOU  413  CE  LYS A  51     6664   6304   9553    577  -1026    270       C  
ATOM    414  NZ  LYS A  51      27.091  20.508  34.440  1.00 60.76           N  
ANISOU  414  NZ  LYS A  51     6804   6481   9803    614   -916    271       N  
ATOM    415  N   GLN A  52      23.465  15.543  33.714  1.00 40.81           N  
ANISOU  415  N   GLN A  52     3996   4015   7495  -1062  -2185   -635       N  
ATOM    416  CA  GLN A  52      22.833  14.235  33.611  1.00 34.56           C  
ANISOU  416  CA  GLN A  52     3576   3727   5827   -953  -2101   -418       C  
ATOM    417  C   GLN A  52      21.891  14.151  32.413  1.00 28.07           C  
ANISOU  417  C   GLN A  52     2863   3080   4722   -567  -1828   -366       C  
ATOM    418  O   GLN A  52      21.112  15.069  32.151  1.00 27.82           O  
ANISOU  418  O   GLN A  52     2927   3059   4582     12  -1574   -700       O  
ATOM    419  CB  GLN A  52      22.063  13.910  34.891  1.00 39.05           C  
ANISOU  419  CB  GLN A  52     4333   4906   5599   -475  -1568   -367       C  
ATOM    420  CG  GLN A  52      21.521  12.483  34.924  1.00 43.04           C  
ANISOU  420  CG  GLN A  52     5054   5469   5828   -137   -887   -415       C  
ATOM    421  CD  GLN A  52      20.542  12.243  36.058  1.00 47.96           C  
ANISOU  421  CD  GLN A  52     5703   6040   6480    370   -397   -575       C  
ATOM    422  OE1 GLN A  52      20.502  12.996  37.030  1.00 50.37           O  
ANISOU  422  OE1 GLN A  52     6058   6388   6691    575    -81   -471       O  
ATOM    423  NE2 GLN A  52      19.741  11.190  35.935  1.00 48.49           N  
ANISOU  423  NE2 GLN A  52     5786   5974   6665    523   -327   -572       N  
ATOM    424  N   GLN A  53      21.980  13.040  31.685  1.00 24.82           N  
ANISOU  424  N   GLN A  53     2232   2503   4694   -474  -1466   -131       N  
ATOM    425  CA  GLN A  53      21.047  12.691  30.624  1.00 20.81           C  
ANISOU  425  CA  GLN A  53     1935   1917   4056   -277   -848    217       C  
ATOM    426  C   GLN A  53      20.103  11.604  31.113  1.00 17.16           C  
ANISOU  426  C   GLN A  53     1416   1696   3408   -288   -941      3       C  
ATOM    427  O   GLN A  53      20.512  10.685  31.827  1.00 19.71           O  
ANISOU  427  O   GLN A  53     1694   2120   3674    -35   -935    -35       O  
ATOM    428  CB  GLN A  53      21.770  12.181  29.377  1.00 22.75           C  
ANISOU  428  CB  GLN A  53     2205   1934   4503   -317   -409    368       C  
ATOM    429  CG  GLN A  53      22.754  13.135  28.753  1.00 26.46           C  
ANISOU  429  CG  GLN A  53     2611   2413   5029    -91      3    467       C  
ATOM    430  CD  GLN A  53      23.686  12.418  27.797  1.00 26.85           C  
ANISOU  430  CD  GLN A  53     2922   2612   4665     -9     97    408       C  
ATOM    431  OE1 GLN A  53      24.305  11.406  28.152  1.00 26.86           O  
ANISOU  431  OE1 GLN A  53     2582   3130   4492   -289    398    367       O  
ATOM    432  NE2 GLN A  53      23.778  12.920  26.575  1.00 27.15           N  
ANISOU  432  NE2 GLN A  53     3356   2340   4618   -425     77    863       N  
ATOM    433  N   THR A  54      18.845  11.698  30.702  1.00 13.83           N  
ANISOU  433  N   THR A  54      928   1525   2803   -240   -451   -185       N  
ATOM    434  CA  THR A  54      17.855  10.674  31.007  1.00 13.18           C  
ANISOU  434  CA  THR A  54      944   1258   2807   -317   -316     25       C  
ATOM    435  C   THR A  54      17.015  10.454  29.765  1.00 13.58           C  
ANISOU  435  C   THR A  54     1099   1226   2834   -230   -426   -426       C  
ATOM    436  O   THR A  54      16.396  11.397  29.274  1.00 15.14           O  
ANISOU  436  O   THR A  54     1351   1152   3251    106   -464     32       O  
ATOM    437  CB  THR A  54      16.948  11.088  32.169  1.00 15.23           C  
ANISOU  437  CB  THR A  54     1707   1423   2659   -172   -218    208       C  
ATOM    438  OG1 THR A  54      17.737  11.373  33.326  1.00 18.23           O  
ANISOU  438  OG1 THR A  54     1726   2200   3001    104   -622    -13       O  
ATOM    439  CG2 THR A  54      15.969   9.970  32.496  1.00 16.48           C  
ANISOU  439  CG2 THR A  54     1948   1643   2673   -189    -37    113       C  
ATOM    440  N   LEU A  55      16.980   9.222  29.258  1.00 12.95           N  
ANISOU  440  N   LEU A  55     1119    996   2806   -346   -100    -24       N  
ATOM    441  CA  LEU A  55      16.057   8.877  28.181  1.00 12.16           C  
ANISOU  441  CA  LEU A  55     1015   1089   2518   -176   -206   -336       C  
ATOM    442  C   LEU A  55      14.741   8.452  28.815  1.00 10.98           C  
ANISOU  442  C   LEU A  55      822    947   2404   -193   -104    247       C  
ATOM    443  O   LEU A  55      14.724   7.531  29.635  1.00 12.50           O  
ANISOU  443  O   LEU A  55     1058   1101   2590   -150   -244    482       O  
ATOM    444  CB  LEU A  55      16.605   7.756  27.296  1.00 12.73           C  
ANISOU  444  CB  LEU A  55     1082   1515   2239     -8   -251    -50       C  
ATOM    445  CG  LEU A  55      15.777   7.533  26.022  1.00 12.05           C  
ANISOU  445  CG  LEU A  55     1005   1151   2422    107   -316    214       C  
ATOM    446  CD1 LEU A  55      16.037   8.640  24.997  1.00 14.18           C  
ANISOU  446  CD1 LEU A  55     1104   1349   2933     30   -260    322       C  
ATOM    447  CD2 LEU A  55      16.048   6.165  25.415  1.00 15.05           C  
ANISOU  447  CD2 LEU A  55     1314   1450   2956    181    -83    -44       C  
ATOM    448  N   VAL A  56      13.649   9.138  28.466  1.00 11.26           N  
ANISOU  448  N   VAL A  56      639   1358   2281    153    -49   -389       N  
ATOM    449  CA  VAL A  56      12.335   8.877  29.042  1.00 11.87           C  
ANISOU  449  CA  VAL A  56      963   1330   2215    171    115   -283       C  
ATOM    450  C   VAL A  56      11.453   8.271  27.963  1.00 10.30           C  
ANISOU  450  C   VAL A  56     1019    830   2065   -396     49    -14       C  
ATOM    451  O   VAL A  56      11.335   8.828  26.867  1.00 12.85           O  
ANISOU  451  O   VAL A  56     1652    986   2244   -172    -87    107       O  
ATOM    452  CB  VAL A  56      11.690  10.162  29.596  1.00 12.16           C  
ANISOU  452  CB  VAL A  56     1233   1037   2350   -149    -70   -492       C  
ATOM    453  CG1 VAL A  56      10.390   9.816  30.327  1.00 12.81           C  
ANISOU  453  CG1 VAL A  56      838   1348   2681    -33     46    -87       C  
ATOM    454  CG2 VAL A  56      12.641  10.902  30.515  1.00 13.82           C  
ANISOU  454  CG2 VAL A  56     1375   1144   2731   -303   -311   -467       C  
ATOM    455  N   TYR A  57      10.821   7.136  28.272  1.00 11.11           N  
ANISOU  455  N   TYR A  57      991    787   2445   -243   -184    -19       N  
ATOM    456  CA  TYR A  57       9.839   6.576  27.357  1.00 10.69           C  
ANISOU  456  CA  TYR A  57      970    816   2276   -258   -268   -125       C  
ATOM    457  C   TYR A  57       8.498   7.275  27.543  1.00 11.39           C  
ANISOU  457  C   TYR A  57      980   1126   2221    -69    -42   -323       C  
ATOM    458  O   TYR A  57       7.989   7.370  28.662  1.00 11.91           O  
ANISOU  458  O   TYR A  57     1090   1213   2224    -39   -167    -64       O  
ATOM    459  CB  TYR A  57       9.703   5.060  27.560  1.00 12.51           C  
ANISOU  459  CB  TYR A  57     1059    974   2721     26   -135   -145       C  
ATOM    460  CG  TYR A  57      10.807   4.323  26.847  1.00 10.80           C  
ANISOU  460  CG  TYR A  57      976    947   2180    202     -1    -69       C  
ATOM    461  CD1 TYR A  57      12.024   4.098  27.474  1.00 13.16           C  
ANISOU  461  CD1 TYR A  57     1029    979   2994    -73   -297    277       C  
ATOM    462  CD2 TYR A  57      10.663   3.905  25.530  1.00 11.44           C  
ANISOU  462  CD2 TYR A  57     1039    855   2452   -120   -146   -104       C  
ATOM    463  CE1 TYR A  57      13.072   3.463  26.812  1.00 13.61           C  
ANISOU  463  CE1 TYR A  57     1056   1258   2860    197    -80   -212       C  
ATOM    464  CE2 TYR A  57      11.706   3.260  24.861  1.00 11.90           C  
ANISOU  464  CE2 TYR A  57     1127    839   2554    147     68    -57       C  
ATOM    465  CZ  TYR A  57      12.906   3.043  25.513  1.00 12.01           C  
ANISOU  465  CZ  TYR A  57     1022    917   2626    170     51   -232       C  
ATOM    466  OH  TYR A  57      13.956   2.408  24.868  1.00 14.06           O  
ANISOU  466  OH  TYR A  57     1201   1277   2863    475    167   -220       O  
ATOM    467  N   LYS A  58       7.947   7.786  26.438  1.00 10.98           N  
ANISOU  467  N   LYS A  58      920    905   2349   -127   -371    -68       N  
ATOM    468  CA  LYS A  58       6.682   8.504  26.512  1.00 10.77           C  
ANISOU  468  CA  LYS A  58      952   1018   2122    105   -204   -111       C  
ATOM    469  C   LYS A  58       5.579   7.653  27.120  1.00 11.12           C  
ANISOU  469  C   LYS A  58      877    803   2543      4   -231    165       C  
ATOM    470  O   LYS A  58       4.722   8.185  27.824  1.00 12.43           O  
ANISOU  470  O   LYS A  58      741   1047   2933     46     44    -26       O  
ATOM    471  CB  LYS A  58       6.258   8.987  25.129  1.00 10.55           C  
ANISOU  471  CB  LYS A  58     1092   1166   1752    -51   -312    -51       C  
ATOM    472  CG  LYS A  58       7.123  10.103  24.550  1.00 10.81           C  
ANISOU  472  CG  LYS A  58     1234    966   1909    -18     -4     12       C  
ATOM    473  CD  LYS A  58       6.627  10.426  23.155  1.00 11.99           C  
ANISOU  473  CD  LYS A  58     1269   1191   2096     58     87    245       C  
ATOM    474  CE  LYS A  58       7.450  11.507  22.458  1.00 12.41           C  
ANISOU  474  CE  LYS A  58     1393   1065   2257    -72    -77    305       C  
ATOM    475  NZ  LYS A  58       6.837  11.789  21.122  1.00 13.20           N  
ANISOU  475  NZ  LYS A  58     1329   1437   2248    154   -246     79       N  
ATOM    476  N   HIS A  59       5.583   6.333  26.883  1.00 11.68           N  
ANISOU  476  N   HIS A  59      827    918   2692   -129   -391     96       N  
ATOM    477  CA  HIS A  59       4.520   5.494  27.438  1.00 12.18           C  
ANISOU  477  CA  HIS A  59     1111    779   2737    -71   -206    -66       C  
ATOM    478  C   HIS A  59       4.497   5.512  28.961  1.00 12.46           C  
ANISOU  478  C   HIS A  59     1091    963   2679   -341     79    103       C  
ATOM    479  O   HIS A  59       3.485   5.120  29.555  1.00 13.77           O  
ANISOU  479  O   HIS A  59     1327   1286   2619   -135   -172    248       O  
ATOM    480  CB  HIS A  59       4.632   4.039  26.936  1.00 12.88           C  
ANISOU  480  CB  HIS A  59      956    886   3049    -85   -375    -75       C  
ATOM    481  CG  HIS A  59       5.920   3.356  27.298  1.00 12.26           C  
ANISOU  481  CG  HIS A  59      922    905   2831     34   -371   -155       C  
ATOM    482  ND1 HIS A  59       6.826   2.933  26.349  1.00 14.17           N  
ANISOU  482  ND1 HIS A  59      956   1127   3303     77   -381     18       N  
ATOM    483  CD2 HIS A  59       6.446   3.015  28.500  1.00 13.59           C  
ANISOU  483  CD2 HIS A  59     1132    953   3080    211   -466   -122       C  
ATOM    484  CE1 HIS A  59       7.855   2.360  26.951  1.00 12.89           C  
ANISOU  484  CE1 HIS A  59     1190    947   2763    -36   -293     36       C  
ATOM    485  NE2 HIS A  59       7.651   2.401  28.256  1.00 13.43           N  
ANISOU  485  NE2 HIS A  59     1351   1029   2722    322   -163   -137       N  
ATOM    486  N   ALA A  60       5.574   5.981  29.603  1.00 12.34           N  
ANISOU  486  N   ALA A  60     1016    909   2764   -262     69   -121       N  
ATOM    487  CA  ALA A  60       5.644   6.064  31.052  1.00 12.41           C  
ANISOU  487  CA  ALA A  60     1062   1150   2504    -25     -4     65       C  
ATOM    488  C   ALA A  60       5.275   7.442  31.586  1.00 13.19           C  
ANISOU  488  C   ALA A  60     1245   1113   2655    136   -154     73       C  
ATOM    489  O   ALA A  60       5.203   7.615  32.802  1.00 15.09           O  
ANISOU  489  O   ALA A  60     1535   1216   2982    -70    -64    122       O  
ATOM    490  CB  ALA A  60       7.046   5.675  31.540  1.00 12.69           C  
ANISOU  490  CB  ALA A  60      954   1593   2276    -56   -163    203       C  
ATOM    491  N   ILE A  61       5.008   8.413  30.711  1.00 12.46           N  
ANISOU  491  N   ILE A  61     1246    749   2740     51   -199    275       N  
ATOM    492  CA  ILE A  61       4.713   9.784  31.115  1.00 10.88           C  
ANISOU  492  CA  ILE A  61      990    962   2181    -47     13    282       C  
ATOM    493  C   ILE A  61       3.213   9.941  31.284  1.00 10.70           C  
ANISOU  493  C   ILE A  61      909   1027   2129    -29   -257    -71       C  
ATOM    494  O   ILE A  61       2.444   9.454  30.457  1.00 13.06           O  
ANISOU  494  O   ILE A  61     1324   1318   2320    104    -73    -99       O  
ATOM    495  CB  ILE A  61       5.239  10.781  30.065  1.00 10.93           C  
ANISOU  495  CB  ILE A  61     1185    870   2100     97   -180    133       C  
ATOM    496  CG1 ILE A  61       6.745  10.618  29.883  1.00 11.86           C  
ANISOU  496  CG1 ILE A  61     1021   1126   2358    -53     28    182       C  
ATOM    497  CG2 ILE A  61       4.875  12.221  30.448  1.00 12.24           C  
ANISOU  497  CG2 ILE A  61     1415   1124   2111    363   -437   -451       C  
ATOM    498  CD1 ILE A  61       7.320  11.492  28.789  1.00 12.95           C  
ANISOU  498  CD1 ILE A  61     1430   1281   2209   -231    101    207       C  
ATOM    499  N   THR A  62       2.795  10.632  32.345  1.00 11.80           N  
ANISOU  499  N   THR A  62     1183   1173   2126    -14    204      4       N  
ATOM    500  CA  THR A  62       1.409  11.083  32.424  1.00 11.82           C  
ANISOU  500  CA  THR A  62     1230   1218   2042    -85    399      0       C  
ATOM    501  C   THR A  62       1.248  12.500  31.873  1.00 12.01           C  
ANISOU  501  C   THR A  62     1207    898   2458   -361    134     39       C  
ATOM    502  O   THR A  62       0.383  12.746  31.023  1.00 12.94           O  
ANISOU  502  O   THR A  62     1376   1278   2265    -11   -188   -187       O  
ATOM    503  CB  THR A  62       0.896  11.028  33.867  1.00 13.83           C  
ANISOU  503  CB  THR A  62     1778   1038   2441   -299     63   -138       C  
ATOM    504  OG1 THR A  62       1.671  11.911  34.694  1.00 15.80           O  
ANISOU  504  OG1 THR A  62     2086   1476   2440   -362     -6     31       O  
ATOM    505  CG2 THR A  62       0.975   9.615  34.413  1.00 14.06           C  
ANISOU  505  CG2 THR A  62     1880   1150   2312   -449     91    234       C  
ATOM    506  N   THR A  63       2.065  13.437  32.353  1.00 12.53           N  
ANISOU  506  N   THR A  63     1333    857   2570   -229    381    -46       N  
ATOM    507  CA  THR A  63       1.934  14.847  32.002  1.00 12.43           C  
ANISOU  507  CA  THR A  63     1273    976   2475    -12    290   -135       C  
ATOM    508  C   THR A  63       3.303  15.507  31.913  1.00 12.21           C  
ANISOU  508  C   THR A  63     1101   1126   2412    -54    149    -96       C  
ATOM    509  O   THR A  63       4.265  15.092  32.564  1.00 13.09           O  
ANISOU  509  O   THR A  63     1285   1121   2568   -131    -76    167       O  
ATOM    510  CB  THR A  63       1.106  15.639  33.032  1.00 15.00           C  
ANISOU  510  CB  THR A  63     1481   1739   2480   -183    444   -172       C  
ATOM    511  OG1 THR A  63       1.674  15.462  34.331  1.00 20.10           O  
ANISOU  511  OG1 THR A  63     1871   3044   2722    277    -83   -695       O  
ATOM    512  CG2 THR A  63      -0.346  15.191  33.062  1.00 15.18           C  
ANISOU  512  CG2 THR A  63     1331   1434   3001   -287    657   -187       C  
ATOM    513  N   ILE A  64       3.362  16.574  31.117  1.00 12.26           N  
ANISOU  513  N   ILE A  64      958   1155   2546   -276   -264   -161       N  
ATOM    514  CA  ILE A  64       4.520  17.461  31.042  1.00 11.26           C  
ANISOU  514  CA  ILE A  64      952   1059   2269   -291   -237     28       C  
ATOM    515  C   ILE A  64       4.038  18.870  31.334  1.00 11.51           C  
ANISOU  515  C   ILE A  64     1093   1273   2009    -24   -450     32       C  
ATOM    516  O   ILE A  64       3.101  19.355  30.690  1.00 12.85           O  
ANISOU  516  O   ILE A  64     1024   1275   2582    -50   -433    -90       O  
ATOM    517  CB  ILE A  64       5.220  17.397  29.673  1.00 11.53           C  
ANISOU  517  CB  ILE A  64     1228    942   2209    -91   -183    195       C  
ATOM    518  CG1 ILE A  64       5.612  15.949  29.345  1.00 12.49           C  
ANISOU  518  CG1 ILE A  64     1415   1094   2238    193   -129     94       C  
ATOM    519  CG2 ILE A  64       6.445  18.340  29.655  1.00 13.13           C  
ANISOU  519  CG2 ILE A  64     1264    926   2800   -225    -74     49       C  
ATOM    520  CD1 ILE A  64       6.239  15.775  27.987  1.00 14.50           C  
ANISOU  520  CD1 ILE A  64     1274   1544   2689     36   -145   -125       C  
ATOM    521  N   VAL A  65       4.671  19.515  32.307  1.00 12.54           N  
ANISOU  521  N   VAL A  65     1406   1302   2058    -17    -18   -289       N  
ATOM    522  CA  VAL A  65       4.285  20.859  32.730  1.00 13.51           C  
ANISOU  522  CA  VAL A  65     1506   1213   2413   -288    180   -453       C  
ATOM    523  C   VAL A  65       5.463  21.797  32.497  1.00 13.68           C  
ANISOU  523  C   VAL A  65     1513   1146   2538   -398   -170   -401       C  
ATOM    524  O   VAL A  65       6.500  21.654  33.154  1.00 14.81           O  
ANISOU  524  O   VAL A  65     1653   1378   2597   -237   -356   -362       O  
ATOM    525  CB  VAL A  65       3.855  20.886  34.205  1.00 15.31           C  
ANISOU  525  CB  VAL A  65     1773   1400   2645   -488    145   -437       C  
ATOM    526  CG1 VAL A  65       3.526  22.315  34.622  1.00 16.34           C  
ANISOU  526  CG1 VAL A  65     1890   1476   2843   -324    385   -518       C  
ATOM    527  CG2 VAL A  65       2.666  19.962  34.445  1.00 18.26           C  
ANISOU  527  CG2 VAL A  65     2022   2146   2768   -492    115   -372       C  
ATOM    528  N   PRO A  66       5.364  22.752  31.578  1.00 13.77           N  
ANISOU  528  N   PRO A  66     1226   1274   2733   -330   -143   -114       N  
ATOM    529  CA  PRO A  66       6.491  23.663  31.345  1.00 14.38           C  
ANISOU  529  CA  PRO A  66     1510   1095   2859   -261     83      2       C  
ATOM    530  C   PRO A  66       6.574  24.714  32.440  1.00 15.34           C  
ANISOU  530  C   PRO A  66     1609   1088   3129   -363    -68   -356       C  
ATOM    531  O   PRO A  66       5.558  25.168  32.971  1.00 18.09           O  
ANISOU  531  O   PRO A  66     1927   1539   3406   -168    269   -518       O  
ATOM    532  CB  PRO A  66       6.155  24.292  29.989  1.00 16.22           C  
ANISOU  532  CB  PRO A  66     1532   1596   3037    -70    -41     67       C  
ATOM    533  CG  PRO A  66       4.648  24.284  29.954  1.00 16.06           C  
ANISOU  533  CG  PRO A  66     1597   1618   2888   -244     -8    463       C  
ATOM    534  CD  PRO A  66       4.213  23.038  30.699  1.00 15.33           C  
ANISOU  534  CD  PRO A  66     1608   1538   2679   -212   -291     72       C  
ATOM    535  N   HIS A  67       7.804  25.089  32.795  1.00 15.58           N  
ANISOU  535  N   HIS A  67     1667   1358   2895   -332   -115   -586       N  
ATOM    536  CA  HIS A  67       8.005  26.076  33.850  1.00 15.72           C  
ANISOU  536  CA  HIS A  67     1793   1371   2810   -226     84   -357       C  
ATOM    537  C   HIS A  67       7.890  27.514  33.350  1.00 16.17           C  
ANISOU  537  C   HIS A  67     1917   1354   2874     53    394   -597       C  
ATOM    538  O   HIS A  67       7.900  28.443  34.167  1.00 20.90           O  
ANISOU  538  O   HIS A  67     2673   1844   3425    205     59   -820       O  
ATOM    539  CB  HIS A  67       9.360  25.854  34.523  1.00 16.92           C  
ANISOU  539  CB  HIS A  67     1937   1681   2810   -298    -70   -355       C  
ATOM    540  CG  HIS A  67       9.467  24.552  35.259  1.00 18.29           C  
ANISOU  540  CG  HIS A  67     2331   2033   2586   -489   -288   -221       C  
ATOM    541  ND1 HIS A  67      10.458  24.301  36.181  1.00 20.46           N  
ANISOU  541  ND1 HIS A  67     2491   2449   2833   -281   -492   -239       N  
ATOM    542  CD2 HIS A  67       8.717  23.424  35.198  1.00 19.47           C  
ANISOU  542  CD2 HIS A  67     2596   2201   2600   -163   -100   -460       C  
ATOM    543  CE1 HIS A  67      10.316  23.077  36.659  1.00 21.82           C  
ANISOU  543  CE1 HIS A  67     2698   2473   3119    -76   -349   -324       C  
ATOM    544  NE2 HIS A  67       9.264  22.525  36.082  1.00 20.24           N  
ANISOU  544  NE2 HIS A  67     2610   2277   2804   -346   -582   -701       N  
ATOM    545  N   GLU A  68       7.791  27.712  32.038  1.00 16.49           N  
ANISOU  545  N   GLU A  68     1553   1420   3293    -23    133    -66       N  
ATOM    546  CA  GLU A  68       7.422  28.982  31.429  1.00 17.69           C  
ANISOU  546  CA  GLU A  68     1504   1599   3619   -123     95   -198       C  
ATOM    547  C   GLU A  68       6.297  28.716  30.444  1.00 18.63           C  
ANISOU  547  C   GLU A  68     1822   1442   3817     56    278   -240       C  
ATOM    548  O   GLU A  68       6.220  27.637  29.859  1.00 18.35           O  
ANISOU  548  O   GLU A  68     1981   1364   3628     87    104   -304       O  
ATOM    549  CB  GLU A  68       8.585  29.632  30.675  1.00 17.35           C  
ANISOU  549  CB  GLU A  68     1632   1443   3519   -336    383     -6       C  
ATOM    550  CG  GLU A  68       9.841  29.833  31.480  1.00 19.66           C  
ANISOU  550  CG  GLU A  68     1805   1769   3896   -518     81   -166       C  
ATOM    551  CD  GLU A  68      10.974  30.371  30.623  1.00 22.08           C  
ANISOU  551  CD  GLU A  68     1962   1932   4495   -563    160   -137       C  
ATOM    552  OE1 GLU A  68      10.960  31.581  30.313  1.00 24.87           O  
ANISOU  552  OE1 GLU A  68     2321   2081   5047   -293    444     13       O  
ATOM    553  OE2 GLU A  68      11.863  29.574  30.240  1.00 23.12           O  
ANISOU  553  OE2 GLU A  68     1976   2410   4398   -602    158   -300       O  
ATOM    554  N   ARG A  69       5.436  29.706  30.239  1.00 21.13           N  
ANISOU  554  N   ARG A  69     1843   2198   3988    300    106    248       N  
ATOM    555  CA  ARG A  69       4.351  29.514  29.291  1.00 23.13           C  
ANISOU  555  CA  ARG A  69     2210   2206   4374    317   -269   -351       C  
ATOM    556  C   ARG A  69       4.917  29.372  27.887  1.00 22.54           C  
ANISOU  556  C   ARG A  69     2495   1722   4346    -51   -218    163       C  
ATOM    557  O   ARG A  69       5.758  30.169  27.459  1.00 25.04           O  
ANISOU  557  O   ARG A  69     2792   2087   4634   -136   -208      9       O  
ATOM    558  CB  ARG A  69       3.353  30.668  29.345  1.00 28.61           C  
ANISOU  558  CB  ARG A  69     2505   2797   5569    566   -615   -924       C  
ATOM    559  CG  ARG A  69       2.189  30.439  28.400  1.00 33.81           C  
ANISOU  559  CG  ARG A  69     2533   3198   7118    484   -461  -1371       C  
ATOM    560  CD  ARG A  69       1.029  31.379  28.638  1.00 38.82           C  
ANISOU  560  CD  ARG A  69     2815   3473   8461    480   -251  -1669       C  
ATOM    561  NE  ARG A  69      -0.020  31.134  27.655  1.00 42.19           N  
ANISOU  561  NE  ARG A  69     2988   3467   9575    290      3  -1479       N  
ATOM    562  CZ  ARG A  69      -0.980  30.228  27.804  1.00 45.04           C  
ANISOU  562  CZ  ARG A  69     3116   3511  10487    285     79  -1475       C  
ATOM    563  NH1 ARG A  69      -1.032  29.489  28.904  1.00 45.71           N  
ANISOU  563  NH1 ARG A  69     3193   3433  10743    367    341  -1409       N  
ATOM    564  NH2 ARG A  69      -1.891  30.068  26.854  1.00 45.59           N  
ANISOU  564  NH2 ARG A  69     3241   3510  10571     47   -108  -1451       N  
ATOM    565  N   LEU A  70       4.472  28.343  27.177  1.00 20.97           N  
ANISOU  565  N   LEU A  70     2679   1623   3666    340   -316     54       N  
ATOM    566  CA  LEU A  70       4.902  28.122  25.809  1.00 21.48           C  
ANISOU  566  CA  LEU A  70     2683   1903   3577    159   -425    224       C  
ATOM    567  C   LEU A  70       3.923  28.809  24.870  1.00 26.40           C  
ANISOU  567  C   LEU A  70     2946   2726   4358   -119   -556    364       C  
ATOM    568  O   LEU A  70       2.705  28.646  25.001  1.00 29.29           O  
ANISOU  568  O   LEU A  70     2972   3448   4710     18   -888    486       O  
ATOM    569  CB  LEU A  70       4.980  26.629  25.489  1.00 19.55           C  
ANISOU  569  CB  LEU A  70     2370   1694   3365    -78    -66    -10       C  
ATOM    570  CG  LEU A  70       5.876  25.743  26.355  1.00 17.57           C  
ANISOU  570  CG  LEU A  70     1979   1704   2993   -454   -476    -32       C  
ATOM    571  CD1 LEU A  70       5.750  24.296  25.884  1.00 18.51           C  
ANISOU  571  CD1 LEU A  70     1880   1742   3413   -614   -346   -300       C  
ATOM    572  CD2 LEU A  70       7.332  26.185  26.315  1.00 18.41           C  
ANISOU  572  CD2 LEU A  70     2007   1797   3189   -332   -506    -46       C  
ATOM    573  N   GLU A  71       4.453  29.588  23.941  1.00 28.46           N  
ANISOU  573  N   GLU A  71     3453   2626   4735   -251   -422    389       N  
ATOM    574  CA  GLU A  71       3.670  30.105  22.825  1.00 33.28           C  
ANISOU  574  CA  GLU A  71     4275   3410   4960    181   -385    356       C  
ATOM    575  C   GLU A  71       3.930  29.125  21.688  1.00 32.78           C  
ANISOU  575  C   GLU A  71     4389   3477   4589    198   -216    263       C  
ATOM    576  O   GLU A  71       4.890  29.258  20.930  1.00 33.42           O  
ANISOU  576  O   GLU A  71     4635   3623   4442    368    -30    122       O  
ATOM    577  CB  GLU A  71       4.067  31.536  22.488  1.00 39.30           C  
ANISOU  577  CB  GLU A  71     4892   4195   5847    725   -400     51       C  
ATOM    578  CG  GLU A  71       4.145  32.453  23.709  1.00 45.52           C  
ANISOU  578  CG  GLU A  71     5463   4925   6909   1059   -510   -348       C  
ATOM    579  CD  GLU A  71       2.814  32.606  24.438  1.00 51.65           C  
ANISOU  579  CD  GLU A  71     6035   5553   8038   1311   -653   -546       C  
ATOM    580  OE1 GLU A  71       1.753  32.389  23.815  1.00 54.06           O  
ANISOU  580  OE1 GLU A  71     6289   5664   8586   1383   -703   -737       O  
ATOM    581  OE2 GLU A  71       2.827  32.950  25.640  1.00 54.52           O  
ANISOU  581  OE2 GLU A  71     6279   5903   8531   1308   -520   -279       O  
ATOM    582  N   ILE A  72       3.071  28.114  21.596  1.00 32.77           N  
ANISOU  582  N   ILE A  72     4361   3481   4609    264    -82    253       N  
ATOM    583  CA  ILE A  72       3.381  26.914  20.828  1.00 34.14           C  
ANISOU  583  CA  ILE A  72     4414   3800   4757    370   -315    -10       C  
ATOM    584  C   ILE A  72       3.520  27.264  19.351  1.00 36.65           C  
ANISOU  584  C   ILE A  72     4487   4298   5140    773   -624     44       C  
ATOM    585  O   ILE A  72       2.603  27.820  18.738  1.00 39.07           O  
ANISOU  585  O   ILE A  72     4651   4405   5790   1053   -934    311       O  
ATOM    586  CB  ILE A  72       2.313  25.839  21.055  1.00 31.07           C  
ANISOU  586  CB  ILE A  72     4266   3241   4299    -95   -411     29       C  
ATOM    587  CG1 ILE A  72       2.378  25.352  22.503  1.00 31.42           C  
ANISOU  587  CG1 ILE A  72     4218   3329   4391   -215   -487   -270       C  
ATOM    588  CG2 ILE A  72       2.519  24.685  20.112  1.00 30.83           C  
ANISOU  588  CG2 ILE A  72     4231   3211   4271   -178   -745    147       C  
ATOM    589  CD1 ILE A  72       1.474  24.194  22.789  1.00 33.18           C  
ANISOU  589  CD1 ILE A  72     4298   3478   4832   -119   -231     12       C  
ATOM    590  N   GLU A  73       4.677  26.939  18.778  1.00 36.01           N  
ATOM    591  CA  GLU A  73       4.963  27.220  17.377  1.00 49.94           C  
ATOM    592  C   GLU A  73       4.415  26.118  16.475  1.00 53.56           C  
ATOM    593  O   GLU A  73       5.034  25.065  16.318  1.00 48.25           O  
ATOM    594  CB  GLU A  73       6.470  27.371  17.159  1.00 46.08           C  
ATOM    595  CG  GLU A  73       7.152  28.348  18.105  1.00 97.10           C  
ATOM    596  CD  GLU A  73       8.667  28.275  18.026  1.00 72.66           C  
ATOM    597  OE1 GLU A  73       9.295  27.799  18.994  1.00 60.50           O  
ATOM    598  OE2 GLU A  73       9.229  28.682  16.989  1.00102.20           O  
TER     599      GLU A  73                                                      
ATOM    600  P     U C   1      17.758  23.135  15.415  1.00 41.47           P  
ANISOU  600  P     U C   1     5661   4194   5903  -1628   1730   -432       P  
ATOM    601  OP1   U C   1      17.466  23.038  16.866  1.00 40.98           O  
ANISOU  601  OP1   U C   1     5821   4098   5650  -1824   2254   -133       O  
ATOM    602  OP2   U C   1      19.159  23.399  14.988  1.00 44.73           O  
ANISOU  602  OP2   U C   1     5924   4959   6111  -1611   1874    157       O  
ATOM    603  O5'   U C   1      17.271  21.792  14.707  1.00 38.46           O  
ANISOU  603  O5'   U C   1     5126   3793   5695  -1194   1317    -82       O  
ATOM    604  C5'   U C   1      17.314  21.655  13.294  1.00 36.46           C  
ANISOU  604  C5'   U C   1     4389   3671   5792   -573    880    481       C  
ATOM    605  C4'   U C   1      16.654  20.377  12.846  1.00 33.09           C  
ANISOU  605  C4'   U C   1     3485   3648   5439   -282    408    718       C  
ATOM    606  O4'   U C   1      17.404  19.244  13.347  1.00 30.25           O  
ANISOU  606  O4'   U C   1     3267   3418   4809   -362    208    826       O  
ATOM    607  C3'   U C   1      15.241  20.149  13.362  1.00 32.13           C  
ANISOU  607  C3'   U C   1     3000   3449   5760   -162    -50    908       C  
ATOM    608  O3'   U C   1      14.268  20.824  12.581  1.00 33.12           O  
ANISOU  608  O3'   U C   1     2803   3784   5995    132   -202   1125       O  
ATOM    609  C2'   U C   1      15.106  18.630  13.328  1.00 30.80           C  
ANISOU  609  C2'   U C   1     2826   3607   5268   -230   -375    671       C  
ATOM    610  O2'   U C   1      14.815  18.182  12.012  1.00 31.67           O  
ANISOU  610  O2'   U C   1     2679   4028   5325   -165   -597    870       O  
ATOM    611  C1'   U C   1      16.528  18.184  13.661  1.00 26.87           C  
ANISOU  611  C1'   U C   1     2765   3252   4194   -489   -311    894       C  
ATOM    612  N1    U C   1      16.738  17.803  15.076  1.00 22.30           N  
ANISOU  612  N1    U C   1     2613   2926   2931   -628   -138    743       N  
ATOM    613  C2    U C   1      16.225  16.598  15.511  1.00 22.19           C  
ANISOU  613  C2    U C   1     2567   3272   2593   -370   -119    422       C  
ATOM    614  O2    U C   1      15.557  15.866  14.795  1.00 22.73           O  
ANISOU  614  O2    U C   1     2634   3289   2714    -19   -751    -46       O  
ATOM    615  N3    U C   1      16.509  16.292  16.822  1.00 21.54           N  
ANISOU  615  N3    U C   1     2363   3432   2389   -566     68    227       N  
ATOM    616  C4    U C   1      17.240  17.050  17.711  1.00 22.12           C  
ANISOU  616  C4    U C   1     2595   3606   2203   -557    375    399       C  
ATOM    617  O4    U C   1      17.414  16.643  18.855  1.00 24.87           O  
ANISOU  617  O4    U C   1     2817   3929   2705   -568    161    288       O  
ATOM    618  C5    U C   1      17.748  18.272  17.178  1.00 22.85           C  
ANISOU  618  C5    U C   1     2853   3387   2444   -269     93    636       C  
ATOM    619  C6    U C   1      17.495  18.593  15.907  1.00 23.81           C  
ANISOU  619  C6    U C   1     2929   3354   2763   -101   -147    555       C  
ATOM    620  P     U C   2      12.912  21.365  13.250  1.00 31.56           P  
ANISOU  620  P     U C   2     2838   3886   5267     60   -346   1464       P  
ATOM    621  OP1   U C   2      12.271  22.283  12.277  1.00 34.08           O  
ANISOU  621  OP1   U C   2     2954   4127   5867    343   -225   1304       O  
ATOM    622  OP2   U C   2      13.209  21.846  14.621  1.00 34.06           O  
ANISOU  622  OP2   U C   2     3027   4033   5881     43    106   1857       O  
ATOM    623  O5'   U C   2      12.007  20.062  13.344  1.00 34.12           O  
ANISOU  623  O5'   U C   2     2854   4266   5844    164    -70   1776       O  
ATOM    624  C5'   U C   2      11.745  19.276  12.185  1.00 33.95           C  
ANISOU  624  C5'   U C   2     2870   4645   5386    487    123   1787       C  
ATOM    625  C4'   U C   2      10.942  18.045  12.518  1.00 31.10           C  
ANISOU  625  C4'   U C   2     2910   4807   4101    487   -128   1150       C  
ATOM    626  O4'   U C   2      11.705  17.210  13.436  1.00 25.04           O  
ANISOU  626  O4'   U C   2     2585   4135   2795    404     96    514       O  
ATOM    627  C3'   U C   2       9.605  18.317  13.202  1.00 33.62           C  
ANISOU  627  C3'   U C   2     3394   5746   3634    932   -172   1252       C  
ATOM    628  O3'   U C   2       8.663  17.320  12.806  1.00 42.45           O  
ANISOU  628  O3'   U C   2     4456   7407   4266   1282  -1078    960       O  
ATOM    629  C2'   U C   2       9.948  18.135  14.678  1.00 25.72           C  
ANISOU  629  C2'   U C   2     2758   4850   2162    431     41   1386       C  
ATOM    630  O2'   U C   2       8.845  17.840  15.515  1.00 27.71           O  
ANISOU  630  O2'   U C   2     2860   5102   2565    579    541   1097       O  
ATOM    631  C1'   U C   2      10.952  16.988  14.612  1.00 22.99           C  
ANISOU  631  C1'   U C   2     2465   3962   2308    290   -175    684       C  
ATOM    632  N1    U C   2      11.880  16.941  15.748  1.00 19.50           N  
ANISOU  632  N1    U C   2     2059   2820   2530    240    -61    509       N  
ATOM    633  C2    U C   2      11.942  15.760  16.460  1.00 18.62           C  
ANISOU  633  C2    U C   2     2012   2505   2556   -270    -66    105       C  
ATOM    634  O2    U C   2      11.280  14.775  16.163  1.00 20.44           O  
ANISOU  634  O2    U C   2     2376   2779   2612   -264     -8   -124       O  
ATOM    635  N3    U C   2      12.815  15.764  17.519  1.00 17.76           N  
ANISOU  635  N3    U C   2     2085   1980   2684    135    143   -601       N  
ATOM    636  C4    U C   2      13.607  16.810  17.930  1.00 15.60           C  
ANISOU  636  C4    U C   2     1942   1765   2221   -262     -7   -103       C  
ATOM    637  O4    U C   2      14.332  16.649  18.903  1.00 17.90           O  
ANISOU  637  O4    U C   2     2242   1902   2658   -143   -436     76       O  
ATOM    638  C5    U C   2      13.481  18.002  17.143  1.00 17.51           C  
ANISOU  638  C5    U C   2     2142   2223   2286     51     65     83       C  
ATOM    639  C6    U C   2      12.640  18.031  16.103  1.00 17.60           C  
ANISOU  639  C6    U C   2     2159   2170   2357    -43     39   -133       C  
ATOM    640  P     U C   3       7.797  17.501  11.465  1.00 50.35           P  
ANISOU  640  P     U C   3     5709   8832   4591   1836  -1561    840       P  
ATOM    641  OP1   U C   3       6.374  17.220  11.802  1.00 54.78           O  
ANISOU  641  OP1   U C   3     6176   9195   5444   2252  -1462    783       O  
ATOM    642  OP2   U C   3       8.149  18.809  10.851  1.00 51.03           O  
ANISOU  642  OP2   U C   3     5984   9204   4200   2072  -1615    671       O  
TER     643        U C   3                                                      
HETATM  644  C1  MRD A 101       5.378   2.112  22.894  1.00 19.64           C  
ANISOU  644  C1  MRD A 101     1662   2540   3259   -364     36    -66       C  
HETATM  645  C2  MRD A 101       6.856   1.751  22.942  1.00 18.22           C  
ANISOU  645  C2  MRD A 101     2178   2045   2698   -167   -466     16       C  
HETATM  646  O2  MRD A 101       7.483   2.827  23.681  1.00 18.61           O  
ANISOU  646  O2  MRD A 101     2367   1439   3264   -276   -707   -257       O  
HETATM  647  CM  MRD A 101       7.093   0.438  23.681  1.00 18.38           C  
ANISOU  647  CM  MRD A 101     2311   1909   2763   -198   -257    515       C  
HETATM  648  C3  MRD A 101       7.419   1.673  21.527  1.00 19.72           C  
ANISOU  648  C3  MRD A 101     2453   2064   2976     96   -519   -383       C  
HETATM  649  C4  MRD A 101       8.926   1.433  21.501  1.00 19.10           C  
ANISOU  649  C4  MRD A 101     2441   2061   2756    118   -383   -444       C  
HETATM  650  O4  MRD A 101       9.561   2.557  22.068  1.00 18.72           O  
ANISOU  650  O4  MRD A 101     2146   1929   3039   -373   -476     36       O  
HETATM  651  C5  MRD A 101       9.432   1.247  20.073  1.00 19.35           C  
ANISOU  651  C5  MRD A 101     2827   1635   2890    580   -487     98       C  
HETATM  652  C1  PEG A 102       0.715  12.308  37.721  1.00 68.70           C  
HETATM  653  O1  PEG A 102       1.642  11.279  37.482  1.00 30.42           O  
HETATM  654  C2  PEG A 102       1.277  13.301  38.738  1.00 51.73           C  
HETATM  655  O2  PEG A 102       0.568  14.511  38.689  1.00 58.98           O  
HETATM  656  C3  PEG A 102       0.542  15.126  37.430  1.00 31.73           C  
HETATM  657  C4  PEG A 102       0.353  16.634  37.596  1.00 33.79           C  
HETATM  658  O4  PEG A 102       0.497  17.265  36.348  1.00 29.47           O  
HETATM  659  O   HOH A 201      -8.500  21.219   5.847  1.00 32.08           O  
HETATM  660  O   HOH A 202       0.479  15.144  16.150  1.00 41.95           O  
HETATM  661  O   HOH A 203      13.020  22.067  27.205  1.00 17.44           O  
ANISOU  661  O   HOH A 203     2397   1680   2548    233   -160   -169       O  
HETATM  662  O   HOH A 204      12.731  27.670  31.881  1.00 20.95           O  
ANISOU  662  O   HOH A 204     2841   1485   3633   -512    227   -675       O  
HETATM  663  O   HOH A 205      16.149  22.349  25.242  1.00 19.24           O  
ANISOU  663  O   HOH A 205     2729   1360   3223   -434   -644    337       O  
HETATM  664  O   HOH A 206      16.828  10.653  35.756  1.00 33.13           O  
HETATM  665  O   HOH A 207      18.280  14.019  33.207  1.00 24.81           O  
ANISOU  665  O   HOH A 207     2747   1953   4728   -353     22   -259       O  
HETATM  666  O   HOH A 208      12.202  26.438  36.787  1.00 32.49           O  
ANISOU  666  O   HOH A 208     3989   3296   5060  -1288  -1006   -819       O  
HETATM  667  O   HOH A 209      18.039  20.720  21.095  1.00 21.32           O  
ANISOU  667  O   HOH A 209     2293   2545   3263   -614    -21    727       O  
HETATM  668  O   HOH A 210       5.933  32.280  31.308  1.00 30.56           O  
HETATM  669  O   HOH A 211      16.547  28.661  29.349  0.50 22.27           O  
ANISOU  669  O   HOH A 211     3091   2007   3364  -1213      0      0       O  
HETATM  670  O   HOH A 212       6.802   5.559  24.337  1.00 15.65           O  
ANISOU  670  O   HOH A 212     1388   1304   3252   -184     81   -315       O  
HETATM  671  O   HOH A 213      -4.023  20.254  17.518  1.00 22.91           O  
ANISOU  671  O   HOH A 213     3394   2756   2556   -215   -335    463       O  
HETATM  672  O   HOH A 214       7.303  29.784  23.568  1.00 33.21           O  
ANISOU  672  O   HOH A 214     4063   4425   4132   -102   -920   -417       O  
HETATM  673  O   HOH A 215      23.093  10.448  33.099  1.00 35.75           O  
HETATM  674  O   HOH A 216      11.401   6.321  19.278  1.00 18.13           O  
ANISOU  674  O   HOH A 216     2209   1615   3065     31    -12    -52       O  
HETATM  675  O   HOH A 217      10.460  10.231  15.377  1.00 45.47           O  
ANISOU  675  O   HOH A 217     2563   9549   5163   -493   -608     13       O  
HETATM  676  O   HOH A 218       6.925  13.353  18.602  1.00 31.72           O  
ANISOU  676  O   HOH A 218     5803   3189   3061  -1948   -322    185       O  
HETATM  677  O   HOH A 219      18.870  22.322  25.610  1.00 24.44           O  
ANISOU  677  O   HOH A 219     1947   1708   5631   -363    -18   -402       O  
HETATM  678  O   HOH A 220      14.878  14.756  37.402  1.00 36.86           O  
ANISOU  678  O   HOH A 220     2368   6282   5354   -334   -636   2872       O  
HETATM  679  O   HOH A 221       9.854  12.559  42.267  1.00 38.65           O  
ANISOU  679  O   HOH A 221     6534   5108   3044    691  -2227   -355       O  
HETATM  680  O   HOH A 222      -9.509  25.103   9.150  1.00 33.37           O  
HETATM  681  O   HOH A 223      24.747  11.708  31.120  1.00 32.66           O  
ANISOU  681  O   HOH A 223     2517   4212   5678    -89    336  -1397       O  
HETATM  682  O   HOH A 224      19.571  21.534  30.677  1.00 34.59           O  
ANISOU  682  O   HOH A 224     2661   2268   8215    161  -1420    -21       O  
HETATM  683  O   HOH A 225      19.985  20.998  27.597  1.00 34.30           O  
ANISOU  683  O   HOH A 225     3156   5937   3939   1206    757    560       O  
HETATM  684  O   HOH A 226      17.513  22.044  33.660  1.00 30.17           O  
HETATM  685  O   HOH A 227      20.241  26.250  33.789  1.00 37.04           O  
ANISOU  685  O   HOH A 227     4587   4301   5185  -1545   -994   -357       O  
HETATM  686  O   HOH A 228      -2.113  15.988  14.131  1.00 40.11           O  
HETATM  687  O   HOH A 229      11.176   7.448  16.300  1.00 42.02           O  
ANISOU  687  O   HOH A 229     2174   7817   5974    537   -770   -308       O  
HETATM  688  O   HOH A 230      -8.681  18.281   6.213  1.00 34.84           O  
ANISOU  688  O   HOH A 230     3487   2721   7030    554    926    235       O  
HETATM  689  O   HOH A 231      -0.021  23.410  17.426  1.00 38.74           O  
ANISOU  689  O   HOH A 231     3934   4837   5947   1681  -2090    -19       O  
HETATM  690  O   HOH A 232      11.948  28.578  34.374  1.00 42.25           O  
ANISOU  690  O   HOH A 232     7301   4662   4090  -2828    620  -1284       O  
HETATM  691  O   HOH A 233       3.639   0.921  29.116  1.00 38.16           O  
ANISOU  691  O   HOH A 233     4661   2036   7801   -273   -684    362       O  
HETATM  692  O   HOH A 234      -0.570   4.602  31.396  1.00 38.98           O  
ANISOU  692  O   HOH A 234     2511   4526   7774    375   -209   2543       O  
HETATM  693  O   HOH C 101      17.459  24.867  18.907  1.00 37.93           O  
ANISOU  693  O   HOH C 101     4517   3635   6261   -478   1223   -928       O  
HETATM  694  O   HOH C 102       9.120  12.971  16.549  1.00 25.69           O  
ANISOU  694  O   HOH C 102     3855   2129   3778    112   -610    600       O  
CONECT  644  645                                                                
CONECT  645  644  646  647  648                                                 
CONECT  646  645                                                                
CONECT  647  645                                                                
CONECT  648  645  649                                                           
CONECT  649  648  650  651                                                      
CONECT  650  649                                                                
CONECT  651  649                                                                
CONECT  652  653  654                                                           
CONECT  653  652                                                                
CONECT  654  652  655                                                           
CONECT  655  654  656                                                           
CONECT  656  655  657                                                           
CONECT  657  656  658                                                           
CONECT  658  657                                                                
MASTER      296    0    2    1    5    0    4    6  684    2   15    8          
END

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Related entries of code: 5sze

Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code	Check Database	Protein Sequence Similarity
No similar entries are found!
Complexes with the same small molecule ligand
PDB Code	Check Database	Ligand Name
No complexes with the same small molecule ligand are found!

Entry Information

PDB ID	5sze
Complex Type	Protein-Nucleic Acid
PDBbind Subset	general set
Protein Name	Aquifex aeolicus RNA-binding protein Hfq
Ligand Name	6-mer U6 RNA
EC.Number	E.C.-.-.-.-
Resolution	1.5(Å)
Affinity (Kd/Ki/IC50)	Kd=21.3nM
Release Year	2017
Protein/NA Sequence	Check fasta file
Primary Reference	(2017) Acta Crystallogr D Struct Biol Vol. 73: pp. 294-315

Links to External Databases

RCSB PDB	The mother database
PDBsum	Enhanced annotations on PDB entries
Pubchem	Comprehensive collection of chemical and biological data
UniProtKB AC	UniProt accession number (AC): O66512
Entrez Gene ID	No matched NCBI Entrez Gene ID found!
ASD	Information of known allosteric effects of PDB entries

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