path: root/plip/test/pdb/4qnb.pdb

HEADER    VIRAL PROTEIN/INHIBITOR                 17-JUN-14   4QNB              
TITLE     DISULFIDE STABILIZED HIV-1 CA HEXAMER IN COMPLEX WITH PHENYL-L-       
TITLE    2 PHENYLALANINAMIDE INHIBITOR                                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAPSID PROTEIN P24;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 (NEW YORK-5 
SOURCE   3 ISOLATE);                                                            
SOURCE   4 ORGANISM_COMMON: HIV-1;                                              
SOURCE   5 ORGANISM_TAXID: 11698;                                               
SOURCE   6 GENE: GAG-POL;                                                       
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET11A                                    
KEYWDS    CAPSID PROTEIN, DISULFIDE CROSSLINK, VIRAL PROTEIN, VIRAL PROTEIN-    
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    O.PORNILLOS                                                           
REVDAT   1   31-DEC-14 4QNB    0                                                
JRNL        AUTH   A.BHATTACHARYA,S.L.ALAM,T.FRICKE,K.ZADROZNY,J.SEDZICKI,      
JRNL        AUTH 2 A.B.TAYLOR,B.DEMELER,O.PORNILLOS,B.K.GANSER-PORNILLOS,       
JRNL        AUTH 3 F.DIAZ-GRIFFERO,D.N.IVANOV,M.YEAGER                          
JRNL        TITL   STRUCTURAL BASIS OF HIV-1 CAPSID RECOGNITION BY PF74 AND     
JRNL        TITL 2 CPSF6.                                                       
JRNL        REF    PROC.NATL.ACAD.SCI.USA                     2014              
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   25518861                                                     
JRNL        DOI    10.1073/PNAS.1419945112                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1692)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.64                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 18417                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.870                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 897                             
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 26.6444 -  3.6252    1.00     2983   154  0.2212 0.2564        
REMARK   3     2  3.6252 -  2.8785    1.00     2922   152  0.2313 0.2818        
REMARK   3     3  2.8785 -  2.5150    1.00     2933   130  0.2210 0.2823        
REMARK   3     4  2.5150 -  2.2851    1.00     2885   160  0.2140 0.2942        
REMARK   3     5  2.2851 -  2.1214    1.00     2922   140  0.2019 0.2633        
REMARK   3     6  2.1214 -  1.9964    1.00     2875   161  0.2074 0.2649        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.530           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.00                          
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      :  0.008           1734                                  
REMARK   3   ANGLE     :  0.997           2356                                  
REMARK   3   CHIRALITY :  0.040            262                                  
REMARK   3   PLANARITY :  0.005            306                                  
REMARK   3   DIHEDRAL  : 14.198            647                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: all                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  24.8716  10.3507  -0.7647              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1573 T22:   0.1716                                     
REMARK   3      T33:   0.1686 T12:  -0.0086                                     
REMARK   3      T13:   0.0037 T23:  -0.0232                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7925 L22:   1.0844                                     
REMARK   3      L33:   1.4389 L12:  -0.3571                                     
REMARK   3      L13:   0.5725 L23:  -0.6160                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0229 S12:   0.1284 S13:   0.0101                       
REMARK   3      S21:  -0.0656 S22:  -0.0921 S23:  -0.0280                       
REMARK   3      S31:  -0.0118 S32:   0.1688 S33:   0.0598                       
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 4QNB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUL-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB086270.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-JAN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18424                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.996                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 11.100                             
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 43.9000                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: 3H47                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.08                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG 8,000, 2% TACSIMATE, 100 MM      
REMARK 280  TRIS, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K               
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                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14990 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 61050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -98.0 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 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     LYS A   182                                                      
REMARK 465     ASN A   183                                                      
REMARK 465     ALA A   184                                                      
REMARK 465     ALA A   185                                                      
REMARK 465     GLY A   220                                                      
REMARK 465     VAL A   221                                                      
REMARK 465     GLY A   222                                                      
REMARK 465     GLY A   223                                                      
REMARK 465     PRO A   224                                                      
REMARK 465     GLY A   225                                                      
REMARK 465     HIS A   226                                                      
REMARK 465     LYS A   227                                                      
REMARK 465     ALA A   228                                                      
REMARK 465     ARG A   229                                                      
REMARK 465     VAL A   230                                                      
REMARK 465     LEU A   231                                                      
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     GLN A   4    CG   CD   OE1  NE2                                  
REMARK 470     LEU A   6    CG   CD1  CD2                                       
REMARK 470     GLN A   7    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH1  ARG A   100     O    HOH A   450              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A   5     -157.95    -97.04                                   
REMARK 500    ALA A  31     -132.83     55.82                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 1B0 A 301                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3H47   RELATED DB: PDB                                   
DBREF  4QNB A    1   231  UNP    P12497   POL_HV1N5      133    363             
SEQADV 4QNB CYS A   14  UNP  P12497    ALA   146 ENGINEERED MUTATION            
SEQADV 4QNB CYS A   45  UNP  P12497    GLU   177 ENGINEERED MUTATION            
SEQADV 4QNB ALA A  184  UNP  P12497    TRP   316 ENGINEERED MUTATION            
SEQADV 4QNB ALA A  185  UNP  P12497    MET   317 ENGINEERED MUTATION            
SEQRES   1 A  231  PRO ILE VAL GLN ASN LEU GLN GLY GLN MET VAL HIS GLN          
SEQRES   2 A  231  CYS ILE SER PRO ARG THR LEU ASN ALA TRP VAL LYS VAL          
SEQRES   3 A  231  VAL GLU GLU LYS ALA PHE SER PRO GLU VAL ILE PRO MET          
SEQRES   4 A  231  PHE SER ALA LEU SER CYS GLY ALA THR PRO GLN ASP LEU          
SEQRES   5 A  231  ASN THR MET LEU ASN THR VAL GLY GLY HIS GLN ALA ALA          
SEQRES   6 A  231  MET GLN MET LEU LYS GLU THR ILE ASN GLU GLU ALA ALA          
SEQRES   7 A  231  GLU TRP ASP ARG LEU HIS PRO VAL HIS ALA GLY PRO ILE          
SEQRES   8 A  231  ALA PRO GLY GLN MET ARG GLU PRO ARG GLY SER ASP ILE          
SEQRES   9 A  231  ALA GLY THR THR SER THR LEU GLN GLU GLN ILE GLY TRP          
SEQRES  10 A  231  MET THR HIS ASN PRO PRO ILE PRO VAL GLY GLU ILE TYR          
SEQRES  11 A  231  LYS ARG TRP ILE ILE LEU GLY LEU ASN LYS ILE VAL ARG          
SEQRES  12 A  231  MET TYR SER PRO THR SER ILE LEU ASP ILE ARG GLN GLY          
SEQRES  13 A  231  PRO LYS GLU PRO PHE ARG ASP TYR VAL ASP ARG PHE TYR          
SEQRES  14 A  231  LYS THR LEU ARG ALA GLU GLN ALA SER GLN GLU VAL LYS          
SEQRES  15 A  231  ASN ALA ALA THR GLU THR LEU LEU VAL GLN ASN ALA ASN          
SEQRES  16 A  231  PRO ASP CYS LYS THR ILE LEU LYS ALA LEU GLY PRO GLY          
SEQRES  17 A  231  ALA THR LEU GLU GLU MET MET THR ALA CYS GLN GLY VAL          
SEQRES  18 A  231  GLY GLY PRO GLY HIS LYS ALA ARG VAL LEU                      
HET    1B0  A 301      59                                                       
HETNAM     1B0 N-METHYL-NALPHA-[(2-METHYL-1H-INDOL-3-YL)ACETYL]-N-              
HETNAM   2 1B0  PHENYL-L-PHENYLALANINAMIDE                                      
FORMUL   2  1B0    C27 H27 N3 O2                                                
FORMUL   3  HOH   *100(H2 O)                                                    
HELIX    1   1 SER A   16  ALA A   31  1                                  16    
HELIX    2   2 GLU A   35  SER A   44  1                                  10    
HELIX    3   3 THR A   48  THR A   58  1                                  11    
HELIX    4   4 HIS A   62  HIS A   84  1                                  23    
HELIX    5   5 ARG A  100  ALA A  105  1                                   6    
HELIX    6   6 THR A  110  HIS A  120  1                                  11    
HELIX    7   7 PRO A  125  SER A  146  1                                  22    
HELIX    8   8 SER A  149  ILE A  153  5                                   5    
HELIX    9   9 PRO A  160  GLN A  176  1                                  17    
HELIX   10  10 GLU A  187  ASN A  193  1                                   7    
HELIX   11  11 ASN A  195  ALA A  204  1                                  10    
HELIX   12  12 THR A  210  CYS A  218  1                                   9    
SHEET    1   A 2 ILE A   2  GLN A   4  0                                        
SHEET    2   A 2 MET A  10  HIS A  12 -1  O  VAL A  11   N  VAL A   3           
SSBOND   1 CYS A   14    CYS A   45                          1555   6555  2.06  
CISPEP   1 GLN A    7    GLY A    8          0        -3.47                     
CISPEP   2 ASN A  121    PRO A  122          0        -1.06                     
SITE     1 AC1 11 ASN A  53  LEU A  56  ASN A  57  GLN A  63                    
SITE     2 AC1 11 MET A  66  LYS A  70  THR A 107  TYR A 130                    
SITE     3 AC1 11 ARG A 173  SER A 178  GLU A 180                               
CRYST1   91.383   91.383   56.587  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      0.010943  0.006318  0.000000        0.00000                         
SCALE2      0.000000  0.012636  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017672        0.00000                         
ATOM      1  N   PRO A   1       9.981  12.464 -12.296  1.00 29.41           N  
ANISOU    1  N   PRO A   1     3777   3613   3786     32   -584   -351       N  
ATOM      2  CA  PRO A   1      11.174  11.956 -12.979  1.00 28.03           C  
ANISOU    2  CA  PRO A   1     3679   3445   3525     51   -568   -381       C  
ATOM      3  C   PRO A   1      10.958  11.828 -14.477  1.00 28.46           C  
ANISOU    3  C   PRO A   1     3802   3502   3509     76   -641   -398       C  
ATOM      4  O   PRO A   1       9.854  12.075 -14.963  1.00 29.85           O  
ANISOU    4  O   PRO A   1     3963   3669   3711     70   -714   -386       O  
ATOM      5  CB  PRO A   1      11.397  10.578 -12.327  1.00 30.38           C  
ANISOU    5  CB  PRO A   1     3973   3718   3851     29   -569   -414       C  
ATOM      6  CG  PRO A   1      10.239  10.377 -11.355  1.00 31.90           C  
ANISOU    6  CG  PRO A   1     4082   3894   4146    -11   -590   -392       C  
ATOM      7  CD  PRO A   1       9.716  11.732 -11.045  1.00 28.75           C  
ANISOU    7  CD  PRO A   1     3632   3516   3775      1   -561   -351       C  
ATOM      8  N   ILE A   2      12.012  11.461 -15.192  1.00 26.97           N  
ANISOU    8  N   ILE A   2     3688   3332   3229    111   -619   -422       N  
ATOM      9  CA  ILE A   2      11.908  11.127 -16.612  1.00 28.30           C  
ANISOU    9  CA  ILE A   2     3939   3503   3311    147   -688   -448       C  
ATOM     10  C   ILE A   2      11.986   9.616 -16.754  1.00 30.65           C  
ANISOU   10  C   ILE A   2     4290   3763   3591    154   -738   -508       C  
ATOM     11  O   ILE A   2      12.921   8.993 -16.253  1.00 31.92           O  
ANISOU   11  O   ILE A   2     4463   3927   3738    169   -681   -528       O  
ATOM     12  CB  ILE A   2      13.031  11.797 -17.451  1.00 32.25           C  
ANISOU   12  CB  ILE A   2     4494   4058   3700    196   -627   -427       C  
ATOM     13  CG1 ILE A   2      13.160  13.269 -17.085  1.00 32.10           C  
ANISOU   13  CG1 ILE A   2     4424   4062   3708    178   -571   -363       C  
ATOM     14  CG2 ILE A   2      12.779  11.634 -18.973  1.00 28.39           C  
ANISOU   14  CG2 ILE A   2     4097   3579   3112    242   -698   -448       C  
ATOM     15  CD1 ILE A   2      12.125  14.136 -17.728  1.00 35.70           C  
ANISOU   15  CD1 ILE A   2     4881   4510   4173    176   -635   -336       C  
ATOM     16  N   VAL A   3      10.984   9.037 -17.405  1.00 35.39           N  
ANISOU   16  N   VAL A   3     4924   4323   4198    142   -854   -534       N  
ATOM     17  CA  VAL A   3      10.951   7.608 -17.725  1.00 42.60           C  
ANISOU   17  CA  VAL A   3     5915   5183   5088    148   -933   -595       C  
ATOM     18  C   VAL A   3      10.570   7.429 -19.192  1.00 43.61           C  
ANISOU   18  C   VAL A   3     6146   5298   5125    185  -1035   -628       C  
ATOM     19  O   VAL A   3      10.121   8.369 -19.831  1.00 41.54           O  
ANISOU   19  O   VAL A   3     5875   5066   4841    191  -1054   -596       O  
ATOM     20  CB  VAL A   3       9.942   6.844 -16.856  1.00 45.25           C  
ANISOU   20  CB  VAL A   3     6186   5460   5546     71  -1002   -591       C  
ATOM     21  CG1 VAL A   3      10.278   7.007 -15.389  1.00 47.43           C  
ANISOU   21  CG1 VAL A   3     6367   5751   5902     40   -901   -558       C  
ATOM     22  CG2 VAL A   3       8.544   7.346 -17.135  1.00 46.40           C  
ANISOU   22  CG2 VAL A   3     6274   5600   5754     26  -1090   -554       C  
ATOM     23  N   GLN A   4      10.741   6.224 -19.724  1.00 48.04           N  
ANISOU   23  N   GLN A   4     6815   5810   5629    215  -1108   -693       N  
ATOM     24  CA  GLN A   4      10.354   5.948 -21.108  1.00 51.42           C  
ANISOU   24  CA  GLN A   4     7360   6216   5961    254  -1221   -734       C  
ATOM     25  C   GLN A   4       8.932   5.398 -21.174  1.00 52.82           C  
ANISOU   25  C   GLN A   4     7526   6319   6226    176  -1381   -740       C  
ATOM     26  O   GLN A   4       8.527   4.629 -20.310  1.00 52.70           O  
ANISOU   26  O   GLN A   4     7462   6248   6311    110  -1418   -739       O  
ATOM     27  CB  GLN A   4      11.332   4.963 -21.757  1.00 52.77           C  
ANISOU   27  CB  GLN A   4     7674   6370   6004    346  -1221   -808       C  
ATOM     28  N   ASN A   5       8.167   5.807 -22.182  1.00 56.10           N  
ANISOU   28  N   ASN A   5     7977   6735   6604    177  -1479   -735       N  
ATOM     29  CA  ASN A   5       6.830   5.245 -22.375  1.00 58.00           C  
ANISOU   29  CA  ASN A   5     8208   6906   6921    101  -1649   -736       C  
ATOM     30  C   ASN A   5       6.870   4.125 -23.415  1.00 61.76           C  
ANISOU   30  C   ASN A   5     8860   7308   7297    137  -1786   -819       C  
ATOM     31  O   ASN A   5       7.924   3.539 -23.655  1.00 62.75           O  
ANISOU   31  O   ASN A   5     9098   7425   7319    217  -1737   -879       O  
ATOM     32  CB  ASN A   5       5.812   6.333 -22.759  1.00 56.00           C  
ANISOU   32  CB  ASN A   5     7877   6693   6707     72  -1694   -674       C  
ATOM     33  CG  ASN A   5       6.123   7.020 -24.088  1.00 56.66           C  
ANISOU   33  CG  ASN A   5     8062   6818   6647    152  -1702   -688       C  
ATOM     34  OD1 ASN A   5       6.816   6.481 -24.952  1.00 58.92           O  
ANISOU   34  OD1 ASN A   5     8498   7092   6798    225  -1722   -752       O  
ATOM     35  ND2 ASN A   5       5.585   8.221 -24.257  1.00 54.48           N  
ANISOU   35  ND2 ASN A   5     7711   6593   6397    146  -1688   -626       N  
ATOM     36  N   LEU A   6       5.730   3.826 -24.026  1.00 65.26           N  
ANISOU   36  N   LEU A   6     9312   7703   7780     85  -1925   -804       N  
ATOM     37  CA  LEU A   6       5.644   2.687 -24.938  1.00 67.95           C  
ANISOU   37  CA  LEU A   6     9787   7965   8066    112  -2006   -847       C  
ATOM     38  C   LEU A   6       5.923   3.078 -26.385  1.00 69.77           C  
ANISOU   38  C   LEU A   6    10142   8225   8144    208  -2017   -877       C  
ATOM     39  O   LEU A   6       5.887   2.234 -27.278  1.00 71.49           O  
ANISOU   39  O   LEU A   6    10484   8381   8298    247  -2086   -916       O  
ATOM     40  CB  LEU A   6       4.267   2.026 -24.837  1.00 69.61           C  
ANISOU   40  CB  LEU A   6     9941   8100   8406      1  -2145   -805       C  
ATOM     41  N   GLN A   7       6.195   4.359 -26.611  1.00 70.28           N  
ANISOU   41  N   GLN A   7    10174   8381   8147    247  -1952   -852       N  
ATOM     42  CA  GLN A   7       6.509   4.856 -27.951  1.00 73.21           C  
ANISOU   42  CA  GLN A   7    10654   8795   8367    339  -1946   -867       C  
ATOM     43  C   GLN A   7       7.783   4.260 -28.584  1.00 74.73           C  
ANISOU   43  C   GLN A   7    10989   8998   8407    462  -1866   -927       C  
ATOM     44  O   GLN A   7       7.825   4.099 -29.807  1.00 76.59           O  
ANISOU   44  O   GLN A   7    11340   9229   8532    531  -1901   -951       O  
ATOM     45  CB  GLN A   7       6.620   6.385 -27.932  1.00 73.47           C  
ANISOU   45  CB  GLN A   7    10618   8928   8370    354  -1883   -815       C  
ATOM     46  N   GLY A   8       8.823   3.948 -27.801  1.00 73.18           N  
ANISOU   46  N   GLY A   8    10784   8821   8200    498  -1755   -948       N  
ATOM     47  CA  GLY A   8       8.899   4.188 -26.368  1.00 69.82           C  
ANISOU   47  CA  GLY A   8    10230   8406   7891    427  -1702   -924       C  
ATOM     48  C   GLY A   8       9.812   5.353 -26.041  1.00 65.65           C  
ANISOU   48  C   GLY A   8     9644   7989   7313    471  -1551   -886       C  
ATOM     49  O   GLY A   8      11.031   5.260 -26.172  1.00 64.83           O  
ANISOU   49  O   GLY A   8     9590   7936   7106    562  -1436   -904       O  
ATOM     50  N   GLN A   9       9.216   6.450 -25.591  1.00 62.76           N  
ANISOU   50  N   GLN A   9     9140   7661   7046    402  -1520   -807       N  
ATOM     51  CA  GLN A   9       9.912   7.728 -25.526  1.00 60.64           C  
ANISOU   51  CA  GLN A   9     8804   7489   6747    433  -1372   -740       C  
ATOM     52  C   GLN A   9      10.146   8.216 -24.097  1.00 54.33           C  
ANISOU   52  C   GLN A   9     7854   6710   6080    373  -1256   -686       C  
ATOM     53  O   GLN A   9       9.438   7.814 -23.174  1.00 52.17           O  
ANISOU   53  O   GLN A   9     7500   6385   5937    296  -1299   -682       O  
ATOM     54  CB  GLN A   9       9.122   8.771 -26.313  1.00 63.12           C  
ANISOU   54  CB  GLN A   9     9108   7831   7044    423  -1430   -692       C  
ATOM     55  CG  GLN A   9       9.708  10.165 -26.293  1.00 64.74           C  
ANISOU   55  CG  GLN A   9     9251   8121   7226    442  -1300   -615       C  
ATOM     56  CD  GLN A   9       9.177  11.013 -27.428  1.00 67.13           C  
ANISOU   56  CD  GLN A   9     9599   8451   7455    465  -1362   -581       C  
ATOM     57  OE1 GLN A   9       8.207  10.643 -28.095  1.00 66.58           O  
ANISOU   57  OE1 GLN A   9     9584   8337   7377    454  -1509   -610       O  
ATOM     58  NE2 GLN A   9       9.817  12.154 -27.663  1.00 68.33           N  
ANISOU   58  NE2 GLN A   9     9732   8675   7556    494  -1258   -514       N  
ATOM     59  N   MET A  10      11.148   9.076 -23.924  1.00 50.43           N  
ANISOU   59  N   MET A  10     7322   6292   5546    407  -1114   -640       N  
ATOM     60  CA  MET A  10      11.466   9.639 -22.614  1.00 46.75           C  
ANISOU   60  CA  MET A  10     6729   5845   5189    357  -1007   -590       C  
ATOM     61  C   MET A  10      10.507  10.771 -22.292  1.00 42.07           C  
ANISOU   61  C   MET A  10     6040   5253   4690    298  -1026   -527       C  
ATOM     62  O   MET A  10      10.463  11.786 -22.996  1.00 37.62           O  
ANISOU   62  O   MET A  10     5490   4729   4076    320  -1019   -485       O  
ATOM     63  CB  MET A  10      12.913  10.141 -22.557  1.00 49.16           C  
ANISOU   63  CB  MET A  10     7032   6227   5421    407   -862   -557       C  
ATOM     64  CG  MET A  10      13.965   9.057 -22.807  1.00 51.80           C  
ANISOU   64  CG  MET A  10     7448   6574   5659    483   -824   -612       C  
ATOM     65  SD  MET A  10      13.582   7.468 -22.029  1.00 66.35           S  
ANISOU   65  SD  MET A  10     9311   8319   7580    455   -900   -691       S  
ATOM     66  CE  MET A  10      13.787   7.841 -20.295  1.00 41.24           C  
ANISOU   66  CE  MET A  10     5979   5141   4548    375   -806   -641       C  
ATOM     67  N   VAL A  11       9.734  10.586 -21.226  1.00 38.38           N  
ANISOU   67  N   VAL A  11     5478   4746   4358    231  -1049   -519       N  
ATOM     68  CA  VAL A  11       8.739  11.577 -20.845  1.00 36.19           C  
ANISOU   68  CA  VAL A  11     5105   4471   4174    189  -1068   -463       C  
ATOM     69  C   VAL A  11       8.775  11.860 -19.352  1.00 32.09           C  
ANISOU   69  C   VAL A  11     4476   3952   3767    148   -985   -433       C  
ATOM     70  O   VAL A  11       9.238  11.037 -18.549  1.00 29.62           O  
ANISOU   70  O   VAL A  11     4148   3621   3485    131   -946   -459       O  
ATOM     71  CB  VAL A  11       7.319  11.133 -21.216  1.00 37.51           C  
ANISOU   71  CB  VAL A  11     5259   4596   4396    152  -1214   -471       C  
ATOM     72  CG1 VAL A  11       7.154  11.063 -22.738  1.00 40.97           C  
ANISOU   72  CG1 VAL A  11     5812   5035   4720    194  -1310   -495       C  
ATOM     73  CG2 VAL A  11       7.007   9.801 -20.557  1.00 37.18           C  
ANISOU   73  CG2 VAL A  11     5200   4501   4425    103  -1265   -508       C  
ATOM     74  N   HIS A  12       8.269  13.030 -18.992  1.00 30.84           N  
ANISOU   74  N   HIS A  12     4246   3808   3663    139   -961   -379       N  
ATOM     75  CA  HIS A  12       8.197  13.421 -17.599  1.00 29.93           C  
ANISOU   75  CA  HIS A  12     4035   3693   3644    112   -888   -351       C  
ATOM     76  C   HIS A  12       7.007  12.763 -16.930  1.00 29.83           C  
ANISOU   76  C   HIS A  12     3940   3655   3739     68   -949   -349       C  
ATOM     77  O   HIS A  12       5.930  12.666 -17.516  1.00 30.72           O  
ANISOU   77  O   HIS A  12     4036   3759   3877     56  -1050   -339       O  
ATOM     78  CB  HIS A  12       8.097  14.934 -17.468  1.00 30.91           C  
ANISOU   78  CB  HIS A  12     4130   3835   3780    130   -845   -299       C  
ATOM     79  CG  HIS A  12       7.959  15.398 -16.055  1.00 32.66           C  
ANISOU   79  CG  HIS A  12     4269   4052   4090    116   -777   -276       C  
ATOM     80  ND1 HIS A  12       6.733  15.617 -15.461  1.00 34.49           N  
ANISOU   80  ND1 HIS A  12     4415   4279   4412    110   -807   -252       N  
ATOM     81  CD2 HIS A  12       8.890  15.661 -15.108  1.00 31.23           C  
ANISOU   81  CD2 HIS A  12     4079   3872   3914    112   -683   -272       C  
ATOM     82  CE1 HIS A  12       6.918  16.014 -14.214  1.00 33.45           C  
ANISOU   82  CE1 HIS A  12     4235   4146   4329    111   -728   -239       C  
ATOM     83  NE2 HIS A  12       8.217  16.042 -13.973  1.00 31.50           N  
ANISOU   83  NE2 HIS A  12     4037   3898   4033    108   -659   -253       N  
ATOM     84  N   GLN A  13       7.222  12.308 -15.703  1.00 28.33           N  
ANISOU   84  N   GLN A  13     3696   3458   3612     41   -889   -351       N  
ATOM     85  CA  GLN A  13       6.183  11.703 -14.898  1.00 33.06           C  
ANISOU   85  CA  GLN A  13     4202   4044   4315     -4   -926   -333       C  
ATOM     86  C   GLN A  13       6.203  12.340 -13.512  1.00 32.25           C  
ANISOU   86  C   GLN A  13     4016   3962   4275     -1   -826   -299       C  
ATOM     87  O   GLN A  13       7.268  12.691 -13.014  1.00 28.73           O  
ANISOU   87  O   GLN A  13     3601   3521   3795     17   -737   -310       O  
ATOM     88  CB  GLN A  13       6.399  10.201 -14.810  1.00 38.31           C  
ANISOU   88  CB  GLN A  13     4900   4671   4985    -42   -969   -373       C  
ATOM     89  CG  GLN A  13       5.441   9.478 -13.899  1.00 42.95           C  
ANISOU   89  CG  GLN A  13     5391   5246   5684   -102  -1003   -343       C  
ATOM     90  CD  GLN A  13       5.698   7.990 -13.908  1.00 46.10           C  
ANISOU   90  CD  GLN A  13     5842   5591   6083   -142  -1060   -382       C  
ATOM     91  OE1 GLN A  13       6.234   7.437 -12.950  1.00 45.99           O  
ANISOU   91  OE1 GLN A  13     5814   5566   6093   -157   -999   -387       O  
ATOM     92  NE2 GLN A  13       5.333   7.334 -15.005  1.00 48.51           N  
ANISOU   92  NE2 GLN A  13     6219   5857   6357   -156  -1185   -412       N  
ATOM     93  N   CYS A  14       5.031  12.523 -12.905  1.00 32.41           N  
ANISOU   93  N   CYS A  14     3934   3997   4383    -14   -843   -256       N  
ATOM     94  CA  CYS A  14       4.976  13.145 -11.584  1.00 30.46           C  
ANISOU   94  CA  CYS A  14     3616   3772   4183      5   -748   -226       C  
ATOM     95  C   CYS A  14       5.667  12.248 -10.561  1.00 26.84           C  
ANISOU   95  C   CYS A  14     3155   3303   3740    -27   -689   -245       C  
ATOM     96  O   CYS A  14       5.604  11.029 -10.671  1.00 24.91           O  
ANISOU   96  O   CYS A  14     2917   3037   3513    -73   -740   -260       O  
ATOM     97  CB  CYS A  14       3.526  13.416 -11.174  1.00 30.43           C  
ANISOU   97  CB  CYS A  14     3495   3800   4266      9   -774   -170       C  
ATOM     98  SG  CYS A  14       2.774  14.772 -12.145  1.00 44.80           S  
ANISOU   98  SG  CYS A  14     5315   5638   6071     68   -823   -142       S  
ATOM     99  N   ILE A  15       6.329  12.858  -9.584  1.00 23.92           N  
ANISOU   99  N   ILE A  15     2785   2942   3362     -1   -592   -243       N  
ATOM    100  CA  ILE A  15       6.918  12.111  -8.480  1.00 26.89           C  
ANISOU  100  CA  ILE A  15     3151   3312   3755    -26   -534   -253       C  
ATOM    101  C   ILE A  15       5.792  11.485  -7.668  1.00 28.07           C  
ANISOU  101  C   ILE A  15     3196   3479   3988    -55   -545   -211       C  
ATOM    102  O   ILE A  15       4.784  12.133  -7.433  1.00 26.57           O  
ANISOU  102  O   ILE A  15     2932   3322   3841    -30   -543   -169       O  
ATOM    103  CB  ILE A  15       7.789  13.015  -7.591  1.00 30.22           C  
ANISOU  103  CB  ILE A  15     3595   3738   4148      8   -439   -256       C  
ATOM    104  CG1 ILE A  15       8.394  12.205  -6.437  1.00 30.09           C  
ANISOU  104  CG1 ILE A  15     3568   3717   4146    -17   -385   -265       C  
ATOM    105  CG2 ILE A  15       6.969  14.213  -7.095  1.00 32.76           C  
ANISOU  105  CG2 ILE A  15     3869   4080   4498     56   -412   -222       C  
ATOM    106  CD1 ILE A  15       9.768  12.694  -5.996  1.00 33.30           C  
ANISOU  106  CD1 ILE A  15     4036   4116   4501     -3   -320   -286       C  
ATOM    107  N   SER A  16       5.929  10.223  -7.263  1.00 25.59           N  
ANISOU  107  N   SER A  16     2875   3147   3702   -107   -559   -216       N  
ATOM    108  CA  SER A  16       4.778   9.564  -6.637  1.00 25.56           C  
ANISOU  108  CA  SER A  16     2765   3164   3784   -148   -583   -160       C  
ATOM    109  C   SER A  16       4.773   9.746  -5.127  1.00 23.83           C  
ANISOU  109  C   SER A  16     2485   2978   3589   -131   -483   -127       C  
ATOM    110  O   SER A  16       5.828   9.900  -4.503  1.00 23.78           O  
ANISOU  110  O   SER A  16     2535   2961   3540   -111   -412   -158       O  
ATOM    111  CB  SER A  16       4.753   8.071  -6.957  1.00 28.17           C  
ANISOU  111  CB  SER A  16     3116   3448   4139   -221   -667   -169       C  
ATOM    112  OG  SER A  16       5.610   7.389  -6.070  1.00 30.37           O  
ANISOU  112  OG  SER A  16     3424   3707   4409   -236   -611   -185       O  
ATOM    113  N   PRO A  17       3.578   9.719  -4.535  1.00 25.55           N  
ANISOU  113  N   PRO A  17     2587   3245   3876   -137   -477    -58       N  
ATOM    114  CA  PRO A  17       3.434   9.801  -3.079  1.00 26.10           C  
ANISOU  114  CA  PRO A  17     2594   3357   3965   -115   -380    -18       C  
ATOM    115  C   PRO A  17       4.227   8.693  -2.418  1.00 26.97           C  
ANISOU  115  C   PRO A  17     2741   3435   4073   -167   -362    -32       C  
ATOM    116  O   PRO A  17       4.806   8.910  -1.350  1.00 26.04           O  
ANISOU  116  O   PRO A  17     2638   3328   3926   -137   -276    -38       O  
ATOM    117  CB  PRO A  17       1.924   9.637  -2.864  1.00 26.92           C  
ANISOU  117  CB  PRO A  17     2556   3524   4151   -130   -402     70       C  
ATOM    118  CG  PRO A  17       1.328  10.233  -4.117  1.00 29.83           C  
ANISOU  118  CG  PRO A  17     2919   3891   4523   -114   -481     66       C  
ATOM    119  CD  PRO A  17       2.277   9.792  -5.230  1.00 29.40           C  
ANISOU  119  CD  PRO A  17     2991   3760   4419   -152   -555     -9       C  
ATOM    120  N   ARG A  18       4.300   7.541  -3.086  1.00 27.42           N  
ANISOU  120  N   ARG A  18     2824   3442   4150   -240   -451    -43       N  
ATOM    121  CA  ARG A  18       5.060   6.408  -2.577  1.00 29.33           C  
ANISOU  121  CA  ARG A  18     3112   3641   4391   -286   -449    -59       C  
ATOM    122  C   ARG A  18       6.513   6.814  -2.373  1.00 26.38           C  
ANISOU  122  C   ARG A  18     2839   3246   3938   -239   -384   -126       C  
ATOM    123  O   ARG A  18       7.098   6.573  -1.321  1.00 27.51           O  
ANISOU  123  O   ARG A  18     2990   3393   4071   -235   -319   -123       O  
ATOM    124  CB  ARG A  18       4.982   5.212  -3.534  1.00 34.67           C  
ANISOU  124  CB  ARG A  18     3833   4251   5089   -356   -571    -76       C  
ATOM    125  CG  ARG A  18       3.586   4.650  -3.778  1.00 41.44           C  
ANISOU  125  CG  ARG A  18     4593   5118   6034   -426   -661     -4       C  
ATOM    126  CD  ARG A  18       2.882   4.321  -2.474  1.00 48.58           C  
ANISOU  126  CD  ARG A  18     5378   6075   7006   -459   -605     89       C  
ATOM    127  NE  ARG A  18       3.681   3.449  -1.614  1.00 53.53           N  
ANISOU  127  NE  ARG A  18     6050   6666   7624   -485   -569     82       N  
ATOM    128  CZ  ARG A  18       3.209   2.371  -0.989  1.00 57.95           C  
ANISOU  128  CZ  ARG A  18     6555   7213   8249   -565   -599    152       C  
ATOM    129  NH1 ARG A  18       1.938   2.016  -1.135  1.00 59.96           N  
ANISOU  129  NH1 ARG A  18     6700   7494   8590   -634   -668    239       N  
ATOM    130  NH2 ARG A  18       4.010   1.641  -0.222  1.00 58.33           N  
ANISOU  130  NH2 ARG A  18     6655   7225   8282   -580   -565    141       N  
ATOM    131  N   THR A  19       7.094   7.448  -3.386  1.00 23.69           N  
ANISOU  131  N   THR A  19     2572   2888   3541   -204   -404   -179       N  
ATOM    132  CA  THR A  19       8.484   7.880  -3.302  1.00 21.32           C  
ANISOU  132  CA  THR A  19     2355   2574   3170   -166   -349   -231       C  
ATOM    133  C   THR A  19       8.666   8.991  -2.263  1.00 24.94           C  
ANISOU  133  C   THR A  19     2794   3070   3612   -118   -257   -217       C  
ATOM    134  O   THR A  19       9.622   8.971  -1.480  1.00 22.46           O  
ANISOU  134  O   THR A  19     2515   2749   3268   -110   -203   -233       O  
ATOM    135  CB  THR A  19       8.988   8.359  -4.675  1.00 21.08           C  
ANISOU  135  CB  THR A  19     2398   2528   3082   -141   -389   -275       C  
ATOM    136  OG1 THR A  19       8.882   7.277  -5.609  1.00 20.85           O  
ANISOU  136  OG1 THR A  19     2408   2460   3055   -174   -478   -298       O  
ATOM    137  CG2 THR A  19      10.434   8.804  -4.598  1.00 21.56           C  
ANISOU  137  CG2 THR A  19     2530   2587   3076   -109   -332   -311       C  
ATOM    138  N   LEU A  20       7.751   9.955  -2.276  1.00 25.66           N  
ANISOU  138  N   LEU A  20     2836   3195   3720    -83   -247   -188       N  
ATOM    139  CA  LEU A  20       7.822  11.103  -1.378  1.00 25.87           C  
ANISOU  139  CA  LEU A  20     2860   3245   3724    -24   -172   -182       C  
ATOM    140  C   LEU A  20       7.796  10.618   0.059  1.00 25.73           C  
ANISOU  140  C   LEU A  20     2806   3249   3721    -27   -110   -155       C  
ATOM    141  O   LEU A  20       8.622  11.022   0.877  1.00 25.22           O  
ANISOU  141  O   LEU A  20     2789   3178   3615     -2    -56   -175       O  
ATOM    142  CB  LEU A  20       6.661  12.065  -1.648  1.00 28.25           C  
ANISOU  142  CB  LEU A  20     3108   3580   4046     24   -179   -151       C  
ATOM    143  CG  LEU A  20       6.761  12.872  -2.955  1.00 30.22           C  
ANISOU  143  CG  LEU A  20     3407   3808   4268     43   -230   -176       C  
ATOM    144  CD1 LEU A  20       5.414  13.453  -3.362  1.00 31.30           C  
ANISOU  144  CD1 LEU A  20     3473   3978   4442     78   -260   -137       C  
ATOM    145  CD2 LEU A  20       7.775  13.973  -2.805  1.00 30.44           C  
ANISOU  145  CD2 LEU A  20     3519   3810   4235     81   -192   -209       C  
ATOM    146  N   ASN A  21       6.861   9.717   0.352  1.00 24.36           N  
ANISOU  146  N   ASN A  21     2549   3101   3606    -64   -124   -104       N  
ATOM    147  CA  ASN A  21       6.729   9.219   1.711  1.00 26.38           C  
ANISOU  147  CA  ASN A  21     2763   3386   3875    -69    -63    -64       C  
ATOM    148  C   ASN A  21       7.933   8.383   2.136  1.00 24.36           C  
ANISOU  148  C   ASN A  21     2573   3089   3594   -106    -56    -95       C  
ATOM    149  O   ASN A  21       8.408   8.518   3.267  1.00 21.40           O  
ANISOU  149  O   ASN A  21     2215   2726   3189    -82      9    -93       O  
ATOM    150  CB  ASN A  21       5.449   8.411   1.857  1.00 32.16           C  
ANISOU  150  CB  ASN A  21     3380   4157   4681   -112    -86     14       C  
ATOM    151  CG  ASN A  21       5.184   8.028   3.287  1.00 37.66           C  
ANISOU  151  CG  ASN A  21     4023   4900   5387   -107    -11     71       C  
ATOM    152  OD1 ASN A  21       5.066   8.895   4.161  1.00 39.69           O  
ANISOU  152  OD1 ASN A  21     4272   5202   5606    -30     70     78       O  
ATOM    153  ND2 ASN A  21       5.099   6.729   3.547  1.00 36.99           N  
ANISOU  153  ND2 ASN A  21     3908   4801   5347   -186    -40    111       N  
ATOM    154  N   ALA A  22       8.447   7.545   1.227  1.00 24.69           N  
ANISOU  154  N   ALA A  22     2658   3081   3642   -155   -124   -126       N  
ATOM    155  CA  ALA A  22       9.633   6.728   1.521  1.00 27.10           C  
ANISOU  155  CA  ALA A  22     3028   3346   3921   -179   -122   -157       C  
ATOM    156  C   ALA A  22      10.801   7.579   1.985  1.00 27.20           C  
ANISOU  156  C   ALA A  22     3103   3359   3871   -134    -66   -196       C  
ATOM    157  O   ALA A  22      11.449   7.263   2.987  1.00 29.64           O  
ANISOU  157  O   ALA A  22     3430   3667   4163   -134    -25   -193       O  
ATOM    158  CB  ALA A  22      10.050   5.905   0.301  1.00 26.86           C  
ANISOU  158  CB  ALA A  22     3052   3265   3891   -212   -203   -196       C  
ATOM    159  N   TRP A  23      11.076   8.660   1.259  1.00 21.59           N  
ANISOU  159  N   TRP A  23     2428   2649   3126    -99    -70   -226       N  
ATOM    160  CA  TRP A  23      12.231   9.489   1.579  1.00 22.13           C  
ANISOU  160  CA  TRP A  23     2557   2711   3140    -71    -34   -256       C  
ATOM    161  C   TRP A  23      12.049  10.188   2.918  1.00 22.82           C  
ANISOU  161  C   TRP A  23     2637   2820   3214    -35     26   -239       C  
ATOM    162  O   TRP A  23      12.992  10.264   3.736  1.00 22.34           O  
ANISOU  162  O   TRP A  23     2618   2751   3121    -32     55   -251       O  
ATOM    163  CB  TRP A  23      12.475  10.518   0.470  1.00 20.32           C  
ANISOU  163  CB  TRP A  23     2365   2474   2882    -50    -58   -279       C  
ATOM    164  CG  TRP A  23      13.499  11.573   0.821  1.00 23.44           C  
ANISOU  164  CG  TRP A  23     2815   2862   3231    -29    -30   -295       C  
ATOM    165  CD1 TRP A  23      13.308  12.925   0.815  1.00 21.49           C  
ANISOU  165  CD1 TRP A  23     2591   2610   2966      5    -24   -294       C  
ATOM    166  CD2 TRP A  23      14.858  11.365   1.221  1.00 23.08           C  
ANISOU  166  CD2 TRP A  23     2808   2806   3154    -45    -15   -308       C  
ATOM    167  NE1 TRP A  23      14.456  13.563   1.180  1.00 22.96           N  
ANISOU  167  NE1 TRP A  23     2831   2778   3114      2    -13   -305       N  
ATOM    168  CE2 TRP A  23      15.427  12.634   1.430  1.00 23.33           C  
ANISOU  168  CE2 TRP A  23     2882   2829   3155    -30     -6   -311       C  
ATOM    169  CE3 TRP A  23      15.651  10.227   1.420  1.00 22.78           C  
ANISOU  169  CE3 TRP A  23     2774   2766   3116    -69    -13   -315       C  
ATOM    170  CZ2 TRP A  23      16.750  12.803   1.836  1.00 23.20           C  
ANISOU  170  CZ2 TRP A  23     2901   2805   3109    -48      1   -314       C  
ATOM    171  CZ3 TRP A  23      16.962  10.395   1.809  1.00 24.34           C  
ANISOU  171  CZ3 TRP A  23     3004   2963   3282    -75      1   -320       C  
ATOM    172  CH2 TRP A  23      17.502  11.675   2.013  1.00 24.07           C  
ANISOU  172  CH2 TRP A  23     3001   2924   3220    -69      7   -317       C  
ATOM    173  N   VAL A  24      10.850  10.718   3.128  1.00 24.29           N  
ANISOU  173  N   VAL A  24     2773   3036   3421     -2     43   -210       N  
ATOM    174  CA  VAL A  24      10.543  11.426   4.360  1.00 28.38           C  
ANISOU  174  CA  VAL A  24     3289   3578   3914     53    103   -196       C  
ATOM    175  C   VAL A  24      10.736  10.508   5.567  1.00 25.45           C  
ANISOU  175  C   VAL A  24     2905   3224   3543     35    142   -172       C  
ATOM    176  O   VAL A  24      11.319  10.915   6.571  1.00 24.12           O  
ANISOU  176  O   VAL A  24     2784   3052   3328     64    179   -185       O  
ATOM    177  CB  VAL A  24       9.110  11.988   4.335  1.00 33.78           C  
ANISOU  177  CB  VAL A  24     3907   4306   4624    103    119   -160       C  
ATOM    178  CG1 VAL A  24       8.573  12.214   5.755  1.00 35.81           C  
ANISOU  178  CG1 VAL A  24     4140   4608   4860    162    192   -129       C  
ATOM    179  CG2 VAL A  24       9.077  13.277   3.515  1.00 34.11           C  
ANISOU  179  CG2 VAL A  24     3991   4325   4644    146     93   -188       C  
ATOM    180  N   LYS A  25      10.267   9.268   5.458  1.00 25.97           N  
ANISOU  180  N   LYS A  25     2910   3298   3658    -17    124   -136       N  
ATOM    181  CA  LYS A  25      10.352   8.324   6.571  1.00 29.37           C  
ANISOU  181  CA  LYS A  25     3323   3743   4093    -40    157   -101       C  
ATOM    182  C   LYS A  25      11.779   7.824   6.824  1.00 30.34           C  
ANISOU  182  C   LYS A  25     3518   3824   4185    -66    146   -137       C  
ATOM    183  O   LYS A  25      12.183   7.668   7.974  1.00 32.68           O  
ANISOU  183  O   LYS A  25     3834   4130   4452    -55    186   -127       O  
ATOM    184  CB  LYS A  25       9.408   7.142   6.323  1.00 30.95           C  
ANISOU  184  CB  LYS A  25     3440   3956   4363    -98    127    -43       C  
ATOM    185  CG  LYS A  25       7.965   7.558   6.152  1.00 35.58           C  
ANISOU  185  CG  LYS A  25     3934   4597   4988    -77    137      9       C  
ATOM    186  CD  LYS A  25       7.341   7.875   7.499  1.00 41.32           C  
ANISOU  186  CD  LYS A  25     4613   5394   5694    -22    225     63       C  
ATOM    187  CE  LYS A  25       6.213   8.876   7.387  1.00 44.55           C  
ANISOU  187  CE  LYS A  25     4957   5861   6107     49    256     91       C  
ATOM    188  NZ  LYS A  25       5.705   9.214   8.743  1.00 46.95           N  
ANISOU  188  NZ  LYS A  25     5228   6238   6372    122    351    137       N  
ATOM    189  N   VAL A  26      12.533   7.570   5.755  1.00 27.42           N  
ANISOU  189  N   VAL A  26     3185   3414   3819    -94     94   -177       N  
ATOM    190  CA  VAL A  26      13.957   7.222   5.853  1.00 28.02           C  
ANISOU  190  CA  VAL A  26     3323   3460   3864   -107     85   -210       C  
ATOM    191  C   VAL A  26      14.752   8.248   6.680  1.00 27.88           C  
ANISOU  191  C   VAL A  26     3354   3448   3791    -71    120   -229       C  
ATOM    192  O   VAL A  26      15.492   7.913   7.621  1.00 26.52           O  
ANISOU  192  O   VAL A  26     3208   3272   3595    -75    137   -226       O  
ATOM    193  CB  VAL A  26      14.592   7.124   4.438  1.00 45.26           C  
ANISOU  193  CB  VAL A  26     5537   5617   6045   -119     35   -248       C  
ATOM    194  CG1 VAL A  26      16.083   7.418   4.485  1.00 45.73           C  
ANISOU  194  CG1 VAL A  26     5650   5667   6060   -110     40   -278       C  
ATOM    195  CG2 VAL A  26      14.304   5.772   3.810  1.00 46.06           C  
ANISOU  195  CG2 VAL A  26     5626   5691   6185   -156    -14   -244       C  
ATOM    196  N   VAL A  27      14.573   9.516   6.347  1.00 26.26           N  
ANISOU  196  N   VAL A  27     3168   3246   3566    -38    122   -246       N  
ATOM    197  CA  VAL A  27      15.244  10.579   7.105  1.00 27.18           C  
ANISOU  197  CA  VAL A  27     3343   3353   3631     -8    139   -264       C  
ATOM    198  C   VAL A  27      14.743  10.637   8.546  1.00 27.18           C  
ANISOU  198  C   VAL A  27     3345   3377   3607     28    187   -244       C  
ATOM    199  O   VAL A  27      15.538  10.787   9.476  1.00 28.94           O  
ANISOU  199  O   VAL A  27     3619   3590   3790     34    195   -254       O  
ATOM    200  CB  VAL A  27      15.048  11.938   6.415  1.00 28.76           C  
ANISOU  200  CB  VAL A  27     3570   3540   3817     20    122   -283       C  
ATOM    201  CG1 VAL A  27      15.630  13.068   7.274  1.00 30.02           C  
ANISOU  201  CG1 VAL A  27     3804   3677   3927     50    126   -301       C  
ATOM    202  CG2 VAL A  27      15.695  11.896   5.033  1.00 29.23           C  
ANISOU  202  CG2 VAL A  27     3635   3585   3888    -15     80   -297       C  
ATOM    203  N   GLU A  28      13.431  10.509   8.732  1.00 29.40           N  
ANISOU  203  N   GLU A  28     3567   3694   3910     55    219   -211       N  
ATOM    204  CA  GLU A  28      12.833  10.537  10.068  1.00 32.56           C  
ANISOU  204  CA  GLU A  28     3958   4132   4280    102    278   -181       C  
ATOM    205  C   GLU A  28      13.401   9.415  10.961  1.00 35.41           C  
ANISOU  205  C   GLU A  28     4322   4497   4635     66    291   -159       C  
ATOM    206  O   GLU A  28      13.726   9.633  12.134  1.00 34.49           O  
ANISOU  206  O   GLU A  28     4252   4389   4463     99    321   -159       O  
ATOM    207  CB  GLU A  28      11.304  10.422   9.978  1.00 32.41           C  
ANISOU  207  CB  GLU A  28     3850   4167   4298    129    311   -131       C  
ATOM    208  CG  GLU A  28      10.601  11.718   9.573  1.00 35.62           C  
ANISOU  208  CG  GLU A  28     4262   4582   4691    199    317   -147       C  
ATOM    209  CD  GLU A  28       9.076  11.625   9.615  1.00 41.07           C  
ANISOU  209  CD  GLU A  28     4848   5340   5415    237    357    -87       C  
ATOM    210  OE1 GLU A  28       8.537  10.522   9.867  1.00 40.68           O  
ANISOU  210  OE1 GLU A  28     4717   5331   5408    194    374    -27       O  
ATOM    211  OE2 GLU A  28       8.413  12.664   9.394  1.00 43.74           O  
ANISOU  211  OE2 GLU A  28     5185   5693   5741    310    369    -95       O  
ATOM    212  N   GLU A  29      13.526   8.222  10.395  1.00 32.37           N  
ANISOU  212  N   GLU A  29     3896   4099   4302      2    261   -141       N  
ATOM    213  CA  GLU A  29      13.998   7.073  11.154  1.00 35.81           C  
ANISOU  213  CA  GLU A  29     4334   4532   4740    -33    266   -114       C  
ATOM    214  C   GLU A  29      15.524   7.027  11.279  1.00 35.76           C  
ANISOU  214  C   GLU A  29     4397   4488   4702    -47    236   -154       C  
ATOM    215  O   GLU A  29      16.041   6.673  12.328  1.00 38.27           O  
ANISOU  215  O   GLU A  29     4744   4809   4989    -45    252   -142       O  
ATOM    216  CB  GLU A  29      13.469   5.781  10.520  0.60 35.92           C  
ANISOU  216  CB  GLU A  29     4288   4538   4825    -92    235    -76       C  
ATOM    217  CG  GLU A  29      11.955   5.653  10.626  0.60 37.55           C  
ANISOU  217  CG  GLU A  29     4407   4792   5069    -91    263    -13       C  
ATOM    218  CD  GLU A  29      11.373   4.551   9.752  0.60 39.63           C  
ANISOU  218  CD  GLU A  29     4615   5033   5410   -161    208     19       C  
ATOM    219  OE1 GLU A  29      12.148   3.809   9.120  0.60 39.43           O  
ANISOU  219  OE1 GLU A  29     4631   4951   5401   -201    151    -13       O  
ATOM    220  OE2 GLU A  29      10.128   4.434   9.697  0.60 41.28           O  
ANISOU  220  OE2 GLU A  29     4741   5282   5662   -173    217     79       O  
ATOM    221  N   LYS A  30      16.248   7.424  10.240  1.00 33.85           N  
ANISOU  221  N   LYS A  30     4179   4218   4466    -60    194   -196       N  
ATOM    222  CA  LYS A  30      17.679   7.119  10.172  1.00 32.95           C  
ANISOU  222  CA  LYS A  30     4104   4078   4337    -81    164   -218       C  
ATOM    223  C   LYS A  30      18.628   8.314  10.248  1.00 32.87           C  
ANISOU  223  C   LYS A  30     4148   4059   4285    -68    149   -249       C  
ATOM    224  O   LYS A  30      19.842   8.130  10.328  1.00 32.91           O  
ANISOU  224  O   LYS A  30     4174   4054   4277    -86    125   -256       O  
ATOM    225  CB  LYS A  30      17.975   6.351   8.881  1.00 32.38           C  
ANISOU  225  CB  LYS A  30     4013   3987   4305   -109    125   -230       C  
ATOM    226  CG  LYS A  30      17.311   4.977   8.797  1.00 33.03           C  
ANISOU  226  CG  LYS A  30     4060   4057   4432   -136    115   -202       C  
ATOM    227  CD  LYS A  30      17.804   4.028   9.868  1.00 34.27           C  
ANISOU  227  CD  LYS A  30     4231   4208   4584   -147    123   -176       C  
ATOM    228  CE  LYS A  30      17.386   2.571   9.564  1.00 35.80           C  
ANISOU  228  CE  LYS A  30     4406   4370   4828   -183     92   -151       C  
ATOM    229  NZ  LYS A  30      18.335   1.857   8.621  1.00 34.75           N  
ANISOU  229  NZ  LYS A  30     4304   4197   4701   -182     44   -187       N  
ATOM    230  N   ALA A  31      18.089   9.530  10.198  1.00 34.55           N  
ANISOU  230  N   ALA A  31     4380   4271   4477    -38    156   -262       N  
ATOM    231  CA  ALA A  31      18.927  10.730  10.228  1.00 35.76           C  
ANISOU  231  CA  ALA A  31     4592   4401   4595    -34    128   -287       C  
ATOM    232  C   ALA A  31      19.952  10.682   9.104  1.00 35.49           C  
ANISOU  232  C   ALA A  31     4547   4358   4580    -74     90   -293       C  
ATOM    233  O   ALA A  31      19.608  10.368   7.968  1.00 38.77           O  
ANISOU  233  O   ALA A  31     4925   4780   5025    -81     86   -294       O  
ATOM    234  CB  ALA A  31      19.619  10.873  11.576  1.00 36.77           C  
ANISOU  234  CB  ALA A  31     4774   4521   4675    -28    124   -288       C  
ATOM    235  N   PHE A  32      21.213  10.971   9.417  1.00 33.02           N  
ANISOU  235  N   PHE A  32     4264   4036   4246    -97     60   -293       N  
ATOM    236  CA  PHE A  32      22.265  10.893   8.398  1.00 31.32           C  
ANISOU  236  CA  PHE A  32     4025   3830   4045   -129     34   -286       C  
ATOM    237  C   PHE A  32      23.218   9.723   8.624  1.00 29.75           C  
ANISOU  237  C   PHE A  32     3800   3651   3854   -142     32   -272       C  
ATOM    238  O   PHE A  32      24.414   9.804   8.336  1.00 31.83           O  
ANISOU  238  O   PHE A  32     4051   3929   4114   -163     10   -256       O  
ATOM    239  CB  PHE A  32      23.015  12.219   8.331  1.00 33.86           C  
ANISOU  239  CB  PHE A  32     4386   4134   4347   -153     -6   -281       C  
ATOM    240  CG  PHE A  32      22.128  13.345   7.953  1.00 36.51           C  
ANISOU  240  CG  PHE A  32     4753   4443   4677   -134    -11   -295       C  
ATOM    241  CD1 PHE A  32      21.725  13.500   6.637  1.00 37.83           C  
ANISOU  241  CD1 PHE A  32     4892   4619   4864   -133     -8   -293       C  
ATOM    242  CD2 PHE A  32      21.618  14.201   8.918  1.00 37.32           C  
ANISOU  242  CD2 PHE A  32     4920   4511   4749   -106    -17   -313       C  
ATOM    243  CE1 PHE A  32      20.867  14.525   6.283  1.00 39.91           C  
ANISOU  243  CE1 PHE A  32     5183   4856   5123   -110    -15   -303       C  
ATOM    244  CE2 PHE A  32      20.755  15.226   8.568  1.00 36.82           C  
ANISOU  244  CE2 PHE A  32     4889   4420   4679    -74    -21   -327       C  
ATOM    245  CZ  PHE A  32      20.380  15.385   7.250  1.00 38.28           C  
ANISOU  245  CZ  PHE A  32     5039   4615   4892    -79    -21   -320       C  
ATOM    246  N   SER A  33      22.667   8.623   9.125  1.00 30.36           N  
ANISOU  246  N   SER A  33     3865   3729   3943   -128     56   -270       N  
ATOM    247  CA  SER A  33      23.362   7.349   9.081  1.00 31.52           C  
ANISOU  247  CA  SER A  33     3987   3885   4103   -130     53   -260       C  
ATOM    248  C   SER A  33      23.728   7.085   7.614  1.00 29.16           C  
ANISOU  248  C   SER A  33     3661   3599   3819   -125     45   -267       C  
ATOM    249  O   SER A  33      22.982   7.469   6.703  1.00 29.83           O  
ANISOU  249  O   SER A  33     3741   3681   3912   -121     48   -280       O  
ATOM    250  CB  SER A  33      22.483   6.234   9.657  1.00 35.63           C  
ANISOU  250  CB  SER A  33     4501   4394   4641   -122     73   -252       C  
ATOM    251  OG  SER A  33      23.253   5.070   9.901  1.00 40.67           O  
ANISOU  251  OG  SER A  33     5135   5031   5288   -121     63   -241       O  
ATOM    252  N   PRO A  34      24.887   6.463   7.371  1.00 27.32           N  
ANISOU  252  N   PRO A  34     3411   3386   3583   -118     37   -257       N  
ATOM    253  CA  PRO A  34      25.342   6.377   5.973  1.00 23.25           C  
ANISOU  253  CA  PRO A  34     2874   2894   3064   -100     36   -262       C  
ATOM    254  C   PRO A  34      24.379   5.652   5.018  1.00 21.45           C  
ANISOU  254  C   PRO A  34     2653   2646   2850    -78     37   -289       C  
ATOM    255  O   PRO A  34      24.336   6.023   3.843  1.00 22.22           O  
ANISOU  255  O   PRO A  34     2747   2760   2937    -67     36   -297       O  
ATOM    256  CB  PRO A  34      26.684   5.620   6.081  1.00 26.85           C  
ANISOU  256  CB  PRO A  34     3308   3381   3513    -79     34   -244       C  
ATOM    257  CG  PRO A  34      26.768   5.118   7.513  1.00 27.32           C  
ANISOU  257  CG  PRO A  34     3382   3419   3578    -89     27   -234       C  
ATOM    258  CD  PRO A  34      25.924   6.036   8.332  1.00 25.60           C  
ANISOU  258  CD  PRO A  34     3191   3179   3356   -120     27   -237       C  
ATOM    259  N   GLU A  35      23.597   4.683   5.494  1.00 23.56           N  
ANISOU  259  N   GLU A  35     2932   2878   3140    -78     33   -296       N  
ATOM    260  CA  GLU A  35      22.751   3.905   4.576  1.00 26.83           C  
ANISOU  260  CA  GLU A  35     3357   3266   3573    -66     16   -318       C  
ATOM    261  C   GLU A  35      21.574   4.744   4.056  1.00 27.70           C  
ANISOU  261  C   GLU A  35     3460   3372   3693    -84     13   -324       C  
ATOM    262  O   GLU A  35      20.813   4.299   3.203  1.00 27.83           O  
ANISOU  262  O   GLU A  35     3482   3368   3724    -81    -11   -340       O  
ATOM    263  CB  GLU A  35      22.252   2.605   5.232  1.00 25.65           C  
ANISOU  263  CB  GLU A  35     3219   3073   3453    -74      0   -313       C  
ATOM    264  CG  GLU A  35      21.178   2.767   6.298  1.00 28.98           C  
ANISOU  264  CG  GLU A  35     3628   3485   3900   -109     13   -287       C  
ATOM    265  CD  GLU A  35      21.755   2.968   7.691  1.00 29.05           C  
ANISOU  265  CD  GLU A  35     3637   3508   3891   -114     36   -263       C  
ATOM    266  OE1 GLU A  35      22.933   3.416   7.820  1.00 26.79           O  
ANISOU  266  OE1 GLU A  35     3356   3246   3577   -101     40   -265       O  
ATOM    267  OE2 GLU A  35      21.021   2.672   8.657  1.00 30.94           O  
ANISOU  267  OE2 GLU A  35     3872   3739   4143   -132     49   -236       O  
ATOM    268  N   VAL A  36      21.467   5.976   4.543  1.00 26.88           N  
ANISOU  268  N   VAL A  36     3349   3285   3580    -98     31   -312       N  
ATOM    269  CA  VAL A  36      20.476   6.916   4.055  1.00 28.03           C  
ANISOU  269  CA  VAL A  36     3489   3430   3730   -102     30   -316       C  
ATOM    270  C   VAL A  36      20.810   7.408   2.643  1.00 26.90           C  
ANISOU  270  C   VAL A  36     3351   3302   3566    -90     17   -328       C  
ATOM    271  O   VAL A  36      19.910   7.683   1.843  1.00 29.12           O  
ANISOU  271  O   VAL A  36     3630   3577   3856    -88      2   -336       O  
ATOM    272  CB  VAL A  36      20.350   8.120   5.029  1.00 32.58           C  
ANISOU  272  CB  VAL A  36     4074   4010   4294   -108     48   -304       C  
ATOM    273  CG1 VAL A  36      19.752   9.310   4.343  1.00 32.88           C  
ANISOU  273  CG1 VAL A  36     4117   4049   4327   -102     42   -309       C  
ATOM    274  CG2 VAL A  36      19.529   7.718   6.251  1.00 30.38           C  
ANISOU  274  CG2 VAL A  36     3789   3725   4030   -108     68   -291       C  
ATOM    275  N   ILE A  37      22.100   7.509   2.344  1.00 23.65           N  
ANISOU  275  N   ILE A  37     2941   2917   3127    -82     22   -321       N  
ATOM    276  CA  ILE A  37      22.575   8.062   1.078  1.00 21.13           C  
ANISOU  276  CA  ILE A  37     2622   2627   2780    -69     20   -318       C  
ATOM    277  C   ILE A  37      22.207   7.209  -0.139  1.00 22.14           C  
ANISOU  277  C   ILE A  37     2765   2751   2896    -37      4   -344       C  
ATOM    278  O   ILE A  37      21.664   7.727  -1.120  1.00 22.90           O  
ANISOU  278  O   ILE A  37     2870   2850   2980    -32     -9   -350       O  
ATOM    279  CB  ILE A  37      24.117   8.266   1.062  1.00 37.70           C  
ANISOU  279  CB  ILE A  37     4703   4769   4851    -67     35   -289       C  
ATOM    280  CG1 ILE A  37      24.561   9.314   2.088  1.00 38.27           C  
ANISOU  280  CG1 ILE A  37     4771   4840   4930   -108     32   -261       C  
ATOM    281  CG2 ILE A  37      24.588   8.661  -0.338  1.00 35.11           C  
ANISOU  281  CG2 ILE A  37     4369   4484   4487    -47     41   -276       C  
ATOM    282  CD1 ILE A  37      23.581  10.448   2.301  1.00 41.12           C  
ANISOU  282  CD1 ILE A  37     5157   5167   5300   -129     20   -265       C  
ATOM    283  N   PRO A  38      22.518   5.903  -0.099  1.00 22.97           N  
ANISOU  283  N   PRO A  38     2881   2843   3001    -11     -3   -362       N  
ATOM    284  CA  PRO A  38      22.070   4.997  -1.171  1.00 22.45           C  
ANISOU  284  CA  PRO A  38     2850   2756   2923     22    -34   -396       C  
ATOM    285  C   PRO A  38      20.548   4.916  -1.284  1.00 22.09           C  
ANISOU  285  C   PRO A  38     2811   2667   2916     -8    -72   -408       C  
ATOM    286  O   PRO A  38      20.024   4.647  -2.360  1.00 19.84           O  
ANISOU  286  O   PRO A  38     2554   2367   2618      7   -109   -432       O  
ATOM    287  CB  PRO A  38      22.652   3.631  -0.752  1.00 21.03           C  
ANISOU  287  CB  PRO A  38     2690   2554   2746     51    -41   -410       C  
ATOM    288  CG  PRO A  38      22.898   3.768   0.727  1.00 21.35           C  
ANISOU  288  CG  PRO A  38     2701   2594   2818     16    -19   -381       C  
ATOM    289  CD  PRO A  38      23.333   5.200   0.905  1.00 22.15           C  
ANISOU  289  CD  PRO A  38     2770   2740   2905     -6     10   -352       C  
ATOM    290  N   MET A  39      19.836   5.106  -0.181  1.00 21.93           N  
ANISOU  290  N   MET A  39     2763   2630   2940    -48    -66   -389       N  
ATOM    291  CA  MET A  39      18.385   5.152  -0.281  1.00 23.66           C  
ANISOU  291  CA  MET A  39     2967   2825   3198    -75    -95   -385       C  
ATOM    292  C   MET A  39      17.987   6.416  -1.062  1.00 20.14           C  
ANISOU  292  C   MET A  39     2514   2403   2736    -70    -94   -383       C  
ATOM    293  O   MET A  39      17.124   6.349  -1.950  1.00 20.03           O  
ANISOU  293  O   MET A  39     2505   2376   2729    -71   -135   -393       O  
ATOM    294  CB  MET A  39      17.719   5.117   1.105  1.00 26.53           C  
ANISOU  294  CB  MET A  39     3295   3181   3605   -107    -75   -355       C  
ATOM    295  CG  MET A  39      16.194   4.995   1.065  1.00 29.55           C  
ANISOU  295  CG  MET A  39     3643   3550   4035   -134   -102   -337       C  
ATOM    296  SD  MET A  39      15.628   3.421   0.337  1.00 32.46           S  
ANISOU  296  SD  MET A  39     4033   3863   4436   -158   -180   -348       S  
ATOM    297  CE  MET A  39      15.767   2.295   1.716  1.00 29.51           C  
ANISOU  297  CE  MET A  39     3651   3463   4097   -187   -169   -317       C  
ATOM    298  N   PHE A  40      18.621   7.552  -0.751  1.00 21.36           N  
ANISOU  298  N   PHE A  40     2663   2586   2868    -67    -58   -367       N  
ATOM    299  CA  PHE A  40      18.332   8.798  -1.476  1.00 20.49           C  
ANISOU  299  CA  PHE A  40     2555   2491   2741    -63    -62   -360       C  
ATOM    300  C   PHE A  40      18.569   8.612  -2.963  1.00 20.40           C  
ANISOU  300  C   PHE A  40     2570   2491   2690    -39    -86   -376       C  
ATOM    301  O   PHE A  40      17.715   8.944  -3.790  1.00 21.27           O  
ANISOU  301  O   PHE A  40     2686   2595   2801    -36   -117   -380       O  
ATOM    302  CB  PHE A  40      19.183   9.976  -0.971  1.00 22.07           C  
ANISOU  302  CB  PHE A  40     2757   2707   2920    -70    -32   -338       C  
ATOM    303  CG  PHE A  40      18.954  11.258  -1.740  1.00 25.29           C  
ANISOU  303  CG  PHE A  40     3177   3121   3312    -68    -43   -325       C  
ATOM    304  CD1 PHE A  40      17.797  11.997  -1.541  1.00 24.94           C  
ANISOU  304  CD1 PHE A  40     3129   3058   3291    -65    -53   -323       C  
ATOM    305  CD2 PHE A  40      19.883  11.711  -2.671  1.00 26.82           C  
ANISOU  305  CD2 PHE A  40     3383   3342   3464    -66    -41   -308       C  
ATOM    306  CE1 PHE A  40      17.569  13.167  -2.253  1.00 26.44           C  
ANISOU  306  CE1 PHE A  40     3336   3245   3466    -59    -69   -310       C  
ATOM    307  CE2 PHE A  40      19.664  12.891  -3.382  1.00 26.55           C  
ANISOU  307  CE2 PHE A  40     3364   3309   3415    -69    -54   -288       C  
ATOM    308  CZ  PHE A  40      18.510  13.619  -3.160  1.00 27.30           C  
ANISOU  308  CZ  PHE A  40     3464   3373   3536    -66    -72   -292       C  
ATOM    309  N   SER A  41      19.728   8.061  -3.295  1.00 22.18           N  
ANISOU  309  N   SER A  41     2812   2737   2878    -16    -71   -382       N  
ATOM    310  CA  SER A  41      20.090   7.843  -4.694  1.00 24.62           C  
ANISOU  310  CA  SER A  41     3153   3068   3132     23    -84   -397       C  
ATOM    311  C   SER A  41      19.094   6.962  -5.435  1.00 24.43           C  
ANISOU  311  C   SER A  41     3163   3005   3113     35   -142   -434       C  
ATOM    312  O   SER A  41      18.748   7.250  -6.579  1.00 23.16           O  
ANISOU  312  O   SER A  41     3030   2853   2918     53   -169   -443       O  
ATOM    313  CB  SER A  41      21.485   7.228  -4.797  1.00 21.32           C  
ANISOU  313  CB  SER A  41     2742   2685   2672     62    -52   -396       C  
ATOM    314  OG  SER A  41      21.877   7.201  -6.154  1.00 25.77           O  
ANISOU  314  OG  SER A  41     3337   3285   3170    111    -52   -403       O  
ATOM    315  N   ALA A  42      18.630   5.889  -4.795  1.00 24.68           N  
ANISOU  315  N   ALA A  42     3197   2993   3189     19   -168   -450       N  
ATOM    316  CA  ALA A  42      17.689   4.984  -5.445  1.00 23.64           C  
ANISOU  316  CA  ALA A  42     3100   2813   3069     17   -240   -480       C  
ATOM    317  C   ALA A  42      16.292   5.610  -5.542  1.00 21.61           C  
ANISOU  317  C   ALA A  42     2808   2545   2857    -23   -275   -462       C  
ATOM    318  O   ALA A  42      15.635   5.514  -6.562  1.00 21.27           O  
ANISOU  318  O   ALA A  42     2792   2487   2801    -19   -333   -479       O  
ATOM    319  CB  ALA A  42      17.631   3.640  -4.705  1.00 24.28           C  
ANISOU  319  CB  ALA A  42     3194   2844   3189      3   -265   -491       C  
ATOM    320  N   LEU A  43      15.835   6.266  -4.490  1.00 23.95           N  
ANISOU  320  N   LEU A  43     3046   2853   3202    -55   -241   -428       N  
ATOM    321  CA  LEU A  43      14.525   6.923  -4.561  1.00 23.43           C  
ANISOU  321  CA  LEU A  43     2938   2788   3176    -78   -266   -405       C  
ATOM    322  C   LEU A  43      14.477   8.051  -5.600  1.00 25.55           C  
ANISOU  322  C   LEU A  43     3222   3081   3404    -54   -272   -405       C  
ATOM    323  O   LEU A  43      13.404   8.382  -6.112  1.00 26.27           O  
ANISOU  323  O   LEU A  43     3295   3168   3516    -61   -315   -396       O  
ATOM    324  CB  LEU A  43      14.135   7.459  -3.186  1.00 21.36           C  
ANISOU  324  CB  LEU A  43     2617   2539   2958    -96   -217   -370       C  
ATOM    325  CG  LEU A  43      13.888   6.326  -2.187  1.00 22.05           C  
ANISOU  325  CG  LEU A  43     2681   2605   3091   -127   -218   -357       C  
ATOM    326  CD1 LEU A  43      13.651   6.895  -0.780  1.00 22.55           C  
ANISOU  326  CD1 LEU A  43     2698   2693   3179   -131   -158   -322       C  
ATOM    327  CD2 LEU A  43      12.691   5.502  -2.651  1.00 23.23           C  
ANISOU  327  CD2 LEU A  43     2810   2727   3290   -162   -292   -346       C  
ATOM    328  N   SER A  44      15.636   8.623  -5.921  1.00 24.34           N  
ANISOU  328  N   SER A  44     3099   2955   3194    -27   -232   -407       N  
ATOM    329  CA  SER A  44      15.703   9.735  -6.882  1.00 25.49           C  
ANISOU  329  CA  SER A  44     3263   3126   3298     -9   -234   -396       C  
ATOM    330  C   SER A  44      16.151   9.290  -8.289  1.00 25.57           C  
ANISOU  330  C   SER A  44     3329   3147   3237     26   -262   -420       C  
ATOM    331  O   SER A  44      16.633  10.089  -9.090  1.00 24.51           O  
ANISOU  331  O   SER A  44     3217   3046   3051     47   -248   -404       O  
ATOM    332  CB  SER A  44      16.631  10.837  -6.347  1.00 24.96           C  
ANISOU  332  CB  SER A  44     3187   3084   3214    -11   -176   -367       C  
ATOM    333  OG  SER A  44      17.982  10.397  -6.254  1.00 25.90           O  
ANISOU  333  OG  SER A  44     3318   3226   3295      0   -139   -368       O  
ATOM    334  N   CYS A  45      15.973   8.009  -8.590  1.00 25.73           N  
ANISOU  334  N   CYS A  45     3382   3138   3255     35   -306   -457       N  
ATOM    335  CA  CYS A  45      16.221   7.483  -9.924  1.00 28.87           C  
ANISOU  335  CA  CYS A  45     3850   3539   3580     80   -345   -490       C  
ATOM    336  C   CYS A  45      15.409   8.246 -11.006  1.00 25.48           C  
ANISOU  336  C   CYS A  45     3437   3116   3127     84   -393   -483       C  
ATOM    337  O   CYS A  45      14.181   8.359 -10.916  1.00 29.48           O  
ANISOU  337  O   CYS A  45     3914   3596   3691     49   -447   -475       O  
ATOM    338  CB  CYS A  45      15.888   5.977  -9.940  1.00 31.31           C  
ANISOU  338  CB  CYS A  45     4200   3790   3904     81   -409   -534       C  
ATOM    339  SG  CYS A  45      16.136   5.113 -11.498  1.00 40.12           S  
ANISOU  339  SG  CYS A  45     5432   4891   4923    149   -473   -591       S  
ATOM    340  N   GLY A  46      16.096   8.798 -12.001  1.00 20.64           N  
ANISOU  340  N   GLY A  46     2864   2548   2431    127   -370   -476       N  
ATOM    341  CA  GLY A  46      15.441   9.546 -13.075  1.00 24.61           C  
ANISOU  341  CA  GLY A  46     3390   3061   2901    136   -414   -464       C  
ATOM    342  C   GLY A  46      14.996  10.966 -12.729  1.00 24.82           C  
ANISOU  342  C   GLY A  46     3363   3098   2968    105   -394   -414       C  
ATOM    343  O   GLY A  46      14.312  11.630 -13.524  1.00 24.14           O  
ANISOU  343  O   GLY A  46     3291   3014   2867    110   -437   -400       O  
ATOM    344  N   ALA A  47      15.391  11.441 -11.547  1.00 25.62           N  
ANISOU  344  N   ALA A  47     3414   3203   3119     78   -335   -388       N  
ATOM    345  CA  ALA A  47      14.960  12.744 -11.038  1.00 24.58           C  
ANISOU  345  CA  ALA A  47     3244   3067   3029     55   -321   -348       C  
ATOM    346  C   ALA A  47      15.420  13.942 -11.872  1.00 22.73           C  
ANISOU  346  C   ALA A  47     3037   2860   2738     67   -308   -308       C  
ATOM    347  O   ALA A  47      16.595  14.062 -12.221  1.00 21.00           O  
ANISOU  347  O   ALA A  47     2836   2679   2462     77   -265   -288       O  
ATOM    348  CB  ALA A  47      15.452  12.931  -9.575  1.00 18.42           C  
ANISOU  348  CB  ALA A  47     2423   2280   2296     30   -264   -336       C  
ATOM    349  N   THR A  48      14.492  14.856 -12.149  1.00 21.02           N  
ANISOU  349  N   THR A  48     2816   2627   2542     66   -345   -288       N  
ATOM    350  CA  THR A  48      14.869  16.198 -12.578  1.00 19.89           C  
ANISOU  350  CA  THR A  48     2694   2494   2369     66   -332   -238       C  
ATOM    351  C   THR A  48      15.417  16.970 -11.387  1.00 18.83           C  
ANISOU  351  C   THR A  48     2537   2342   2275     38   -287   -212       C  
ATOM    352  O   THR A  48      15.182  16.596 -10.232  1.00 16.86           O  
ANISOU  352  O   THR A  48     2255   2071   2080     28   -271   -235       O  
ATOM    353  CB  THR A  48      13.693  16.997 -13.120  1.00 21.35           C  
ANISOU  353  CB  THR A  48     2885   2658   2570     79   -389   -223       C  
ATOM    354  OG1 THR A  48      12.778  17.211 -12.049  1.00 20.51           O  
ANISOU  354  OG1 THR A  48     2731   2517   2543     75   -395   -231       O  
ATOM    355  CG2 THR A  48      12.999  16.275 -14.253  1.00 22.69           C  
ANISOU  355  CG2 THR A  48     3079   2837   2706    101   -452   -250       C  
ATOM    356  N   PRO A  49      16.117  18.075 -11.660  1.00 19.72           N  
ANISOU  356  N   PRO A  49     2674   2460   2360     23   -273   -161       N  
ATOM    357  CA  PRO A  49      16.513  18.979 -10.575  1.00 18.39           C  
ANISOU  357  CA  PRO A  49     2502   2257   2230     -6   -254   -137       C  
ATOM    358  C   PRO A  49      15.310  19.430  -9.721  1.00 20.53           C  
ANISOU  358  C   PRO A  49     2763   2476   2563     12   -277   -159       C  
ATOM    359  O   PRO A  49      15.450  19.578  -8.508  1.00 17.92           O  
ANISOU  359  O   PRO A  49     2423   2119   2268      2   -256   -169       O  
ATOM    360  CB  PRO A  49      17.130  20.154 -11.319  1.00 21.89           C  
ANISOU  360  CB  PRO A  49     2980   2704   2634    -27   -262    -71       C  
ATOM    361  CG  PRO A  49      17.730  19.490 -12.568  1.00 22.76           C  
ANISOU  361  CG  PRO A  49     3095   2883   2669    -12   -245    -57       C  
ATOM    362  CD  PRO A  49      16.699  18.460 -12.955  1.00 20.51           C  
ANISOU  362  CD  PRO A  49     2808   2599   2384     30   -274   -119       C  
ATOM    363  N   GLN A  50      14.151  19.649 -10.340  1.00 20.00           N  
ANISOU  363  N   GLN A  50     2697   2399   2504     43   -320   -164       N  
ATOM    364  CA  GLN A  50      12.949  19.983  -9.575  1.00 20.20           C  
ANISOU  364  CA  GLN A  50     2698   2391   2586     75   -335   -180       C  
ATOM    365  C   GLN A  50      12.592  18.888  -8.566  1.00 20.72           C  
ANISOU  365  C   GLN A  50     2710   2468   2694     75   -309   -216       C  
ATOM    366  O   GLN A  50      12.276  19.177  -7.399  1.00 20.84           O  
ANISOU  366  O   GLN A  50     2710   2463   2746     90   -286   -223       O  
ATOM    367  CB  GLN A  50      11.769  20.212 -10.515  1.00 21.08           C  
ANISOU  367  CB  GLN A  50     2804   2505   2701    109   -390   -173       C  
ATOM    368  CG  GLN A  50      10.480  20.663  -9.807  1.00 24.03           C  
ANISOU  368  CG  GLN A  50     3142   2857   3132    154   -402   -177       C  
ATOM    369  CD  GLN A  50       9.294  20.679 -10.742  1.00 25.80           C  
ANISOU  369  CD  GLN A  50     3341   3095   3367    185   -461   -167       C  
ATOM    370  OE1 GLN A  50       8.955  19.664 -11.342  1.00 30.18           O  
ANISOU  370  OE1 GLN A  50     3868   3680   3921    169   -491   -182       O  
ATOM    371  NE2 GLN A  50       8.671  21.835 -10.888  1.00 27.73           N  
ANISOU  371  NE2 GLN A  50     3604   3312   3620    229   -488   -143       N  
ATOM    372  N   ASP A  51      12.623  17.635  -9.024  1.00 21.47           N  
ANISOU  372  N   ASP A  51     2784   2594   2781     61   -315   -238       N  
ATOM    373  CA  ASP A  51      12.328  16.482  -8.162  1.00 20.14           C  
ANISOU  373  CA  ASP A  51     2567   2431   2652     51   -298   -265       C  
ATOM    374  C   ASP A  51      13.323  16.385  -7.009  1.00 18.55           C  
ANISOU  374  C   ASP A  51     2370   2225   2454     33   -243   -270       C  
ATOM    375  O   ASP A  51      12.946  16.080  -5.878  1.00 19.54           O  
ANISOU  375  O   ASP A  51     2462   2344   2617     35   -219   -279       O  
ATOM    376  CB  ASP A  51      12.347  15.166  -8.957  1.00 20.97           C  
ANISOU  376  CB  ASP A  51     2673   2555   2741     39   -328   -290       C  
ATOM    377  CG  ASP A  51      11.229  15.078  -9.977  1.00 27.49           C  
ANISOU  377  CG  ASP A  51     3493   3382   3572     51   -398   -289       C  
ATOM    378  OD1 ASP A  51      10.166  15.698  -9.751  1.00 29.14           O  
ANISOU  378  OD1 ASP A  51     3663   3584   3824     68   -417   -270       O  
ATOM    379  OD2 ASP A  51      11.415  14.382 -11.005  1.00 25.53           O  
ANISOU  379  OD2 ASP A  51     3279   3140   3280     50   -436   -308       O  
ATOM    380  N   LEU A  52      14.594  16.627  -7.308  1.00 16.68           N  
ANISOU  380  N   LEU A  52     2170   1997   2172     13   -224   -258       N  
ATOM    381  CA  LEU A  52      15.633  16.602  -6.278  1.00 19.27           C  
ANISOU  381  CA  LEU A  52     2500   2322   2501    -10   -183   -255       C  
ATOM    382  C   LEU A  52      15.397  17.679  -5.220  1.00 19.97           C  
ANISOU  382  C   LEU A  52     2603   2371   2614     -3   -176   -247       C  
ATOM    383  O   LEU A  52      15.489  17.405  -4.008  1.00 20.43           O  
ANISOU  383  O   LEU A  52     2649   2420   2692     -5   -150   -261       O  
ATOM    384  CB  LEU A  52      17.024  16.748  -6.922  1.00 17.61           C  
ANISOU  384  CB  LEU A  52     2313   2138   2240    -32   -168   -229       C  
ATOM    385  CG  LEU A  52      17.443  15.538  -7.765  1.00 19.96           C  
ANISOU  385  CG  LEU A  52     2605   2477   2501    -21   -163   -245       C  
ATOM    386  CD1 LEU A  52      18.563  15.859  -8.795  1.00 24.60           C  
ANISOU  386  CD1 LEU A  52     3212   3110   3025    -24   -147   -207       C  
ATOM    387  CD2 LEU A  52      17.888  14.394  -6.864  1.00 19.68           C  
ANISOU  387  CD2 LEU A  52     2545   2446   2485    -27   -135   -272       C  
ATOM    388  N   ASN A  53      15.059  18.892  -5.650  1.00 19.36           N  
ANISOU  388  N   ASN A  53     2560   2267   2530     12   -203   -226       N  
ATOM    389  CA  ASN A  53      14.722  19.934  -4.683  1.00 20.36           C  
ANISOU  389  CA  ASN A  53     2717   2346   2673     34   -206   -225       C  
ATOM    390  C   ASN A  53      13.480  19.595  -3.877  1.00 19.38           C  
ANISOU  390  C   ASN A  53     2553   2225   2585     83   -190   -250       C  
ATOM    391  O   ASN A  53      13.395  19.887  -2.675  1.00 21.11           O  
ANISOU  391  O   ASN A  53     2786   2423   2812    106   -168   -262       O  
ATOM    392  CB  ASN A  53      14.556  21.283  -5.391  1.00 22.94           C  
ANISOU  392  CB  ASN A  53     3097   2635   2986     46   -246   -197       C  
ATOM    393  CG  ASN A  53      15.888  21.851  -5.825  1.00 22.26           C  
ANISOU  393  CG  ASN A  53     3051   2539   2868    -11   -258   -156       C  
ATOM    394  OD1 ASN A  53      16.909  21.580  -5.187  1.00 23.81           O  
ANISOU  394  OD1 ASN A  53     3245   2740   3060    -51   -238   -153       O  
ATOM    395  ND2 ASN A  53      15.903  22.585  -6.936  1.00 19.14           N  
ANISOU  395  ND2 ASN A  53     2684   2136   2450    -17   -290   -118       N  
ATOM    396  N   THR A  54      12.519  18.951  -4.525  1.00 19.00           N  
ANISOU  396  N   THR A  54     2454   2207   2557     99   -203   -252       N  
ATOM    397  CA  THR A  54      11.313  18.537  -3.821  1.00 20.49           C  
ANISOU  397  CA  THR A  54     2585   2415   2787    138   -188   -259       C  
ATOM    398  C   THR A  54      11.653  17.616  -2.663  1.00 20.61           C  
ANISOU  398  C   THR A  54     2574   2445   2814    119   -143   -272       C  
ATOM    399  O   THR A  54      11.173  17.809  -1.531  1.00 20.11           O  
ANISOU  399  O   THR A  54     2497   2382   2762    157   -110   -273       O  
ATOM    400  CB  THR A  54      10.314  17.816  -4.759  1.00 19.94           C  
ANISOU  400  CB  THR A  54     2456   2377   2744    137   -223   -251       C  
ATOM    401  OG1 THR A  54       9.774  18.762  -5.684  1.00 21.90           O  
ANISOU  401  OG1 THR A  54     2724   2614   2984    168   -265   -235       O  
ATOM    402  CG2 THR A  54       9.172  17.225  -3.947  1.00 21.27           C  
ANISOU  402  CG2 THR A  54     2544   2575   2961    160   -204   -242       C  
ATOM    403  N   MET A  55      12.467  16.599  -2.949  1.00 21.22           N  
ANISOU  403  N   MET A  55     2646   2536   2882     70   -142   -281       N  
ATOM    404  CA  MET A  55      12.802  15.615  -1.929  1.00 20.78           C  
ANISOU  404  CA  MET A  55     2565   2491   2837     50   -107   -290       C  
ATOM    405  C   MET A  55      13.560  16.268  -0.795  1.00 19.56           C  
ANISOU  405  C   MET A  55     2455   2314   2662     56    -76   -295       C  
ATOM    406  O   MET A  55      13.299  15.985   0.374  1.00 20.45           O  
ANISOU  406  O   MET A  55     2553   2434   2785     72    -43   -298       O  
ATOM    407  CB  MET A  55      13.618  14.467  -2.530  1.00 20.37           C  
ANISOU  407  CB  MET A  55     2513   2451   2774      8   -117   -301       C  
ATOM    408  CG  MET A  55      12.830  13.613  -3.532  1.00 22.45           C  
ANISOU  408  CG  MET A  55     2747   2727   3058      1   -159   -304       C  
ATOM    409  SD  MET A  55      13.899  12.420  -4.399  1.00 32.84           S  
ANISOU  409  SD  MET A  55     4092   4046   4338    -25   -176   -327       S  
ATOM    410  CE  MET A  55      14.339  11.330  -3.041  1.00 27.17           C  
ANISOU  410  CE  MET A  55     3354   3325   3645    -45   -139   -334       C  
ATOM    411  N   LEU A  56      14.486  17.165  -1.138  1.00 17.26           N  
ANISOU  411  N   LEU A  56     2222   1998   2340     41    -93   -291       N  
ATOM    412  CA  LEU A  56      15.280  17.836  -0.122  1.00 18.54           C  
ANISOU  412  CA  LEU A  56     2434   2127   2481     36    -84   -293       C  
ATOM    413  C   LEU A  56      14.394  18.751   0.730  1.00 20.92           C  
ANISOU  413  C   LEU A  56     2766   2401   2783     98    -78   -303       C  
ATOM    414  O   LEU A  56      14.574  18.850   1.960  1.00 24.21           O  
ANISOU  414  O   LEU A  56     3209   2803   3185    115    -57   -316       O  
ATOM    415  CB  LEU A  56      16.430  18.630  -0.768  1.00 19.04           C  
ANISOU  415  CB  LEU A  56     2545   2169   2519     -6   -115   -273       C  
ATOM    416  CG  LEU A  56      17.542  17.817  -1.460  1.00 23.05           C  
ANISOU  416  CG  LEU A  56     3027   2715   3014    -55   -109   -258       C  
ATOM    417  CD1 LEU A  56      18.589  18.749  -2.068  1.00 21.90           C  
ANISOU  417  CD1 LEU A  56     2917   2559   2846    -95   -135   -219       C  
ATOM    418  CD2 LEU A  56      18.218  16.833  -0.508  1.00 22.26           C  
ANISOU  418  CD2 LEU A  56     2906   2634   2919    -73    -81   -269       C  
ATOM    419  N   ASN A  57      13.432  19.404   0.076  1.00 18.24           N  
ANISOU  419  N   ASN A  57     2423   2055   2453    140    -96   -296       N  
ATOM    420  CA  ASN A  57      12.530  20.321   0.749  1.00 18.55           C  
ANISOU  420  CA  ASN A  57     2491   2071   2488    219    -89   -304       C  
ATOM    421  C   ASN A  57      11.515  19.636   1.673  1.00 19.81           C  
ANISOU  421  C   ASN A  57     2587   2278   2664    270    -37   -305       C  
ATOM    422  O   ASN A  57      10.964  20.288   2.572  1.00 20.25           O  
ANISOU  422  O   ASN A  57     2671   2323   2701    346    -14   -315       O  
ATOM    423  CB  ASN A  57      11.775  21.183  -0.278  1.00 18.71           C  
ANISOU  423  CB  ASN A  57     2519   2074   2514    256   -126   -291       C  
ATOM    424  CG  ASN A  57      12.591  22.381  -0.765  1.00 20.04           C  
ANISOU  424  CG  ASN A  57     2780   2176   2657    233   -176   -283       C  
ATOM    425  OD1 ASN A  57      13.472  22.878  -0.058  1.00 21.58           O  
ANISOU  425  OD1 ASN A  57     3044   2324   2829    212   -187   -292       O  
ATOM    426  ND2 ASN A  57      12.289  22.857  -1.985  1.00 20.98           N  
ANISOU  426  ND2 ASN A  57     2902   2290   2782    232   -214   -261       N  
ATOM    427  N   THR A  58      11.243  18.346   1.462  1.00 20.06           N  
ANISOU  427  N   THR A  58     2535   2361   2728    233    -21   -292       N  
ATOM    428  CA  THR A  58      10.217  17.708   2.275  1.00 24.09           C  
ANISOU  428  CA  THR A  58     2972   2922   3261    272     26   -276       C  
ATOM    429  C   THR A  58      10.800  17.282   3.609  1.00 26.38           C  
ANISOU  429  C   THR A  58     3284   3214   3526    268     68   -286       C  
ATOM    430  O   THR A  58      10.060  16.875   4.506  1.00 28.83           O  
ANISOU  430  O   THR A  58     3546   3567   3841    307    117   -268       O  
ATOM    431  CB  THR A  58       9.543  16.483   1.586  1.00 27.95           C  
ANISOU  431  CB  THR A  58     3362   3456   3800    229     15   -249       C  
ATOM    432  OG1 THR A  58      10.525  15.531   1.171  1.00 23.34           O  
ANISOU  432  OG1 THR A  58     2789   2863   3218    152     -5   -261       O  
ATOM    433  CG2 THR A  58       8.706  16.924   0.386  1.00 31.26           C  
ANISOU  433  CG2 THR A  58     3752   3882   4244    246    -29   -235       C  
ATOM    434  N   VAL A  59      12.118  17.398   3.744  1.00 24.05           N  
ANISOU  434  N   VAL A  59     3057   2879   3202    222     50   -307       N  
ATOM    435  CA  VAL A  59      12.770  17.191   5.035  1.00 27.23           C  
ANISOU  435  CA  VAL A  59     3499   3276   3573    222     77   -319       C  
ATOM    436  C   VAL A  59      12.463  18.353   5.978  1.00 24.30           C  
ANISOU  436  C   VAL A  59     3202   2876   3157    304     90   -338       C  
ATOM    437  O   VAL A  59      12.793  19.511   5.697  1.00 26.10           O  
ANISOU  437  O   VAL A  59     3510   3046   3363    320     48   -356       O  
ATOM    438  CB  VAL A  59      14.307  17.050   4.916  1.00 27.53           C  
ANISOU  438  CB  VAL A  59     3583   3282   3596    149     46   -330       C  
ATOM    439  CG1 VAL A  59      14.911  16.801   6.295  1.00 28.82           C  
ANISOU  439  CG1 VAL A  59     3783   3440   3727    150     67   -340       C  
ATOM    440  CG2 VAL A  59      14.686  15.931   3.948  1.00 27.48           C  
ANISOU  440  CG2 VAL A  59     3518   3302   3622     85     35   -318       C  
ATOM    441  N   GLY A  60      11.836  18.030   7.100  1.00 24.85           N  
ANISOU  441  N   GLY A  60     3250   2983   3208    361    145   -331       N  
ATOM    442  CA  GLY A  60      11.426  19.023   8.070  1.00 27.28           C  
ANISOU  442  CA  GLY A  60     3632   3273   3461    462    167   -352       C  
ATOM    443  C   GLY A  60      12.535  19.449   9.021  1.00 30.67           C  
ANISOU  443  C   GLY A  60     4175   3645   3831    453    143   -387       C  
ATOM    444  O   GLY A  60      12.722  20.637   9.258  1.00 31.52           O  
ANISOU  444  O   GLY A  60     4391   3687   3897    500    106   -419       O  
ATOM    445  N   GLY A  61      13.274  18.497   9.576  1.00 30.34           N  
ANISOU  445  N   GLY A  61     4117   3622   3787    393    154   -380       N  
ATOM    446  CA  GLY A  61      14.274  18.866  10.577  1.00 32.78           C  
ANISOU  446  CA  GLY A  61     4531   3883   4039    387    126   -409       C  
ATOM    447  C   GLY A  61      15.651  19.078   9.971  1.00 27.51           C  
ANISOU  447  C   GLY A  61     3903   3161   3389    288     52   -415       C  
ATOM    448  O   GLY A  61      15.760  19.453   8.804  1.00 25.93           O  
ANISOU  448  O   GLY A  61     3686   2941   3224    251     17   -406       O  
ATOM    449  N   HIS A  62      16.691  18.844  10.769  1.00 23.52           N  
ANISOU  449  N   HIS A  62     3443   2637   2856    246     28   -422       N  
ATOM    450  CA  HIS A  62      18.062  18.791  10.265  1.00 23.56           C  
ANISOU  450  CA  HIS A  62     3453   2614   2883    146    -32   -411       C  
ATOM    451  C   HIS A  62      18.477  20.000   9.432  1.00 19.90           C  
ANISOU  451  C   HIS A  62     3046   2086   2429    116   -102   -412       C  
ATOM    452  O   HIS A  62      19.177  19.846   8.440  1.00 17.90           O  
ANISOU  452  O   HIS A  62     2747   1840   2213     41   -127   -384       O  
ATOM    453  CB  HIS A  62      18.233  17.526   9.416  1.00 24.92           C  
ANISOU  453  CB  HIS A  62     3511   2847   3112     88     -3   -380       C  
ATOM    454  CG  HIS A  62      17.817  16.274  10.116  1.00 27.58           C  
ANISOU  454  CG  HIS A  62     3790   3239   3451    104     56   -369       C  
ATOM    455  ND1 HIS A  62      18.478  15.787  11.224  1.00 33.17           N  
ANISOU  455  ND1 HIS A  62     4525   3950   4128     93     57   -370       N  
ATOM    456  CD2 HIS A  62      16.810  15.404   9.865  1.00 30.15           C  
ANISOU  456  CD2 HIS A  62     4033   3617   3808    125    109   -350       C  
ATOM    457  CE1 HIS A  62      17.894  14.673  11.627  1.00 32.71           C  
ANISOU  457  CE1 HIS A  62     4405   3943   4081    107    113   -350       C  
ATOM    458  NE2 HIS A  62      16.879  14.419  10.820  1.00 31.76           N  
ANISOU  458  NE2 HIS A  62     4216   3851   4001    123    143   -337       N  
ATOM    459  N   GLN A  63      18.028  21.192   9.812  1.00 21.83           N  
ANISOU  459  N   GLN A  63     3392   2268   2636    179   -132   -440       N  
ATOM    460  CA  GLN A  63      18.251  22.364   8.976  1.00 22.91           C  
ANISOU  460  CA  GLN A  63     3585   2336   2784    155   -200   -436       C  
ATOM    461  C   GLN A  63      19.717  22.858   8.996  1.00 22.24           C  
ANISOU  461  C   GLN A  63     3555   2193   2700     54   -289   -417       C  
ATOM    462  O   GLN A  63      20.152  23.571   8.090  1.00 20.23           O  
ANISOU  462  O   GLN A  63     3315   1900   2472     -2   -344   -389       O  
ATOM    463  CB  GLN A  63      17.281  23.472   9.397  1.00 24.08           C  
ANISOU  463  CB  GLN A  63     3833   2427   2890    265   -209   -474       C  
ATOM    464  CG  GLN A  63      15.843  23.125   8.981  1.00 23.53           C  
ANISOU  464  CG  GLN A  63     3681   2423   2837    352   -130   -471       C  
ATOM    465  CD  GLN A  63      15.758  22.937   7.474  1.00 27.28           C  
ANISOU  465  CD  GLN A  63     4068   2924   3373    295   -135   -434       C  
ATOM    466  OE1 GLN A  63      16.039  23.870   6.708  1.00 28.42           O  
ANISOU  466  OE1 GLN A  63     4263   3008   3527    268   -196   -425       O  
ATOM    467  NE2 GLN A  63      15.422  21.720   7.035  1.00 24.19           N  
ANISOU  467  NE2 GLN A  63     3554   2617   3019    272    -78   -411       N  
ATOM    468  N   ALA A  64      20.475  22.486  10.024  1.00 21.50           N  
ANISOU  468  N   ALA A  64     3490   2097   2581     27   -306   -425       N  
ATOM    469  CA  ALA A  64      21.914  22.738   9.994  1.00 21.77           C  
ANISOU  469  CA  ALA A  64     3543   2098   2630    -82   -388   -392       C  
ATOM    470  C   ALA A  64      22.534  21.953   8.836  1.00 22.98           C  
ANISOU  470  C   ALA A  64     3565   2324   2840   -160   -361   -337       C  
ATOM    471  O   ALA A  64      23.230  22.517   7.995  1.00 22.29           O  
ANISOU  471  O   ALA A  64     3470   2219   2781   -233   -412   -293       O  
ATOM    472  CB  ALA A  64      22.570  22.363  11.336  1.00 20.34           C  
ANISOU  472  CB  ALA A  64     3406   1911   2411    -92   -411   -408       C  
ATOM    473  N   ALA A  65      22.259  20.655   8.783  1.00 24.55           N  
ANISOU  473  N   ALA A  65     3669   2607   3053   -140   -282   -336       N  
ATOM    474  CA  ALA A  65      22.721  19.843   7.668  1.00 22.30           C  
ANISOU  474  CA  ALA A  65     3272   2390   2810   -190   -251   -296       C  
ATOM    475  C   ALA A  65      22.294  20.423   6.338  1.00 22.60           C  
ANISOU  475  C   ALA A  65     3294   2423   2869   -192   -254   -277       C  
ATOM    476  O   ALA A  65      23.090  20.470   5.412  1.00 23.26           O  
ANISOU  476  O   ALA A  65     3333   2529   2973   -254   -272   -231       O  
ATOM    477  CB  ALA A  65      22.213  18.427   7.794  1.00 17.98           C  
ANISOU  477  CB  ALA A  65     2648   1913   2272   -153   -174   -308       C  
ATOM    478  N   MET A  66      21.037  20.852   6.237  1.00 18.11           N  
ANISOU  478  N   MET A  66     2757   1833   2293   -119   -234   -308       N  
ATOM    479  CA  MET A  66      20.516  21.306   4.942  1.00 19.12           C  
ANISOU  479  CA  MET A  66     2864   1961   2439   -114   -235   -291       C  
ATOM    480  C   MET A  66      21.221  22.557   4.514  1.00 20.07           C  
ANISOU  480  C   MET A  66     3050   2017   2560   -170   -312   -258       C  
ATOM    481  O   MET A  66      21.448  22.761   3.321  1.00 21.50           O  
ANISOU  481  O   MET A  66     3196   2216   2759   -207   -320   -217       O  
ATOM    482  CB  MET A  66      18.994  21.544   4.993  1.00 17.06           C  
ANISOU  482  CB  MET A  66     2619   1692   2172    -19   -202   -326       C  
ATOM    483  CG  MET A  66      18.177  20.260   5.125  1.00 22.00           C  
ANISOU  483  CG  MET A  66     3157   2390   2810     22   -128   -339       C  
ATOM    484  SD  MET A  66      18.595  18.980   3.902  1.00 29.34           S  
ANISOU  484  SD  MET A  66     3979   3392   3775    -34   -103   -310       S  
ATOM    485  CE  MET A  66      20.004  18.204   4.693  1.00 48.19           C  
ANISOU  485  CE  MET A  66     6355   5798   6155    -92   -103   -300       C  
ATOM    486  N   GLN A  67      21.563  23.416   5.472  1.00 17.48           N  
ANISOU  486  N   GLN A  67     2822   1611   2209   -177   -374   -273       N  
ATOM    487  CA  GLN A  67      22.300  24.609   5.087  1.00 20.95           C  
ANISOU  487  CA  GLN A  67     3327   1978   2656   -246   -463   -232       C  
ATOM    488  C   GLN A  67      23.719  24.241   4.618  1.00 23.08           C  
ANISOU  488  C   GLN A  67     3522   2297   2951   -357   -482   -162       C  
ATOM    489  O   GLN A  67      24.236  24.839   3.675  1.00 23.67           O  
ANISOU  489  O   GLN A  67     3584   2365   3045   -421   -518   -101       O  
ATOM    490  CB  GLN A  67      22.351  25.641   6.240  1.00 24.29           C  
ANISOU  490  CB  GLN A  67     3894   2290   3046   -230   -543   -268       C  
ATOM    491  CG  GLN A  67      23.307  26.780   5.969  1.00 27.82           C  
ANISOU  491  CG  GLN A  67     4410   2654   3507   -327   -654   -216       C  
ATOM    492  CD  GLN A  67      22.884  27.646   4.802  1.00 32.59           C  
ANISOU  492  CD  GLN A  67     5033   3221   4129   -330   -678   -184       C  
ATOM    493  OE1 GLN A  67      21.712  27.682   4.435  1.00 32.60           O  
ANISOU  493  OE1 GLN A  67     5036   3230   4122   -237   -629   -219       O  
ATOM    494  NE2 GLN A  67      23.839  28.363   4.219  1.00 33.66           N  
ANISOU  494  NE2 GLN A  67     5180   3320   4291   -440   -756   -108       N  
ATOM    495  N   MET A  68      24.347  23.262   5.268  1.00 24.43           N  
ANISOU  495  N   MET A  68     3638   2522   3122   -375   -455   -164       N  
ATOM    496  CA  MET A  68      25.644  22.775   4.807  1.00 22.84           C  
ANISOU  496  CA  MET A  68     3347   2386   2944   -461   -458    -96       C  
ATOM    497  C   MET A  68      25.541  22.195   3.392  1.00 21.75           C  
ANISOU  497  C   MET A  68     3112   2332   2820   -455   -394    -63       C  
ATOM    498  O   MET A  68      26.422  22.399   2.555  1.00 19.27           O  
ANISOU  498  O   MET A  68     2746   2055   2519   -520   -407     10       O  
ATOM    499  CB  MET A  68      26.198  21.723   5.764  1.00 21.94           C  
ANISOU  499  CB  MET A  68     3193   2318   2826   -461   -435   -111       C  
ATOM    500  CG  MET A  68      26.737  22.301   7.047  1.00 27.25           C  
ANISOU  500  CG  MET A  68     3952   2919   3482   -494   -517   -122       C  
ATOM    501  SD  MET A  68      27.847  21.145   7.862  1.00 44.78           S  
ANISOU  501  SD  MET A  68     6099   5207   5706   -529   -508   -102       S  
ATOM    502  CE  MET A  68      26.676  19.981   8.473  1.00 21.35           C  
ANISOU  502  CE  MET A  68     3127   2274   2713   -418   -411   -179       C  
ATOM    503  N   LEU A  69      24.465  21.462   3.130  1.00 22.30           N  
ANISOU  503  N   LEU A  69     3156   2433   2882   -376   -325   -112       N  
ATOM    504  CA  LEU A  69      24.230  20.941   1.796  1.00 23.89           C  
ANISOU  504  CA  LEU A  69     3288   2701   3089   -361   -275    -92       C  
ATOM    505  C   LEU A  69      24.100  22.077   0.758  1.00 24.96           C  
ANISOU  505  C   LEU A  69     3454   2804   3224   -385   -312    -51       C  
ATOM    506  O   LEU A  69      24.646  21.994  -0.352  1.00 22.26           O  
ANISOU  506  O   LEU A  69     3058   2519   2880   -416   -298      5       O  
ATOM    507  CB  LEU A  69      22.980  20.042   1.805  1.00 22.40           C  
ANISOU  507  CB  LEU A  69     3078   2535   2897   -279   -216   -153       C  
ATOM    508  CG  LEU A  69      22.570  19.376   0.484  1.00 23.01           C  
ANISOU  508  CG  LEU A  69     3096   2671   2974   -254   -174   -148       C  
ATOM    509  CD1 LEU A  69      23.731  18.568  -0.124  1.00 20.62           C  
ANISOU  509  CD1 LEU A  69     2724   2444   2665   -286   -149   -107       C  
ATOM    510  CD2 LEU A  69      21.362  18.471   0.733  1.00 23.90           C  
ANISOU  510  CD2 LEU A  69     3191   2796   3094   -189   -133   -202       C  
ATOM    511  N   LYS A  70      23.375  23.136   1.107  1.00 25.34           N  
ANISOU  511  N   LYS A  70     3593   2764   3269   -362   -358    -75       N  
ATOM    512  CA  LYS A  70      23.246  24.281   0.211  1.00 26.68           C  
ANISOU  512  CA  LYS A  70     3807   2890   3441   -385   -404    -33       C  
ATOM    513  C   LYS A  70      24.603  24.891  -0.122  1.00 27.44           C  
ANISOU  513  C   LYS A  70     3893   2985   3548   -492   -458     56       C  
ATOM    514  O   LYS A  70      24.856  25.314  -1.265  1.00 24.36           O  
ANISOU  514  O   LYS A  70     3480   2618   3159   -528   -463    121       O  
ATOM    515  CB  LYS A  70      22.367  25.369   0.824  1.00 25.42           C  
ANISOU  515  CB  LYS A  70     3762   2622   3275   -338   -456    -76       C  
ATOM    516  CG  LYS A  70      20.897  25.085   0.760  1.00 26.64           C  
ANISOU  516  CG  LYS A  70     3917   2784   3422   -233   -408   -137       C  
ATOM    517  CD  LYS A  70      20.161  26.360   1.177  1.00 30.09           C  
ANISOU  517  CD  LYS A  70     4471   3113   3848   -181   -465   -165       C  
ATOM    518  CE  LYS A  70      18.679  26.176   1.155  1.00 27.63           C  
ANISOU  518  CE  LYS A  70     4151   2816   3531    -69   -418   -215       C  
ATOM    519  NZ  LYS A  70      18.056  27.335   1.877  1.00 26.52           N  
ANISOU  519  NZ  LYS A  70     4132   2573   3371      2   -466   -252       N  
ATOM    520  N   GLU A  71      25.471  24.942   0.883  1.00 24.74           N  
ANISOU  520  N   GLU A  71     3566   2620   3215   -545   -499     65       N  
ATOM    521  CA  GLU A  71      26.796  25.540   0.710  1.00 25.75           C  
ANISOU  521  CA  GLU A  71     3676   2746   3362   -659   -562    160       C  
ATOM    522  C   GLU A  71      27.652  24.677  -0.220  1.00 26.10           C  
ANISOU  522  C   GLU A  71     3587   2922   3409   -688   -496    229       C  
ATOM    523  O   GLU A  71      28.382  25.203  -1.075  1.00 26.84           O  
ANISOU  523  O   GLU A  71     3642   3045   3509   -759   -515    326       O  
ATOM    524  CB  GLU A  71      27.477  25.760   2.077  1.00 23.89           C  
ANISOU  524  CB  GLU A  71     3490   2453   3136   -707   -633    150       C  
ATOM    525  CG  GLU A  71      26.920  27.011   2.795  1.00 29.20           C  
ANISOU  525  CG  GLU A  71     4318   2978   3800   -698   -728    109       C  
ATOM    526  CD  GLU A  71      27.631  27.392   4.104  1.00 36.06           C  
ANISOU  526  CD  GLU A  71     5262   3771   4669   -752   -822    100       C  
ATOM    527  OE1 GLU A  71      28.755  26.913   4.377  1.00 38.31           O  
ANISOU  527  OE1 GLU A  71     5471   4113   4972   -827   -835    152       O  
ATOM    528  OE2 GLU A  71      27.042  28.190   4.873  1.00 37.57           O  
ANISOU  528  OE2 GLU A  71     5594   3845   4837   -712   -887     39       O  
ATOM    529  N   THR A  72      27.534  23.360  -0.078  1.00 22.40           N  
ANISOU  529  N   THR A  72     3051   2531   2928   -628   -417    183       N  
ATOM    530  CA  THR A  72      28.214  22.427  -0.974  1.00 21.34           C  
ANISOU  530  CA  THR A  72     2804   2520   2784   -624   -346    231       C  
ATOM    531  C   THR A  72      27.691  22.552  -2.404  1.00 21.72           C  
ANISOU  531  C   THR A  72     2840   2605   2809   -592   -308    252       C  
ATOM    532  O   THR A  72      28.463  22.604  -3.365  1.00 25.13           O  
ANISOU  532  O   THR A  72     3207   3113   3228   -626   -287    336       O  
ATOM    533  CB  THR A  72      28.050  20.958  -0.493  1.00 22.82           C  
ANISOU  533  CB  THR A  72     2945   2763   2963   -555   -279    164       C  
ATOM    534  OG1 THR A  72      28.777  20.774   0.732  1.00 23.44           O  
ANISOU  534  OG1 THR A  72     3020   2827   3058   -591   -312    164       O  
ATOM    535  CG2 THR A  72      28.587  20.003  -1.539  1.00 20.70           C  
ANISOU  535  CG2 THR A  72     2581   2610   2673   -526   -207    200       C  
ATOM    536  N   ILE A  73      26.374  22.585  -2.552  1.00 24.64           N  
ANISOU  536  N   ILE A  73     3265   2928   3169   -524   -299    179       N  
ATOM    537  CA  ILE A  73      25.760  22.803  -3.865  1.00 24.77           C  
ANISOU  537  CA  ILE A  73     3285   2966   3162   -492   -278    194       C  
ATOM    538  C   ILE A  73      26.248  24.102  -4.539  1.00 27.08           C  
ANISOU  538  C   ILE A  73     3602   3232   3456   -566   -331    289       C  
ATOM    539  O   ILE A  73      26.582  24.116  -5.731  1.00 26.95           O  
ANISOU  539  O   ILE A  73     3543   3285   3413   -575   -302    354       O  
ATOM    540  CB  ILE A  73      24.231  22.819  -3.745  1.00 20.23           C  
ANISOU  540  CB  ILE A  73     2768   2333   2587   -416   -278    109       C  
ATOM    541  CG1 ILE A  73      23.726  21.407  -3.409  1.00 21.05           C  
ANISOU  541  CG1 ILE A  73     2830   2480   2687   -350   -220     35       C  
ATOM    542  CG2 ILE A  73      23.573  23.350  -5.041  1.00 24.13           C  
ANISOU  542  CG2 ILE A  73     3281   2827   3060   -394   -283    132       C  
ATOM    543  CD1 ILE A  73      22.311  21.351  -2.913  1.00 19.89           C  
ANISOU  543  CD1 ILE A  73     2724   2282   2552   -284   -221    -40       C  
ATOM    544  N   ASN A  74      26.290  25.192  -3.788  1.00 25.30           N  
ANISOU  544  N   ASN A  74     3452   2902   3257   -618   -412    299       N  
ATOM    545  CA  ASN A  74      26.739  26.446  -4.356  1.00 29.04           C  
ANISOU  545  CA  ASN A  74     3959   3333   3740   -698   -477    393       C  
ATOM    546  C   ASN A  74      28.202  26.381  -4.788  1.00 29.03           C  
ANISOU  546  C   ASN A  74     3864   3422   3743   -788   -469    512       C  
ATOM    547  O   ASN A  74      28.571  26.996  -5.788  1.00 26.98           O  
ANISOU  547  O   ASN A  74     3587   3191   3474   -836   -477    609       O  
ATOM    548  CB  ASN A  74      26.520  27.594  -3.372  1.00 33.54           C  
ANISOU  548  CB  ASN A  74     4647   3760   4338   -732   -579    373       C  
ATOM    549  CG  ASN A  74      25.041  27.939  -3.194  1.00 39.87           C  
ANISOU  549  CG  ASN A  74     5542   4477   5129   -636   -588    280       C  
ATOM    550  OD1 ASN A  74      24.229  27.755  -4.104  1.00 40.96           O  
ANISOU  550  OD1 ASN A  74     5666   4648   5248   -574   -546    265       O  
ATOM    551  ND2 ASN A  74      24.689  28.440  -2.015  1.00 42.87           N  
ANISOU  551  ND2 ASN A  74     6019   4752   5519   -617   -646    219       N  
ATOM    552  N   GLU A  75      29.024  25.637  -4.042  1.00 25.16           N  
ANISOU  552  N   GLU A  75     3309   2983   3266   -807   -450    512       N  
ATOM    553  CA  GLU A  75      30.434  25.446  -4.385  1.00 29.10           C  
ANISOU  553  CA  GLU A  75     3698   3586   3771   -881   -432    627       C  
ATOM    554  C   GLU A  75      30.569  24.693  -5.711  1.00 27.97           C  
ANISOU  554  C   GLU A  75     3468   3579   3580   -823   -331    663       C  
ATOM    555  O   GLU A  75      31.357  25.080  -6.570  1.00 29.30           O  
ANISOU  555  O   GLU A  75     3574   3821   3737   -877   -319    783       O  
ATOM    556  CB  GLU A  75      31.186  24.667  -3.283  1.00 31.66           C  
ANISOU  556  CB  GLU A  75     3970   3943   4117   -892   -429    607       C  
ATOM    557  CG  GLU A  75      31.391  25.403  -1.961  1.00 39.17           C  
ANISOU  557  CG  GLU A  75     4999   4777   5109   -964   -538    593       C  
ATOM    558  CD  GLU A  75      31.749  24.465  -0.796  1.00 44.19           C  
ANISOU  558  CD  GLU A  75     5605   5433   5753   -941   -526    537       C  
ATOM    559  OE1 GLU A  75      31.963  23.255  -1.029  1.00 46.15           O  
ANISOU  559  OE1 GLU A  75     5764   5787   5982   -879   -437    521       O  
ATOM    560  OE2 GLU A  75      31.799  24.934   0.361  1.00 46.14           O  
ANISOU  560  OE2 GLU A  75     5928   5583   6019   -980   -611    506       O  
ATOM    561  N   GLU A  76      29.803  23.612  -5.864  1.00 24.61           N  
ANISOU  561  N   GLU A  76     3041   3186   3122   -713   -261    563       N  
ATOM    562  CA  GLU A  76      29.858  22.801  -7.086  1.00 26.48           C  
ANISOU  562  CA  GLU A  76     3218   3541   3302   -643   -173    577       C  
ATOM    563  C   GLU A  76      29.337  23.572  -8.297  1.00 22.46           C  
ANISOU  563  C   GLU A  76     2748   3026   2760   -641   -178    620       C  
ATOM    564  O   GLU A  76      29.845  23.430  -9.408  1.00 26.06           O  
ANISOU  564  O   GLU A  76     3148   3586   3167   -628   -125    696       O  
ATOM    565  CB  GLU A  76      29.073  21.495  -6.891  1.00 28.23           C  
ANISOU  565  CB  GLU A  76     3450   3774   3504   -535   -120    454       C  
ATOM    566  CG  GLU A  76      29.657  20.583  -5.804  1.00 29.15           C  
ANISOU  566  CG  GLU A  76     3520   3910   3644   -528   -105    420       C  
ATOM    567  CD  GLU A  76      31.154  20.279  -6.025  1.00 34.98           C  
ANISOU  567  CD  GLU A  76     4151   4766   4375   -558    -68    521       C  
ATOM    568  OE1 GLU A  76      31.519  19.704  -7.077  1.00 34.76           O  
ANISOU  568  OE1 GLU A  76     4068   4845   4294   -502      2    555       O  
ATOM    569  OE2 GLU A  76      31.963  20.619  -5.142  1.00 35.63           O  
ANISOU  569  OE2 GLU A  76     4203   4836   4501   -634   -112    569       O  
ATOM    570  N   ALA A  77      28.347  24.425  -8.066  1.00 21.75           N  
ANISOU  570  N   ALA A  77     2755   2816   2692   -649   -243    577       N  
ATOM    571  CA  ALA A  77      27.750  25.219  -9.134  1.00 26.43           C  
ANISOU  571  CA  ALA A  77     3397   3388   3258   -645   -260    613       C  
ATOM    572  C   ALA A  77      28.711  26.325  -9.594  1.00 28.08           C  
ANISOU  572  C   ALA A  77     3586   3607   3476   -753   -300    761       C  
ATOM    573  O   ALA A  77      28.805  26.631 -10.792  1.00 29.92           O  
ANISOU  573  O   ALA A  77     3805   3899   3666   -754   -275    839       O  
ATOM    574  CB  ALA A  77      26.421  25.825  -8.670  1.00 25.24           C  
ANISOU  574  CB  ALA A  77     3353   3104   3132   -614   -321    527       C  
ATOM    575  N   ALA A  78      29.413  26.926  -8.641  1.00 28.00           N  
ANISOU  575  N   ALA A  78     3579   3539   3521   -848   -367    805       N  
ATOM    576  CA  ALA A  78      30.449  27.894  -8.978  1.00 31.65           C  
ANISOU  576  CA  ALA A  78     4007   4015   4003   -970   -413    959       C  
ATOM    577  C   ALA A  78      31.531  27.250  -9.840  1.00 32.30           C  
ANISOU  577  C   ALA A  78     3953   4274   4046   -973   -322   1065       C  
ATOM    578  O   ALA A  78      32.001  27.847 -10.808  1.00 34.36           O  
ANISOU  578  O   ALA A  78     4180   4592   4285  -1023   -314   1193       O  
ATOM    579  CB  ALA A  78      31.057  28.489  -7.717  1.00 34.10           C  
ANISOU  579  CB  ALA A  78     4342   4233   4381  -1072   -510    979       C  
ATOM    580  N   GLU A  79      31.915  26.025  -9.490  1.00 33.66           N  
ANISOU  580  N   GLU A  79     4050   4535   4205   -911   -250   1015       N  
ATOM    581  CA  GLU A  79      32.938  25.297 -10.238  1.00 32.92           C  
ANISOU  581  CA  GLU A  79     3827   4616   4065   -887   -154   1104       C  
ATOM    582  C   GLU A  79      32.429  24.888 -11.624  1.00 30.86           C  
ANISOU  582  C   GLU A  79     3572   4437   3716   -786    -73   1094       C  
ATOM    583  O   GLU A  79      33.165  25.000 -12.597  1.00 30.37           O  
ANISOU  583  O   GLU A  79     3436   4496   3607   -795    -18   1216       O  
ATOM    584  CB  GLU A  79      33.413  24.073  -9.449  1.00 35.20           C  
ANISOU  584  CB  GLU A  79     4049   4963   4362   -834   -107   1041       C  
ATOM    585  CG  GLU A  79      34.328  23.122 -10.219  1.00 40.19           C  
ANISOU  585  CG  GLU A  79     4559   5776   4935   -767      4   1104       C  
ATOM    586  CD  GLU A  79      35.750  23.669 -10.452  1.00 42.86           C  
ANISOU  586  CD  GLU A  79     4772   6223   5292   -866      9   1290       C  
ATOM    587  OE1 GLU A  79      36.097  24.757  -9.934  1.00 40.72           O  
ANISOU  587  OE1 GLU A  79     4507   5876   5088  -1004    -88   1372       O  
ATOM    588  OE2 GLU A  79      36.523  22.995 -11.164  1.00 45.99           O  
ANISOU  588  OE2 GLU A  79     5061   6781   5632   -804    107   1358       O  
ATOM    589  N   TRP A  80      31.176  24.431 -11.717  1.00 29.38           N  
ANISOU  589  N   TRP A  80     3472   4187   3504   -692    -67    957       N  
ATOM    590  CA  TRP A  80      30.554  24.197 -13.025  1.00 30.15           C  
ANISOU  590  CA  TRP A  80     3600   4337   3520   -606    -17    943       C  
ATOM    591  C   TRP A  80      30.682  25.428 -13.933  1.00 32.16           C  
ANISOU  591  C   TRP A  80     3871   4593   3757   -676    -46   1071       C  
ATOM    592  O   TRP A  80      31.053  25.307 -15.107  1.00 35.00           O  
ANISOU  592  O   TRP A  80     4190   5069   4039   -641     20   1149       O  
ATOM    593  CB  TRP A  80      29.069  23.815 -12.880  1.00 29.25           C  
ANISOU  593  CB  TRP A  80     3585   4127   3404   -525    -41    790       C  
ATOM    594  CG  TRP A  80      28.392  23.589 -14.216  1.00 30.13           C  
ANISOU  594  CG  TRP A  80     3733   4282   3432   -442     -7    773       C  
ATOM    595  CD1 TRP A  80      27.702  24.507 -14.959  1.00 31.20           C  
ANISOU  595  CD1 TRP A  80     3935   4369   3549   -455    -49    803       C  
ATOM    596  CD2 TRP A  80      28.346  22.361 -14.950  1.00 29.57           C  
ANISOU  596  CD2 TRP A  80     3645   4308   3282   -331     67    720       C  
ATOM    597  NE1 TRP A  80      27.225  23.921 -16.116  1.00 33.00           N  
ANISOU  597  NE1 TRP A  80     4185   4663   3690   -361     -6    773       N  
ATOM    598  CE2 TRP A  80      27.616  22.605 -16.134  1.00 31.83           C  
ANISOU  598  CE2 TRP A  80     3992   4602   3501   -284     64    720       C  
ATOM    599  CE3 TRP A  80      28.852  21.073 -14.719  1.00 30.60           C  
ANISOU  599  CE3 TRP A  80     3725   4512   3388   -262    130    670       C  
ATOM    600  CZ2 TRP A  80      27.386  21.614 -17.088  1.00 30.84           C  
ANISOU  600  CZ2 TRP A  80     3883   4553   3282   -173    116    669       C  
ATOM    601  CZ3 TRP A  80      28.617  20.087 -15.672  1.00 32.24           C  
ANISOU  601  CZ3 TRP A  80     3953   4792   3505   -147    183    619       C  
ATOM    602  CH2 TRP A  80      27.892  20.367 -16.841  1.00 29.77           C  
ANISOU  602  CH2 TRP A  80     3706   4482   3123   -106    173    617       C  
ATOM    603  N   ASP A  81      30.382  26.606 -13.388  1.00 30.99           N  
ANISOU  603  N   ASP A  81     3789   4312   3675   -769   -145   1093       N  
ATOM    604  CA  ASP A  81      30.416  27.848 -14.159  1.00 33.55           C  
ANISOU  604  CA  ASP A  81     4146   4609   3992   -843   -191   1213       C  
ATOM    605  C   ASP A  81      31.816  28.231 -14.590  1.00 36.20           C  
ANISOU  605  C   ASP A  81     4374   5058   4323   -937   -165   1396       C  
ATOM    606  O   ASP A  81      31.996  28.877 -15.621  1.00 38.43           O  
ANISOU  606  O   ASP A  81     4651   5387   4565   -968   -156   1515       O  
ATOM    607  CB  ASP A  81      29.807  29.000 -13.360  1.00 33.99           C  
ANISOU  607  CB  ASP A  81     4309   4482   4124   -916   -314   1188       C  
ATOM    608  CG  ASP A  81      28.322  28.860 -13.198  1.00 33.09           C  
ANISOU  608  CG  ASP A  81     4299   4268   4006   -821   -337   1037       C  
ATOM    609  OD1 ASP A  81      27.721  28.079 -13.968  1.00 29.90           O  
ANISOU  609  OD1 ASP A  81     3891   3930   3539   -718   -273    978       O  
ATOM    610  OD2 ASP A  81      27.755  29.523 -12.303  1.00 35.42           O  
ANISOU  610  OD2 ASP A  81     4679   4419   4359   -846   -423    981       O  
ATOM    611  N   ARG A  82      32.801  27.864 -13.782  1.00 38.37           N  
ANISOU  611  N   ARG A  82     4559   5378   4642   -985   -157   1429       N  
ATOM    612  CA  ARG A  82      34.191  28.091 -14.140  1.00 41.97           C  
ANISOU  612  CA  ARG A  82     4885   5965   5098  -1069   -123   1611       C  
ATOM    613  C   ARG A  82      34.554  27.205 -15.326  1.00 43.49           C  
ANISOU  613  C   ARG A  82     4994   6347   5183   -958     14   1650       C  
ATOM    614  O   ARG A  82      35.155  27.663 -16.299  1.00 43.94           O  
ANISOU  614  O   ARG A  82     4990   6510   5196   -992     54   1804       O  
ATOM    615  CB  ARG A  82      35.115  27.810 -12.956  1.00 41.85           C  
ANISOU  615  CB  ARG A  82     4789   5957   5156  -1136   -150   1627       C  
ATOM    616  CG  ARG A  82      36.588  27.937 -13.289  1.00 46.64           C  
ANISOU  616  CG  ARG A  82     5236   6717   5767  -1218   -111   1822       C  
ATOM    617  CD  ARG A  82      37.480  27.504 -12.134  1.00 49.79           C  
ANISOU  617  CD  ARG A  82     5548   7136   6234  -1267   -135   1829       C  
ATOM    618  NE  ARG A  82      37.695  26.058 -12.094  1.00 50.45           N  
ANISOU  618  NE  ARG A  82     5560   7342   6269  -1129    -22   1748       N  
ATOM    619  CZ  ARG A  82      38.579  25.407 -12.848  1.00 51.99           C  
ANISOU  619  CZ  ARG A  82     5618   7732   6403  -1067     94   1844       C  
ATOM    620  NH1 ARG A  82      39.333  26.067 -13.720  1.00 53.59           N  
ANISOU  620  NH1 ARG A  82     5735   8039   6587  -1126    118   2019       N  
ATOM    621  NH2 ARG A  82      38.703  24.090 -12.735  1.00 51.41           N  
ANISOU  621  NH2 ARG A  82     5502   7744   6285   -932    183   1754       N  
ATOM    622  N   LEU A  83      34.170  25.936 -15.241  1.00 41.83           N  
ANISOU  622  N   LEU A  83     4788   6177   4928   -822     83   1510       N  
ATOM    623  CA  LEU A  83      34.484  24.968 -16.285  1.00 45.62           C  
ANISOU  623  CA  LEU A  83     5210   6825   5299   -694    208   1522       C  
ATOM    624  C   LEU A  83      33.670  25.168 -17.569  1.00 45.10           C  
ANISOU  624  C   LEU A  83     5225   6770   5139   -624    232   1512       C  
ATOM    625  O   LEU A  83      34.180  24.944 -18.664  1.00 46.00           O  
ANISOU  625  O   LEU A  83     5288   7034   5157   -565    321   1600       O  
ATOM    626  CB  LEU A  83      34.274  23.548 -15.757  1.00 46.98           C  
ANISOU  626  CB  LEU A  83     5382   7012   5455   -573    256   1368       C  
ATOM    627  CG  LEU A  83      35.422  22.950 -14.949  1.00 47.85           C  
ANISOU  627  CG  LEU A  83     5372   7202   5606   -589    288   1407       C  
ATOM    628  CD1 LEU A  83      34.989  21.646 -14.304  1.00 45.89           C  
ANISOU  628  CD1 LEU A  83     5156   6924   5355   -479    310   1239       C  
ATOM    629  CD2 LEU A  83      36.629  22.735 -15.850  1.00 48.44           C  
ANISOU  629  CD2 LEU A  83     5314   7480   5609   -556    394   1560       C  
ATOM    630  N   HIS A  84      32.413  25.584 -17.441  1.00 43.80           N  
ANISOU  630  N   HIS A  84     5188   6455   4999   -623    153   1408       N  
ATOM    631  CA  HIS A  84      31.536  25.708 -18.607  1.00 42.96           C  
ANISOU  631  CA  HIS A  84     5166   6351   4808   -551    164   1384       C  
ATOM    632  C   HIS A  84      30.791  27.039 -18.637  1.00 43.31           C  
ANISOU  632  C   HIS A  84     5302   6254   4900   -638     60   1413       C  
ATOM    633  O   HIS A  84      29.572  27.070 -18.450  1.00 40.80           O  
ANISOU  633  O   HIS A  84     5086   5818   4600   -597      4   1289       O  
ATOM    634  CB  HIS A  84      30.511  24.566 -18.640  1.00 39.91           C  
ANISOU  634  CB  HIS A  84     4850   5933   4380   -415    181   1199       C  
ATOM    635  CG  HIS A  84      31.093  23.210 -18.383  1.00 40.57           C  
ANISOU  635  CG  HIS A  84     4869   6113   4433   -326    261   1140       C  
ATOM    636  ND1 HIS A  84      31.160  22.656 -17.122  1.00 41.20           N  
ANISOU  636  ND1 HIS A  84     4927   6134   4592   -339    239   1056       N  
ATOM    637  CD2 HIS A  84      31.621  22.291 -19.225  1.00 42.32           C  
ANISOU  637  CD2 HIS A  84     5052   6481   4547   -214    360   1151       C  
ATOM    638  CE1 HIS A  84      31.714  21.459 -17.196  1.00 41.56           C  
ANISOU  638  CE1 HIS A  84     4921   6283   4588   -244    318   1022       C  
ATOM    639  NE2 HIS A  84      32.003  21.213 -18.461  1.00 43.39           N  
ANISOU  639  NE2 HIS A  84     5143   6638   4705   -163    392   1075       N  
ATOM    640  N   PRO A  85      31.510  28.142 -18.884  1.00 47.25           N  
ANISOU  640  N   PRO A  85     5766   6767   5422   -757     32   1583       N  
ATOM    641  CA  PRO A  85      30.847  29.453 -18.951  1.00 50.57           C  
ANISOU  641  CA  PRO A  85     6283   7044   5886   -838    -74   1619       C  
ATOM    642  C   PRO A  85      29.756  29.482 -20.023  1.00 52.82           C  
ANISOU  642  C   PRO A  85     6663   7318   6090   -745    -70   1567       C  
ATOM    643  O   PRO A  85      29.937  28.878 -21.078  1.00 53.11           O  
ANISOU  643  O   PRO A  85     6669   7492   6018   -660     19   1594       O  
ATOM    644  CB  PRO A  85      31.993  30.411 -19.307  1.00 50.12           C  
ANISOU  644  CB  PRO A  85     6152   7047   5844   -972    -82   1836       C  
ATOM    645  CG  PRO A  85      33.020  29.547 -19.961  1.00 49.60           C  
ANISOU  645  CG  PRO A  85     5955   7196   5696   -917     50   1918       C  
ATOM    646  CD  PRO A  85      32.934  28.220 -19.260  1.00 48.20           C  
ANISOU  646  CD  PRO A  85     5752   7043   5519   -814    100   1761       C  
ATOM    647  N   VAL A  86      28.638  30.151 -19.752  1.00 54.29           N  
ANISOU  647  N   VAL A  86     6961   7344   6321   -752   -165   1493       N  
ATOM    648  CA  VAL A  86      27.580  30.253 -20.752  1.00 57.29           C  
ANISOU  648  CA  VAL A  86     7427   7708   6632   -670   -175   1452       C  
ATOM    649  C   VAL A  86      27.621  31.608 -21.434  1.00 60.95           C  
ANISOU  649  C   VAL A  86     7939   8129   7092   -754   -234   1597       C  
ATOM    650  O   VAL A  86      27.896  32.629 -20.808  1.00 61.17           O  
ANISOU  650  O   VAL A  86     7987   8050   7205   -869   -316   1666       O  
ATOM    651  CB  VAL A  86      26.172  30.026 -20.149  1.00 56.49           C  
ANISOU  651  CB  VAL A  86     7415   7474   6574   -600   -237   1275       C  
ATOM    652  CG1 VAL A  86      26.109  28.673 -19.451  1.00 55.26           C  
ANISOU  652  CG1 VAL A  86     7215   7356   6426   -526   -185   1140       C  
ATOM    653  CG2 VAL A  86      25.791  31.155 -19.195  1.00 55.44           C  
ANISOU  653  CG2 VAL A  86     7351   7169   6547   -682   -348   1271       C  
ATOM    654  N   HIS A  87      27.355  31.608 -22.731  1.00 66.02           N  
ANISOU  654  N   HIS A  87     8606   8849   7631   -695   -198   1643       N  
ATOM    655  CA  HIS A  87      27.401  32.838 -23.494  1.00 70.92           C  
ANISOU  655  CA  HIS A  87     9271   9439   8235   -768   -247   1791       C  
ATOM    656  C   HIS A  87      26.216  33.727 -23.164  1.00 72.10           C  
ANISOU  656  C   HIS A  87     9546   9399   8451   -776   -370   1724       C  
ATOM    657  O   HIS A  87      25.060  33.325 -23.318  1.00 71.14           O  
ANISOU  657  O   HIS A  87     9487   9235   8306   -672   -387   1591       O  
ATOM    658  CB  HIS A  87      27.449  32.538 -24.991  1.00 73.59           C  
ANISOU  658  CB  HIS A  87     9605   9924   8431   -691   -169   1858       C  
ATOM    659  CG  HIS A  87      28.831  32.570 -25.561  1.00 76.06           C  
ANISOU  659  CG  HIS A  87     9809  10405   8687   -744    -78   2040       C  
ATOM    660  ND1 HIS A  87      29.241  33.527 -26.463  1.00 78.40           N  
ANISOU  660  ND1 HIS A  87    10107  10744   8939   -815    -82   2228       N  
ATOM    661  CD2 HIS A  87      29.904  31.774 -25.341  1.00 76.41           C  
ANISOU  661  CD2 HIS A  87     9731  10590   8712   -736     20   2074       C  
ATOM    662  CE1 HIS A  87      30.505  33.314 -26.783  1.00 79.38           C  
ANISOU  662  CE1 HIS A  87    10106  11036   9018   -849     15   2374       C  
ATOM    663  NE2 HIS A  87      30.931  32.256 -26.117  1.00 78.07           N  
ANISOU  663  NE2 HIS A  87     9862  10934   8867   -798     79   2282       N  
ATOM    664  N   ALA A  88      26.519  34.934 -22.697  1.00 74.02           N  
ANISOU  664  N   ALA A  88     9823   9527   8776   -900   -460   1820       N  
ATOM    665  CA  ALA A  88      25.503  35.948 -22.470  1.00 75.08           C  
ANISOU  665  CA  ALA A  88    10084   9478   8966   -907   -580   1783       C  
ATOM    666  C   ALA A  88      24.992  36.446 -23.814  1.00 76.69           C  
ANISOU  666  C   ALA A  88    10348   9705   9087   -872   -590   1857       C  
ATOM    667  O   ALA A  88      25.470  36.016 -24.866  1.00 77.68           O  
ANISOU  667  O   ALA A  88    10418   9988   9109   -846   -503   1939       O  
ATOM    668  CB  ALA A  88      26.062  37.097 -21.644  1.00 76.35           C  
ANISOU  668  CB  ALA A  88    10278   9504   9229  -1050   -681   1871       C  
ATOM    669  N   GLY A  89      24.027  37.359 -23.777  1.00 76.75           N  
ANISOU  669  N   GLY A  89    10472   9558   9133   -862   -696   1831       N  
ATOM    670  CA  GLY A  89      23.387  37.835 -24.990  1.00 76.00           C  
ANISOU  670  CA  GLY A  89    10446   9469   8964   -818   -719   1886       C  
ATOM    671  C   GLY A  89      22.146  37.008 -25.263  1.00 73.93           C  
ANISOU  671  C   GLY A  89    10211   9222   8656   -667   -703   1723       C  
ATOM    672  O   GLY A  89      22.016  35.899 -24.741  1.00 73.56           O  
ANISOU  672  O   GLY A  89    10109   9228   8613   -603   -646   1595       O  
ATOM    673  N   PRO A  90      21.224  37.538 -26.081  1.00 71.90           N  
ANISOU  673  N   PRO A  90    10039   8919   8359   -613   -760   1732       N  
ATOM    674  CA  PRO A  90      19.977  36.811 -26.340  1.00 67.48           C  
ANISOU  674  CA  PRO A  90     9505   8369   7767   -478   -763   1585       C  
ATOM    675  C   PRO A  90      20.249  35.503 -27.076  1.00 60.99           C  
ANISOU  675  C   PRO A  90     8615   7723   6834   -409   -657   1550       C  
ATOM    676  O   PRO A  90      21.053  35.483 -28.014  1.00 61.30           O  
ANISOU  676  O   PRO A  90     8629   7883   6779   -432   -597   1671       O  
ATOM    677  CB  PRO A  90      19.179  37.783 -27.211  1.00 70.12           C  
ANISOU  677  CB  PRO A  90     9939   8632   8072   -454   -848   1645       C  
ATOM    678  CG  PRO A  90      20.226  38.589 -27.915  1.00 72.78           C  
ANISOU  678  CG  PRO A  90    10279   9008   8366   -560   -839   1843       C  
ATOM    679  CD  PRO A  90      21.347  38.745 -26.918  1.00 73.45           C  
ANISOU  679  CD  PRO A  90    10304   9073   8530   -675   -820   1892       C  
ATOM    680  N   ILE A  91      19.603  34.421 -26.659  1.00 53.72           N  
ANISOU  680  N   ILE A  91     7669   6819   5922   -322   -636   1392       N  
ATOM    681  CA  ILE A  91      19.837  33.156 -27.333  1.00 49.29           C  
ANISOU  681  CA  ILE A  91     7063   6408   5256   -250   -549   1348       C  
ATOM    682  C   ILE A  91      18.964  33.063 -28.578  1.00 46.60           C  
ANISOU  682  C   ILE A  91     6789   6101   4816   -165   -582   1337       C  
ATOM    683  O   ILE A  91      18.001  33.814 -28.733  1.00 43.80           O  
ANISOU  683  O   ILE A  91     6502   5647   4493   -149   -673   1332       O  
ATOM    684  CB  ILE A  91      19.573  31.956 -26.422  1.00 46.64           C  
ANISOU  684  CB  ILE A  91     6676   6078   4967   -200   -518   1191       C  
ATOM    685  CG1 ILE A  91      20.186  30.696 -27.041  1.00 45.35           C  
ANISOU  685  CG1 ILE A  91     6466   6070   4694   -142   -421   1170       C  
ATOM    686  CG2 ILE A  91      18.089  31.800 -26.153  1.00 44.10           C  
ANISOU  686  CG2 ILE A  91     6398   5664   4694   -128   -596   1062       C  
ATOM    687  CD1 ILE A  91      19.720  29.439 -26.424  1.00 42.52           C  
ANISOU  687  CD1 ILE A  91     6080   5714   4363    -77   -406   1013       C  
ATOM    688  N   ALA A  92      19.327  32.146 -29.468  1.00 44.72           N  
ANISOU  688  N   ALA A  92     6536   6004   4453   -104   -509   1335       N  
ATOM    689  CA  ALA A  92      18.618  31.957 -30.722  1.00 43.45           C  
ANISOU  689  CA  ALA A  92     6443   5888   4177    -20   -538   1325       C  
ATOM    690  C   ALA A  92      17.197  31.464 -30.466  1.00 39.60           C  
ANISOU  690  C   ALA A  92     5988   5321   3737     53   -620   1171       C  
ATOM    691  O   ALA A  92      16.977  30.592 -29.619  1.00 36.35           O  
ANISOU  691  O   ALA A  92     5532   4893   3388     74   -608   1050       O  
ATOM    692  CB  ALA A  92      19.374  30.981 -31.616  1.00 44.14           C  
ANISOU  692  CB  ALA A  92     6514   6142   4114     41   -439   1341       C  
ATOM    693  N   PRO A  93      16.226  32.050 -31.183  1.00 37.84           N  
ANISOU  693  N   PRO A  93     5839   5050   3490     88   -708   1185       N  
ATOM    694  CA  PRO A  93      14.803  31.699 -31.093  1.00 36.28           C  
ANISOU  694  CA  PRO A  93     5665   4785   3333    156   -798   1062       C  
ATOM    695  C   PRO A  93      14.553  30.201 -31.299  1.00 36.04           C  
ANISOU  695  C   PRO A  93     5620   4829   3246    228   -777    939       C  
ATOM    696  O   PRO A  93      14.934  29.628 -32.336  1.00 33.91           O  
ANISOU  696  O   PRO A  93     5385   4662   2836    275   -741    955       O  
ATOM    697  CB  PRO A  93      14.167  32.523 -32.221  1.00 38.00           C  
ANISOU  697  CB  PRO A  93     5966   4987   3484    183   -877   1137       C  
ATOM    698  CG  PRO A  93      15.064  33.715 -32.358  1.00 38.97           C  
ANISOU  698  CG  PRO A  93     6105   5097   3602    102   -852   1297       C  
ATOM    699  CD  PRO A  93      16.461  33.203 -32.070  1.00 39.65           C  
ANISOU  699  CD  PRO A  93     6125   5280   3660     54   -732   1336       C  
ATOM    700  N   GLY A  94      13.929  29.584 -30.297  1.00 37.17           N  
ANISOU  700  N   GLY A  94     5715   4913   3493    237   -799    820       N  
ATOM    701  CA  GLY A  94      13.498  28.201 -30.377  1.00 37.43           C  
ANISOU  701  CA  GLY A  94     5739   4987   3497    296   -805    698       C  
ATOM    702  C   GLY A  94      14.597  27.217 -30.064  1.00 36.28           C  
ANISOU  702  C   GLY A  94     5552   4919   3314    293   -701    669       C  
ATOM    703  O   GLY A  94      14.393  26.004 -30.154  1.00 37.80           O  
ANISOU  703  O   GLY A  94     5746   5143   3471    343   -702    571       O  
ATOM    704  N   GLN A  95      15.768  27.733 -29.694  1.00 35.54           N  
ANISOU  704  N   GLN A  95     5422   4854   3230    235   -619    759       N  
ATOM    705  CA  GLN A  95      16.920  26.877 -29.489  1.00 33.10           C  
ANISOU  705  CA  GLN A  95     5067   4634   2876    238   -515    752       C  
ATOM    706  C   GLN A  95      17.208  26.654 -28.019  1.00 31.62           C  
ANISOU  706  C   GLN A  95     4801   4394   2818    186   -485    703       C  
ATOM    707  O   GLN A  95      16.866  27.460 -27.155  1.00 31.14           O  
ANISOU  707  O   GLN A  95     4722   4237   2873    131   -524    714       O  
ATOM    708  CB  GLN A  95      18.166  27.454 -30.174  1.00 38.85           C  
ANISOU  708  CB  GLN A  95     5792   5460   3509    211   -433    898       C  
ATOM    709  CG  GLN A  95      17.979  27.789 -31.646  1.00 42.24           C  
ANISOU  709  CG  GLN A  95     6303   5950   3798    260   -454    967       C  
ATOM    710  CD  GLN A  95      17.401  26.633 -32.439  1.00 43.39           C  
ANISOU  710  CD  GLN A  95     6511   6142   3835    367   -480    858       C  
ATOM    711  OE1 GLN A  95      18.005  25.560 -32.531  1.00 43.85           O  
ANISOU  711  OE1 GLN A  95     6559   6279   3821    422   -412    807       O  
ATOM    712  NE2 GLN A  95      16.209  26.838 -32.994  1.00 42.60           N  
ANISOU  712  NE2 GLN A  95     6478   5983   3723    399   -588    821       N  
ATOM    713  N   MET A  96      17.865  25.542 -27.744  1.00 31.83           N  
ANISOU  713  N   MET A  96     4791   4485   2818    212   -415    649       N  
ATOM    714  CA  MET A  96      18.213  25.185 -26.385  1.00 29.76           C  
ANISOU  714  CA  MET A  96     4457   4185   2665    169   -382    601       C  
ATOM    715  C   MET A  96      19.390  26.020 -25.896  1.00 31.53           C  
ANISOU  715  C   MET A  96     4629   4426   2924     87   -323    716       C  
ATOM    716  O   MET A  96      20.400  26.145 -26.596  1.00 29.84           O  
ANISOU  716  O   MET A  96     4404   4314   2621     84   -256    815       O  
ATOM    717  CB  MET A  96      18.531  23.696 -26.324  1.00 31.14           C  
ANISOU  717  CB  MET A  96     4617   4421   2795    230   -335    508       C  
ATOM    718  CG  MET A  96      19.021  23.185 -24.990  1.00 32.07           C  
ANISOU  718  CG  MET A  96     4661   4516   3008    194   -292    463       C  
ATOM    719  SD  MET A  96      19.244  21.399 -25.083  1.00 43.65           S  
ANISOU  719  SD  MET A  96     6133   6041   4411    279   -254    350       S  
ATOM    720  CE  MET A  96      20.517  21.274 -26.343  1.00 42.82           C  
ANISOU  720  CE  MET A  96     6047   6087   4136    339   -159    441       C  
ATOM    721  N   ARG A  97      19.258  26.600 -24.699  1.00 29.85           N  
ANISOU  721  N   ARG A  97     4385   4117   2838     20   -352    709       N  
ATOM    722  CA  ARG A  97      20.337  27.388 -24.128  1.00 33.61           C  
ANISOU  722  CA  ARG A  97     4818   4593   3361    -70   -316    813       C  
ATOM    723  C   ARG A  97      21.240  26.477 -23.301  1.00 32.46           C  
ANISOU  723  C   ARG A  97     4597   4498   3239    -79   -243    777       C  
ATOM    724  O   ARG A  97      20.887  25.343 -23.015  1.00 34.86           O  
ANISOU  724  O   ARG A  97     4891   4811   3542    -20   -231    665       O  
ATOM    725  CB  ARG A  97      19.793  28.554 -23.282  1.00 33.56           C  
ANISOU  725  CB  ARG A  97     4837   4448   3468   -132   -394    825       C  
ATOM    726  CG  ARG A  97      18.963  28.150 -22.073  1.00 29.92           C  
ANISOU  726  CG  ARG A  97     4364   3898   3107   -113   -429    699       C  
ATOM    727  CD  ARG A  97      18.384  29.366 -21.329  1.00 32.19           C  
ANISOU  727  CD  ARG A  97     4692   4051   3488   -151   -505    710       C  
ATOM    728  NE  ARG A  97      17.702  28.976 -20.089  1.00 32.77           N  
ANISOU  728  NE  ARG A  97     4747   4054   3649   -128   -522    599       N  
ATOM    729  CZ  ARG A  97      18.296  28.891 -18.900  1.00 31.91           C  
ANISOU  729  CZ  ARG A  97     4605   3918   3603   -172   -498    581       C  
ATOM    730  NH1 ARG A  97      19.588  29.172 -18.769  1.00 31.34           N  
ANISOU  730  NH1 ARG A  97     4507   3877   3524   -249   -464    666       N  
ATOM    731  NH2 ARG A  97      17.598  28.519 -17.842  1.00 31.10           N  
ANISOU  731  NH2 ARG A  97     4489   3760   3567   -141   -510    483       N  
ATOM    732  N   GLU A  98      22.419  26.965 -22.951  1.00 31.11           N  
ANISOU  732  N   GLU A  98     4371   4360   3087   -156   -200    881       N  
ATOM    733  CA  GLU A  98      23.338  26.200 -22.126  1.00 30.38           C  
ANISOU  733  CA  GLU A  98     4202   4317   3025   -170   -137    861       C  
ATOM    734  C   GLU A  98      22.981  26.409 -20.651  1.00 31.18           C  
ANISOU  734  C   GLU A  98     4295   4297   3255   -220   -187    793       C  
ATOM    735  O   GLU A  98      22.702  27.527 -20.232  1.00 32.54           O  
ANISOU  735  O   GLU A  98     4501   4370   3493   -283   -252    831       O  
ATOM    736  CB  GLU A  98      24.798  26.605 -22.388  1.00 31.91           C  
ANISOU  736  CB  GLU A  98     4326   4612   3185   -232    -71   1013       C  
ATOM    737  CG  GLU A  98      25.228  26.641 -23.863  1.00 38.01           C  
ANISOU  737  CG  GLU A  98     5106   5513   3824   -189    -15   1111       C  
ATOM    738  CD  GLU A  98      26.310  27.686 -24.129  1.00 45.31           C  
ANISOU  738  CD  GLU A  98     5979   6491   4747   -289      8   1300       C  
ATOM    739  OE1 GLU A  98      27.493  27.296 -24.232  1.00 47.72           O  
ANISOU  739  OE1 GLU A  98     6195   6925   5013   -293     97   1380       O  
ATOM    740  OE2 GLU A  98      25.982  28.899 -24.236  1.00 46.98           O  
ANISOU  740  OE2 GLU A  98     6237   6616   4998   -365    -64   1374       O  
ATOM    741  N   PRO A  99      22.978  25.326 -19.862  1.00 31.42           N  
ANISOU  741  N   PRO A  99     4289   4333   3315   -185   -158    692       N  
ATOM    742  CA  PRO A  99      22.700  25.450 -18.425  1.00 29.94           C  
ANISOU  742  CA  PRO A  99     4093   4044   3237   -226   -196    630       C  
ATOM    743  C   PRO A  99      23.930  25.906 -17.629  1.00 30.08           C  
ANISOU  743  C   PRO A  99     4056   4068   3304   -317   -179    712       C  
ATOM    744  O   PRO A  99      25.033  25.410 -17.869  1.00 28.73           O  
ANISOU  744  O   PRO A  99     3818   4006   3091   -323   -110    769       O  
ATOM    745  CB  PRO A  99      22.281  24.028 -18.024  1.00 28.27           C  
ANISOU  745  CB  PRO A  99     3864   3850   3026   -153   -169    504       C  
ATOM    746  CG  PRO A  99      22.968  23.144 -19.006  1.00 32.52           C  
ANISOU  746  CG  PRO A  99     4379   4514   3461    -96   -100    523       C  
ATOM    747  CD  PRO A  99      23.021  23.922 -20.305  1.00 30.87           C  
ANISOU  747  CD  PRO A  99     4206   4350   3173    -94   -103    618       C  
ATOM    748  N   ARG A 100      23.744  26.853 -16.711  1.00 28.62           N  
ANISOU  748  N   ARG A 100     3901   3770   3203   -384   -244    719       N  
ATOM    749  CA  ARG A 100      24.798  27.175 -15.765  1.00 33.04           C  
ANISOU  749  CA  ARG A 100     4417   4318   3820   -472   -247    775       C  
ATOM    750  C   ARG A 100      24.477  26.493 -14.437  1.00 25.73           C  
ANISOU  750  C   ARG A 100     3483   3338   2954   -450   -251    658       C  
ATOM    751  O   ARG A 100      23.456  25.810 -14.322  1.00 23.05           O  
ANISOU  751  O   ARG A 100     3167   2977   2614   -372   -249    549       O  
ATOM    752  CB  ARG A 100      24.963  28.691 -15.605  1.00 45.14           C  
ANISOU  752  CB  ARG A 100     6000   5754   5398   -568   -327    869       C  
ATOM    753  CG  ARG A 100      23.702  29.456 -15.286  1.00 53.34           C  
ANISOU  753  CG  ARG A 100     7138   6652   6477   -543   -409    803       C  
ATOM    754  CD  ARG A 100      23.841  30.923 -15.726  1.00 60.79           C  
ANISOU  754  CD  ARG A 100     8144   7521   7432   -619   -482    917       C  
ATOM    755  NE  ARG A 100      24.356  31.791 -14.667  1.00 63.51           N  
ANISOU  755  NE  ARG A 100     8522   7759   7851   -712   -554    951       N  
ATOM    756  CZ  ARG A 100      25.646  32.038 -14.443  1.00 66.02           C  
ANISOU  756  CZ  ARG A 100     8786   8110   8188   -819   -557   1058       C  
ATOM    757  NH1 ARG A 100      26.581  31.476 -15.198  1.00 67.59           N  
ANISOU  757  NH1 ARG A 100     8885   8459   8337   -839   -476   1146       N  
ATOM    758  NH2 ARG A 100      26.003  32.849 -13.455  1.00 66.78           N  
ANISOU  758  NH2 ARG A 100     8930   8090   8352   -904   -642   1078       N  
ATOM    759  N   GLY A 101      25.343  26.671 -13.446  1.00 25.36           N  
ANISOU  759  N   GLY A 101     3403   3273   2959   -522   -261    689       N  
ATOM    760  CA  GLY A 101      25.215  25.953 -12.185  1.00 23.26           C  
ANISOU  760  CA  GLY A 101     3124   2973   2740   -502   -257    591       C  
ATOM    761  C   GLY A 101      23.832  26.089 -11.581  1.00 24.50           C  
ANISOU  761  C   GLY A 101     3354   3023   2932   -449   -302    482       C  
ATOM    762  O   GLY A 101      23.229  25.100 -11.164  1.00 26.19           O  
ANISOU  762  O   GLY A 101     3555   3246   3151   -384   -274    385       O  
ATOM    763  N   SER A 102      23.308  27.314 -11.571  1.00 25.87           N  
ANISOU  763  N   SER A 102     3604   3096   3130   -473   -374    505       N  
ATOM    764  CA  SER A 102      22.002  27.579 -10.971  1.00 26.06           C  
ANISOU  764  CA  SER A 102     3695   3022   3187   -414   -415    413       C  
ATOM    765  C   SER A 102      20.845  26.922 -11.724  1.00 23.63           C  
ANISOU  765  C   SER A 102     3382   2748   2847   -322   -391    349       C  
ATOM    766  O   SER A 102      19.780  26.684 -11.140  1.00 23.36           O  
ANISOU  766  O   SER A 102     3366   2669   2841   -261   -402    264       O  
ATOM    767  CB  SER A 102      21.750  29.092 -10.886  1.00 26.54           C  
ANISOU  767  CB  SER A 102     3847   2964   3273   -451   -501    457       C  
ATOM    768  OG  SER A 102      21.698  29.671 -12.177  1.00 29.03           O  
ANISOU  768  OG  SER A 102     4180   3300   3551   -461   -515    536       O  
ATOM    769  N   ASP A 103      21.024  26.665 -13.021  1.00 23.02           N  
ANISOU  769  N   ASP A 103     3284   2752   2711   -311   -364    396       N  
ATOM    770  CA  ASP A 103      20.004  25.946 -13.792  1.00 23.14           C  
ANISOU  770  CA  ASP A 103     3298   2803   2691   -230   -351    337       C  
ATOM    771  C   ASP A 103      20.015  24.467 -13.397  1.00 21.29           C  
ANISOU  771  C   ASP A 103     3008   2626   2454   -190   -298    258       C  
ATOM    772  O   ASP A 103      18.967  23.850 -13.244  1.00 24.48           O  
ANISOU  772  O   ASP A 103     3412   3016   2874   -134   -307    179       O  
ATOM    773  CB  ASP A 103      20.233  26.088 -15.309  1.00 25.06           C  
ANISOU  773  CB  ASP A 103     3548   3116   2858   -224   -341    408       C  
ATOM    774  CG  ASP A 103      20.092  27.536 -15.802  1.00 25.87           C  
ANISOU  774  CG  ASP A 103     3712   3156   2962   -260   -400    490       C  
ATOM    775  OD1 ASP A 103      19.086  28.208 -15.452  1.00 24.51           O  
ANISOU  775  OD1 ASP A 103     3592   2888   2831   -234   -459    454       O  
ATOM    776  OD2 ASP A 103      21.001  27.998 -16.526  1.00 27.77           O  
ANISOU  776  OD2 ASP A 103     3947   3445   3161   -311   -387    596       O  
ATOM    777  N   ILE A 104      21.212  23.915 -13.229  1.00 20.93           N  
ANISOU  777  N   ILE A 104     2913   2647   2391   -221   -248    288       N  
ATOM    778  CA  ILE A 104      21.378  22.510 -12.856  1.00 21.06           C  
ANISOU  778  CA  ILE A 104     2884   2715   2404   -184   -200    221       C  
ATOM    779  C   ILE A 104      20.817  22.256 -11.446  1.00 22.05           C  
ANISOU  779  C   ILE A 104     3007   2772   2599   -181   -215    146       C  
ATOM    780  O   ILE A 104      20.212  21.210 -11.180  1.00 24.60           O  
ANISOU  780  O   ILE A 104     3313   3102   2931   -135   -201     71       O  
ATOM    781  CB  ILE A 104      22.859  22.107 -12.949  1.00 22.52           C  
ANISOU  781  CB  ILE A 104     3013   2988   2557   -214   -143    281       C  
ATOM    782  CG1 ILE A 104      23.289  22.077 -14.423  1.00 25.08           C  
ANISOU  782  CG1 ILE A 104     3333   3402   2793   -189   -111    345       C  
ATOM    783  CG2 ILE A 104      23.143  20.756 -12.244  1.00 25.90           C  
ANISOU  783  CG2 ILE A 104     3397   3448   2995   -182   -101    213       C  
ATOM    784  CD1 ILE A 104      24.769  22.222 -14.604  1.00 28.13           C  
ANISOU  784  CD1 ILE A 104     3661   3876   3152   -233    -62    448       C  
ATOM    785  N   ALA A 105      21.002  23.230 -10.558  1.00 23.72           N  
ANISOU  785  N   ALA A 105     3243   2914   2857   -229   -247    169       N  
ATOM    786  CA  ALA A 105      20.494  23.137  -9.192  1.00 21.96           C  
ANISOU  786  CA  ALA A 105     3030   2627   2688   -219   -260    104       C  
ATOM    787  C   ALA A 105      19.012  23.488  -9.159  1.00 23.47           C  
ANISOU  787  C   ALA A 105     3258   2759   2901   -163   -294     55       C  
ATOM    788  O   ALA A 105      18.380  23.434  -8.106  1.00 25.19           O  
ANISOU  788  O   ALA A 105     3483   2931   3156   -136   -299      2       O  
ATOM    789  CB  ALA A 105      21.305  24.071  -8.242  1.00 20.27           C  
ANISOU  789  CB  ALA A 105     2841   2354   2505   -286   -291    145       C  
ATOM    790  N   GLY A 106      18.469  23.868 -10.319  1.00 24.55           N  
ANISOU  790  N   GLY A 106     3415   2903   3009   -140   -317     78       N  
ATOM    791  CA  GLY A 106      17.049  24.129 -10.457  1.00 25.97           C  
ANISOU  791  CA  GLY A 106     3616   3043   3207    -82   -350     40       C  
ATOM    792  C   GLY A 106      16.547  25.410  -9.817  1.00 27.77           C  
ANISOU  792  C   GLY A 106     3903   3178   3469    -71   -397     45       C  
ATOM    793  O   GLY A 106      15.354  25.531  -9.514  1.00 32.24           O  
ANISOU  793  O   GLY A 106     4475   3713   4062     -9   -413      3       O  
ATOM    794  N   THR A 107      17.437  26.374  -9.615  1.00 25.28           N  
ANISOU  794  N   THR A 107     3634   2817   3154   -128   -422    100       N  
ATOM    795  CA  THR A 107      17.054  27.643  -9.004  1.00 27.50           C  
ANISOU  795  CA  THR A 107     3994   2992   3461   -117   -477    102       C  
ATOM    796  C   THR A 107      16.641  28.672 -10.057  1.00 31.27           C  
ANISOU  796  C   THR A 107     4526   3433   3923   -108   -530    155       C  
ATOM    797  O   THR A 107      15.822  29.560  -9.798  1.00 32.91           O  
ANISOU  797  O   THR A 107     4796   3559   4149    -57   -576    140       O  
ATOM    798  CB  THR A 107      18.201  28.224  -8.151  1.00 31.24           C  
ANISOU  798  CB  THR A 107     4507   3415   3948   -191   -500    134       C  
ATOM    799  OG1 THR A 107      19.328  28.529  -8.986  1.00 32.62           O  
ANISOU  799  OG1 THR A 107     4672   3621   4100   -276   -508    227       O  
ATOM    800  CG2 THR A 107      18.624  27.221  -7.085  1.00 30.60           C  
ANISOU  800  CG2 THR A 107     4376   3371   3881   -198   -453     85       C  
ATOM    801  N   THR A 108      17.205  28.539 -11.252  1.00 29.08           N  
ANISOU  801  N   THR A 108     4226   3217   3605   -148   -520    218       N  
ATOM    802  CA  THR A 108      16.972  29.514 -12.309  1.00 30.22           C  
ANISOU  802  CA  THR A 108     4423   3332   3726   -151   -569    283       C  
ATOM    803  C   THR A 108      16.503  28.868 -13.600  1.00 29.14           C  
ANISOU  803  C   THR A 108     4249   3279   3542   -114   -549    288       C  
ATOM    804  O   THR A 108      16.518  29.504 -14.648  1.00 30.05           O  
ANISOU  804  O   THR A 108     4400   3396   3623   -124   -579    354       O  
ATOM    805  CB  THR A 108      18.250  30.329 -12.611  1.00 30.86           C  
ANISOU  805  CB  THR A 108     4534   3396   3794   -250   -592    387       C  
ATOM    806  OG1 THR A 108      19.287  29.439 -13.037  1.00 26.74           O  
ANISOU  806  OG1 THR A 108     3937   2987   3238   -296   -528    423       O  
ATOM    807  CG2 THR A 108      18.726  31.090 -11.363  1.00 32.61           C  
ANISOU  807  CG2 THR A 108     4811   3517   4063   -296   -636    386       C  
ATOM    808  N   SER A 109      16.101  27.603 -13.535  1.00 27.44           N  
ANISOU  808  N   SER A 109     3972   3131   3323    -73   -506    220       N  
ATOM    809  CA  SER A 109      15.572  26.933 -14.718  1.00 28.97           C  
ANISOU  809  CA  SER A 109     4144   3393   3471    -34   -502    213       C  
ATOM    810  C   SER A 109      14.154  26.433 -14.479  1.00 31.89           C  
ANISOU  810  C   SER A 109     4489   3753   3875     38   -522    138       C  
ATOM    811  O   SER A 109      13.778  26.129 -13.348  1.00 30.10           O  
ANISOU  811  O   SER A 109     4235   3501   3699     56   -507     84       O  
ATOM    812  CB  SER A 109      16.462  25.759 -15.116  1.00 29.21           C  
ANISOU  812  CB  SER A 109     4127   3520   3453    -54   -443    211       C  
ATOM    813  OG  SER A 109      16.508  24.799 -14.064  1.00 31.09           O  
ANISOU  813  OG  SER A 109     4317   3767   3729    -49   -406    143       O  
ATOM    814  N   THR A 110      13.372  26.339 -15.550  1.00 31.14           N  
ANISOU  814  N   THR A 110     4399   3682   3750     76   -557    141       N  
ATOM    815  CA  THR A 110      12.019  25.813 -15.447  1.00 29.16           C  
ANISOU  815  CA  THR A 110     4111   3433   3535    136   -584     84       C  
ATOM    816  C   THR A 110      12.023  24.289 -15.587  1.00 28.21           C  
ANISOU  816  C   THR A 110     3938   3379   3400    134   -557     33       C  
ATOM    817  O   THR A 110      13.013  23.706 -16.027  1.00 24.65           O  
ANISOU  817  O   THR A 110     3492   2977   2896    104   -522     43       O  
ATOM    818  CB  THR A 110      11.107  26.425 -16.519  1.00 27.49           C  
ANISOU  818  CB  THR A 110     3930   3212   3304    177   -650    113       C  
ATOM    819  OG1 THR A 110      11.537  25.992 -17.811  1.00 27.50           O  
ANISOU  819  OG1 THR A 110     3950   3273   3225    162   -655    139       O  
ATOM    820  CG2 THR A 110      11.141  27.950 -16.452  1.00 27.59           C  
ANISOU  820  CG2 THR A 110     4008   3148   3328    180   -684    168       C  
ATOM    821  N   LEU A 111      10.917  23.640 -15.228  1.00 28.90           N  
ANISOU  821  N   LEU A 111     3975   3469   3535    168   -577    -15       N  
ATOM    822  CA  LEU A 111      10.816  22.198 -15.425  1.00 27.63           C  
ANISOU  822  CA  LEU A 111     3777   3357   3366    163   -572    -61       C  
ATOM    823  C   LEU A 111      10.934  21.877 -16.916  1.00 26.43           C  
ANISOU  823  C   LEU A 111     3665   3244   3133    169   -608    -49       C  
ATOM    824  O   LEU A 111      11.579  20.904 -17.305  1.00 24.12           O  
ANISOU  824  O   LEU A 111     3382   2992   2790    158   -587    -72       O  
ATOM    825  CB  LEU A 111       9.501  21.651 -14.868  1.00 27.62           C  
ANISOU  825  CB  LEU A 111     3710   3350   3435    189   -601    -98       C  
ATOM    826  CG  LEU A 111       9.219  20.205 -15.297  1.00 29.67           C  
ANISOU  826  CG  LEU A 111     3942   3645   3685    177   -626   -138       C  
ATOM    827  CD1 LEU A 111      10.245  19.261 -14.695  1.00 28.34           C  
ANISOU  827  CD1 LEU A 111     3770   3492   3507    145   -566   -168       C  
ATOM    828  CD2 LEU A 111       7.788  19.753 -14.947  1.00 30.56           C  
ANISOU  828  CD2 LEU A 111     3981   3758   3873    193   -673   -152       C  
ATOM    829  N   GLN A 112      10.305  22.700 -17.750  1.00 28.63           N  
ANISOU  829  N   GLN A 112     3975   3510   3392    194   -664    -14       N  
ATOM    830  CA  GLN A 112      10.355  22.483 -19.190  1.00 29.91           C  
ANISOU  830  CA  GLN A 112     4186   3710   3468    206   -704      0       C  
ATOM    831  C   GLN A 112      11.791  22.529 -19.737  1.00 25.97           C  
ANISOU  831  C   GLN A 112     3734   3253   2882    185   -647     37       C  
ATOM    832  O   GLN A 112      12.158  21.718 -20.585  1.00 27.15           O  
ANISOU  832  O   GLN A 112     3912   3452   2952    199   -645     20       O  
ATOM    833  CB  GLN A 112       9.492  23.510 -19.914  1.00 37.83           C  
ANISOU  833  CB  GLN A 112     5217   4689   4467    237   -773     42       C  
ATOM    834  CG  GLN A 112       9.230  23.147 -21.362  1.00 43.47           C  
ANISOU  834  CG  GLN A 112     5978   5441   5097    258   -832     46       C  
ATOM    835  CD  GLN A 112       8.437  21.854 -21.494  1.00 50.78           C  
ANISOU  835  CD  GLN A 112     6873   6382   6039    266   -885    -19       C  
ATOM    836  OE1 GLN A 112       7.323  21.740 -20.974  1.00 55.03           O  
ANISOU  836  OE1 GLN A 112     7349   6898   6662    274   -929    -36       O  
ATOM    837  NE2 GLN A 112       9.014  20.868 -22.179  1.00 50.72           N  
ANISOU  837  NE2 GLN A 112     6908   6413   5950    267   -881    -50       N  
ATOM    838  N   GLU A 113      12.589  23.484 -19.275  1.00 24.79           N  
ANISOU  838  N   GLU A 113     3593   3084   2743    154   -604     90       N  
ATOM    839  CA  GLU A 113      13.997  23.560 -19.680  1.00 26.68           C  
ANISOU  839  CA  GLU A 113     3855   3372   2910    124   -544    142       C  
ATOM    840  C   GLU A 113      14.767  22.329 -19.182  1.00 26.87           C  
ANISOU  840  C   GLU A 113     3842   3440   2926    118   -483     95       C  
ATOM    841  O   GLU A 113      15.563  21.738 -19.921  1.00 26.97           O  
ANISOU  841  O   GLU A 113     3871   3520   2854    131   -447    105       O  
ATOM    842  CB  GLU A 113      14.650  24.846 -19.159  1.00 27.65           C  
ANISOU  842  CB  GLU A 113     3988   3453   3063     77   -527    214       C  
ATOM    843  CG  GLU A 113      14.079  26.137 -19.777  1.00 30.41           C  
ANISOU  843  CG  GLU A 113     4390   3756   3409     85   -587    274       C  
ATOM    844  CD  GLU A 113      14.592  27.411 -19.111  1.00 30.64           C  
ANISOU  844  CD  GLU A 113     4443   3717   3483     36   -590    336       C  
ATOM    845  OE1 GLU A 113      14.877  27.376 -17.895  1.00 28.34           O  
ANISOU  845  OE1 GLU A 113     4126   3389   3253     12   -566    306       O  
ATOM    846  OE2 GLU A 113      14.705  28.456 -19.804  1.00 31.80           O  
ANISOU  846  OE2 GLU A 113     4642   3841   3601     21   -623    415       O  
ATOM    847  N   GLN A 114      14.537  21.942 -17.928  1.00 25.70           N  
ANISOU  847  N   GLN A 114     3648   3256   2861    104   -470     46       N  
ATOM    848  CA  GLN A 114      15.176  20.732 -17.395  1.00 26.81           C  
ANISOU  848  CA  GLN A 114     3757   3429   3002    101   -420     -1       C  
ATOM    849  C   GLN A 114      14.852  19.492 -18.227  1.00 26.94           C  
ANISOU  849  C   GLN A 114     3793   3482   2962    143   -444    -55       C  
ATOM    850  O   GLN A 114      15.738  18.695 -18.541  1.00 26.94           O  
ANISOU  850  O   GLN A 114     3803   3533   2900    159   -401    -66       O  
ATOM    851  CB  GLN A 114      14.763  20.505 -15.944  1.00 24.87           C  
ANISOU  851  CB  GLN A 114     3463   3135   2852     85   -413    -45       C  
ATOM    852  CG  GLN A 114      15.224  21.624 -15.025  1.00 25.29           C  
ANISOU  852  CG  GLN A 114     3513   3147   2950     48   -392     -3       C  
ATOM    853  CD  GLN A 114      14.608  21.524 -13.644  1.00 24.68           C  
ANISOU  853  CD  GLN A 114     3401   3021   2956     49   -390    -47       C  
ATOM    854  OE1 GLN A 114      14.066  20.483 -13.257  1.00 20.97           O  
ANISOU  854  OE1 GLN A 114     2894   2560   2514     64   -389   -101       O  
ATOM    855  NE2 GLN A 114      14.681  22.608 -12.899  1.00 22.81           N  
ANISOU  855  NE2 GLN A 114     3180   2730   2755     34   -394    -22       N  
ATOM    856  N   ILE A 115      13.576  19.340 -18.567  1.00 26.25           N  
ANISOU  856  N   ILE A 115     3712   3365   2897    164   -518    -88       N  
ATOM    857  CA  ILE A 115      13.109  18.262 -19.433  1.00 27.47           C  
ANISOU  857  CA  ILE A 115     3900   3537   3000    198   -570   -138       C  
ATOM    858  C   ILE A 115      13.815  18.272 -20.803  1.00 26.06           C  
ANISOU  858  C   ILE A 115     3792   3417   2692    234   -560   -112       C  
ATOM    859  O   ILE A 115      14.292  17.229 -21.291  1.00 24.65           O  
ANISOU  859  O   ILE A 115     3651   3273   2442    269   -549   -152       O  
ATOM    860  CB  ILE A 115      11.578  18.363 -19.647  1.00 23.77           C  
ANISOU  860  CB  ILE A 115     3421   3030   2582    205   -664   -156       C  
ATOM    861  CG1 ILE A 115      10.822  17.998 -18.366  1.00 27.83           C  
ANISOU  861  CG1 ILE A 115     3859   3504   3212    181   -670   -187       C  
ATOM    862  CG2 ILE A 115      11.125  17.464 -20.800  1.00 25.26           C  
ANISOU  862  CG2 ILE A 115     3664   3231   2701    235   -739   -196       C  
ATOM    863  CD1 ILE A 115       9.330  17.854 -18.596  1.00 29.91           C  
ANISOU  863  CD1 ILE A 115     4093   3745   3527    187   -764   -199       C  
ATOM    864  N   GLY A 116      13.876  19.453 -21.409  1.00 26.19           N  
ANISOU  864  N   GLY A 116     3833   3444   2676    232   -564    -43       N  
ATOM    865  CA  GLY A 116      14.579  19.638 -22.671  1.00 29.85           C  
ANISOU  865  CA  GLY A 116     4357   3972   3013    265   -543      3       C  
ATOM    866  C   GLY A 116      16.030  19.180 -22.621  1.00 29.51           C  
ANISOU  866  C   GLY A 116     4307   3998   2909    274   -447     21       C  
ATOM    867  O   GLY A 116      16.501  18.504 -23.529  1.00 32.00           O  
ANISOU  867  O   GLY A 116     4672   4374   3114    330   -429      8       O  
ATOM    868  N   TRP A 117      16.746  19.545 -21.561  1.00 25.53           N  
ANISOU  868  N   TRP A 117     3742   3486   2471    225   -386     53       N  
ATOM    869  CA  TRP A 117      18.152  19.174 -21.455  1.00 26.64           C  
ANISOU  869  CA  TRP A 117     3858   3699   2564    230   -295     83       C  
ATOM    870  C   TRP A 117      18.298  17.661 -21.331  1.00 24.80           C  
ANISOU  870  C   TRP A 117     3634   3482   2308    280   -283     -4       C  
ATOM    871  O   TRP A 117      19.078  17.052 -22.038  1.00 23.51           O  
ANISOU  871  O   TRP A 117     3499   3392   2042    338   -237     -2       O  
ATOM    872  CB  TRP A 117      18.811  19.883 -20.268  1.00 26.80           C  
ANISOU  872  CB  TRP A 117     3813   3697   2672    158   -252    133       C  
ATOM    873  CG  TRP A 117      19.023  21.348 -20.509  1.00 26.11           C  
ANISOU  873  CG  TRP A 117     3730   3601   2589    109   -258    235       C  
ATOM    874  CD1 TRP A 117      19.433  21.943 -21.675  1.00 27.48           C  
ANISOU  874  CD1 TRP A 117     3937   3834   2672    120   -245    318       C  
ATOM    875  CD2 TRP A 117      18.813  22.407 -19.569  1.00 26.71           C  
ANISOU  875  CD2 TRP A 117     3787   3598   2762     45   -284    265       C  
ATOM    876  NE1 TRP A 117      19.497  23.309 -21.510  1.00 28.61           N  
ANISOU  876  NE1 TRP A 117     4079   3935   2857     55   -266    404       N  
ATOM    877  CE2 TRP A 117      19.122  23.618 -20.226  1.00 29.16           C  
ANISOU  877  CE2 TRP A 117     4124   3915   3041     12   -293    368       C  
ATOM    878  CE3 TRP A 117      18.398  22.447 -18.228  1.00 22.78           C  
ANISOU  878  CE3 TRP A 117     3261   3026   2369     16   -301    216       C  
ATOM    879  CZ2 TRP A 117      19.021  24.861 -19.589  1.00 29.43           C  
ANISOU  879  CZ2 TRP A 117     4165   3869   3149    -49   -330    417       C  
ATOM    880  CZ3 TRP A 117      18.305  23.675 -17.598  1.00 25.17           C  
ANISOU  880  CZ3 TRP A 117     3572   3257   2735    -34   -330    261       C  
ATOM    881  CH2 TRP A 117      18.613  24.870 -18.279  1.00 27.87           C  
ANISOU  881  CH2 TRP A 117     3949   3594   3048    -66   -349    357       C  
ATOM    882  N   MET A 118      17.481  17.070 -20.469  1.00 24.98           N  
ANISOU  882  N   MET A 118     3636   3433   2420    263   -328    -78       N  
ATOM    883  CA  MET A 118      17.586  15.664 -20.125  1.00 26.82           C  
ANISOU  883  CA  MET A 118     3875   3661   2654    295   -325   -157       C  
ATOM    884  C   MET A 118      17.163  14.730 -21.244  1.00 27.51           C  
ANISOU  884  C   MET A 118     4047   3756   2650    364   -381   -218       C  
ATOM    885  O   MET A 118      17.549  13.556 -21.258  1.00 28.32           O  
ANISOU  885  O   MET A 118     4180   3867   2715    410   -371   -276       O  
ATOM    886  CB  MET A 118      16.747  15.375 -18.875  1.00 27.89           C  
ANISOU  886  CB  MET A 118     3963   3719   2916    248   -363   -204       C  
ATOM    887  CG  MET A 118      17.308  16.031 -17.628  1.00 29.81           C  
ANISOU  887  CG  MET A 118     4137   3951   3238    192   -306   -163       C  
ATOM    888  SD  MET A 118      16.221  15.906 -16.194  1.00 27.59           S  
ANISOU  888  SD  MET A 118     3803   3589   3092    148   -343   -206       S  
ATOM    889  CE  MET A 118      16.315  14.152 -15.872  1.00 22.65           C  
ANISOU  889  CE  MET A 118     3182   2956   2467    171   -346   -283       C  
ATOM    890  N   THR A 119      16.383  15.238 -22.190  1.00 24.96           N  
ANISOU  890  N   THR A 119     3772   3425   2285    375   -446   -206       N  
ATOM    891  CA  THR A 119      15.864  14.378 -23.237  1.00 27.28           C  
ANISOU  891  CA  THR A 119     4158   3715   2494    436   -519   -269       C  
ATOM    892  C   THR A 119      16.425  14.761 -24.608  1.00 32.03           C  
ANISOU  892  C   THR A 119     4830   4394   2945    501   -494   -226       C  
ATOM    893  O   THR A 119      16.107  14.139 -25.616  1.00 30.79           O  
ANISOU  893  O   THR A 119     4768   4242   2690    564   -552   -274       O  
ATOM    894  CB  THR A 119      14.314  14.406 -23.272  1.00 32.68           C  
ANISOU  894  CB  THR A 119     4846   4323   3249    402   -641   -303       C  
ATOM    895  OG1 THR A 119      13.850  15.723 -23.589  1.00 32.43           O  
ANISOU  895  OG1 THR A 119     4797   4295   3232    377   -658   -235       O  
ATOM    896  CG2 THR A 119      13.756  14.009 -21.914  1.00 33.63           C  
ANISOU  896  CG2 THR A 119     4887   4379   3511    343   -656   -334       C  
ATOM    897  N   HIS A 120      17.282  15.771 -24.639  1.00 36.03           N  
ANISOU  897  N   HIS A 120     5296   4963   3430    484   -409   -131       N  
ATOM    898  CA  HIS A 120      17.887  16.185 -25.897  1.00 41.15           C  
ANISOU  898  CA  HIS A 120     6000   5699   3935    542   -371    -70       C  
ATOM    899  C   HIS A 120      18.796  15.092 -26.437  1.00 37.53           C  
ANISOU  899  C   HIS A 120     5595   5313   3353    641   -313   -109       C  
ATOM    900  O   HIS A 120      19.121  14.142 -25.730  1.00 37.50           O  
ANISOU  900  O   HIS A 120     5572   5290   3385    655   -293   -169       O  
ATOM    901  CB  HIS A 120      18.676  17.477 -25.716  1.00 44.87           C  
ANISOU  901  CB  HIS A 120     6405   6221   4424    489   -292     53       C  
ATOM    902  CG  HIS A 120      19.181  18.057 -26.999  1.00 50.97           C  
ANISOU  902  CG  HIS A 120     7226   7085   5058    534   -257    136       C  
ATOM    903  ND1 HIS A 120      20.508  18.000 -27.371  1.00 53.35           N  
ANISOU  903  ND1 HIS A 120     7507   7501   5263    576   -146    206       N  
ATOM    904  CD2 HIS A 120      18.537  18.699 -28.003  1.00 53.92           C  
ANISOU  904  CD2 HIS A 120     7663   7457   5368    547   -315    169       C  
ATOM    905  CE1 HIS A 120      20.661  18.589 -28.543  1.00 56.74           C  
ANISOU  905  CE1 HIS A 120     7985   7999   5575    611   -133    281       C  
ATOM    906  NE2 HIS A 120      19.479  19.021 -28.949  1.00 57.58           N  
ANISOU  906  NE2 HIS A 120     8148   8034   5697    593   -237    257       N  
ATOM    907  N   ASN A 121      19.203  15.225 -27.692  1.00 36.82           N  
ANISOU  907  N   ASN A 121     5575   5307   3110    718   -287    -72       N  
ATOM    908  CA  ASN A 121      20.179  14.302 -28.267  1.00 41.26           C  
ANISOU  908  CA  ASN A 121     6188   5954   3534    832   -215    -96       C  
ATOM    909  C   ASN A 121      21.367  15.058 -28.879  1.00 45.19           C  
ANISOU  909  C   ASN A 121     6650   6590   3929    864    -93     31       C  
ATOM    910  O   ASN A 121      21.224  15.733 -29.892  1.00 47.11           O  
ANISOU  910  O   ASN A 121     6941   6880   4078    884   -100     91       O  
ATOM    911  CB  ASN A 121      19.501  13.419 -29.317  1.00 44.51           C  
ANISOU  911  CB  ASN A 121     6745   6339   3827    927   -306   -194       C  
ATOM    912  CG  ASN A 121      20.361  12.232 -29.745  1.00 49.32           C  
ANISOU  912  CG  ASN A 121     7427   7008   4303   1060   -251   -253       C  
ATOM    913  OD1 ASN A 121      21.131  11.667 -28.953  1.00 49.45           O  
ANISOU  913  OD1 ASN A 121     7386   7040   4363   1073   -180   -266       O  
ATOM    914  ND2 ASN A 121      20.217  11.838 -31.004  1.00 50.51           N  
ANISOU  914  ND2 ASN A 121     7713   7189   4288   1170   -287   -293       N  
ATOM    915  N   PRO A 122      22.551  14.955 -28.261  1.00 45.68           N  
ANISOU  915  N   PRO A 122     6622   6723   4011    864     18     82       N  
ATOM    916  CA  PRO A 122      22.806  14.200 -27.038  1.00 44.03           C  
ANISOU  916  CA  PRO A 122     6354   6466   3910    840     30     21       C  
ATOM    917  C   PRO A 122      22.245  14.939 -25.828  1.00 40.19           C  
ANISOU  917  C   PRO A 122     5783   5883   3605    700    -14     39       C  
ATOM    918  O   PRO A 122      22.174  16.171 -25.836  1.00 36.14           O  
ANISOU  918  O   PRO A 122     5227   5373   3130    623    -13    131       O  
ATOM    919  CB  PRO A 122      24.331  14.131 -26.987  1.00 44.30           C  
ANISOU  919  CB  PRO A 122     6313   6633   3887    888    168    104       C  
ATOM    920  CG  PRO A 122      24.759  15.394 -27.652  1.00 44.68           C  
ANISOU  920  CG  PRO A 122     6322   6771   3884    852    221    248       C  
ATOM    921  CD  PRO A 122      23.786  15.569 -28.787  1.00 46.51           C  
ANISOU  921  CD  PRO A 122     6673   6975   4023    892    141    216       C  
ATOM    922  N   PRO A 123      21.839  14.196 -24.804  1.00 40.98           N  
ANISOU  922  N   PRO A 123     5866   5895   3810    672    -55    -48       N  
ATOM    923  CA  PRO A 123      21.262  14.848 -23.625  1.00 40.55           C  
ANISOU  923  CA  PRO A 123     5737   5752   3916    554    -94    -38       C  
ATOM    924  C   PRO A 123      22.322  15.509 -22.757  1.00 37.22           C  
ANISOU  924  C   PRO A 123     5208   5374   3558    490    -10     52       C  
ATOM    925  O   PRO A 123      23.468  15.059 -22.749  1.00 34.68           O  
ANISOU  925  O   PRO A 123     4853   5139   3186    536     75     81       O  
ATOM    926  CB  PRO A 123      20.598  13.689 -22.881  1.00 42.05           C  
ANISOU  926  CB  PRO A 123     5946   5852   4177    557   -155   -154       C  
ATOM    927  CG  PRO A 123      21.423  12.504 -23.258  1.00 41.61           C  
ANISOU  927  CG  PRO A 123     5935   5852   4022    662   -108   -200       C  
ATOM    928  CD  PRO A 123      21.870  12.730 -24.675  1.00 42.10           C  
ANISOU  928  CD  PRO A 123     6061   6011   3924    750    -71   -158       C  
ATOM    929  N   ILE A 124      21.932  16.571 -22.051  1.00 36.51           N  
ANISOU  929  N   ILE A 124     5071   5226   3577    389    -39     98       N  
ATOM    930  CA  ILE A 124      22.737  17.146 -20.984  1.00 33.43           C  
ANISOU  930  CA  ILE A 124     4590   4841   3272    312     10    164       C  
ATOM    931  C   ILE A 124      22.091  16.702 -19.661  1.00 31.07           C  
ANISOU  931  C   ILE A 124     4268   4442   3095    270    -34     81       C  
ATOM    932  O   ILE A 124      21.042  17.217 -19.275  1.00 28.09           O  
ANISOU  932  O   ILE A 124     3901   3979   2792    225   -101     58       O  
ATOM    933  CB  ILE A 124      22.819  18.696 -21.084  1.00 34.12           C  
ANISOU  933  CB  ILE A 124     4654   4924   3388    231      3    275       C  
ATOM    934  CG1 ILE A 124      23.659  19.122 -22.295  1.00 35.79           C  
ANISOU  934  CG1 ILE A 124     4868   5250   3479    263     63    380       C  
ATOM    935  CG2 ILE A 124      23.430  19.305 -19.811  1.00 31.00           C  
ANISOU  935  CG2 ILE A 124     4180   4498   3100    138     21    325       C  
ATOM    936  CD1 ILE A 124      22.954  19.016 -23.638  1.00 36.66           C  
ANISOU  936  CD1 ILE A 124     5070   5379   3479    336     28    357       C  
ATOM    937  N   PRO A 125      22.689  15.711 -18.980  1.00 29.99           N  
ANISOU  937  N   PRO A 125     4101   4320   2976    294      5     39       N  
ATOM    938  CA  PRO A 125      21.950  15.075 -17.879  1.00 26.99           C  
ANISOU  938  CA  PRO A 125     3713   3848   2693    269    -41    -46       C  
ATOM    939  C   PRO A 125      21.925  15.908 -16.601  1.00 25.63           C  
ANISOU  939  C   PRO A 125     3481   3622   2634    178    -46    -13       C  
ATOM    940  O   PRO A 125      22.558  15.511 -15.628  1.00 26.00           O  
ANISOU  940  O   PRO A 125     3482   3672   2726    160    -13    -19       O  
ATOM    941  CB  PRO A 125      22.715  13.759 -17.666  1.00 30.40           C  
ANISOU  941  CB  PRO A 125     4140   4317   3092    332      3    -92       C  
ATOM    942  CG  PRO A 125      24.136  14.099 -18.058  1.00 33.98           C  
ANISOU  942  CG  PRO A 125     4547   4885   3478    353     92      0       C  
ATOM    943  CD  PRO A 125      24.057  15.179 -19.129  1.00 31.92           C  
ANISOU  943  CD  PRO A 125     4307   4666   3154    344     92     77       C  
ATOM    944  N   VAL A 126      21.184  17.017 -16.584  1.00 24.83           N  
ANISOU  944  N   VAL A 126     3390   3470   2574    130    -91     15       N  
ATOM    945  CA  VAL A 126      21.252  17.949 -15.453  1.00 25.00           C  
ANISOU  945  CA  VAL A 126     3373   3440   2686     54    -97     50       C  
ATOM    946  C   VAL A 126      20.775  17.304 -14.152  1.00 23.02           C  
ANISOU  946  C   VAL A 126     3100   3127   2518     41   -111    -21       C  
ATOM    947  O   VAL A 126      21.248  17.662 -13.082  1.00 20.83           O  
ANISOU  947  O   VAL A 126     2789   2829   2297     -6    -96     -2       O  
ATOM    948  CB  VAL A 126      20.448  19.255 -15.719  1.00 21.04           C  
ANISOU  948  CB  VAL A 126     2902   2884   2208     21   -150     86       C  
ATOM    949  CG1 VAL A 126      21.100  20.055 -16.851  1.00 22.15           C  
ANISOU  949  CG1 VAL A 126     3059   3086   2273     15   -132    181       C  
ATOM    950  CG2 VAL A 126      18.980  18.973 -16.051  1.00 20.90           C  
ANISOU  950  CG2 VAL A 126     2922   2817   2203     57   -214     19       C  
ATOM    951  N   GLY A 127      19.860  16.343 -14.241  1.00 23.16           N  
ANISOU  951  N   GLY A 127     3140   3117   2541     80   -144    -99       N  
ATOM    952  CA  GLY A 127      19.448  15.605 -13.059  1.00 20.63           C  
ANISOU  952  CA  GLY A 127     2795   2750   2294     69   -152   -157       C  
ATOM    953  C   GLY A 127      20.582  14.796 -12.435  1.00 23.30           C  
ANISOU  953  C   GLY A 127     3102   3123   2628     74    -99   -161       C  
ATOM    954  O   GLY A 127      20.770  14.810 -11.209  1.00 21.59           O  
ANISOU  954  O   GLY A 127     2852   2878   2474     38    -86   -164       O  
ATOM    955  N   GLU A 128      21.330  14.071 -13.265  1.00 24.29           N  
ANISOU  955  N   GLU A 128     3243   3311   2676    126    -67   -162       N  
ATOM    956  CA  GLU A 128      22.469  13.287 -12.775  1.00 25.37           C  
ANISOU  956  CA  GLU A 128     3347   3491   2802    146    -14   -161       C  
ATOM    957  C   GLU A 128      23.581  14.177 -12.248  1.00 22.60           C  
ANISOU  957  C   GLU A 128     2939   3181   2469     95     30    -78       C  
ATOM    958  O   GLU A 128      24.222  13.854 -11.244  1.00 21.63           O  
ANISOU  958  O   GLU A 128     2774   3058   2385     75     53    -76       O  
ATOM    959  CB  GLU A 128      23.023  12.383 -13.875  1.00 29.22           C  
ANISOU  959  CB  GLU A 128     3869   4042   3190    233     12   -178       C  
ATOM    960  CG  GLU A 128      22.134  11.205 -14.162  1.00 34.04           C  
ANISOU  960  CG  GLU A 128     4544   4601   3791    280    -41   -269       C  
ATOM    961  CD  GLU A 128      21.645  10.544 -12.876  1.00 36.19           C  
ANISOU  961  CD  GLU A 128     4795   4800   4156    243    -68   -316       C  
ATOM    962  OE1 GLU A 128      22.484  10.004 -12.112  1.00 35.30           O  
ANISOU  962  OE1 GLU A 128     4650   4703   4060    250    -28   -314       O  
ATOM    963  OE2 GLU A 128      20.421  10.584 -12.622  1.00 37.23           O  
ANISOU  963  OE2 GLU A 128     4937   4865   4344    208   -127   -347       O  
ATOM    964  N   ILE A 129      23.832  15.286 -12.934  1.00 20.23           N  
ANISOU  964  N   ILE A 129     2636   2912   2138     70     35     -5       N  
ATOM    965  CA  ILE A 129      24.872  16.215 -12.481  1.00 22.28           C  
ANISOU  965  CA  ILE A 129     2842   3203   2419      6     62     86       C  
ATOM    966  C   ILE A 129      24.506  16.826 -11.123  1.00 22.67           C  
ANISOU  966  C   ILE A 129     2885   3167   2563    -65     23     75       C  
ATOM    967  O   ILE A 129      25.346  16.936 -10.224  1.00 20.12           O  
ANISOU  967  O   ILE A 129     2519   2851   2276   -107     37    106       O  
ATOM    968  CB  ILE A 129      25.104  17.351 -13.504  1.00 24.89           C  
ANISOU  968  CB  ILE A 129     3180   3573   2705    -17     64    175       C  
ATOM    969  CG1 ILE A 129      25.515  16.772 -14.857  1.00 26.68           C  
ANISOU  969  CG1 ILE A 129     3417   3896   2823     64    110    191       C  
ATOM    970  CG2 ILE A 129      26.194  18.312 -13.006  1.00 24.63           C  
ANISOU  970  CG2 ILE A 129     3089   3565   2705   -100     77    279       C  
ATOM    971  CD1 ILE A 129      25.339  17.749 -16.005  1.00 28.96           C  
ANISOU  971  CD1 ILE A 129     3735   4212   3055     56    101    260       C  
ATOM    972  N   TYR A 130      23.245  17.211 -10.960  1.00 19.10           N  
ANISOU  972  N   TYR A 130     2475   2635   2145    -71    -27     30       N  
ATOM    973  CA  TYR A 130      22.828  17.803  -9.685  1.00 20.96           C  
ANISOU  973  CA  TYR A 130     2715   2792   2457   -119    -59     15       C  
ATOM    974  C   TYR A 130      22.847  16.759  -8.554  1.00 19.74           C  
ANISOU  974  C   TYR A 130     2538   2623   2340   -108    -45    -44       C  
ATOM    975  O   TYR A 130      23.262  17.051  -7.424  1.00 20.74           O  
ANISOU  975  O   TYR A 130     2651   2722   2509   -149    -48    -34       O  
ATOM    976  CB  TYR A 130      21.440  18.421  -9.832  1.00 22.64           C  
ANISOU  976  CB  TYR A 130     2972   2938   2693   -110   -108    -16       C  
ATOM    977  CG  TYR A 130      20.943  19.231  -8.650  1.00 21.78           C  
ANISOU  977  CG  TYR A 130     2880   2749   2645   -141   -139    -27       C  
ATOM    978  CD1 TYR A 130      21.813  19.770  -7.721  1.00 20.01           C  
ANISOU  978  CD1 TYR A 130     2649   2506   2447   -193   -140      7       C  
ATOM    979  CD2 TYR A 130      19.577  19.469  -8.485  1.00 22.20           C  
ANISOU  979  CD2 TYR A 130     2959   2748   2729   -112   -172    -70       C  
ATOM    980  CE1 TYR A 130      21.335  20.522  -6.635  1.00 19.33           C  
ANISOU  980  CE1 TYR A 130     2598   2342   2405   -208   -173    -11       C  
ATOM    981  CE2 TYR A 130      19.103  20.221  -7.416  1.00 21.64           C  
ANISOU  981  CE2 TYR A 130     2910   2611   2703   -120   -195    -82       C  
ATOM    982  CZ  TYR A 130      19.986  20.745  -6.495  1.00 19.23           C  
ANISOU  982  CZ  TYR A 130     2615   2280   2413   -165   -196    -57       C  
ATOM    983  OH  TYR A 130      19.495  21.488  -5.425  1.00 19.91           O  
ANISOU  983  OH  TYR A 130     2741   2294   2531   -161   -222    -78       O  
ATOM    984  N   LYS A 131      22.417  15.542  -8.865  1.00 21.22           N  
ANISOU  984  N   LYS A 131     2730   2823   2511    -54    -36   -102       N  
ATOM    985  CA  LYS A 131      22.443  14.457  -7.886  1.00 23.26           C  
ANISOU  985  CA  LYS A 131     2971   3066   2801    -43    -25   -151       C  
ATOM    986  C   LYS A 131      23.863  14.196  -7.348  1.00 22.20           C  
ANISOU  986  C   LYS A 131     2794   2979   2661    -57     14   -114       C  
ATOM    987  O   LYS A 131      24.046  13.979  -6.156  1.00 19.23           O  
ANISOU  987  O   LYS A 131     2401   2576   2328    -80     14   -126       O  
ATOM    988  CB  LYS A 131      21.866  13.172  -8.488  1.00 23.84           C  
ANISOU  988  CB  LYS A 131     3065   3142   2851     13    -33   -211       C  
ATOM    989  CG  LYS A 131      21.562  12.106  -7.412  1.00 23.34           C  
ANISOU  989  CG  LYS A 131     2993   3041   2835     15    -37   -260       C  
ATOM    990  CD  LYS A 131      21.288  10.711  -8.021  1.00 27.35           C  
ANISOU  990  CD  LYS A 131     3529   3547   3316     66    -52   -313       C  
ATOM    991  CE  LYS A 131      19.925  10.595  -8.676  1.00 30.49           C  
ANISOU  991  CE  LYS A 131     3959   3905   3720     73   -108   -346       C  
ATOM    992  NZ  LYS A 131      19.500   9.136  -8.784  1.00 33.17           N  
ANISOU  992  NZ  LYS A 131     4329   4212   4064    100   -143   -402       N  
ATOM    993  N   ARG A 132      24.863  14.236  -8.228  1.00 22.53           N  
ANISOU  993  N   ARG A 132     2814   3097   2648    -40     47    -62       N  
ATOM    994  CA  ARG A 132      26.250  14.080  -7.800  1.00 23.40           C  
ANISOU  994  CA  ARG A 132     2868   3267   2756    -53     84    -11       C  
ATOM    995  C   ARG A 132      26.663  15.162  -6.785  1.00 21.24           C  
ANISOU  995  C   ARG A 132     2573   2961   2536   -139     59     39       C  
ATOM    996  O   ARG A 132      27.303  14.856  -5.772  1.00 21.76           O  
ANISOU  996  O   ARG A 132     2608   3027   2632   -160     62     44       O  
ATOM    997  CB  ARG A 132      27.187  14.112  -9.012  1.00 25.29           C  
ANISOU  997  CB  ARG A 132     3078   3607   2923    -18    129     53       C  
ATOM    998  CG  ARG A 132      28.600  13.642  -8.714  1.00 32.51           C  
ANISOU  998  CG  ARG A 132     3921   4604   3827     -6    176    103       C  
ATOM    999  CD  ARG A 132      29.592  14.097  -9.788  1.00 36.59           C  
ANISOU  999  CD  ARG A 132     4389   5232   4282      7    225    201       C  
ATOM   1000  NE  ARG A 132      29.037  14.050 -11.139  1.00 41.09           N  
ANISOU 1000  NE  ARG A 132     5011   5826   4777     69    237    185       N  
ATOM   1001  CZ  ARG A 132      28.510  15.094 -11.776  1.00 45.34           C  
ANISOU 1001  CZ  ARG A 132     5578   6344   5303     28    212    220       C  
ATOM   1002  NH1 ARG A 132      28.452  16.279 -11.176  1.00 46.71           N  
ANISOU 1002  NH1 ARG A 132     5741   6466   5540    -72    170    270       N  
ATOM   1003  NH2 ARG A 132      28.035  14.955 -13.015  1.00 45.22           N  
ANISOU 1003  NH2 ARG A 132     5613   6357   5213     92    221    204       N  
ATOM   1004  N   TRP A 133      26.314  16.418  -7.066  1.00 19.36           N  
ANISOU 1004  N   TRP A 133     2361   2689   2305   -186     26     77       N  
ATOM   1005  CA  TRP A 133      26.589  17.526  -6.132  1.00 20.67           C  
ANISOU 1005  CA  TRP A 133     2533   2803   2519   -265    -16    116       C  
ATOM   1006  C   TRP A 133      25.934  17.296  -4.768  1.00 21.68           C  
ANISOU 1006  C   TRP A 133     2691   2854   2694   -268    -41     47       C  
ATOM   1007  O   TRP A 133      26.537  17.551  -3.721  1.00 22.58           O  
ANISOU 1007  O   TRP A 133     2796   2946   2837   -313    -61     64       O  
ATOM   1008  CB  TRP A 133      26.098  18.863  -6.690  1.00 22.36           C  
ANISOU 1008  CB  TRP A 133     2790   2973   2732   -302    -56    154       C  
ATOM   1009  CG  TRP A 133      26.705  19.293  -7.980  1.00 23.00           C  
ANISOU 1009  CG  TRP A 133     2848   3126   2767   -311    -35    237       C  
ATOM   1010  CD1 TRP A 133      27.740  18.703  -8.638  1.00 24.33           C  
ANISOU 1010  CD1 TRP A 133     2951   3402   2890   -290     20    290       C  
ATOM   1011  CD2 TRP A 133      26.303  20.409  -8.776  1.00 24.07           C  
ANISOU 1011  CD2 TRP A 133     3022   3234   2889   -337    -67    283       C  
ATOM   1012  NE1 TRP A 133      28.019  19.397  -9.801  1.00 26.41           N  
ANISOU 1012  NE1 TRP A 133     3209   3716   3110   -303     31    371       N  
ATOM   1013  CE2 TRP A 133      27.149  20.449  -9.903  1.00 27.32           C  
ANISOU 1013  CE2 TRP A 133     3389   3745   3245   -336    -26    369       C  
ATOM   1014  CE3 TRP A 133      25.304  21.384  -8.648  1.00 25.10           C  
ANISOU 1014  CE3 TRP A 133     3222   3268   3045   -352   -124    263       C  
ATOM   1015  CZ2 TRP A 133      27.011  21.409 -10.904  1.00 26.69           C  
ANISOU 1015  CZ2 TRP A 133     3335   3670   3137   -359    -42    438       C  
ATOM   1016  CZ3 TRP A 133      25.180  22.345  -9.639  1.00 24.57           C  
ANISOU 1016  CZ3 TRP A 133     3183   3198   2953   -373   -146    327       C  
ATOM   1017  CH2 TRP A 133      26.031  22.352 -10.749  1.00 24.61           C  
ANISOU 1017  CH2 TRP A 133     3145   3302   2905   -381   -107    415       C  
ATOM   1018  N   ILE A 134      24.685  16.834  -4.793  1.00 21.53           N  
ANISOU 1018  N   ILE A 134     2705   2796   2679   -220    -43    -25       N  
ATOM   1019  CA  ILE A 134      23.921  16.593  -3.577  1.00 19.66           C  
ANISOU 1019  CA  ILE A 134     2492   2497   2480   -212    -57    -83       C  
ATOM   1020  C   ILE A 134      24.554  15.456  -2.763  1.00 19.44           C  
ANISOU 1020  C   ILE A 134     2429   2495   2461   -203    -31   -102       C  
ATOM   1021  O   ILE A 134      24.715  15.562  -1.548  1.00 19.30           O  
ANISOU 1021  O   ILE A 134     2420   2445   2469   -226    -45   -110       O  
ATOM   1022  CB  ILE A 134      22.449  16.265  -3.896  1.00 17.88           C  
ANISOU 1022  CB  ILE A 134     2290   2242   2261   -165    -62   -140       C  
ATOM   1023  CG1 ILE A 134      21.737  17.495  -4.481  1.00 17.50           C  
ANISOU 1023  CG1 ILE A 134     2281   2157   2211   -170    -95   -123       C  
ATOM   1024  CG2 ILE A 134      21.713  15.794  -2.639  1.00 16.78           C  
ANISOU 1024  CG2 ILE A 134     2158   2062   2157   -152    -62   -189       C  
ATOM   1025  CD1 ILE A 134      20.363  17.150  -5.109  1.00 16.15           C  
ANISOU 1025  CD1 ILE A 134     2119   1976   2042   -123   -104   -165       C  
ATOM   1026  N   ILE A 135      24.938  14.384  -3.434  1.00 20.94           N  
ANISOU 1026  N   ILE A 135     2589   2741   2624   -163      2   -109       N  
ATOM   1027  CA  ILE A 135      25.532  13.254  -2.722  1.00 22.88           C  
ANISOU 1027  CA  ILE A 135     2808   3008   2879   -145     23   -126       C  
ATOM   1028  C   ILE A 135      26.889  13.649  -2.119  1.00 22.97           C  
ANISOU 1028  C   ILE A 135     2779   3052   2896   -190     23    -66       C  
ATOM   1029  O   ILE A 135      27.254  13.201  -1.020  1.00 22.64           O  
ANISOU 1029  O   ILE A 135     2728   2999   2876   -199     18    -76       O  
ATOM   1030  CB  ILE A 135      25.640  12.014  -3.658  1.00 24.42           C  
ANISOU 1030  CB  ILE A 135     2994   3248   3037    -79     52   -151       C  
ATOM   1031  CG1 ILE A 135      24.232  11.489  -3.940  1.00 25.86           C  
ANISOU 1031  CG1 ILE A 135     3217   3381   3228    -50     32   -213       C  
ATOM   1032  CG2 ILE A 135      26.490  10.890  -3.029  1.00 24.71           C  
ANISOU 1032  CG2 ILE A 135     3002   3311   3076    -53     74   -157       C  
ATOM   1033  CD1 ILE A 135      24.181  10.339  -4.926  1.00 27.92           C  
ANISOU 1033  CD1 ILE A 135     3494   3664   3449     13     40   -247       C  
ATOM   1034  N   LEU A 136      27.620  14.505  -2.823  1.00 22.57           N  
ANISOU 1034  N   LEU A 136     2704   3043   2828   -222     21      3       N  
ATOM   1035  CA  LEU A 136      28.879  15.040  -2.326  1.00 23.33           C  
ANISOU 1035  CA  LEU A 136     2755   3170   2938   -282      8     76       C  
ATOM   1036  C   LEU A 136      28.635  15.784  -1.002  1.00 22.69           C  
ANISOU 1036  C   LEU A 136     2718   3006   2896   -339    -48     62       C  
ATOM   1037  O   LEU A 136      29.372  15.616  -0.036  1.00 19.98           O  
ANISOU 1037  O   LEU A 136     2354   2666   2572   -368    -65     78       O  
ATOM   1038  CB  LEU A 136      29.511  15.962  -3.388  1.00 27.01           C  
ANISOU 1038  CB  LEU A 136     3190   3688   3383   -317     10    163       C  
ATOM   1039  CG  LEU A 136      30.876  16.625  -3.198  1.00 35.37           C  
ANISOU 1039  CG  LEU A 136     4184   4797   4457   -392     -7    268       C  
ATOM   1040  CD1 LEU A 136      31.362  17.183  -4.530  1.00 38.15           C  
ANISOU 1040  CD1 LEU A 136     4496   5225   4775   -403     19    355       C  
ATOM   1041  CD2 LEU A 136      30.840  17.723  -2.147  1.00 38.98           C  
ANISOU 1041  CD2 LEU A 136     4687   5165   4960   -481    -86    281       C  
ATOM   1042  N   GLY A 137      27.589  16.604  -0.960  1.00 23.79           N  
ANISOU 1042  N   GLY A 137     2924   3073   3044   -347    -78     32       N  
ATOM   1043  CA  GLY A 137      27.216  17.300   0.258  1.00 21.18           C  
ANISOU 1043  CA  GLY A 137     2653   2660   2736   -378   -128      7       C  
ATOM   1044  C   GLY A 137      26.725  16.371   1.360  1.00 22.66           C  
ANISOU 1044  C   GLY A 137     2854   2825   2931   -339   -112    -58       C  
ATOM   1045  O   GLY A 137      27.093  16.543   2.532  1.00 24.75           O  
ANISOU 1045  O   GLY A 137     3140   3058   3205   -366   -143    -61       O  
ATOM   1046  N   LEU A 138      25.886  15.406   0.999  1.00 22.61           N  
ANISOU 1046  N   LEU A 138     2839   2832   2919   -279    -71   -106       N  
ATOM   1047  CA  LEU A 138      25.324  14.481   1.983  1.00 24.01           C  
ANISOU 1047  CA  LEU A 138     3025   2990   3106   -246    -54   -157       C  
ATOM   1048  C   LEU A 138      26.449  13.638   2.611  1.00 23.46           C  
ANISOU 1048  C   LEU A 138     2916   2958   3039   -255    -46   -139       C  
ATOM   1049  O   LEU A 138      26.429  13.355   3.813  1.00 24.13           O  
ANISOU 1049  O   LEU A 138     3020   3018   3131   -256    -55   -158       O  
ATOM   1050  CB  LEU A 138      24.268  13.566   1.353  1.00 23.41           C  
ANISOU 1050  CB  LEU A 138     2941   2920   3031   -194    -24   -199       C  
ATOM   1051  CG  LEU A 138      22.911  14.133   0.935  1.00 23.74           C  
ANISOU 1051  CG  LEU A 138     3014   2928   3079   -174    -31   -223       C  
ATOM   1052  CD1 LEU A 138      22.104  13.075   0.165  1.00 20.85           C  
ANISOU 1052  CD1 LEU A 138     2629   2577   2717   -136    -14   -253       C  
ATOM   1053  CD2 LEU A 138      22.147  14.696   2.124  1.00 21.35           C  
ANISOU 1053  CD2 LEU A 138     2750   2574   2786   -169    -42   -245       C  
ATOM   1054  N   ASN A 139      27.440  13.275   1.805  1.00 23.44           N  
ANISOU 1054  N   ASN A 139     2860   3020   3026   -254    -29    -99       N  
ATOM   1055  CA  ASN A 139      28.582  12.508   2.314  1.00 25.85           C  
ANISOU 1055  CA  ASN A 139     3118   3370   3334   -253    -21    -74       C  
ATOM   1056  C   ASN A 139      29.348  13.300   3.381  1.00 23.78           C  
ANISOU 1056  C   ASN A 139     2861   3088   3085   -318    -70    -37       C  
ATOM   1057  O   ASN A 139      29.729  12.750   4.424  1.00 23.81           O  
ANISOU 1057  O   ASN A 139     2863   3088   3097   -318    -81    -44       O  
ATOM   1058  CB  ASN A 139      29.513  12.100   1.170  1.00 28.94           C  
ANISOU 1058  CB  ASN A 139     3445   3846   3704   -228     13    -29       C  
ATOM   1059  CG  ASN A 139      28.953  10.957   0.349  1.00 31.66           C  
ANISOU 1059  CG  ASN A 139     3797   4205   4028   -151     52    -77       C  
ATOM   1060  OD1 ASN A 139      27.985  10.314   0.749  1.00 34.02           O  
ANISOU 1060  OD1 ASN A 139     4136   4453   4338   -127     50   -135       O  
ATOM   1061  ND2 ASN A 139      29.553  10.705  -0.809  1.00 33.04           N  
ANISOU 1061  ND2 ASN A 139     3935   4450   4168   -112     85    -48       N  
ATOM   1062  N   LYS A 140      29.565  14.587   3.128  1.00 25.54           N  
ANISOU 1062  N   LYS A 140     3098   3293   3312   -375   -109      4       N  
ATOM   1063  CA  LYS A 140      30.165  15.479   4.131  1.00 28.25           C  
ANISOU 1063  CA  LYS A 140     3468   3596   3668   -444   -177     34       C  
ATOM   1064  C   LYS A 140      29.348  15.480   5.424  1.00 27.73           C  
ANISOU 1064  C   LYS A 140     3483   3456   3597   -426   -198    -31       C  
ATOM   1065  O   LYS A 140      29.897  15.468   6.521  1.00 27.76           O  
ANISOU 1065  O   LYS A 140     3504   3443   3602   -452   -238    -27       O  
ATOM   1066  CB  LYS A 140      30.285  16.920   3.599  1.00 33.15           C  
ANISOU 1066  CB  LYS A 140     4114   4186   4295   -508   -227     82       C  
ATOM   1067  CG  LYS A 140      31.244  17.105   2.431  1.00 37.61           C  
ANISOU 1067  CG  LYS A 140     4595   4832   4862   -540   -211    170       C  
ATOM   1068  CD  LYS A 140      31.254  18.549   1.917  1.00 41.36           C  
ANISOU 1068  CD  LYS A 140     5104   5266   5345   -610   -265    222       C  
ATOM   1069  CE  LYS A 140      31.637  19.544   3.009  1.00 43.00           C  
ANISOU 1069  CE  LYS A 140     5372   5392   5575   -691   -364    240       C  
ATOM   1070  NZ  LYS A 140      31.876  20.933   2.495  1.00 44.51           N  
ANISOU 1070  NZ  LYS A 140     5592   5538   5780   -774   -432    309       N  
ATOM   1071  N   ILE A 141      28.026  15.510   5.290  1.00 29.18           N  
ANISOU 1071  N   ILE A 141     3715   3601   3772   -379   -172    -88       N  
ATOM   1072  CA  ILE A 141      27.148  15.513   6.447  1.00 26.48           C  
ANISOU 1072  CA  ILE A 141     3442   3202   3418   -348   -177   -143       C  
ATOM   1073  C   ILE A 141      27.224  14.197   7.222  1.00 28.42           C  
ANISOU 1073  C   ILE A 141     3663   3475   3662   -316   -144   -162       C  
ATOM   1074  O   ILE A 141      27.276  14.197   8.456  1.00 30.48           O  
ANISOU 1074  O   ILE A 141     3966   3707   3907   -317   -166   -178       O  
ATOM   1075  CB  ILE A 141      25.698  15.756   6.051  1.00 27.50           C  
ANISOU 1075  CB  ILE A 141     3605   3301   3541   -299   -148   -186       C  
ATOM   1076  CG1 ILE A 141      25.538  17.183   5.500  1.00 26.37           C  
ANISOU 1076  CG1 ILE A 141     3509   3113   3397   -325   -191   -171       C  
ATOM   1077  CG2 ILE A 141      24.774  15.518   7.261  1.00 28.37           C  
ANISOU 1077  CG2 ILE A 141     3765   3378   3636   -253   -133   -234       C  
ATOM   1078  CD1 ILE A 141      24.206  17.411   4.864  1.00 25.23           C  
ANISOU 1078  CD1 ILE A 141     3382   2953   3252   -274   -164   -202       C  
ATOM   1079  N   VAL A 142      27.229  13.083   6.500  1.00 23.09           N  
ANISOU 1079  N   VAL A 142     2927   2849   2996   -285    -97   -162       N  
ATOM   1080  CA  VAL A 142      27.339  11.767   7.138  1.00 23.58           C  
ANISOU 1080  CA  VAL A 142     2968   2930   3060   -256    -71   -176       C  
ATOM   1081  C   VAL A 142      28.648  11.695   7.954  1.00 25.11           C  
ANISOU 1081  C   VAL A 142     3146   3143   3254   -289   -107   -140       C  
ATOM   1082  O   VAL A 142      28.677  11.225   9.101  1.00 25.14           O  
ANISOU 1082  O   VAL A 142     3174   3131   3249   -282   -116   -152       O  
ATOM   1083  CB  VAL A 142      27.282  10.642   6.082  1.00 21.29           C  
ANISOU 1083  CB  VAL A 142     2629   2681   2780   -216    -29   -181       C  
ATOM   1084  CG1 VAL A 142      27.876   9.342   6.625  1.00 22.86           C  
ANISOU 1084  CG1 VAL A 142     2802   2901   2982   -193    -18   -178       C  
ATOM   1085  CG2 VAL A 142      25.860  10.432   5.576  1.00 20.65           C  
ANISOU 1085  CG2 VAL A 142     2568   2575   2704   -185     -5   -220       C  
ATOM   1086  N   ARG A 143      29.731  12.175   7.357  1.00 25.24           N  
ANISOU 1086  N   ARG A 143     3116   3197   3278   -328   -131    -88       N  
ATOM   1087  CA  ARG A 143      31.020  12.205   8.040  1.00 29.64           C  
ANISOU 1087  CA  ARG A 143     3642   3779   3841   -369   -175    -41       C  
ATOM   1088  C   ARG A 143      31.016  13.160   9.249  1.00 28.44           C  
ANISOU 1088  C   ARG A 143     3566   3562   3677   -415   -244    -48       C  
ATOM   1089  O   ARG A 143      31.642  12.881  10.262  1.00 27.86           O  
ANISOU 1089  O   ARG A 143     3499   3488   3598   -430   -280    -37       O  
ATOM   1090  CB  ARG A 143      32.141  12.581   7.053  1.00 33.34           C  
ANISOU 1090  CB  ARG A 143     4030   4312   4324   -404   -182     32       C  
ATOM   1091  CG  ARG A 143      32.525  11.448   6.102  1.00 37.15           C  
ANISOU 1091  CG  ARG A 143     4436   4873   4805   -343   -117     45       C  
ATOM   1092  CD  ARG A 143      33.793  11.732   5.305  1.00 42.25           C  
ANISOU 1092  CD  ARG A 143     4988   5605   5459   -368   -116    131       C  
ATOM   1093  NE  ARG A 143      33.540  12.732   4.277  1.00 46.15           N  
ANISOU 1093  NE  ARG A 143     5485   6103   5949   -399   -114    157       N  
ATOM   1094  CZ  ARG A 143      33.316  12.453   2.996  1.00 44.96           C  
ANISOU 1094  CZ  ARG A 143     5308   5997   5777   -349    -56    157       C  
ATOM   1095  NH1 ARG A 143      33.351  11.199   2.562  1.00 45.89           N  
ANISOU 1095  NH1 ARG A 143     5401   6160   5877   -263      0    129       N  
ATOM   1096  NH2 ARG A 143      33.071  13.436   2.151  1.00 43.64           N  
ANISOU 1096  NH2 ARG A 143     5149   5827   5603   -383    -61    185       N  
ATOM   1097  N   MET A 144      30.294  14.269   9.165  1.00 30.15           N  
ANISOU 1097  N   MET A 144     3851   3720   3884   -431   -268    -70       N  
ATOM   1098  CA  MET A 144      30.279  15.214  10.284  1.00 31.12           C  
ANISOU 1098  CA  MET A 144     4067   3773   3985   -463   -341    -85       C  
ATOM   1099  C   MET A 144      29.549  14.645  11.489  1.00 29.90           C  
ANISOU 1099  C   MET A 144     3973   3590   3796   -408   -320   -139       C  
ATOM   1100  O   MET A 144      29.997  14.798  12.644  1.00 32.69           O  
ANISOU 1100  O   MET A 144     4378   3916   4125   -426   -375   -142       O  
ATOM   1101  CB  MET A 144      29.626  16.545   9.888  1.00 32.53           C  
ANISOU 1101  CB  MET A 144     4317   3887   4157   -478   -372    -99       C  
ATOM   1102  CG  MET A 144      29.300  17.440  11.107  1.00 34.43           C  
ANISOU 1102  CG  MET A 144     4684   4039   4360   -478   -439   -139       C  
ATOM   1103  SD  MET A 144      28.911  19.120  10.609  1.00 99.49           S  
ANISOU 1103  SD  MET A 144    13012  12193  12598   -508   -504   -141       S  
ATOM   1104  CE  MET A 144      30.359  19.497   9.635  1.00 39.99           C  
ANISOU 1104  CE  MET A 144     5384   4698   5112   -619   -557    -39       C  
ATOM   1105  N   TYR A 145      28.420  14.004  11.232  1.00 25.81           N  
ANISOU 1105  N   TYR A 145     3451   3080   3274   -345   -246   -178       N  
ATOM   1106  CA  TYR A 145      27.581  13.519  12.326  1.00 29.38           C  
ANISOU 1106  CA  TYR A 145     3955   3514   3693   -293   -217   -218       C  
ATOM   1107  C   TYR A 145      27.988  12.118  12.808  1.00 27.57           C  
ANISOU 1107  C   TYR A 145     3678   3328   3470   -278   -189   -205       C  
ATOM   1108  O   TYR A 145      27.371  11.574  13.712  1.00 27.22           O  
ANISOU 1108  O   TYR A 145     3666   3276   3400   -240   -162   -225       O  
ATOM   1109  CB  TYR A 145      26.119  13.524  11.904  1.00 33.12           C  
ANISOU 1109  CB  TYR A 145     4440   3980   4166   -239   -157   -253       C  
ATOM   1110  CG  TYR A 145      25.582  14.913  11.625  1.00 37.00           C  
ANISOU 1110  CG  TYR A 145     4994   4420   4643   -236   -185   -271       C  
ATOM   1111  CD1 TYR A 145      26.379  16.046  11.822  1.00 39.12           C  
ANISOU 1111  CD1 TYR A 145     5319   4643   4901   -285   -266   -259       C  
ATOM   1112  CD2 TYR A 145      24.288  15.095  11.166  1.00 36.91           C  
ANISOU 1112  CD2 TYR A 145     4988   4404   4633   -185   -139   -297       C  
ATOM   1113  CE1 TYR A 145      25.900  17.317  11.560  1.00 40.34           C  
ANISOU 1113  CE1 TYR A 145     5544   4739   5045   -281   -301   -276       C  
ATOM   1114  CE2 TYR A 145      23.797  16.365  10.914  1.00 38.59           C  
ANISOU 1114  CE2 TYR A 145     5262   4567   4833   -173   -167   -313       C  
ATOM   1115  CZ  TYR A 145      24.606  17.470  11.108  1.00 39.74           C  
ANISOU 1115  CZ  TYR A 145     5475   4659   4966   -218   -248   -305       C  
ATOM   1116  OH  TYR A 145      24.117  18.729  10.856  1.00 44.01           O  
ANISOU 1116  OH  TYR A 145     6089   5138   5494   -204   -284   -322       O  
ATOM   1117  N   SER A 146      28.996  11.525  12.176  1.00 28.42           N  
ANISOU 1117  N   SER A 146     3707   3482   3610   -301   -193   -167       N  
ATOM   1118  CA  SER A 146      29.618  10.297  12.698  1.00 27.43           C  
ANISOU 1118  CA  SER A 146     3544   3390   3490   -287   -184   -150       C  
ATOM   1119  C   SER A 146      30.091  10.560  14.141  1.00 26.69           C  
ANISOU 1119  C   SER A 146     3509   3270   3360   -306   -240   -146       C  
ATOM   1120  O   SER A 146      30.980  11.363  14.366  1.00 26.44           O  
ANISOU 1120  O   SER A 146     3488   3231   3328   -357   -310   -121       O  
ATOM   1121  CB  SER A 146      30.791   9.867  11.793  1.00 29.13           C  
ANISOU 1121  CB  SER A 146     3668   3662   3737   -302   -187   -104       C  
ATOM   1122  OG  SER A 146      31.330   8.601  12.161  1.00 29.85           O  
ANISOU 1122  OG  SER A 146     3722   3784   3835   -272   -173    -90       O  
ATOM   1123  N   PRO A 147      29.481   9.902  15.129  1.00 28.09           N  
ANISOU 1123  N   PRO A 147     3729   3436   3509   -267   -215   -167       N  
ATOM   1124  CA  PRO A 147      29.791  10.319  16.504  1.00 32.94           C  
ANISOU 1124  CA  PRO A 147     4421   4022   4073   -277   -270   -171       C  
ATOM   1125  C   PRO A 147      31.113   9.767  17.059  1.00 32.89           C  
ANISOU 1125  C   PRO A 147     4381   4041   4073   -305   -324   -130       C  
ATOM   1126  O   PRO A 147      31.575  10.252  18.088  1.00 30.71           O  
ANISOU 1126  O   PRO A 147     4168   3740   3758   -326   -392   -129       O  
ATOM   1127  CB  PRO A 147      28.621   9.758  17.298  1.00 32.92           C  
ANISOU 1127  CB  PRO A 147     4466   4011   4033   -220   -212   -197       C  
ATOM   1128  CG  PRO A 147      28.281   8.501  16.577  1.00 32.27           C  
ANISOU 1128  CG  PRO A 147     4306   3960   3995   -199   -148   -185       C  
ATOM   1129  CD  PRO A 147      28.552   8.765  15.094  1.00 29.64           C  
ANISOU 1129  CD  PRO A 147     3909   3643   3712   -219   -144   -180       C  
ATOM   1130  N   THR A 148      31.717   8.774  16.409  1.00 33.00           N  
ANISOU 1130  N   THR A 148     4303   4104   4131   -298   -299    -99       N  
ATOM   1131  CA  THR A 148      32.851   8.104  17.047  1.00 32.17           C  
ANISOU 1131  CA  THR A 148     4166   4027   4029   -306   -342    -59       C  
ATOM   1132  C   THR A 148      34.019   7.848  16.101  1.00 29.65           C  
ANISOU 1132  C   THR A 148     3738   3768   3761   -323   -352    -10       C  
ATOM   1133  O   THR A 148      33.830   7.542  14.926  1.00 28.65           O  
ANISOU 1133  O   THR A 148     3555   3667   3664   -299   -297    -11       O  
ATOM   1134  CB  THR A 148      32.399   6.773  17.682  1.00 36.07           C  
ANISOU 1134  CB  THR A 148     4672   4522   4510   -254   -297    -66       C  
ATOM   1135  OG1 THR A 148      31.397   7.044  18.673  1.00 38.02           O  
ANISOU 1135  OG1 THR A 148     5013   4730   4702   -237   -284    -98       O  
ATOM   1136  CG2 THR A 148      33.577   6.048  18.341  1.00 33.89           C  
ANISOU 1136  CG2 THR A 148     4365   4275   4238   -255   -344    -23       C  
ATOM   1137  N   SER A 149      35.234   8.013  16.616  1.00 26.89           N  
ANISOU 1137  N   SER A 149     3357   3442   3417   -361   -425     38       N  
ATOM   1138  CA  SER A 149      36.429   7.716  15.841  1.00 29.47           C  
ANISOU 1138  CA  SER A 149     3566   3842   3788   -368   -432     99       C  
ATOM   1139  C   SER A 149      36.663   6.204  15.862  1.00 27.31           C  
ANISOU 1139  C   SER A 149     3249   3603   3525   -295   -387    106       C  
ATOM   1140  O   SER A 149      36.333   5.535  16.844  1.00 25.82           O  
ANISOU 1140  O   SER A 149     3117   3382   3310   -268   -390     87       O  
ATOM   1141  CB  SER A 149      37.645   8.471  16.399  1.00 32.47           C  
ANISOU 1141  CB  SER A 149     3918   4240   4178   -443   -536    159       C  
ATOM   1142  OG  SER A 149      38.870   7.979  15.872  1.00 33.68           O  
ANISOU 1142  OG  SER A 149     3943   4480   4373   -438   -539    231       O  
ATOM   1143  N   ILE A 150      37.217   5.673  14.777  1.00 22.10           N  
ANISOU 1143  N   ILE A 150     2495   3005   2896   -256   -344    135       N  
ATOM   1144  CA  ILE A 150      37.553   4.261  14.713  1.00 22.06           C  
ANISOU 1144  CA  ILE A 150     2453   3028   2900   -177   -310    142       C  
ATOM   1145  C   ILE A 150      38.567   3.923  15.807  1.00 22.44           C  
ANISOU 1145  C   ILE A 150     2480   3099   2949   -184   -376    189       C  
ATOM   1146  O   ILE A 150      38.631   2.794  16.271  1.00 20.87           O  
ANISOU 1146  O   ILE A 150     2293   2892   2746   -126   -366    185       O  
ATOM   1147  CB  ILE A 150      38.125   3.864  13.323  1.00 24.38           C  
ANISOU 1147  CB  ILE A 150     2652   3394   3218   -122   -257    168       C  
ATOM   1148  CG1 ILE A 150      38.145   2.336  13.169  1.00 24.41           C  
ANISOU 1148  CG1 ILE A 150     2653   3398   3222    -21   -216    151       C  
ATOM   1149  CG2 ILE A 150      39.547   4.439  13.128  1.00 27.31           C  
ANISOU 1149  CG2 ILE A 150     2911   3855   3613   -156   -297    253       C  
ATOM   1150  CD1 ILE A 150      36.733   1.689  13.138  1.00 23.03           C  
ANISOU 1150  CD1 ILE A 150     2576   3141   3035      7   -177     79       C  
ATOM   1151  N   LEU A 151      39.336   4.915  16.241  1.00 22.32           N  
ANISOU 1151  N   LEU A 151     2439   3103   2939   -260   -453    234       N  
ATOM   1152  CA  LEU A 151      40.328   4.697  17.290  1.00 27.19           C  
ANISOU 1152  CA  LEU A 151     3033   3742   3556   -278   -531    283       C  
ATOM   1153  C   LEU A 151      39.707   4.412  18.656  1.00 27.43           C  
ANISOU 1153  C   LEU A 151     3181   3700   3540   -277   -562    242       C  
ATOM   1154  O   LEU A 151      40.379   3.874  19.542  1.00 27.33           O  
ANISOU 1154  O   LEU A 151     3163   3700   3520   -266   -614    274       O  
ATOM   1155  CB  LEU A 151      41.267   5.905  17.401  1.00 31.53           C  
ANISOU 1155  CB  LEU A 151     3531   4323   4126   -375   -622    346       C  
ATOM   1156  CG  LEU A 151      42.074   6.219  16.143  1.00 34.55           C  
ANISOU 1156  CG  LEU A 151     3777   4796   4554   -384   -596    413       C  
ATOM   1157  CD1 LEU A 151      42.627   7.646  16.190  1.00 35.00           C  
ANISOU 1157  CD1 LEU A 151     3811   4856   4632   -505   -688    468       C  
ATOM   1158  CD2 LEU A 151      43.199   5.212  16.013  1.00 37.04           C  
ANISOU 1158  CD2 LEU A 151     3971   5205   4897   -317   -585    479       C  
ATOM   1159  N   ASP A 152      38.436   4.767  18.839  1.00 24.28           N  
ANISOU 1159  N   ASP A 152     2886   3233   3106   -283   -530    178       N  
ATOM   1160  CA  ASP A 152      37.741   4.463  20.101  1.00 27.55           C  
ANISOU 1160  CA  ASP A 152     3411   3591   3467   -270   -542    144       C  
ATOM   1161  C   ASP A 152      36.854   3.220  20.029  1.00 27.91           C  
ANISOU 1161  C   ASP A 152     3482   3615   3509   -199   -460    116       C  
ATOM   1162  O   ASP A 152      36.094   2.932  20.958  1.00 27.55           O  
ANISOU 1162  O   ASP A 152     3522   3526   3418   -187   -450     94       O  
ATOM   1163  CB  ASP A 152      36.886   5.650  20.540  1.00 32.68           C  
ANISOU 1163  CB  ASP A 152     4163   4182   4071   -313   -561     99       C  
ATOM   1164  CG  ASP A 152      37.731   6.870  20.909  1.00 37.70           C  
ANISOU 1164  CG  ASP A 152     4809   4814   4702   -392   -669    125       C  
ATOM   1165  OD1 ASP A 152      38.702   6.714  21.677  1.00 37.15           O  
ANISOU 1165  OD1 ASP A 152     4725   4762   4628   -414   -750    167       O  
ATOM   1166  OD2 ASP A 152      37.423   7.976  20.425  1.00 39.45           O  
ANISOU 1166  OD2 ASP A 152     5054   5010   4926   -435   -681    106       O  
ATOM   1167  N   ILE A 153      36.926   2.490  18.924  1.00 26.84           N  
ANISOU 1167  N   ILE A 153     3277   3506   3416   -153   -403    119       N  
ATOM   1168  CA  ILE A 153      36.170   1.251  18.827  1.00 25.37           C  
ANISOU 1168  CA  ILE A 153     3119   3288   3232    -92   -345     97       C  
ATOM   1169  C   ILE A 153      37.065   0.101  19.239  1.00 25.32           C  
ANISOU 1169  C   ILE A 153     3082   3301   3238    -43   -370    137       C  
ATOM   1170  O   ILE A 153      37.847  -0.411  18.433  1.00 24.02           O  
ANISOU 1170  O   ILE A 153     2839   3180   3107      4   -359    158       O  
ATOM   1171  CB  ILE A 153      35.630   0.991  17.412  1.00 24.87           C  
ANISOU 1171  CB  ILE A 153     3023   3226   3200    -60   -278     68       C  
ATOM   1172  CG1 ILE A 153      34.750   2.158  16.952  1.00 22.53           C  
ANISOU 1172  CG1 ILE A 153     2754   2913   2895   -106   -256     33       C  
ATOM   1173  CG2 ILE A 153      34.807  -0.314  17.401  1.00 25.60           C  
ANISOU 1173  CG2 ILE A 153     3158   3270   3299    -10   -237     48       C  
ATOM   1174  CD1 ILE A 153      33.479   2.351  17.812  1.00 21.26           C  
ANISOU 1174  CD1 ILE A 153     2684   2697   2697   -123   -239      2       C  
ATOM   1175  N   ARG A 154      36.931  -0.310  20.497  1.00 22.89           N  
ANISOU 1175  N   ARG A 154     2838   2963   2896    -45   -400    148       N  
ATOM   1176  CA  ARG A 154      37.740  -1.393  21.032  1.00 27.23           C  
ANISOU 1176  CA  ARG A 154     3371   3524   3453      3   -432    188       C  
ATOM   1177  C   ARG A 154      36.821  -2.448  21.639  1.00 27.60           C  
ANISOU 1177  C   ARG A 154     3496   3509   3480     31   -403    180       C  
ATOM   1178  O   ARG A 154      35.747  -2.134  22.184  1.00 29.21           O  
ANISOU 1178  O   ARG A 154     3773   3678   3649     -1   -380    159       O  
ATOM   1179  CB  ARG A 154      38.743  -0.868  22.062  1.00 29.72           C  
ANISOU 1179  CB  ARG A 154     3678   3869   3744    -34   -520    230       C  
ATOM   1180  CG  ARG A 154      39.601   0.306  21.569  1.00 34.56           C  
ANISOU 1180  CG  ARG A 154     4214   4537   4379    -86   -563    251       C  
ATOM   1181  CD  ARG A 154      40.598   0.719  22.637  1.00 40.92           C  
ANISOU 1181  CD  ARG A 154     5016   5366   5166   -128   -668    297       C  
ATOM   1182  NE  ARG A 154      41.148  -0.475  23.271  1.00 45.94           N  
ANISOU 1182  NE  ARG A 154     5643   6009   5801    -70   -690    333       N  
ATOM   1183  CZ  ARG A 154      41.286  -0.643  24.583  1.00 48.10           C  
ANISOU 1183  CZ  ARG A 154     5986   6260   6029    -81   -754    350       C  
ATOM   1184  NH1 ARG A 154      40.943   0.327  25.424  1.00 47.10           N  
ANISOU 1184  NH1 ARG A 154     5946   6103   5846   -145   -804    329       N  
ATOM   1185  NH2 ARG A 154      41.785  -1.782  25.049  1.00 49.20           N  
ANISOU 1185  NH2 ARG A 154     6114   6407   6173    -23   -771    386       N  
ATOM   1186  N   GLN A 155      37.220  -3.705  21.509  1.00 25.28           N  
ANISOU 1186  N   GLN A 155     3187   3205   3212     94   -404    201       N  
ATOM   1187  CA  GLN A 155      36.371  -4.804  21.948  1.00 26.46           C  
ANISOU 1187  CA  GLN A 155     3408   3288   3355    116   -382    203       C  
ATOM   1188  C   GLN A 155      36.249  -4.820  23.474  1.00 27.14           C  
ANISOU 1188  C   GLN A 155     3562   3361   3388     88   -417    235       C  
ATOM   1189  O   GLN A 155      37.253  -4.723  24.179  1.00 19.50           O  
ANISOU 1189  O   GLN A 155     2580   2425   2403     92   -479    268       O  
ATOM   1190  CB  GLN A 155      36.929  -6.143  21.451  1.00 23.37           C  
ANISOU 1190  CB  GLN A 155     2998   2879   3003    196   -388    217       C  
ATOM   1191  CG  GLN A 155      36.119  -7.365  21.877  1.00 22.91           C  
ANISOU 1191  CG  GLN A 155     3017   2740   2947    212   -380    229       C  
ATOM   1192  CD  GLN A 155      36.701  -8.665  21.353  1.00 22.14           C  
ANISOU 1192  CD  GLN A 155     2916   2609   2886    300   -397    237       C  
ATOM   1193  OE1 GLN A 155      37.851  -8.709  20.939  1.00 23.67           O  
ANISOU 1193  OE1 GLN A 155     3046   2854   3093    360   -416    245       O  
ATOM   1194  NE2 GLN A 155      35.900  -9.737  21.368  1.00 21.47           N  
ANISOU 1194  NE2 GLN A 155     2902   2439   2817    310   -393    239       N  
ATOM   1195  N   GLY A 156      35.029  -4.953  23.981  1.00 26.62           N  
ANISOU 1195  N   GLY A 156     3567   3255   3294     63   -379    230       N  
ATOM   1196  CA  GLY A 156      34.817  -5.054  25.421  1.00 27.92           C  
ANISOU 1196  CA  GLY A 156     3802   3410   3396     47   -400    265       C  
ATOM   1197  C   GLY A 156      35.402  -6.347  25.959  1.00 32.05           C  
ANISOU 1197  C   GLY A 156     4340   3909   3928     89   -439    315       C  
ATOM   1198  O   GLY A 156      35.570  -7.311  25.217  1.00 32.72           O  
ANISOU 1198  O   GLY A 156     4400   3964   4068    132   -433    318       O  
ATOM   1199  N   PRO A 157      35.735  -6.377  27.256  1.00 34.20           N  
ANISOU 1199  N   PRO A 157     4663   4191   4142     84   -483    354       N  
ATOM   1200  CA  PRO A 157      36.314  -7.595  27.824  1.00 33.93           C  
ANISOU 1200  CA  PRO A 157     4647   4131   4114    126   -526    408       C  
ATOM   1201  C   PRO A 157      35.338  -8.752  27.737  1.00 34.40           C  
ANISOU 1201  C   PRO A 157     4750   4125   4197    134   -482    431       C  
ATOM   1202  O   PRO A 157      35.755  -9.906  27.692  1.00 35.64           O  
ANISOU 1202  O   PRO A 157     4913   4241   4388    178   -512    462       O  
ATOM   1203  CB  PRO A 157      36.592  -7.212  29.286  1.00 36.38           C  
ANISOU 1203  CB  PRO A 157     5018   4464   4339    107   -575    441       C  
ATOM   1204  CG  PRO A 157      35.656  -6.088  29.568  1.00 36.96           C  
ANISOU 1204  CG  PRO A 157     5135   4554   4356     62   -532    406       C  
ATOM   1205  CD  PRO A 157      35.546  -5.323  28.269  1.00 35.07           C  
ANISOU 1205  CD  PRO A 157     4827   4328   4170     46   -499    349       C  
ATOM   1206  N   LYS A 158      34.050  -8.435  27.702  1.00 36.91           N  
ANISOU 1206  N   LYS A 158     5095   4429   4498     92   -418    419       N  
ATOM   1207  CA  LYS A 158      33.010  -9.452  27.636  1.00 41.47           C  
ANISOU 1207  CA  LYS A 158     5707   4947   5103     80   -382    452       C  
ATOM   1208  C   LYS A 158      32.200  -9.372  26.345  1.00 38.06           C  
ANISOU 1208  C   LYS A 158     5238   4491   4731     64   -334    408       C  
ATOM   1209  O   LYS A 158      31.169 -10.046  26.197  1.00 36.81           O  
ANISOU 1209  O   LYS A 158     5101   4284   4600     37   -305    434       O  
ATOM   1210  CB  LYS A 158      32.073  -9.323  28.838  1.00 47.25           C  
ANISOU 1210  CB  LYS A 158     6498   5691   5762     43   -346    502       C  
ATOM   1211  CG  LYS A 158      32.733  -9.629  30.175  1.00 51.80           C  
ANISOU 1211  CG  LYS A 158     7129   6281   6273     61   -395    556       C  
ATOM   1212  CD  LYS A 158      31.710  -9.585  31.299  1.00 55.24           C  
ANISOU 1212  CD  LYS A 158     7626   6734   6630     33   -347    611       C  
ATOM   1213  CE  LYS A 158      30.719 -10.734  31.188  1.00 56.30           C  
ANISOU 1213  CE  LYS A 158     7770   6814   6809      7   -310    676       C  
ATOM   1214  NZ  LYS A 158      31.364 -12.058  31.443  1.00 56.73           N  
ANISOU 1214  NZ  LYS A 158     7853   6806   6896     30   -373    732       N  
ATOM   1215  N   GLU A 159      32.660  -8.546  25.412  1.00 32.84           N  
ANISOU 1215  N   GLU A 159     4522   3865   4091     75   -331    347       N  
ATOM   1216  CA  GLU A 159      31.928  -8.358  24.168  1.00 28.64           C  
ANISOU 1216  CA  GLU A 159     3959   3316   3607     62   -289    301       C  
ATOM   1217  C   GLU A 159      32.282  -9.461  23.176  1.00 31.37           C  
ANISOU 1217  C   GLU A 159     4296   3605   4017    109   -314    289       C  
ATOM   1218  O   GLU A 159      33.454  -9.715  22.929  1.00 32.38           O  
ANISOU 1218  O   GLU A 159     4400   3746   4156    167   -352    282       O  
ATOM   1219  CB  GLU A 159      32.225  -6.973  23.575  1.00 23.06           C  
ANISOU 1219  CB  GLU A 159     3203   2670   2891     52   -275    246       C  
ATOM   1220  CG  GLU A 159      31.419  -6.658  22.328  1.00 25.45           C  
ANISOU 1220  CG  GLU A 159     3476   2961   3234     38   -231    200       C  
ATOM   1221  CD  GLU A 159      31.836  -5.351  21.704  1.00 26.78           C  
ANISOU 1221  CD  GLU A 159     3596   3183   3394     31   -224    154       C  
ATOM   1222  OE1 GLU A 159      32.946  -4.864  22.016  1.00 29.83           O  
ANISOU 1222  OE1 GLU A 159     3961   3612   3762     42   -263    159       O  
ATOM   1223  OE2 GLU A 159      31.068  -4.807  20.893  1.00 26.76           O  
ANISOU 1223  OE2 GLU A 159     3578   3182   3409     11   -186    119       O  
ATOM   1224  N   PRO A 160      31.267 -10.128  22.612  1.00 31.99           N  
ANISOU 1224  N   PRO A 160     4398   3621   4137     88   -297    289       N  
ATOM   1225  CA  PRO A 160      31.503 -11.141  21.573  1.00 31.59           C  
ANISOU 1225  CA  PRO A 160     4360   3502   4141    138   -328    265       C  
ATOM   1226  C   PRO A 160      32.227 -10.549  20.370  1.00 26.11           C  
ANISOU 1226  C   PRO A 160     3611   2851   3458    188   -319    200       C  
ATOM   1227  O   PRO A 160      31.961  -9.416  20.008  1.00 26.28           O  
ANISOU 1227  O   PRO A 160     3590   2928   3467    156   -282    169       O  
ATOM   1228  CB  PRO A 160      30.093 -11.599  21.189  1.00 30.77           C  
ANISOU 1228  CB  PRO A 160     4285   3333   4073     81   -313    274       C  
ATOM   1229  CG  PRO A 160      29.233 -11.232  22.376  1.00 30.73           C  
ANISOU 1229  CG  PRO A 160     4287   3357   4032     11   -278    333       C  
ATOM   1230  CD  PRO A 160      29.834  -9.966  22.920  1.00 30.82           C  
ANISOU 1230  CD  PRO A 160     4265   3461   3983     20   -253    314       C  
ATOM   1231  N   PHE A 161      33.125 -11.301  19.746  1.00 27.09           N  
ANISOU 1231  N   PHE A 161     3737   2952   3603    272   -352    183       N  
ATOM   1232  CA  PHE A 161      33.922 -10.711  18.669  1.00 25.55           C  
ANISOU 1232  CA  PHE A 161     3480   2819   3409    329   -336    134       C  
ATOM   1233  C   PHE A 161      33.044 -10.147  17.526  1.00 22.43           C  
ANISOU 1233  C   PHE A 161     3074   2422   3028    298   -298     82       C  
ATOM   1234  O   PHE A 161      33.323  -9.082  16.977  1.00 22.24           O  
ANISOU 1234  O   PHE A 161     2989   2471   2992    293   -267     56       O  
ATOM   1235  CB  PHE A 161      34.922 -11.741  18.150  1.00 26.08           C  
ANISOU 1235  CB  PHE A 161     3557   2860   3490    442   -370    127       C  
ATOM   1236  CG  PHE A 161      35.923 -11.177  17.189  1.00 22.70           C  
ANISOU 1236  CG  PHE A 161     3051   2517   3055    512   -347     96       C  
ATOM   1237  CD1 PHE A 161      36.918 -10.307  17.632  1.00 22.81           C  
ANISOU 1237  CD1 PHE A 161     2982   2635   3052    509   -344    126       C  
ATOM   1238  CD2 PHE A 161      35.866 -11.500  15.847  1.00 20.18           C  
ANISOU 1238  CD2 PHE A 161     2745   2179   2746    579   -332     44       C  
ATOM   1239  CE1 PHE A 161      37.825  -9.774  16.753  1.00 24.46           C  
ANISOU 1239  CE1 PHE A 161     3106   2930   3257    565   -321    115       C  
ATOM   1240  CE2 PHE A 161      36.788 -10.996  14.964  1.00 22.95           C  
ANISOU 1240  CE2 PHE A 161     3019   2619   3083    650   -302     27       C  
ATOM   1241  CZ  PHE A 161      37.755 -10.114  15.400  1.00 24.57           C  
ANISOU 1241  CZ  PHE A 161     3126   2933   3276    638   -293     67       C  
ATOM   1242  N   ARG A 162      31.966 -10.840  17.194  1.00 23.54           N  
ANISOU 1242  N   ARG A 162     3272   2476   3195    270   -306     73       N  
ATOM   1243  CA  ARG A 162      31.112 -10.423  16.098  1.00 26.67           C  
ANISOU 1243  CA  ARG A 162     3663   2864   3608    244   -282     26       C  
ATOM   1244  C   ARG A 162      30.482  -9.067  16.382  1.00 22.89           C  
ANISOU 1244  C   ARG A 162     3136   2451   3110    167   -234     28       C  
ATOM   1245  O   ARG A 162      30.410  -8.210  15.491  1.00 24.82           O  
ANISOU 1245  O   ARG A 162     3341   2739   3350    166   -206    -12       O  
ATOM   1246  CB  ARG A 162      30.014 -11.462  15.830  1.00 33.93           C  
ANISOU 1246  CB  ARG A 162     4654   3673   4565    213   -316     29       C  
ATOM   1247  CG  ARG A 162      29.125 -11.121  14.617  1.00 40.63           C  
ANISOU 1247  CG  ARG A 162     5501   4506   5432    188   -305    -20       C  
ATOM   1248  CD  ARG A 162      27.798 -11.904  14.654  1.00 42.20           C  
ANISOU 1248  CD  ARG A 162     5752   4607   5674    115   -342      6       C  
ATOM   1249  NE  ARG A 162      28.030 -13.326  14.877  1.00 46.19           N  
ANISOU 1249  NE  ARG A 162     6338   5009   6202    147   -410     27       N  
ATOM   1250  CZ  ARG A 162      27.081 -14.214  15.167  1.00 46.46           C  
ANISOU 1250  CZ  ARG A 162     6426   4948   6280     79   -458     72       C  
ATOM   1251  NH1 ARG A 162      25.814 -13.828  15.282  1.00 42.86           N  
ANISOU 1251  NH1 ARG A 162     5937   4500   5849    -22   -440    106       N  
ATOM   1252  NH2 ARG A 162      27.412 -15.490  15.352  1.00 46.78           N  
ANISOU 1252  NH2 ARG A 162     6549   4886   6340    114   -527     90       N  
ATOM   1253  N   ASP A 163      30.076  -8.856  17.631  1.00 19.41           N  
ANISOU 1253  N   ASP A 163     2702   2021   2652    111   -226     77       N  
ATOM   1254  CA  ASP A 163      29.483  -7.585  18.021  1.00 23.22           C  
ANISOU 1254  CA  ASP A 163     3153   2562   3107     52   -182     77       C  
ATOM   1255  C   ASP A 163      30.520  -6.466  17.913  1.00 20.32           C  
ANISOU 1255  C   ASP A 163     2736   2273   2710     73   -175     55       C  
ATOM   1256  O   ASP A 163      30.192  -5.349  17.525  1.00 16.67           O  
ANISOU 1256  O   ASP A 163     2246   1850   2237     45   -147     28       O  
ATOM   1257  CB  ASP A 163      28.919  -7.663  19.443  1.00 28.20           C  
ANISOU 1257  CB  ASP A 163     3812   3192   3711      6   -173    136       C  
ATOM   1258  CG  ASP A 163      27.691  -8.555  19.536  1.00 33.14           C  
ANISOU 1258  CG  ASP A 163     4468   3753   4370    -37   -172    174       C  
ATOM   1259  OD1 ASP A 163      26.958  -8.692  18.531  1.00 32.73           O  
ANISOU 1259  OD1 ASP A 163     4409   3668   4359    -54   -171    148       O  
ATOM   1260  OD2 ASP A 163      27.451  -9.118  20.625  1.00 35.41           O  
ANISOU 1260  OD2 ASP A 163     4786   4024   4643    -59   -177    236       O  
ATOM   1261  N   TYR A 164      31.779  -6.780  18.209  1.00 22.27           N  
ANISOU 1261  N   TYR A 164     2971   2542   2949    121   -207     70       N  
ATOM   1262  CA  TYR A 164      32.850  -5.787  18.087  1.00 21.49           C  
ANISOU 1262  CA  TYR A 164     2814   2519   2831    133   -212     63       C  
ATOM   1263  C   TYR A 164      33.114  -5.426  16.612  1.00 19.30           C  
ANISOU 1263  C   TYR A 164     2490   2270   2573    165   -191     22       C  
ATOM   1264  O   TYR A 164      33.269  -4.255  16.260  1.00 19.91           O  
ANISOU 1264  O   TYR A 164     2524   2400   2639    136   -176     10       O  
ATOM   1265  CB  TYR A 164      34.106  -6.311  18.771  1.00 20.53           C  
ANISOU 1265  CB  TYR A 164     2680   2418   2702    177   -255    101       C  
ATOM   1266  CG  TYR A 164      35.403  -5.722  18.285  1.00 20.71           C  
ANISOU 1266  CG  TYR A 164     2625   2518   2726    210   -268    104       C  
ATOM   1267  CD1 TYR A 164      35.681  -4.368  18.445  1.00 20.16           C  
ANISOU 1267  CD1 TYR A 164     2515   2506   2638    156   -272    107       C  
ATOM   1268  CD2 TYR A 164      36.376  -6.527  17.702  1.00 24.43           C  
ANISOU 1268  CD2 TYR A 164     3062   3004   3217    297   -280    112       C  
ATOM   1269  CE1 TYR A 164      36.877  -3.829  18.015  1.00 22.42           C  
ANISOU 1269  CE1 TYR A 164     2720   2867   2933    173   -289    126       C  
ATOM   1270  CE2 TYR A 164      37.583  -5.988  17.267  1.00 25.09           C  
ANISOU 1270  CE2 TYR A 164     3056   3175   3303    328   -286    130       C  
ATOM   1271  CZ  TYR A 164      37.821  -4.644  17.419  1.00 25.19           C  
ANISOU 1271  CZ  TYR A 164     3020   3247   3304    258   -291    142       C  
ATOM   1272  OH  TYR A 164      39.006  -4.093  16.988  1.00 24.22           O  
ANISOU 1272  OH  TYR A 164     2799   3213   3191    274   -302    176       O  
ATOM   1273  N   VAL A 165      33.133  -6.436  15.754  1.00 20.57           N  
ANISOU 1273  N   VAL A 165     2668   2391   2758    225   -194      2       N  
ATOM   1274  CA  VAL A 165      33.371  -6.225  14.320  1.00 19.44           C  
ANISOU 1274  CA  VAL A 165     2491   2274   2620    271   -172    -37       C  
ATOM   1275  C   VAL A 165      32.214  -5.420  13.692  1.00 21.65           C  
ANISOU 1275  C   VAL A 165     2777   2547   2904    212   -141    -70       C  
ATOM   1276  O   VAL A 165      32.457  -4.519  12.884  1.00 20.80           O  
ANISOU 1276  O   VAL A 165     2623   2493   2787    212   -118    -87       O  
ATOM   1277  CB  VAL A 165      33.550  -7.555  13.589  1.00 17.53           C  
ANISOU 1277  CB  VAL A 165     2292   1978   2392    359   -189    -59       C  
ATOM   1278  CG1 VAL A 165      33.926  -7.316  12.097  1.00 17.59           C  
ANISOU 1278  CG1 VAL A 165     2268   2026   2388    424   -161    -99       C  
ATOM   1279  CG2 VAL A 165      34.618  -8.410  14.294  1.00 18.82           C  
ANISOU 1279  CG2 VAL A 165     2455   2141   2554    425   -222    -23       C  
ATOM   1280  N   ASP A 166      30.964  -5.723  14.073  1.00 21.02           N  
ANISOU 1280  N   ASP A 166     2746   2403   2836    161   -142    -71       N  
ATOM   1281  CA  ASP A 166      29.834  -4.899  13.647  1.00 22.30           C  
ANISOU 1281  CA  ASP A 166     2905   2567   3003    104   -114    -93       C  
ATOM   1282  C   ASP A 166      30.065  -3.406  13.968  1.00 19.71           C  
ANISOU 1282  C   ASP A 166     2534   2306   2647     65    -93    -88       C  
ATOM   1283  O   ASP A 166      29.928  -2.566  13.083  1.00 21.04           O  
ANISOU 1283  O   ASP A 166     2676   2504   2814     58    -73   -114       O  
ATOM   1284  CB  ASP A 166      28.526  -5.347  14.307  1.00 25.41           C  
ANISOU 1284  CB  ASP A 166     3338   2903   3413     49   -115    -72       C  
ATOM   1285  CG  ASP A 166      27.898  -6.563  13.644  1.00 29.25           C  
ANISOU 1285  CG  ASP A 166     3869   3309   3936     60   -144    -83       C  
ATOM   1286  OD1 ASP A 166      28.235  -6.880  12.469  1.00 31.25           O  
ANISOU 1286  OD1 ASP A 166     4131   3547   4194    113   -158   -125       O  
ATOM   1287  OD2 ASP A 166      27.033  -7.188  14.308  1.00 27.69           O  
ANISOU 1287  OD2 ASP A 166     3701   3062   3759     15   -155    -46       O  
ATOM   1288  N   ARG A 167      30.395  -3.077  15.224  1.00 17.63           N  
ANISOU 1288  N   ARG A 167     2275   2062   2362     41   -103    -56       N  
ATOM   1289  CA  ARG A 167      30.646  -1.666  15.600  1.00 21.45           C  
ANISOU 1289  CA  ARG A 167     2737   2595   2817      3   -100    -54       C  
ATOM   1290  C   ARG A 167      31.814  -1.059  14.799  1.00 21.74           C  
ANISOU 1290  C   ARG A 167     2715   2688   2856     22   -109    -57       C  
ATOM   1291  O   ARG A 167      31.769   0.103  14.382  1.00 19.49           O  
ANISOU 1291  O   ARG A 167     2409   2431   2563     -9   -102    -67       O  
ATOM   1292  CB  ARG A 167      30.940  -1.523  17.109  1.00 22.49           C  
ANISOU 1292  CB  ARG A 167     2898   2733   2915    -18   -123    -21       C  
ATOM   1293  CG  ARG A 167      29.802  -1.987  18.021  1.00 24.20           C  
ANISOU 1293  CG  ARG A 167     3166   2911   3117    -37   -104     -5       C  
ATOM   1294  CD  ARG A 167      29.999  -1.545  19.472  1.00 23.91           C  
ANISOU 1294  CD  ARG A 167     3167   2890   3026    -54   -120     21       C  
ATOM   1295  NE  ARG A 167      31.152  -2.193  20.094  1.00 23.91           N  
ANISOU 1295  NE  ARG A 167     3168   2897   3020    -31   -166     52       N  
ATOM   1296  CZ  ARG A 167      32.226  -1.537  20.529  1.00 26.83           C  
ANISOU 1296  CZ  ARG A 167     3525   3302   3366    -37   -211     60       C  
ATOM   1297  NH1 ARG A 167      32.278  -0.212  20.420  1.00 25.43           N  
ANISOU 1297  NH1 ARG A 167     3344   3148   3169    -69   -219     38       N  
ATOM   1298  NH2 ARG A 167      33.250  -2.200  21.075  1.00 24.46           N  
ANISOU 1298  NH2 ARG A 167     3217   3011   3066    -13   -256     95       N  
ATOM   1299  N   PHE A 168      32.861  -1.854  14.608  1.00 22.46           N  
ANISOU 1299  N   PHE A 168     2778   2798   2957     76   -126    -39       N  
ATOM   1300  CA  PHE A 168      34.078  -1.387  13.953  1.00 22.65           C  
ANISOU 1300  CA  PHE A 168     2731   2893   2984     99   -132    -22       C  
ATOM   1301  C   PHE A 168      33.790  -0.983  12.505  1.00 21.13           C  
ANISOU 1301  C   PHE A 168     2514   2719   2797    114    -96    -51       C  
ATOM   1302  O   PHE A 168      34.130   0.136  12.089  1.00 22.62           O  
ANISOU 1302  O   PHE A 168     2658   2956   2981     80    -92    -40       O  
ATOM   1303  CB  PHE A 168      35.148  -2.474  14.020  1.00 22.80           C  
ANISOU 1303  CB  PHE A 168     2724   2930   3011    174   -149      4       C  
ATOM   1304  CG  PHE A 168      36.490  -2.064  13.451  1.00 27.59           C  
ANISOU 1304  CG  PHE A 168     3237   3627   3620    205   -151     40       C  
ATOM   1305  CD1 PHE A 168      36.741  -2.162  12.085  1.00 22.79           C  
ANISOU 1305  CD1 PHE A 168     2590   3058   3012    264   -112     26       C  
ATOM   1306  CD2 PHE A 168      37.511  -1.618  14.291  1.00 26.22           C  
ANISOU 1306  CD2 PHE A 168     3013   3503   3445    177   -194     93       C  
ATOM   1307  CE1 PHE A 168      37.977  -1.813  11.567  1.00 25.10           C  
ANISOU 1307  CE1 PHE A 168     2785   3448   3305    297   -104     73       C  
ATOM   1308  CE2 PHE A 168      38.756  -1.262  13.776  1.00 28.46           C  
ANISOU 1308  CE2 PHE A 168     3194   3880   3738    199   -197    141       C  
ATOM   1309  CZ  PHE A 168      38.986  -1.356  12.420  1.00 28.57           C  
ANISOU 1309  CZ  PHE A 168     3159   3942   3753    260   -147    135       C  
ATOM   1310  N   TYR A 169      33.165  -1.876  11.736  1.00 18.67           N  
ANISOU 1310  N   TYR A 169     2236   2364   2493    160    -77    -86       N  
ATOM   1311  CA  TYR A 169      32.928  -1.571  10.325  1.00 20.33           C  
ANISOU 1311  CA  TYR A 169     2431   2592   2699    183    -48   -116       C  
ATOM   1312  C   TYR A 169      31.767  -0.583  10.148  1.00 21.39           C  
ANISOU 1312  C   TYR A 169     2586   2705   2835    114    -35   -139       C  
ATOM   1313  O   TYR A 169      31.734   0.125   9.156  1.00 19.39           O  
ANISOU 1313  O   TYR A 169     2309   2485   2574    112    -15   -149       O  
ATOM   1314  CB  TYR A 169      32.709  -2.862   9.504  1.00 19.81           C  
ANISOU 1314  CB  TYR A 169     2409   2482   2636    262    -45   -151       C  
ATOM   1315  CG  TYR A 169      34.046  -3.534   9.217  1.00 23.18           C  
ANISOU 1315  CG  TYR A 169     2799   2957   3051    357    -43   -132       C  
ATOM   1316  CD1 TYR A 169      34.506  -4.578   9.997  1.00 22.18           C  
ANISOU 1316  CD1 TYR A 169     2695   2799   2932    400    -71   -116       C  
ATOM   1317  CD2 TYR A 169      34.863  -3.073   8.192  1.00 25.26           C  
ANISOU 1317  CD2 TYR A 169     2999   3306   3292    407    -11   -121       C  
ATOM   1318  CE1 TYR A 169      35.741  -5.164   9.750  1.00 24.91           C  
ANISOU 1318  CE1 TYR A 169     3002   3197   3267    498    -68    -95       C  
ATOM   1319  CE2 TYR A 169      36.085  -3.635   7.938  1.00 27.31           C  
ANISOU 1319  CE2 TYR A 169     3212   3626   3538    503     -1    -95       C  
ATOM   1320  CZ  TYR A 169      36.527  -4.677   8.725  1.00 27.18           C  
ANISOU 1320  CZ  TYR A 169     3218   3577   3532    552    -30    -84       C  
ATOM   1321  OH  TYR A 169      37.750  -5.231   8.467  1.00 29.93           O  
ANISOU 1321  OH  TYR A 169     3515   3991   3866    660    -18    -56       O  
ATOM   1322  N   LYS A 170      30.837  -0.511  11.105  1.00 23.30           N  
ANISOU 1322  N   LYS A 170     2870   2900   3082     63    -43   -141       N  
ATOM   1323  CA  LYS A 170      29.773   0.508  11.026  1.00 25.04           C  
ANISOU 1323  CA  LYS A 170     3104   3109   3300      9    -28   -157       C  
ATOM   1324  C   LYS A 170      30.381   1.899  11.241  1.00 21.38           C  
ANISOU 1324  C   LYS A 170     2610   2692   2820    -29    -36   -139       C  
ATOM   1325  O   LYS A 170      30.027   2.853  10.562  1.00 18.96           O  
ANISOU 1325  O   LYS A 170     2296   2396   2511    -52    -25   -151       O  
ATOM   1326  CB  LYS A 170      28.663   0.240  12.051  1.00 32.95           C  
ANISOU 1326  CB  LYS A 170     4151   4063   4306    -23    -26   -155       C  
ATOM   1327  CG  LYS A 170      27.506   1.248  11.997  1.00 41.99           C  
ANISOU 1327  CG  LYS A 170     5305   5202   5446    -63     -6   -170       C  
ATOM   1328  CD  LYS A 170      26.190   0.632  12.488  1.00 48.06           C  
ANISOU 1328  CD  LYS A 170     6101   5931   6230    -78      8   -164       C  
ATOM   1329  CE  LYS A 170      25.028   1.638  12.476  1.00 52.61           C  
ANISOU 1329  CE  LYS A 170     6677   6512   6801   -104     33   -173       C  
ATOM   1330  NZ  LYS A 170      24.629   2.086  11.102  1.00 52.22           N  
ANISOU 1330  NZ  LYS A 170     6609   6465   6769   -101     36   -202       N  
ATOM   1331  N   THR A 171      31.312   1.994  12.194  1.00 21.43           N  
ANISOU 1331  N   THR A 171     2605   2720   2817    -40    -64   -107       N  
ATOM   1332  CA  THR A 171      32.045   3.231  12.440  1.00 23.62           C  
ANISOU 1332  CA  THR A 171     2858   3034   3083    -84    -91    -82       C  
ATOM   1333  C   THR A 171      32.886   3.608  11.232  1.00 24.01           C  
ANISOU 1333  C   THR A 171     2839   3142   3142    -73    -83    -62       C  
ATOM   1334  O   THR A 171      32.919   4.774  10.809  1.00 26.72           O  
ANISOU 1334  O   THR A 171     3169   3501   3483   -115    -90    -53       O  
ATOM   1335  CB  THR A 171      32.964   3.120  13.671  1.00 24.88           C  
ANISOU 1335  CB  THR A 171     3015   3206   3232    -97   -136    -46       C  
ATOM   1336  OG1 THR A 171      32.174   2.836  14.834  1.00 27.79           O  
ANISOU 1336  OG1 THR A 171     3452   3527   3580   -106   -139    -59       O  
ATOM   1337  CG2 THR A 171      33.745   4.424  13.872  1.00 23.97           C  
ANISOU 1337  CG2 THR A 171     2877   3120   3110   -155   -182    -17       C  
ATOM   1338  N   LEU A 172      33.576   2.623  10.675  1.00 19.51           N  
ANISOU 1338  N   LEU A 172     2230   2605   2580    -10    -67    -51       N  
ATOM   1339  CA  LEU A 172      34.372   2.854   9.478  1.00 20.65           C  
ANISOU 1339  CA  LEU A 172     2305   2819   2724     20    -46    -26       C  
ATOM   1340  C   LEU A 172      33.529   3.418   8.326  1.00 21.36           C  
ANISOU 1340  C   LEU A 172     2411   2900   2806     14    -15    -58       C  
ATOM   1341  O   LEU A 172      33.940   4.340   7.605  1.00 22.78           O  
ANISOU 1341  O   LEU A 172     2546   3129   2982    -10     -8    -28       O  
ATOM   1342  CB  LEU A 172      35.046   1.548   9.043  1.00 26.04           C  
ANISOU 1342  CB  LEU A 172     2961   3530   3404    115    -26    -23       C  
ATOM   1343  CG  LEU A 172      36.391   1.713   8.343  1.00 31.22           C  
ANISOU 1343  CG  LEU A 172     3520   4288   4055    154    -10     34       C  
ATOM   1344  CD1 LEU A 172      37.404   2.347   9.306  1.00 31.92           C  
ANISOU 1344  CD1 LEU A 172     3548   4422   4160     95    -57    100       C  
ATOM   1345  CD2 LEU A 172      36.905   0.363   7.817  1.00 33.31           C  
ANISOU 1345  CD2 LEU A 172     3776   4575   4307    275     17     24       C  
ATOM   1346  N   ARG A 173      32.339   2.862   8.156  1.00 18.95           N  
ANISOU 1346  N   ARG A 173     2166   2531   2501     31     -1   -110       N  
ATOM   1347  CA  ARG A 173      31.457   3.276   7.070  1.00 16.86           C  
ANISOU 1347  CA  ARG A 173     1921   2254   2230     29     21   -141       C  
ATOM   1348  C   ARG A 173      31.026   4.739   7.203  1.00 20.21           C  
ANISOU 1348  C   ARG A 173     2351   2673   2655    -43     10   -133       C  
ATOM   1349  O   ARG A 173      30.927   5.442   6.213  1.00 20.55           O  
ANISOU 1349  O   ARG A 173     2379   2739   2690    -49     23   -131       O  
ATOM   1350  CB  ARG A 173      30.229   2.367   7.017  1.00 17.68           C  
ANISOU 1350  CB  ARG A 173     2086   2288   2344     49     24   -190       C  
ATOM   1351  CG  ARG A 173      29.311   2.640   5.798  1.00 24.11           C  
ANISOU 1351  CG  ARG A 173     2920   3088   3152     54     37   -224       C  
ATOM   1352  CD  ARG A 173      27.985   1.902   5.911  1.00 22.43           C  
ANISOU 1352  CD  ARG A 173     2760   2804   2960     49     26   -260       C  
ATOM   1353  NE  ARG A 173      27.203   2.029   4.680  1.00 26.86           N  
ANISOU 1353  NE  ARG A 173     3338   3353   3515     60     27   -291       N  
ATOM   1354  CZ  ARG A 173      26.054   1.397   4.458  1.00 25.15           C  
ANISOU 1354  CZ  ARG A 173     3159   3078   3317     54      8   -319       C  
ATOM   1355  NH1 ARG A 173      25.556   0.603   5.387  1.00 24.98           N  
ANISOU 1355  NH1 ARG A 173     3158   3009   3324     35     -8   -313       N  
ATOM   1356  NH2 ARG A 173      25.410   1.556   3.312  1.00 22.27           N  
ANISOU 1356  NH2 ARG A 173     2810   2706   2945     63      0   -345       N  
ATOM   1357  N   ALA A 174      30.748   5.190   8.420  1.00 22.67           N  
ANISOU 1357  N   ALA A 174     2692   2950   2970    -89    -15   -131       N  
ATOM   1358  CA  ALA A 174      30.336   6.573   8.615  1.00 25.52           C  
ANISOU 1358  CA  ALA A 174     3075   3294   3326   -146    -33   -130       C  
ATOM   1359  C   ALA A 174      31.514   7.530   8.455  1.00 29.47           C  
ANISOU 1359  C   ALA A 174     3530   3841   3826   -187    -62    -79       C  
ATOM   1360  O   ALA A 174      31.409   8.541   7.740  1.00 25.11           O  
ANISOU 1360  O   ALA A 174     2973   3295   3273   -217    -65    -68       O  
ATOM   1361  CB  ALA A 174      29.701   6.745   9.960  1.00 25.23           C  
ANISOU 1361  CB  ALA A 174     3095   3210   3281   -168    -50   -146       C  
ATOM   1362  N   GLU A 175      32.627   7.209   9.128  1.00 31.51           N  
ANISOU 1362  N   GLU A 175     3752   4131   4089   -193    -88    -40       N  
ATOM   1363  CA  GLU A 175      33.830   8.042   9.094  1.00 33.36           C  
ANISOU 1363  CA  GLU A 175     3930   4414   4332   -243   -127     24       C  
ATOM   1364  C   GLU A 175      34.313   8.222   7.670  1.00 34.22           C  
ANISOU 1364  C   GLU A 175     3969   4590   4443   -227    -93     60       C  
ATOM   1365  O   GLU A 175      34.963   9.217   7.354  1.00 37.00           O  
ANISOU 1365  O   GLU A 175     4280   4975   4803   -284   -119    116       O  
ATOM   1366  CB  GLU A 175      34.962   7.433   9.942  1.00 34.48           C  
ANISOU 1366  CB  GLU A 175     4029   4591   4481   -239   -159     65       C  
ATOM   1367  CG  GLU A 175      34.743   7.468  11.458  1.00 36.04           C  
ANISOU 1367  CG  GLU A 175     4294   4732   4667   -267   -208     46       C  
ATOM   1368  CD  GLU A 175      34.933   8.855  12.065  1.00 40.75           C  
ANISOU 1368  CD  GLU A 175     4927   5297   5258   -351   -280     64       C  
ATOM   1369  OE1 GLU A 175      36.098   9.244  12.315  1.00 41.33           O  
ANISOU 1369  OE1 GLU A 175     4948   5408   5347   -399   -338    126       O  
ATOM   1370  OE2 GLU A 175      33.916   9.551  12.305  1.00 40.47           O  
ANISOU 1370  OE2 GLU A 175     4975   5198   5204   -366   -283     19       O  
ATOM   1371  N   GLN A 176      34.006   7.257   6.811  1.00 33.25           N  
ANISOU 1371  N   GLN A 176     3839   4486   4310   -150    -37     31       N  
ATOM   1372  CA  GLN A 176      34.408   7.325   5.411  1.00 37.44           C  
ANISOU 1372  CA  GLN A 176     4314   5085   4827   -115      4     59       C  
ATOM   1373  C   GLN A 176      33.228   7.551   4.458  1.00 37.20           C  
ANISOU 1373  C   GLN A 176     4335   5018   4780   -101     32      9       C  
ATOM   1374  O   GLN A 176      33.397   7.442   3.238  1.00 35.35           O  
ANISOU 1374  O   GLN A 176     4073   4835   4523    -56     70     20       O  
ATOM   1375  CB  GLN A 176      35.141   6.046   5.001  1.00 41.29           C  
ANISOU 1375  CB  GLN A 176     4755   5632   5301    -20     43     66       C  
ATOM   1376  CG  GLN A 176      36.574   5.935   5.517  1.00 45.54           C  
ANISOU 1376  CG  GLN A 176     5204   6245   5853    -23     26    141       C  
ATOM   1377  CD  GLN A 176      37.177   4.559   5.270  1.00 48.14           C  
ANISOU 1377  CD  GLN A 176     5504   6620   6168     90     63    137       C  
ATOM   1378  OE1 GLN A 176      36.533   3.679   4.692  1.00 46.83           O  
ANISOU 1378  OE1 GLN A 176     5393   6420   5979    168     96     75       O  
ATOM   1379  NE2 GLN A 176      38.419   4.368   5.708  1.00 49.26           N  
ANISOU 1379  NE2 GLN A 176     5559   6833   6322    101     51    205       N  
ATOM   1380  N   ALA A 177      32.058   7.862   5.021  1.00 37.55           N  
ANISOU 1380  N   ALA A 177     4453   4982   4833   -132     12    -41       N  
ATOM   1381  CA  ALA A 177      30.796   8.044   4.271  1.00 38.50           C  
ANISOU 1381  CA  ALA A 177     4623   5062   4946   -120     29    -89       C  
ATOM   1382  C   ALA A 177      30.566   6.981   3.190  1.00 41.16           C  
ANISOU 1382  C   ALA A 177     4960   5416   5262    -42     66   -119       C  
ATOM   1383  O   ALA A 177      30.257   7.312   2.039  1.00 42.44           O  
ANISOU 1383  O   ALA A 177     5125   5596   5404    -27     84   -124       O  
ATOM   1384  CB  ALA A 177      30.740   9.441   3.646  1.00 37.67           C  
ANISOU 1384  CB  ALA A 177     4513   4964   4836   -171     17    -58       C  
ATOM   1385  N   SER A 178      30.717   5.710   3.568  1.00 41.22           N  
ANISOU 1385  N   SER A 178     4976   5414   5273      9     72   -142       N  
ATOM   1386  CA  SER A 178      30.540   4.576   2.651  1.00 41.60           C  
ANISOU 1386  CA  SER A 178     5045   5462   5300     90     93   -178       C  
ATOM   1387  C   SER A 178      31.415   4.624   1.401  1.00 45.23           C  
ANISOU 1387  C   SER A 178     5463   6005   5719    147    127   -151       C  
ATOM   1388  O   SER A 178      31.029   4.087   0.360  1.00 46.20           O  
ANISOU 1388  O   SER A 178     5621   6124   5810    209    141   -188       O  
ATOM   1389  CB  SER A 178      29.079   4.461   2.215  1.00 38.76           C  
ANISOU 1389  CB  SER A 178     4746   5036   4944     83     82   -232       C  
ATOM   1390  OG  SER A 178      28.239   4.256   3.329  1.00 35.23           O  
ANISOU 1390  OG  SER A 178     4330   4525   4531     44     60   -251       O  
ATOM   1391  N   GLN A 179      32.588   5.245   1.505  1.00 48.14           N  
ANISOU 1391  N   GLN A 179     5756   6450   6085    128    139    -82       N  
ATOM   1392  CA  GLN A 179      33.588   5.203   0.437  1.00 53.75           C  
ANISOU 1392  CA  GLN A 179     6407   7261   6755    192    183    -37       C  
ATOM   1393  C   GLN A 179      34.801   4.390   0.899  1.00 57.60           C  
ANISOU 1393  C   GLN A 179     6837   7807   7243    250    196     -1       C  
ATOM   1394  O   GLN A 179      35.359   4.659   1.960  1.00 55.60           O  
ANISOU 1394  O   GLN A 179     6541   7558   7026    195    168     39       O  
ATOM   1395  CB  GLN A 179      34.031   6.616   0.033  1.00 57.44           C  
ANISOU 1395  CB  GLN A 179     6815   7787   7222    121    187     37       C  
ATOM   1396  CG  GLN A 179      32.945   7.685   0.103  1.00 59.56           C  
ANISOU 1396  CG  GLN A 179     7136   7984   7509     37    154     16       C  
ATOM   1397  CD  GLN A 179      31.961   7.610  -1.050  1.00 60.41           C  
ANISOU 1397  CD  GLN A 179     7300   8070   7583     77    171    -33       C  
ATOM   1398  OE1 GLN A 179      30.791   7.271  -0.861  1.00 60.95           O  
ANISOU 1398  OE1 GLN A 179     7438   8057   7664     76    149   -101       O  
ATOM   1399  NE2 GLN A 179      32.427   7.941  -2.251  1.00 61.10           N  
ANISOU 1399  NE2 GLN A 179     7355   8234   7626    109    208      8       N  
ATOM   1400  N   GLU A 180      35.214   3.405   0.108  1.00 64.60           N  
ANISOU 1400  N   GLU A 180     7725   8735   8085    368    235    -18       N  
ATOM   1401  CA  GLU A 180      36.346   2.559   0.485  1.00 68.99           C  
ANISOU 1401  CA  GLU A 180     8228   9348   8638    445    250     13       C  
ATOM   1402  C   GLU A 180      37.697   3.239   0.262  1.00 70.84           C  
ANISOU 1402  C   GLU A 180     8331   9717   8866    440    284    120       C  
ATOM   1403  O   GLU A 180      37.776   4.309  -0.343  1.00 71.22           O  
ANISOU 1403  O   GLU A 180     8336   9816   8906    384    299    172       O  
ATOM   1404  CB  GLU A 180      36.314   1.242  -0.293  1.00 72.48           C  
ANISOU 1404  CB  GLU A 180     8729   9781   9028    589    277    -47       C  
ATOM   1405  CG  GLU A 180      35.148   0.337   0.054  1.00 74.95           C  
ANISOU 1405  CG  GLU A 180     9162   9959   9357    593    231   -140       C  
ATOM   1406  CD  GLU A 180      35.371  -1.098  -0.395  1.00 77.67           C  
ANISOU 1406  CD  GLU A 180     9569  10281   9660    735    237   -191       C  
ATOM   1407  OE1 GLU A 180      36.289  -1.338  -1.213  1.00 78.88           O  
ANISOU 1407  OE1 GLU A 180     9685  10530   9757    848    288   -167       O  
ATOM   1408  OE2 GLU A 180      34.633  -1.988   0.078  1.00 77.90           O  
ANISOU 1408  OE2 GLU A 180     9688  10199   9712    736    189   -251       O  
ATOM   1409  N   VAL A 181      38.756   2.607   0.761  1.00 72.54           N  
ANISOU 1409  N   VAL A 181     8481   9991   9090    497    291    162       N  
ATOM   1410  CA  VAL A 181      40.122   3.055   0.502  1.00 73.83           C  
ANISOU 1410  CA  VAL A 181     8503  10299   9249    509    327    275       C  
ATOM   1411  C   VAL A 181      40.988   1.869   0.070  1.00 74.08           C  
ANISOU 1411  C   VAL A 181     8499  10410   9236    676    380    281       C  
ATOM   1412  O   VAL A 181      42.186   1.818   0.349  1.00 74.12           O  
ANISOU 1412  O   VAL A 181     8385  10521   9254    704    396    369       O  
ATOM   1413  CB  VAL A 181      40.755   3.738   1.740  1.00 74.10           C  
ANISOU 1413  CB  VAL A 181     8461  10344   9350    390    268    349       C  
ATOM   1414  CG1 VAL A 181      39.899   4.914   2.201  1.00 73.02           C  
ANISOU 1414  CG1 VAL A 181     8376  10119   9248    240    211    335       C  
ATOM   1415  CG2 VAL A 181      40.957   2.736   2.871  1.00 73.75           C  
ANISOU 1415  CG2 VAL A 181     8440  10251   9332    426    231    319       C  
ATOM   1416  N   THR A 186      43.118  -1.501   8.341  1.00 69.10           N  
ANISOU 1416  N   THR A 186     7867   9530   8858    581     27    327       N  
ATOM   1417  CA  THR A 186      41.853  -2.129   8.692  1.00 67.06           C  
ANISOU 1417  CA  THR A 186     7757   9130   8592    576     10    231       C  
ATOM   1418  C   THR A 186      42.090  -3.449   9.421  1.00 66.79           C  
ANISOU 1418  C   THR A 186     7767   9047   8562    661    -17    216       C  
ATOM   1419  O   THR A 186      41.770  -3.574  10.604  1.00 68.54           O  
ANISOU 1419  O   THR A 186     8041   9199   8804    597    -72    210       O  
ATOM   1420  CB  THR A 186      40.977  -2.365   7.439  1.00 67.25           C  
ANISOU 1420  CB  THR A 186     7854   9118   8581    632     63    159       C  
ATOM   1421  OG1 THR A 186      39.812  -3.125   7.791  1.00 65.38           O  
ANISOU 1421  OG1 THR A 186     7750   8746   8345    630     39     78       O  
ATOM   1422  CG2 THR A 186      41.764  -3.098   6.350  1.00 68.46           C  
ANISOU 1422  CG2 THR A 186     7963   9354   8696    791    122    169       C  
ATOM   1423  N   GLU A 187      42.659  -4.423   8.715  1.00 65.36           N  
ANISOU 1423  N   GLU A 187     7573   8905   8358    812     22    211       N  
ATOM   1424  CA  GLU A 187      42.939  -5.736   9.288  1.00 64.02           C  
ANISOU 1424  CA  GLU A 187     7450   8684   8189    910     -5    197       C  
ATOM   1425  C   GLU A 187      43.737  -5.610  10.576  1.00 61.63           C  
ANISOU 1425  C   GLU A 187     7081   8415   7921    860    -63    268       C  
ATOM   1426  O   GLU A 187      43.407  -6.232  11.592  1.00 61.14           O  
ANISOU 1426  O   GLU A 187     7095   8263   7872    843   -114    250       O  
ATOM   1427  CB  GLU A 187      43.709  -6.618   8.298  1.00 67.54           C  
ANISOU 1427  CB  GLU A 187     7868   9195   8599   1095     47    196       C  
ATOM   1428  CG  GLU A 187      44.406  -7.806   8.964  1.00 71.55           C  
ANISOU 1428  CG  GLU A 187     8387   9686   9114   1207     15    211       C  
ATOM   1429  CD  GLU A 187      45.305  -8.594   8.020  1.00 75.12           C  
ANISOU 1429  CD  GLU A 187     8799  10219   9524   1408     70    218       C  
ATOM   1430  OE1 GLU A 187      45.812  -8.015   7.035  1.00 76.60           O  
ANISOU 1430  OE1 GLU A 187     8892  10531   9683   1451    137    252       O  
ATOM   1431  OE2 GLU A 187      45.506  -9.801   8.269  1.00 76.04           O  
ANISOU 1431  OE2 GLU A 187     8984  10275   9633   1528     46    192       O  
ATOM   1432  N   THR A 188      44.786  -4.793  10.525  1.00 53.39           N  
ANISOU 1432  N   THR A 188     5893   7502   6891    833    -59    355       N  
ATOM   1433  CA  THR A 188      45.712  -4.679  11.638  1.00 44.91           C  
ANISOU 1433  CA  THR A 188     4739   6475   5848    795   -121    433       C  
ATOM   1434  C   THR A 188      45.094  -3.950  12.825  1.00 33.97           C  
ANISOU 1434  C   THR A 188     3414   5012   4482    635   -193    426       C  
ATOM   1435  O   THR A 188      45.255  -4.381  13.968  1.00 32.90           O  
ANISOU 1435  O   THR A 188     3309   4835   4356    621   -254    439       O  
ATOM   1436  CB  THR A 188      47.003  -3.956  11.219  1.00 47.50           C  
ANISOU 1436  CB  THR A 188     4885   6969   6192    797   -105    541       C  
ATOM   1437  OG1 THR A 188      47.598  -4.642  10.110  1.00 50.24           O  
ANISOU 1437  OG1 THR A 188     5175   7404   6511    965    -26    552       O  
ATOM   1438  CG2 THR A 188      47.987  -3.936  12.374  1.00 47.97           C  
ANISOU 1438  CG2 THR A 188     4861   7076   6288    762   -182    625       C  
ATOM   1439  N   LEU A 189      44.407  -2.843  12.563  1.00 29.13           N  
ANISOU 1439  N   LEU A 189     2821   4381   3868    523   -187    406       N  
ATOM   1440  CA  LEU A 189      43.762  -2.102  13.644  1.00 30.88           C  
ANISOU 1440  CA  LEU A 189     3111   4527   4095    386   -249    391       C  
ATOM   1441  C   LEU A 189      42.637  -2.939  14.296  1.00 26.34           C  
ANISOU 1441  C   LEU A 189     2683   3823   3505    397   -257    316       C  
ATOM   1442  O   LEU A 189      42.430  -2.891  15.512  1.00 25.84           O  
ANISOU 1442  O   LEU A 189     2673   3708   3439    337   -314    319       O  
ATOM   1443  CB  LEU A 189      43.214  -0.772  13.132  1.00 29.79           C  
ANISOU 1443  CB  LEU A 189     2972   4390   3955    282   -238    382       C  
ATOM   1444  CG  LEU A 189      42.668   0.157  14.210  1.00 31.23           C  
ANISOU 1444  CG  LEU A 189     3223   4505   4137    150   -305    370       C  
ATOM   1445  CD1 LEU A 189      43.816   0.697  15.044  1.00 36.12           C  
ANISOU 1445  CD1 LEU A 189     3762   5185   4779     88   -388    454       C  
ATOM   1446  CD2 LEU A 189      41.879   1.295  13.563  1.00 34.70           C  
ANISOU 1446  CD2 LEU A 189     3690   4922   4571     73   -283    341       C  
ATOM   1447  N   LEU A 190      41.926  -3.709  13.481  1.00 25.89           N  
ANISOU 1447  N   LEU A 190     2688   3714   3434    474   -203    254       N  
ATOM   1448  CA  LEU A 190      40.900  -4.598  14.006  1.00 26.28           C  
ANISOU 1448  CA  LEU A 190     2865   3646   3476    483   -213    198       C  
ATOM   1449  C   LEU A 190      41.464  -5.601  15.000  1.00 27.15           C  
ANISOU 1449  C   LEU A 190     2991   3734   3591    535   -259    227       C  
ATOM   1450  O   LEU A 190      40.858  -5.856  16.032  1.00 28.29           O  
ANISOU 1450  O   LEU A 190     3215   3802   3731    485   -294    218       O  
ATOM   1451  CB  LEU A 190      40.198  -5.352  12.872  1.00 27.77           C  
ANISOU 1451  CB  LEU A 190     3114   3784   3654    563   -163    134       C  
ATOM   1452  CG  LEU A 190      39.032  -6.230  13.373  1.00 26.25           C  
ANISOU 1452  CG  LEU A 190     3048   3462   3463    552   -181     85       C  
ATOM   1453  CD1 LEU A 190      37.842  -5.403  13.768  1.00 23.83           C  
ANISOU 1453  CD1 LEU A 190     2790   3108   3156    432   -181     61       C  
ATOM   1454  CD2 LEU A 190      38.646  -7.229  12.289  1.00 29.72           C  
ANISOU 1454  CD2 LEU A 190     3548   3849   3895    651   -156     31       C  
ATOM   1455  N   VAL A 191      42.629  -6.165  14.696  1.00 29.03           N  
ANISOU 1455  N   VAL A 191     3151   4044   3836    639   -256    268       N  
ATOM   1456  CA  VAL A 191      43.287  -7.054  15.638  1.00 28.12           C  
ANISOU 1456  CA  VAL A 191     3040   3918   3728    693   -306    305       C  
ATOM   1457  C   VAL A 191      43.778  -6.276  16.854  1.00 29.58           C  
ANISOU 1457  C   VAL A 191     3181   4138   3919    591   -372    364       C  
ATOM   1458  O   VAL A 191      43.590  -6.723  17.978  1.00 28.74           O  
ANISOU 1458  O   VAL A 191     3142   3971   3806    569   -422    370       O  
ATOM   1459  CB  VAL A 191      44.468  -7.805  15.008  1.00 28.50           C  
ANISOU 1459  CB  VAL A 191     3004   4045   3779    843   -286    340       C  
ATOM   1460  CG1 VAL A 191      45.179  -8.627  16.067  1.00 24.92           C  
ANISOU 1460  CG1 VAL A 191     2550   3583   3336    893   -346    386       C  
ATOM   1461  CG2 VAL A 191      43.976  -8.692  13.850  1.00 30.92           C  
ANISOU 1461  CG2 VAL A 191     3382   4300   4067    960   -231    272       C  
ATOM   1462  N   GLN A 192      44.380  -5.107  16.625  1.00 29.83           N  
ANISOU 1462  N   GLN A 192     3110   4263   3961    526   -379    408       N  
ATOM   1463  CA  GLN A 192      44.926  -4.288  17.712  1.00 31.99           C  
ANISOU 1463  CA  GLN A 192     3346   4569   4242    424   -458    464       C  
ATOM   1464  C   GLN A 192      43.874  -3.878  18.747  1.00 30.06           C  
ANISOU 1464  C   GLN A 192     3225   4225   3969    322   -494    422       C  
ATOM   1465  O   GLN A 192      44.152  -3.839  19.943  1.00 31.12           O  
ANISOU 1465  O   GLN A 192     3387   4346   4093    281   -566    451       O  
ATOM   1466  CB  GLN A 192      45.589  -3.028  17.150  1.00 34.85           C  
ANISOU 1466  CB  GLN A 192     3588   5031   4623    356   -463    516       C  
ATOM   1467  CG  GLN A 192      46.269  -2.128  18.203  1.00 37.65           C  
ANISOU 1467  CG  GLN A 192     3900   5417   4989    244   -564    580       C  
ATOM   1468  CD  GLN A 192      47.516  -2.757  18.823  1.00 40.49           C  
ANISOU 1468  CD  GLN A 192     4172   5845   5369    299   -622    659       C  
ATOM   1469  OE1 GLN A 192      47.436  -3.769  19.521  1.00 43.39           O  
ANISOU 1469  OE1 GLN A 192     4604   6161   5722    362   -640    644       O  
ATOM   1470  NE2 GLN A 192      48.674  -2.158  18.569  1.00 41.20           N  
ANISOU 1470  NE2 GLN A 192     4109   6051   5493    272   -655    751       N  
ATOM   1471  N   ASN A 193      42.676  -3.548  18.283  1.00 28.64           N  
ANISOU 1471  N   ASN A 193     3121   3984   3775    286   -445    357       N  
ATOM   1472  CA  ASN A 193      41.623  -3.089  19.180  1.00 26.18           C  
ANISOU 1472  CA  ASN A 193     2920   3594   3434    200   -465    321       C  
ATOM   1473  C   ASN A 193      40.772  -4.251  19.725  1.00 27.48           C  
ANISOU 1473  C   ASN A 193     3191   3669   3583    242   -450    289       C  
ATOM   1474  O   ASN A 193      39.798  -4.021  20.446  1.00 27.67           O  
ANISOU 1474  O   ASN A 193     3305   3632   3578    185   -452    264       O  
ATOM   1475  CB  ASN A 193      40.735  -2.061  18.469  1.00 25.20           C  
ANISOU 1475  CB  ASN A 193     2815   3453   3304    138   -423    275       C  
ATOM   1476  CG  ASN A 193      41.474  -0.752  18.158  1.00 29.04           C  
ANISOU 1476  CG  ASN A 193     3218   4013   3805     69   -454    314       C  
ATOM   1477  OD1 ASN A 193      42.640  -0.581  18.510  1.00 30.91           O  
ANISOU 1477  OD1 ASN A 193     3374   4313   4057     58   -511    379       O  
ATOM   1478  ND2 ASN A 193      40.791   0.164  17.478  1.00 31.87           N  
ANISOU 1478  ND2 ASN A 193     3591   4359   4161     19   -421    281       N  
ATOM   1479  N   ALA A 194      41.140  -5.490  19.382  1.00 27.16           N  
ANISOU 1479  N   ALA A 194     3141   3620   3559    342   -437    296       N  
ATOM   1480  CA  ALA A 194      40.487  -6.673  19.941  1.00 25.50           C  
ANISOU 1480  CA  ALA A 194     3028   3320   3341    378   -439    283       C  
ATOM   1481  C   ALA A 194      40.866  -6.829  21.408  1.00 27.75           C  
ANISOU 1481  C   ALA A 194     3343   3597   3602    352   -506    329       C  
ATOM   1482  O   ALA A 194      41.881  -6.280  21.832  1.00 29.72           O  
ANISOU 1482  O   ALA A 194     3525   3915   3850    334   -557    373       O  
ATOM   1483  CB  ALA A 194      40.873  -7.917  19.159  1.00 28.68           C  
ANISOU 1483  CB  ALA A 194     3423   3708   3766    500   -420    276       C  
ATOM   1484  N   ASN A 195      40.078  -7.574  22.189  1.00 26.99           N  
ANISOU 1484  N   ASN A 195     3347   3420   3486    346   -511    326       N  
ATOM   1485  CA  ASN A 195      40.434  -7.727  23.606  1.00 30.58           C  
ANISOU 1485  CA  ASN A 195     3839   3871   3909    325   -573    373       C  
ATOM   1486  C   ASN A 195      41.585  -8.718  23.725  1.00 31.64           C  
ANISOU 1486  C   ASN A 195     3932   4025   4065    417   -617    418       C  
ATOM   1487  O   ASN A 195      41.933  -9.383  22.743  1.00 29.84           O  
ANISOU 1487  O   ASN A 195     3665   3799   3872    504   -591    407       O  
ATOM   1488  CB  ASN A 195      39.209  -8.115  24.483  1.00 21.97           C  
ANISOU 1488  CB  ASN A 195     2864   2701   2781    283   -559    369       C  
ATOM   1489  CG  ASN A 195      38.647  -9.502  24.201  1.00 25.90           C  
ANISOU 1489  CG  ASN A 195     3418   3118   3306    337   -538    368       C  
ATOM   1490  OD1 ASN A 195      39.367 -10.444  23.863  1.00 27.88           O  
ANISOU 1490  OD1 ASN A 195     3651   3357   3587    421   -560    383       O  
ATOM   1491  ND2 ASN A 195      37.335  -9.639  24.387  1.00 28.23           N  
ANISOU 1491  ND2 ASN A 195     3784   3353   3588    288   -500    356       N  
ATOM   1492  N   PRO A 196      42.214  -8.788  24.912  1.00 32.07           N  
ANISOU 1492  N   PRO A 196     3996   4095   4094    406   -688    469       N  
ATOM   1493  CA  PRO A 196      43.415  -9.611  25.091  1.00 33.35           C  
ANISOU 1493  CA  PRO A 196     4105   4288   4278    495   -738    521       C  
ATOM   1494  C   PRO A 196      43.302 -11.044  24.567  1.00 33.09           C  
ANISOU 1494  C   PRO A 196     4110   4190   4273    603   -714    513       C  
ATOM   1495  O   PRO A 196      44.161 -11.472  23.799  1.00 34.22           O  
ANISOU 1495  O   PRO A 196     4178   4375   4448    702   -709    521       O  
ATOM   1496  CB  PRO A 196      43.608  -9.609  26.619  1.00 35.61           C  
ANISOU 1496  CB  PRO A 196     4447   4564   4518    453   -814    568       C  
ATOM   1497  CG  PRO A 196      43.048  -8.294  27.047  1.00 35.36           C  
ANISOU 1497  CG  PRO A 196     4445   4546   4444    342   -816    543       C  
ATOM   1498  CD  PRO A 196      41.840  -8.086  26.153  1.00 32.67           C  
ANISOU 1498  CD  PRO A 196     4137   4164   4113    319   -726    481       C  
ATOM   1499  N   ASP A 197      42.269 -11.773  24.974  1.00 34.60           N  
ANISOU 1499  N   ASP A 197     4417   4280   4450    588   -702    501       N  
ATOM   1500  CA  ASP A 197      42.130 -13.184  24.613  1.00 37.45           C  
ANISOU 1500  CA  ASP A 197     4837   4557   4837    680   -700    497       C  
ATOM   1501  C   ASP A 197      41.901 -13.394  23.112  1.00 37.10           C  
ANISOU 1501  C   ASP A 197     4774   4497   4826    740   -644    438       C  
ATOM   1502  O   ASP A 197      42.477 -14.301  22.506  1.00 38.22           O  
ANISOU 1502  O   ASP A 197     4910   4620   4990    859   -651    434       O  
ATOM   1503  CB  ASP A 197      40.978 -13.822  25.400  1.00 40.81           C  
ANISOU 1503  CB  ASP A 197     5387   4877   5242    625   -704    510       C  
ATOM   1504  CG  ASP A 197      41.245 -13.868  26.902  1.00 45.50           C  
ANISOU 1504  CG  ASP A 197     6018   5478   5793    591   -761    573       C  
ATOM   1505  OD1 ASP A 197      42.424 -13.777  27.316  1.00 45.63           O  
ANISOU 1505  OD1 ASP A 197     5975   5558   5805    633   -816    611       O  
ATOM   1506  OD2 ASP A 197      40.266 -13.995  27.668  1.00 47.99           O  
ANISOU 1506  OD2 ASP A 197     6419   5739   6075    523   -752    591       O  
ATOM   1507  N   CYS A 198      41.045 -12.566  22.519  1.00 32.97           N  
ANISOU 1507  N   CYS A 198     4247   3979   4300    666   -590    391       N  
ATOM   1508  CA  CYS A 198      40.815 -12.627  21.086  1.00 33.24           C  
ANISOU 1508  CA  CYS A 198     4264   4007   4357    716   -540    334       C  
ATOM   1509  C   CYS A 198      42.062 -12.190  20.309  1.00 36.26           C  
ANISOU 1509  C   CYS A 198     4524   4504   4749    793   -526    341       C  
ATOM   1510  O   CYS A 198      42.417 -12.809  19.295  1.00 35.57           O  
ANISOU 1510  O   CYS A 198     4426   4415   4674    906   -503    315       O  
ATOM   1511  CB  CYS A 198      39.607 -11.765  20.700  1.00 33.92           C  
ANISOU 1511  CB  CYS A 198     4371   4080   4437    613   -490    290       C  
ATOM   1512  SG  CYS A 198      38.003 -12.536  21.091  1.00 42.87           S  
ANISOU 1512  SG  CYS A 198     5635   5079   5574    549   -488    281       S  
ATOM   1513  N   LYS A 199      42.736 -11.144  20.786  1.00 36.03           N  
ANISOU 1513  N   LYS A 199     4404   4573   4711    736   -543    380       N  
ATOM   1514  CA  LYS A 199      43.951 -10.671  20.121  1.00 36.66           C  
ANISOU 1514  CA  LYS A 199     4350   4775   4806    794   -534    407       C  
ATOM   1515  C   LYS A 199      45.002 -11.786  20.060  1.00 39.25           C  
ANISOU 1515  C   LYS A 199     4645   5120   5147    941   -557    442       C  
ATOM   1516  O   LYS A 199      45.724 -11.921  19.071  1.00 39.62           O  
ANISOU 1516  O   LYS A 199     4612   5238   5203   1046   -521    443       O  
ATOM   1517  CB  LYS A 199      44.530  -9.435  20.826  1.00 36.66           C  
ANISOU 1517  CB  LYS A 199     4267   4863   4801    694   -574    456       C  
ATOM   1518  CG  LYS A 199      45.684  -8.778  20.047  1.00 37.68           C  
ANISOU 1518  CG  LYS A 199     4239   5125   4951    726   -561    497       C  
ATOM   1519  CD  LYS A 199      46.351  -7.642  20.822  1.00 39.25           C  
ANISOU 1519  CD  LYS A 199     4360   5400   5152    620   -626    556       C  
ATOM   1520  CE  LYS A 199      45.481  -6.405  20.877  1.00 38.23           C  
ANISOU 1520  CE  LYS A 199     4274   5246   5006    485   -618    519       C  
ATOM   1521  NZ  LYS A 199      46.051  -5.299  21.702  1.00 38.92           N  
ANISOU 1521  NZ  LYS A 199     4316   5383   5090    376   -698    569       N  
ATOM   1522  N   THR A 200      45.068 -12.592  21.114  1.00 38.58           N  
ANISOU 1522  N   THR A 200     4627   4973   5058    957   -615    472       N  
ATOM   1523  CA  THR A 200      46.024 -13.691  21.182  1.00 39.14           C  
ANISOU 1523  CA  THR A 200     4681   5049   5140   1100   -647    507       C  
ATOM   1524  C   THR A 200      45.753 -14.733  20.105  1.00 39.45           C  
ANISOU 1524  C   THR A 200     4787   5017   5184   1230   -608    451       C  
ATOM   1525  O   THR A 200      46.666 -15.154  19.379  1.00 40.65           O  
ANISOU 1525  O   THR A 200     4873   5231   5342   1375   -589    459       O  
ATOM   1526  CB  THR A 200      45.989 -14.378  22.560  1.00 40.31           C  
ANISOU 1526  CB  THR A 200     4910   5126   5279   1082   -722    550       C  
ATOM   1527  OG1 THR A 200      46.450 -13.461  23.558  1.00 40.15           O  
ANISOU 1527  OG1 THR A 200     4828   5181   5246    984   -771    604       O  
ATOM   1528  CG2 THR A 200      46.879 -15.620  22.562  1.00 41.87           C  
ANISOU 1528  CG2 THR A 200     5109   5310   5491   1243   -756    580       C  
ATOM   1529  N   ILE A 201      44.493 -15.151  20.023  1.00 36.92           N  
ANISOU 1529  N   ILE A 201     4600   4569   4861   1181   -600    398       N  
ATOM   1530  CA  ILE A 201      44.042 -16.099  19.009  1.00 39.05           C  
ANISOU 1530  CA  ILE A 201     4960   4746   5133   1282   -578    335       C  
ATOM   1531  C   ILE A 201      44.312 -15.564  17.598  1.00 36.81           C  
ANISOU 1531  C   ILE A 201     4599   4547   4840   1344   -508    293       C  
ATOM   1532  O   ILE A 201      44.768 -16.299  16.716  1.00 37.41           O  
ANISOU 1532  O   ILE A 201     4689   4617   4907   1499   -491    264       O  
ATOM   1533  CB  ILE A 201      42.531 -16.407  19.184  1.00 40.64           C  
ANISOU 1533  CB  ILE A 201     5299   4805   5338   1178   -587    297       C  
ATOM   1534  CG1 ILE A 201      42.327 -17.324  20.393  1.00 41.63           C  
ANISOU 1534  CG1 ILE A 201     5519   4831   5469   1159   -655    343       C  
ATOM   1535  CG2 ILE A 201      41.948 -17.019  17.911  1.00 41.34           C  
ANISOU 1535  CG2 ILE A 201     5468   4811   5429   1249   -564    221       C  
ATOM   1536  CD1 ILE A 201      40.904 -17.348  20.938  1.00 41.29           C  
ANISOU 1536  CD1 ILE A 201     5573   4686   5428   1019   -662    341       C  
ATOM   1537  N   LEU A 202      44.055 -14.273  17.412  1.00 33.60           N  
ANISOU 1537  N   LEU A 202     4117   4219   4431   1230   -469    292       N  
ATOM   1538  CA  LEU A 202      44.208 -13.601  16.121  1.00 35.31           C  
ANISOU 1538  CA  LEU A 202     4259   4520   4636   1263   -401    261       C  
ATOM   1539  C   LEU A 202      45.665 -13.453  15.671  1.00 40.63           C  
ANISOU 1539  C   LEU A 202     4789   5343   5307   1383   -376    312       C  
ATOM   1540  O   LEU A 202      45.980 -13.679  14.503  1.00 39.46           O  
ANISOU 1540  O   LEU A 202     4617   5237   5139   1505   -323    283       O  
ATOM   1541  CB  LEU A 202      43.545 -12.222  16.177  1.00 33.61           C  
ANISOU 1541  CB  LEU A 202     4006   4343   4421   1100   -376    256       C  
ATOM   1542  CG  LEU A 202      42.012 -12.279  16.223  1.00 33.15           C  
ANISOU 1542  CG  LEU A 202     4072   4160   4362   1002   -376    199       C  
ATOM   1543  CD1 LEU A 202      41.406 -10.927  16.487  1.00 35.34           C  
ANISOU 1543  CD1 LEU A 202     4315   4474   4638    851   -358    201       C  
ATOM   1544  CD2 LEU A 202      41.507 -12.836  14.901  1.00 32.86           C  
ANISOU 1544  CD2 LEU A 202     4100   4068   4317   1084   -341    129       C  
ATOM   1545  N   LYS A 203      46.541 -13.055  16.592  1.00 44.37           N  
ANISOU 1545  N   LYS A 203     5162   5900   5796   1347   -415    391       N  
ATOM   1546  CA  LYS A 203      47.964 -12.907  16.284  1.00 50.82           C  
ANISOU 1546  CA  LYS A 203     5821   6870   6620   1450   -399    460       C  
ATOM   1547  C   LYS A 203      48.556 -14.237  15.828  1.00 53.96           C  
ANISOU 1547  C   LYS A 203     6249   7250   7005   1660   -390    449       C  
ATOM   1548  O   LYS A 203      49.414 -14.284  14.944  1.00 54.92           O  
ANISOU 1548  O   LYS A 203     6269   7484   7113   1794   -336    470       O  
ATOM   1549  CB  LYS A 203      48.733 -12.386  17.504  1.00 52.34           C  
ANISOU 1549  CB  LYS A 203     5919   7133   6836   1367   -467    549       C  
ATOM   1550  CG  LYS A 203      48.293 -11.002  17.972  1.00 53.83           C  
ANISOU 1550  CG  LYS A 203     6079   7344   7030   1172   -485    561       C  
ATOM   1551  CD  LYS A 203      48.710 -10.748  19.419  1.00 58.10           C  
ANISOU 1551  CD  LYS A 203     6601   7891   7581   1084   -577    624       C  
ATOM   1552  CE  LYS A 203      50.152 -10.257  19.523  1.00 61.69           C  
ANISOU 1552  CE  LYS A 203     6875   8502   8063   1102   -609    724       C  
ATOM   1553  NZ  LYS A 203      50.212  -8.773  19.707  1.00 61.38           N  
ANISOU 1553  NZ  LYS A 203     6761   8527   8033    938   -635    757       N  
ATOM   1554  N   ALA A 204      48.085 -15.317  16.442  1.00 54.14           N  
ANISOU 1554  N   ALA A 204     6414   7129   7029   1691   -444    419       N  
ATOM   1555  CA  ALA A 204      48.583 -16.654  16.154  1.00 54.76           C  
ANISOU 1555  CA  ALA A 204     6550   7160   7096   1890   -454    405       C  
ATOM   1556  C   ALA A 204      48.008 -17.227  14.865  1.00 57.51           C  
ANISOU 1556  C   ALA A 204     7005   7435   7412   1998   -406    312       C  
ATOM   1557  O   ALA A 204      48.370 -18.330  14.464  1.00 58.16           O  
ANISOU 1557  O   ALA A 204     7155   7467   7475   2178   -414    286       O  
ATOM   1558  CB  ALA A 204      48.279 -17.577  17.309  1.00 54.05           C  
ANISOU 1558  CB  ALA A 204     6581   6934   7021   1873   -540    415       C  
ATOM   1559  N   LEU A 205      47.106 -16.490  14.224  1.00 58.48           N  
ANISOU 1559  N   LEU A 205     7152   7544   7525   1892   -365    261       N  
ATOM   1560  CA  LEU A 205      46.571 -16.907  12.933  1.00 62.01           C  
ANISOU 1560  CA  LEU A 205     7693   7932   7935   1985   -323    174       C  
ATOM   1561  C   LEU A 205      47.539 -16.532  11.824  1.00 67.29           C  
ANISOU 1561  C   LEU A 205     8233   8765   8567   2125   -239    189       C  
ATOM   1562  O   LEU A 205      47.548 -17.146  10.758  1.00 70.77           O  
ANISOU 1562  O   LEU A 205     8744   9184   8963   2281   -205    128       O  
ATOM   1563  CB  LEU A 205      45.204 -16.269  12.672  1.00 61.08           C  
ANISOU 1563  CB  LEU A 205     7647   7739   7821   1819   -314    118       C  
ATOM   1564  CG  LEU A 205      43.957 -16.972  13.207  1.00 60.26           C  
ANISOU 1564  CG  LEU A 205     7716   7443   7738   1731   -381     74       C  
ATOM   1565  CD1 LEU A 205      42.785 -16.004  13.211  1.00 58.52           C  
ANISOU 1565  CD1 LEU A 205     7503   7202   7529   1543   -365     52       C  
ATOM   1566  CD2 LEU A 205      43.632 -18.204  12.367  1.00 61.26           C  
ANISOU 1566  CD2 LEU A 205     7997   7439   7840   1873   -404     -4       C  
ATOM   1567  N   GLY A 206      48.355 -15.517  12.089  1.00 68.87           N  
ANISOU 1567  N   GLY A 206     8249   9134   8786   2066   -210    276       N  
ATOM   1568  CA  GLY A 206      49.280 -14.996  11.100  1.00 70.10           C  
ANISOU 1568  CA  GLY A 206     8254   9469   8913   2170   -126    316       C  
ATOM   1569  C   GLY A 206      48.610 -13.943  10.239  1.00 70.39           C  
ANISOU 1569  C   GLY A 206     8273   9542   8932   2063    -68    285       C  
ATOM   1570  O   GLY A 206      47.390 -13.779  10.294  1.00 70.43           O  
ANISOU 1570  O   GLY A 206     8398   9420   8943   1939    -92    219       O  
ATOM   1571  N   PRO A 207      49.403 -13.215   9.440  1.00 70.25           N  
ANISOU 1571  N   PRO A 207     8098   9701   8893   2111      9    342       N  
ATOM   1572  CA  PRO A 207      48.844 -12.224   8.517  1.00 67.65           C  
ANISOU 1572  CA  PRO A 207     7748   9413   8541   2026     68    319       C  
ATOM   1573  C   PRO A 207      48.013 -12.888   7.423  1.00 64.14           C  
ANISOU 1573  C   PRO A 207     7468   8865   8036   2130     98    204       C  
ATOM   1574  O   PRO A 207      48.211 -14.071   7.133  1.00 65.03           O  
ANISOU 1574  O   PRO A 207     7675   8920   8114   2311     93    157       O  
ATOM   1575  CB  PRO A 207      50.088 -11.546   7.920  1.00 69.82           C  
ANISOU 1575  CB  PRO A 207     7813   9910   8804   2093    144    423       C  
ATOM   1576  CG  PRO A 207      51.214 -11.905   8.833  1.00 71.44           C  
ANISOU 1576  CG  PRO A 207     7912  10184   9047   2134    104    511       C  
ATOM   1577  CD  PRO A 207      50.872 -13.260   9.374  1.00 71.76           C  
ANISOU 1577  CD  PRO A 207     8116  10066   9083   2235     45    440       C  
ATOM   1578  N   GLY A 208      47.085 -12.138   6.838  1.00 60.38           N  
ANISOU 1578  N   GLY A 208     7034   8359   7549   2016    119    159       N  
ATOM   1579  CA  GLY A 208      46.331 -12.619   5.693  1.00 57.88           C  
ANISOU 1579  CA  GLY A 208     6858   7961   7171   2104    145     58       C  
ATOM   1580  C   GLY A 208      45.145 -13.521   5.993  1.00 53.08           C  
ANISOU 1580  C   GLY A 208     6458   7137   6575   2073     66    -41       C  
ATOM   1581  O   GLY A 208      44.554 -14.098   5.071  1.00 50.58           O  
ANISOU 1581  O   GLY A 208     6276   6734   6208   2159     68   -129       O  
ATOM   1582  N   ALA A 209      44.804 -13.665   7.273  1.00 49.06           N  
ANISOU 1582  N   ALA A 209     5975   6537   6127   1951     -7    -21       N  
ATOM   1583  CA  ALA A 209      43.557 -14.319   7.647  1.00 44.71           C  
ANISOU 1583  CA  ALA A 209     5598   5790   5598   1874    -81    -93       C  
ATOM   1584  C   ALA A 209      42.405 -13.518   7.071  1.00 41.68           C  
ANISOU 1584  C   ALA A 209     5252   5374   5212   1741    -66   -138       C  
ATOM   1585  O   ALA A 209      42.416 -12.292   7.119  1.00 42.01           O  
ANISOU 1585  O   ALA A 209     5181   5513   5267   1625    -29    -94       O  
ATOM   1586  CB  ALA A 209      43.420 -14.431   9.163  1.00 43.41           C  
ANISOU 1586  CB  ALA A 209     5434   5565   5495   1754   -148    -45       C  
ATOM   1587  N   THR A 210      41.416 -14.204   6.518  1.00 40.02           N  
ANISOU 1587  N   THR A 210     5200   5020   4985   1758   -103   -224       N  
ATOM   1588  CA  THR A 210      40.197 -13.529   6.079  1.00 38.19           C  
ANISOU 1588  CA  THR A 210     5010   4740   4759   1622   -104   -265       C  
ATOM   1589  C   THR A 210      39.367 -13.168   7.315  1.00 37.69           C  
ANISOU 1589  C   THR A 210     4949   4609   4763   1429   -152   -234       C  
ATOM   1590  O   THR A 210      39.590 -13.733   8.390  1.00 40.37           O  
ANISOU 1590  O   THR A 210     5302   4901   5136   1417   -196   -200       O  
ATOM   1591  CB  THR A 210      39.371 -14.413   5.156  1.00 34.93           C  
ANISOU 1591  CB  THR A 210     4767   4191   4312   1690   -146   -361       C  
ATOM   1592  OG1 THR A 210      38.810 -15.472   5.936  1.00 37.31           O  
ANISOU 1592  OG1 THR A 210     5192   4329   4656   1661   -235   -377       O  
ATOM   1593  CG2 THR A 210      40.257 -15.010   4.052  1.00 36.89           C  
ANISOU 1593  CG2 THR A 210     5044   4490   4481   1916   -107   -398       C  
ATOM   1594  N   LEU A 211      38.408 -12.254   7.170  1.00 34.12           N  
ANISOU 1594  N   LEU A 211     4487   4153   4326   1288   -141   -245       N  
ATOM   1595  CA  LEU A 211      37.565 -11.877   8.312  1.00 30.64           C  
ANISOU 1595  CA  LEU A 211     4048   3655   3937   1119   -176   -217       C  
ATOM   1596  C   LEU A 211      36.790 -13.103   8.766  1.00 30.47           C  
ANISOU 1596  C   LEU A 211     4164   3470   3942   1111   -250   -244       C  
ATOM   1597  O   LEU A 211      36.680 -13.373   9.973  1.00 28.48           O  
ANISOU 1597  O   LEU A 211     3919   3176   3726   1045   -286   -200       O  
ATOM   1598  CB  LEU A 211      36.611 -10.726   7.973  1.00 26.76           C  
ANISOU 1598  CB  LEU A 211     3531   3184   3452    990   -150   -229       C  
ATOM   1599  CG  LEU A 211      35.625 -10.300   9.088  1.00 25.12           C  
ANISOU 1599  CG  LEU A 211     3332   2923   3289    828   -177   -204       C  
ATOM   1600  CD1 LEU A 211      36.348  -9.936  10.414  1.00 24.45           C  
ANISOU 1600  CD1 LEU A 211     3172   2896   3222    784   -180   -135       C  
ATOM   1601  CD2 LEU A 211      34.713  -9.167   8.664  1.00 26.37           C  
ANISOU 1601  CD2 LEU A 211     3465   3104   3450    723   -149   -219       C  
ATOM   1602  N   GLU A 212      36.289 -13.862   7.792  1.00 27.69           N  
ANISOU 1602  N   GLU A 212     3925   3027   3570   1179   -279   -312       N  
ATOM   1603  CA  GLU A 212      35.612 -15.116   8.092  1.00 34.13           C  
ANISOU 1603  CA  GLU A 212     4880   3675   4412   1177   -364   -336       C  
ATOM   1604  C   GLU A 212      36.433 -15.994   9.040  1.00 35.48           C  
ANISOU 1604  C   GLU A 212     5067   3818   4597   1246   -398   -295       C  
ATOM   1605  O   GLU A 212      35.914 -16.503  10.033  1.00 36.55           O  
ANISOU 1605  O   GLU A 212     5251   3862   4776   1163   -452   -260       O  
ATOM   1606  CB  GLU A 212      35.311 -15.892   6.809  1.00 39.57           C  
ANISOU 1606  CB  GLU A 212     5696   4275   5064   1282   -400   -419       C  
ATOM   1607  CG  GLU A 212      34.691 -17.254   7.074  1.00 45.54           C  
ANISOU 1607  CG  GLU A 212     6608   4843   5850   1283   -505   -441       C  
ATOM   1608  CD  GLU A 212      34.307 -17.978   5.800  1.00 51.28           C  
ANISOU 1608  CD  GLU A 212     7478   5467   6538   1376   -558   -531       C  
ATOM   1609  OE1 GLU A 212      35.056 -17.868   4.802  1.00 51.76           O  
ANISOU 1609  OE1 GLU A 212     7535   5601   6528   1526   -511   -577       O  
ATOM   1610  OE2 GLU A 212      33.252 -18.649   5.800  1.00 53.58           O  
ANISOU 1610  OE2 GLU A 212     7885   5604   6867   1297   -650   -550       O  
ATOM   1611  N   GLU A 213      37.715 -16.152   8.740  1.00 34.27           N  
ANISOU 1611  N   GLU A 213     4865   3750   4405   1400   -364   -290       N  
ATOM   1612  CA  GLU A 213      38.576 -16.994   9.561  1.00 36.53           C  
ANISOU 1612  CA  GLU A 213     5162   4016   4701   1485   -397   -251       C  
ATOM   1613  C   GLU A 213      38.780 -16.380  10.949  1.00 33.71           C  
ANISOU 1613  C   GLU A 213     4705   3722   4383   1365   -391   -167       C  
ATOM   1614  O   GLU A 213      38.833 -17.098  11.950  1.00 35.38           O  
ANISOU 1614  O   GLU A 213     4962   3861   4621   1353   -445   -130       O  
ATOM   1615  CB  GLU A 213      39.916 -17.217   8.861  1.00 38.75           C  
ANISOU 1615  CB  GLU A 213     5395   4397   4930   1686   -352   -259       C  
ATOM   1616  CG  GLU A 213      39.780 -17.966   7.545  1.00 44.18           C  
ANISOU 1616  CG  GLU A 213     6208   5014   5566   1834   -364   -348       C  
ATOM   1617  CD  GLU A 213      41.027 -17.883   6.679  1.00 48.29           C  
ANISOU 1617  CD  GLU A 213     6655   5674   6019   2031   -289   -352       C  
ATOM   1618  OE1 GLU A 213      41.888 -17.017   6.940  1.00 46.87           O  
ANISOU 1618  OE1 GLU A 213     6306   5663   5841   2023   -221   -282       O  
ATOM   1619  OE2 GLU A 213      41.133 -18.678   5.719  1.00 52.11           O  
ANISOU 1619  OE2 GLU A 213     7254   6100   6446   2195   -301   -424       O  
ATOM   1620  N   MET A 214      38.890 -15.056  11.002  1.00 31.12           N  
ANISOU 1620  N   MET A 214     4250   3522   4052   1279   -332   -138       N  
ATOM   1621  CA  MET A 214      39.051 -14.348  12.276  1.00 30.28           C  
ANISOU 1621  CA  MET A 214     4059   3474   3972   1162   -332    -67       C  
ATOM   1622  C   MET A 214      37.825 -14.481  13.177  1.00 30.12           C  
ANISOU 1622  C   MET A 214     4114   3347   3985   1018   -374    -55       C  
ATOM   1623  O   MET A 214      37.950 -14.714  14.384  1.00 28.97           O  
ANISOU 1623  O   MET A 214     3971   3182   3855    974   -407     -2       O  
ATOM   1624  CB  MET A 214      39.353 -12.865  12.036  1.00 28.85           C  
ANISOU 1624  CB  MET A 214     3745   3437   3781   1097   -270    -44       C  
ATOM   1625  CG  MET A 214      40.791 -12.577  11.597  1.00 33.29           C  
ANISOU 1625  CG  MET A 214     4188   4140   4319   1211   -229    -11       C  
ATOM   1626  SD  MET A 214      41.120 -10.802  11.408  1.00 47.84           S  
ANISOU 1626  SD  MET A 214     5878   6140   6161   1107   -174     32       S  
ATOM   1627  CE  MET A 214      40.873 -10.234  13.081  1.00 42.30           C  
ANISOU 1627  CE  MET A 214     5161   5420   5491    949   -224     86       C  
ATOM   1628  N   MET A 215      36.644 -14.316  12.594  1.00 29.33           N  
ANISOU 1628  N   MET A 215     4068   3184   3892    946   -371    -99       N  
ATOM   1629  CA  MET A 215      35.405 -14.438  13.352  1.00 31.40           C  
ANISOU 1629  CA  MET A 215     4389   3356   4186    812   -403    -80       C  
ATOM   1630  C   MET A 215      35.154 -15.880  13.790  1.00 32.14           C  
ANISOU 1630  C   MET A 215     4600   3308   4303    840   -477    -69       C  
ATOM   1631  O   MET A 215      34.724 -16.125  14.923  1.00 34.47           O  
ANISOU 1631  O   MET A 215     4917   3560   4620    756   -505    -14       O  
ATOM   1632  CB  MET A 215      34.232 -13.910  12.536  1.00 30.14           C  
ANISOU 1632  CB  MET A 215     4246   3173   4032    734   -385   -124       C  
ATOM   1633  CG  MET A 215      34.296 -12.395  12.351  1.00 31.99           C  
ANISOU 1633  CG  MET A 215     4371   3533   4250    676   -319   -121       C  
ATOM   1634  SD  MET A 215      32.969 -11.778  11.328  1.00 42.87           S  
ANISOU 1634  SD  MET A 215     5767   4887   5633    601   -301   -172       S  
ATOM   1635  CE  MET A 215      31.579 -11.967  12.442  1.00 50.43           C  
ANISOU 1635  CE  MET A 215     6766   5763   6632    459   -330   -128       C  
ATOM   1636  N   THR A 216      35.450 -16.831  12.911  1.00 33.63           N  
ANISOU 1636  N   THR A 216     4871   3426   4483    963   -512   -119       N  
ATOM   1637  CA  THR A 216      35.466 -18.238  13.297  1.00 37.47           C  
ANISOU 1637  CA  THR A 216     5474   3774   4988   1015   -591   -109       C  
ATOM   1638  C   THR A 216      36.413 -18.499  14.470  1.00 37.08           C  
ANISOU 1638  C   THR A 216     5388   3762   4939   1050   -602    -42       C  
ATOM   1639  O   THR A 216      36.064 -19.207  15.414  1.00 39.30           O  
ANISOU 1639  O   THR A 216     5733   3953   5247    998   -656      7       O  
ATOM   1640  CB  THR A 216      35.881 -19.139  12.117  1.00 42.12           C  
ANISOU 1640  CB  THR A 216     6160   4294   5552   1177   -624   -182       C  
ATOM   1641  OG1 THR A 216      34.820 -19.179  11.154  1.00 43.23           O  
ANISOU 1641  OG1 THR A 216     6373   4356   5696   1130   -647   -241       O  
ATOM   1642  CG2 THR A 216      36.185 -20.550  12.597  1.00 42.57           C  
ANISOU 1642  CG2 THR A 216     6333   4217   5623   1256   -708   -167       C  
ATOM   1643  N   ALA A 217      37.612 -17.929  14.414  1.00 34.42           N  
ANISOU 1643  N   ALA A 217     4944   3560   4574   1135   -553    -32       N  
ATOM   1644  CA  ALA A 217      38.631 -18.246  15.413  1.00 36.96           C  
ANISOU 1644  CA  ALA A 217     5229   3919   4895   1189   -573     29       C  
ATOM   1645  C   ALA A 217      38.307 -17.634  16.779  1.00 37.12           C  
ANISOU 1645  C   ALA A 217     5203   3974   4927   1043   -574    100       C  
ATOM   1646  O   ALA A 217      38.785 -18.110  17.800  1.00 40.66           O  
ANISOU 1646  O   ALA A 217     5661   4408   5379   1056   -613    156       O  
ATOM   1647  CB  ALA A 217      40.002 -17.785  14.938  1.00 35.82           C  
ANISOU 1647  CB  ALA A 217     4970   3920   4721   1315   -525     31       C  
ATOM   1648  N   CYS A 218      37.514 -16.569  16.794  1.00 35.26           N  
ANISOU 1648  N   CYS A 218     4921   3785   4691    915   -531     95       N  
ATOM   1649  CA  CYS A 218      37.162 -15.892  18.044  1.00 36.10           C  
ANISOU 1649  CA  CYS A 218     4991   3929   4795    789   -525    154       C  
ATOM   1650  C   CYS A 218      35.708 -16.114  18.475  1.00 39.09           C  
ANISOU 1650  C   CYS A 218     5445   4214   5193    666   -537    168       C  
ATOM   1651  O   CYS A 218      35.236 -15.478  19.413  1.00 40.65           O  
ANISOU 1651  O   CYS A 218     5618   4447   5379    564   -519    210       O  
ATOM   1652  CB  CYS A 218      37.434 -14.387  17.921  1.00 34.58           C  
ANISOU 1652  CB  CYS A 218     4683   3874   4583    737   -467    149       C  
ATOM   1653  SG  CYS A 218      39.205 -13.984  17.847  1.00 41.23           S  
ANISOU 1653  SG  CYS A 218     5405   4852   5408    843   -460    173       S  
ATOM   1654  N   GLN A 219      35.004 -17.020  17.803  1.00 40.99           N  
ANISOU 1654  N   GLN A 219     5778   4335   5460    678   -571    138       N  
ATOM   1655  CA  GLN A 219      33.584 -17.247  18.091  1.00 45.47           C  
ANISOU 1655  CA  GLN A 219     6403   4818   6055    556   -586    162       C  
ATOM   1656  C   GLN A 219      33.384 -17.767  19.514  1.00 46.79           C  
ANISOU 1656  C   GLN A 219     6606   4947   6227    496   -617    249       C  
ATOM   1657  O   GLN A 219      34.302 -18.352  20.104  1.00 48.28           O  
ANISOU 1657  O   GLN A 219     6814   5127   6406    568   -652    280       O  
ATOM   1658  CB  GLN A 219      32.982 -18.230  17.074  1.00 49.44           C  
ANISOU 1658  CB  GLN A 219     7007   5188   6591    583   -639    117       C  
ATOM   1659  CG  GLN A 219      31.494 -18.035  16.806  1.00 52.27           C  
ANISOU 1659  CG  GLN A 219     7381   5499   6979    456   -638    119       C  
ATOM   1660  CD  GLN A 219      31.044 -18.642  15.482  1.00 54.94           C  
ANISOU 1660  CD  GLN A 219     7800   5736   7339    492   -686     51       C  
ATOM   1661  OE1 GLN A 219      31.749 -19.457  14.889  1.00 57.99           O  
ANISOU 1661  OE1 GLN A 219     8259   6058   7718    613   -733      6       O  
ATOM   1662  NE2 GLN A 219      29.867 -18.237  15.013  1.00 53.57           N  
ANISOU 1662  NE2 GLN A 219     7616   5549   7189    392   -679     41       N  
TER    1663      GLN A 219                                                      
HETATM 1664  O24 1B0 A 301      16.149  26.725  -0.227  1.00 26.22           O  
ANISOU 1664  O24 1B0 A 301     3954   2645   3363     89   -391   -234       O  
HETATM 1665  C23 1B0 A 301      15.304  25.902  -0.020  1.00 26.40           C  
ANISOU 1665  C23 1B0 A 301     3908   2729   3392    147   -333   -263       C  
HETATM 1666  N4  1B0 A 301      15.225  24.695  -0.783  1.00 25.14           N  
ANISOU 1666  N4  1B0 A 301     3640   2662   3252    118   -289   -249       N  
HETATM 1667  C5  1B0 A 301      16.121  24.407  -1.852  1.00 23.37           C  
ANISOU 1667  C5  1B0 A 301     3384   2470   3028     36   -300   -206       C  
HETATM 1668  C13 1B0 A 301      15.485  24.900  -3.135  1.00 25.73           C  
ANISOU 1668  C13 1B0 A 301     3681   2768   3327     55   -325   -180       C  
HETATM 1669  N15 1B0 A 301      16.277  25.489  -4.212  1.00 27.10           N  
ANISOU 1669  N15 1B0 A 301     3880   2931   3487     -8   -363   -124       N  
HETATM 1670  C17 1B0 A 301      17.723  25.617  -4.002  1.00 28.59           C  
ANISOU 1670  C17 1B0 A 301     4084   3112   3667    -96   -377    -86       C  
HETATM 1671  C22 1B0 A 301      18.578  24.624  -4.466  1.00 26.51           C  
ANISOU 1671  C22 1B0 A 301     3749   2929   3394   -146   -338    -63       C  
HETATM 1672  C21 1B0 A 301      19.956  24.733  -4.238  1.00 27.91           C  
ANISOU 1672  C21 1B0 A 301     3925   3112   3568   -226   -349    -18       C  
HETATM 1673  C20 1B0 A 301      20.456  25.831  -3.557  1.00 29.99           C  
ANISOU 1673  C20 1B0 A 301     4264   3291   3841   -267   -408      3       C  
HETATM 1674  C19 1B0 A 301      19.598  26.823  -3.086  1.00 30.00           C  
ANISOU 1674  C19 1B0 A 301     4355   3198   3847   -217   -454    -28       C  
HETATM 1675  C18 1B0 A 301      18.227  26.721  -3.306  1.00 29.20           C  
ANISOU 1675  C18 1B0 A 301     4250   3100   3746   -124   -433    -73       C  
HETATM 1676  C16 1B0 A 301      15.615  25.929  -5.460  1.00 29.84           C  
ANISOU 1676  C16 1B0 A 301     4230   3281   3828     16   -388    -97       C  
HETATM 1677  O14 1B0 A 301      14.308  24.778  -3.276  1.00 27.63           O  
ANISOU 1677  O14 1B0 A 301     3895   3025   3580    123   -313   -200       O  
HETATM 1678  C6  1B0 A 301      16.314  22.898  -2.033  1.00 22.29           C  
ANISOU 1678  C6  1B0 A 301     3153   2419   2898     12   -248   -213       C  
HETATM 1679  C7  1B0 A 301      17.248  22.447  -0.920  1.00 22.61           C  
ANISOU 1679  C7  1B0 A 301     3197   2461   2935    -25   -231   -224       C  
HETATM 1680  C12 1B0 A 301      18.627  22.477  -1.112  1.00 24.28           C  
ANISOU 1680  C12 1B0 A 301     3411   2678   3137   -103   -248   -187       C  
HETATM 1681  C11 1B0 A 301      19.468  22.087  -0.071  1.00 24.90           C  
ANISOU 1681  C11 1B0 A 301     3490   2757   3214   -135   -241   -194       C  
HETATM 1682  C10 1B0 A 301      18.929  21.696   1.150  1.00 23.07           C  
ANISOU 1682  C10 1B0 A 301     3268   2517   2982    -87   -216   -240       C  
HETATM 1683  C9  1B0 A 301      17.547  21.687   1.334  1.00 21.29           C  
ANISOU 1683  C9  1B0 A 301     3039   2290   2761     -8   -192   -273       C  
HETATM 1684  C8  1B0 A 301      16.716  22.073   0.300  1.00 21.02           C  
ANISOU 1684  C8  1B0 A 301     2995   2257   2736     23   -201   -264       C  
HETATM 1685  C25 1B0 A 301      14.247  26.154   1.097  1.00 27.82           C  
ANISOU 1685  C25 1B0 A 301     4122   2889   3558    261   -308   -311       C  
HETATM 1686  C1  1B0 A 301      14.863  26.302   2.484  1.00 26.30           C  
ANISOU 1686  C1  1B0 A 301     4003   2653   3336    262   -315   -343       C  
HETATM 1687  C26 1B0 A 301      15.178  27.479   3.176  1.00 24.80           C  
ANISOU 1687  C26 1B0 A 301     3950   2357   3115    285   -379   -363       C  
HETATM 1688  C31 1B0 A 301      15.051  28.832   2.830  1.00 27.08           C  
ANISOU 1688  C31 1B0 A 301     4349   2546   3396    309   -453   -359       C  
HETATM 1689  C30 1B0 A 301      15.436  29.809   3.726  1.00 30.53           C  
ANISOU 1689  C30 1B0 A 301     4931   2872   3797    329   -521   -388       C  
HETATM 1690  C29 1B0 A 301      15.945  29.455   4.975  1.00 28.76           C  
ANISOU 1690  C29 1B0 A 301     4743   2642   3541    325   -514   -423       C  
HETATM 1691  C28 1B0 A 301      16.079  28.125   5.306  1.00 25.23           C  
ANISOU 1691  C28 1B0 A 301     4182   2303   3103    300   -436   -422       C  
HETATM 1692  C27 1B0 A 301      15.674  27.132   4.399  1.00 24.35           C  
ANISOU 1692  C27 1B0 A 301     3925   2296   3032    281   -368   -392       C  
HETATM 1693  N3  1B0 A 301      15.682  25.735   4.474  1.00 23.13           N  
ANISOU 1693  N3  1B0 A 301     3649   2246   2895    255   -294   -386       N  
HETATM 1694  C2  1B0 A 301      15.177  25.236   3.276  1.00 25.46           C  
ANISOU 1694  C2  1B0 A 301     3844   2602   3226    243   -266   -357       C  
HETATM 1695  C32 1B0 A 301      15.218  23.723   3.428  1.00 25.52           C  
ANISOU 1695  C32 1B0 A 301     3739   2705   3251    215   -199   -354       C  
HETATM 1696  H4  1B0 A 301      14.555  24.109  -0.604  1.00 30.17           H  
HETATM 1697 H251 1B0 A 301      13.752  26.980   0.888  1.00 33.38           H  
HETATM 1698 H252 1B0 A 301      13.623  25.411   1.105  1.00 33.38           H  
HETATM 1699  H5  1B0 A 301      17.006  24.860  -1.703  1.00 28.05           H  
HETATM 1700 H61C 1B0 A 301      16.718  22.724  -2.897  1.00 26.75           H  
HETATM 1701 H62C 1B0 A 301      15.442  22.436  -1.958  1.00 26.75           H  
HETATM 1702 H161 1B0 A 301      15.018  26.701  -5.264  1.00 35.81           H  
HETATM 1703 H162 1B0 A 301      15.076  25.180  -5.835  1.00 35.81           H  
HETATM 1704 H163 1B0 A 301      16.305  26.203  -6.122  1.00 35.81           H  
HETATM 1705  H22 1B0 A 301      18.215  23.839  -4.949  1.00 31.81           H  
HETATM 1706  H18 1B0 A 301      17.624  27.414  -2.974  1.00 35.04           H  
HETATM 1707  H21 1B0 A 301      20.575  24.031  -4.575  1.00 33.49           H  
HETATM 1708  H20 1B0 A 301      21.434  25.913  -3.403  1.00 35.99           H  
HETATM 1709  H19 1B0 A 301      19.960  27.596  -2.608  1.00 36.01           H  
HETATM 1710  H12 1B0 A 301      19.022  22.770  -2.022  1.00 29.14           H  
HETATM 1711  H8  1B0 A 301      15.746  22.069   0.427  1.00 25.23           H  
HETATM 1712  H11 1B0 A 301      20.446  22.090  -0.199  1.00 29.88           H  
HETATM 1713  H10 1B0 A 301      19.540  21.409   1.904  1.00 27.69           H  
HETATM 1714  H9  1B0 A 301      17.152  21.398   2.224  1.00 25.55           H  
HETATM 1715  H31 1B0 A 301      14.681  29.080   1.972  1.00 32.50           H  
HETATM 1716  H30 1B0 A 301      15.347  30.764   3.482  1.00 36.64           H  
HETATM 1717  H29 1B0 A 301      16.235  30.150   5.604  1.00 34.51           H  
HETATM 1718  H28 1B0 A 301      16.447  27.869   6.188  1.00 30.28           H  
HETATM 1719  H3  1B0 A 301      15.984  25.231   5.192  1.00 27.76           H  
HETATM 1720 H321 1B0 A 301      15.538  23.326   2.608  1.00 30.62           H  
HETATM 1721 H322 1B0 A 301      15.836  23.478   4.184  1.00 30.62           H  
HETATM 1722 H323 1B0 A 301      14.311  23.386   3.623  1.00 30.62           H  
HETATM 1723  O   HOH A 401      14.623  20.538   4.162  1.00 21.99           O  
ANISOU 1723  O   HOH A 401     3076   2436   2842    203    -60   -353       O  
HETATM 1724  O   HOH A 402      12.264  22.853   8.665  1.00 26.38           O  
ANISOU 1724  O   HOH A 402     3880   2927   3217    599     33   -456       O  
HETATM 1725  O   HOH A 403      27.462  19.309   2.851  1.00 28.86           O  
ANISOU 1725  O   HOH A 403     3769   3460   3734   -476   -273      0       O  
HETATM 1726  O   HOH A 404      27.073  -3.083  12.037  1.00 18.27           O  
ANISOU 1726  O   HOH A 404     2376   2055   2511      4    -57   -152       O  
HETATM 1727  O   HOH A 405      32.433  -6.069  27.640  1.00 31.68           O  
ANISOU 1727  O   HOH A 405     4443   3830   3763     18   -322    346       O  
HETATM 1728  O   HOH A 406      34.711   1.038  22.042  1.00 28.78           O  
ANISOU 1728  O   HOH A 406     3771   3629   3536   -114   -376     86       O  
HETATM 1729  O   HOH A 407      27.133  -9.101  11.145  1.00 25.60           O  
ANISOU 1729  O   HOH A 407     3541   2650   3537    136   -252   -163       O  
HETATM 1730  O   HOH A 408      27.469  -4.472  17.659  1.00 22.60           O  
ANISOU 1730  O   HOH A 408     3011   2587   2990    -52    -75     29       O  
HETATM 1731  O   HOH A 409      31.659 -13.639  18.172  1.00 33.07           O  
ANISOU 1731  O   HOH A 409     4636   3480   4448    297   -412    147       O  
HETATM 1732  O   HOH A 410      26.661   9.634  10.155  1.00 24.50           O  
ANISOU 1732  O   HOH A 410     3135   3014   3158   -203    -45   -216       O  
HETATM 1733  O   HOH A 411      33.238 -13.972  20.460  1.00 35.30           O  
ANISOU 1733  O   HOH A 411     4914   3817   4682    336   -449    250       O  
HETATM 1734  O   HOH A 412      11.929  13.917   6.968  1.00 37.18           O  
ANISOU 1734  O   HOH A 412     4590   4657   4878    184    187   -254       O  
HETATM 1735  O   HOH A 413      10.423  21.995  -3.864  1.00 24.65           O  
ANISOU 1735  O   HOH A 413     3237   2839   3291    264   -237   -236       O  
HETATM 1736  O   HOH A 414      33.054 -14.299  15.904  1.00 33.94           O  
ANISOU 1736  O   HOH A 414     4762   3573   4561    503   -436     34       O  
HETATM 1737  O   HOH A 415      27.593  10.451  -6.909  1.00 29.10           O  
ANISOU 1737  O   HOH A 415     3553   4050   3454     99    153   -109       O  
HETATM 1738  O   HOH A 416      26.743   7.675  11.781  1.00 28.80           O  
ANISOU 1738  O   HOH A 416     3684   3561   3696   -172    -25   -208       O  
HETATM 1739  O   HOH A 417      19.582  13.772 -15.646  1.00 27.33           O  
ANISOU 1739  O   HOH A 417     3748   3682   2956    207   -169   -220       O  
HETATM 1740  O   HOH A 418      39.838  -4.283  23.645  1.00 26.82           O  
ANISOU 1740  O   HOH A 418     3339   3469   3380    124   -573    321       O  
HETATM 1741  O   HOH A 419      26.652   3.174   0.980  1.00 33.39           O  
ANISOU 1741  O   HOH A 419     4177   4238   4270    119     44   -336       O  
HETATM 1742  O   HOH A 420      15.007  20.390  13.890  1.00 31.48           O  
ANISOU 1742  O   HOH A 420     4675   3620   3667    540     99   -499       O  
HETATM 1743  O   HOH A 421      27.770  28.303 -16.568  1.00 39.84           O  
ANISOU 1743  O   HOH A 421     5136   5349   4651   -669   -197   1121       O  
HETATM 1744  O   HOH A 422      28.911  12.558  -5.698  1.00 31.17           O  
ANISOU 1744  O   HOH A 422     3721   4340   3783    -54    142     34       O  
HETATM 1745  O   HOH A 423      16.608  18.234  13.744  1.00 35.72           O  
ANISOU 1745  O   HOH A 423     5080   4214   4276    347     93   -445       O  
HETATM 1746  O   HOH A 424      23.210  29.644 -23.913  1.00 32.97           O  
ANISOU 1746  O   HOH A 424     4647   4566   3315   -314   -255   1180       O  
HETATM 1747  O   HOH A 425      24.463  11.281 -10.512  1.00 30.76           O  
ANISOU 1747  O   HOH A 425     3940   4202   3544    165     68   -189       O  
HETATM 1748  O   HOH A 426      29.266  27.760  -0.886  1.00 32.67           O  
ANISOU 1748  O   HOH A 426     4510   3609   4294   -943   -721    457       O  
HETATM 1749  O   HOH A 427      25.198  29.645 -11.600  1.00 27.76           O  
ANISOU 1749  O   HOH A 427     3877   3258   3411   -695   -484    748       O  
HETATM 1750  O   HOH A 428      35.843   9.113  19.076  1.00 37.13           O  
ANISOU 1750  O   HOH A 428     4804   4668   4636   -434   -594     38       O  
HETATM 1751  O   HOH A 429      13.385  23.560 -10.504  1.00 22.22           O  
ANISOU 1751  O   HOH A 429     3098   2545   2799     78   -403    -71       O  
HETATM 1752  O   HOH A 430      13.196  23.238  -7.605  1.00 27.35           O  
ANISOU 1752  O   HOH A 430     3718   3150   3524    103   -342   -141       O  
HETATM 1753  O   HOH A 431      27.526  29.054  -0.022  1.00 45.28           O  
ANISOU 1753  O   HOH A 431     6342   4986   5875   -854   -812    324       O  
HETATM 1754  O   HOH A 432       9.813  17.230 -12.093  1.00 29.80           O  
ANISOU 1754  O   HOH A 432     3825   3670   3826    108   -502   -235       O  
HETATM 1755  O   HOH A 433      21.699  29.941 -20.620  1.00 31.92           O  
ANISOU 1755  O   HOH A 433     4550   4112   3465   -353   -398    933       O  
HETATM 1756  O   HOH A 434      11.205  21.728  -6.401  1.00 22.86           O  
ANISOU 1756  O   HOH A 434     3025   2634   3028    180   -302   -202       O  
HETATM 1757  O   HOH A 435       9.764  15.743   6.851  1.00 35.17           O  
ANISOU 1757  O   HOH A 435     4307   4439   4617    341    221   -238       O  
HETATM 1758  O   HOH A 436      49.351 -15.408  19.707  1.00 42.36           O  
ANISOU 1758  O   HOH A 436     4848   5668   5580   1571   -630    596       O  
HETATM 1759  O   HOH A 437      39.567 -19.994  11.440  1.00 49.72           O  
ANISOU 1759  O   HOH A 437     7034   5443   6416   1667   -568   -194       O  
HETATM 1760  O   HOH A 438      43.336 -16.152  23.938  1.00 42.46           O  
ANISOU 1760  O   HOH A 438     5533   5071   5527    972   -759    521       O  
HETATM 1761  O   HOH A 439       6.283   4.891   0.967  1.00 40.80           O  
ANISOU 1761  O   HOH A 439     4546   5107   5849   -319   -266      2       O  
HETATM 1762  O   HOH A 440      16.462  23.314 -22.310  1.00 29.53           O  
ANISOU 1762  O   HOH A 440     4289   3932   2999    138   -442    279       O  
HETATM 1763  O   HOH A 441      16.526  25.728 -23.049  1.00 31.10           O  
ANISOU 1763  O   HOH A 441     4544   4085   3187     82   -487    448       O  
HETATM 1764  O   HOH A 442      39.972 -21.171  14.191  1.00 45.13           O  
ANISOU 1764  O   HOH A 442     6491   4753   5904   1595   -681    -50       O  
HETATM 1765  O   HOH A 443      18.542  25.112   6.369  1.00 25.95           O  
ANISOU 1765  O   HOH A 443     4076   2566   3218     82   -360   -385       O  
HETATM 1766  O   HOH A 444       8.831  25.329 -13.942  1.00 35.01           O  
ANISOU 1766  O   HOH A 444     4728   4146   4426    272   -627    -15       O  
HETATM 1767  O   HOH A 445       8.171   8.788  -7.963  1.00 26.72           O  
ANISOU 1767  O   HOH A 445     3193   3221   3739   -125   -569   -314       O  
HETATM 1768  O   HOH A 446      34.458  15.864   4.125  1.00 49.68           O  
ANISOU 1768  O   HOH A 446     5941   6502   6434   -613   -258    301       O  
HETATM 1769  O   HOH A 447      40.508 -20.439  17.947  1.00 42.17           O  
ANISOU 1769  O   HOH A 447     5961   4490   5573   1351   -716    177       O  
HETATM 1770  O   HOH A 448       2.654  11.872 -14.504  1.00 39.39           O  
ANISOU 1770  O   HOH A 448     4750   4878   5338    -65  -1089   -214       O  
HETATM 1771  O   HOH A 449      25.963  12.326 -15.507  1.00 52.65           O  
ANISOU 1771  O   HOH A 449     6781   7264   5958    356    180    -38       O  
HETATM 1772  O   HOH A 450      27.799  31.787 -16.957  1.00 49.46           O  
ANISOU 1772  O   HOH A 450     6500   6340   5954   -905   -408   1374       O  
HETATM 1773  O   HOH A 451      32.207  30.608 -10.890  1.00 41.53           O  
ANISOU 1773  O   HOH A 451     5208   5297   5273  -1253   -519   1382       O  
HETATM 1774  O   HOH A 452      22.027  29.226  -1.233  1.00 43.39           O  
ANISOU 1774  O   HOH A 452     6258   4668   5562   -409   -661     53       O  
HETATM 1775  O   HOH A 453       7.546  15.433 -10.595  1.00 30.78           O  
ANISOU 1775  O   HOH A 453     3779   3805   4111     82   -542   -244       O  
HETATM 1776  O   HOH A 454      30.379  16.861  -9.752  1.00 39.64           O  
ANISOU 1776  O   HOH A 454     4717   5622   4722   -187    177    399       O  
HETATM 1777  O   HOH A 455      15.568   9.095 -16.964  1.00 43.91           O  
ANISOU 1777  O   HOH A 455     6058   5550   5074    283   -525   -524       O  
HETATM 1778  O   HOH A 456      19.268  12.567 -18.250  1.00 39.61           O  
ANISOU 1778  O   HOH A 456     5452   5287   4311    347   -226   -285       O  
HETATM 1779  O   HOH A 457      10.060  13.413  -0.123  1.00 32.46           O  
ANISOU 1779  O   HOH A 457     3855   4044   4435     62    -62   -244       O  
HETATM 1780  O   HOH A 458      20.506  31.171 -15.793  1.00 35.73           O  
ANISOU 1780  O   HOH A 458     5122   4179   4275   -413   -569    699       O  
HETATM 1781  O   HOH A 459       7.701  15.152 -21.175  1.00 37.52           O  
ANISOU 1781  O   HOH A 459     5172   4697   4388    204  -1035   -307       O  
HETATM 1782  O   HOH A 460      39.375  -5.203  26.701  1.00 41.03           O  
ANISOU 1782  O   HOH A 460     5331   5195   5062    108   -655    378       O  
HETATM 1783  O   HOH A 461      22.887  11.259  11.908  1.00 38.82           O  
ANISOU 1783  O   HOH A 461     5091   4751   4908   -113     18   -286       O  
HETATM 1784  O   HOH A 462      21.694   3.519  -4.325  1.00 25.37           O  
ANISOU 1784  O   HOH A 462     3340   3100   3200    133   -113   -483       O  
HETATM 1785  O   HOH A 463      18.114  12.036 -13.553  1.00 37.98           O  
ANISOU 1785  O   HOH A 463     5058   4898   4472    163   -237   -338       O  
HETATM 1786  O   HOH A 464       8.941  17.570  -7.900  1.00 31.82           O  
ANISOU 1786  O   HOH A 464     3942   3908   4242    134   -363   -230       O  
HETATM 1787  O   HOH A 465       6.986  17.410   3.866  1.00 31.53           O  
ANISOU 1787  O   HOH A 465     3720   4009   4250    439    141   -195       O  
HETATM 1788  O   HOH A 466       6.075  11.822   8.679  1.00 42.77           O  
ANISOU 1788  O   HOH A 466     4834   5683   5734    296    383     29       O  
HETATM 1789  O   HOH A 467       5.246  13.135   6.100  1.00 40.13           O  
ANISOU 1789  O   HOH A 467     4475   5310   5462    312    270     -7       O  
HETATM 1790  O   HOH A 468       6.074  15.839   5.898  1.00 44.17           O  
ANISOU 1790  O   HOH A 468     5187   5731   5865    457    260   -119       O  
HETATM 1791  O   HOH A 469      18.837  16.360  14.070  1.00 51.86           O  
ANISOU 1791  O   HOH A 469     7062   6283   6360    174     51   -407       O  
HETATM 1792  O   HOH A 470      21.079  16.721  11.705  1.00 42.24           O  
ANISOU 1792  O   HOH A 470     5785   5018   5245    -14    -74   -374       O  
HETATM 1793  O   HOH A 471      19.360  26.734   4.653  1.00 38.27           O  
ANISOU 1793  O   HOH A 471     5697   4030   4815    -27   -481   -312       O  
HETATM 1794  O   HOH A 472      21.014  29.814   2.948  1.00 45.92           O  
ANISOU 1794  O   HOH A 472     6851   4776   5822   -229   -733   -173       O  
HETATM 1795  O   HOH A 473      29.197  22.458   3.463  1.00 33.41           O  
ANISOU 1795  O   HOH A 473     4463   3886   4344   -691   -502    136       O  
HETATM 1796  O   HOH A 474      21.754  30.124  -4.027  1.00 56.17           O  
ANISOU 1796  O   HOH A 474     7845   6321   7176   -446   -672    184       O  
HETATM 1797  O   HOH A 475      33.526  26.270  -5.737  1.00 41.14           O  
ANISOU 1797  O   HOH A 475     4985   5324   5322  -1107   -440    995       O  
HETATM 1798  O   HOH A 476      34.605  21.908  -5.498  1.00 54.32           O  
ANISOU 1798  O   HOH A 476     6391   7340   6910   -829   -154    865       O  
HETATM 1799  O   HOH A 477      34.248  17.861  -6.918  1.00 50.47           O  
ANISOU 1799  O   HOH A 477     5819   7098   6259   -443    124    673       O  
HETATM 1800  O   HOH A 478      40.018  25.653 -16.048  1.00 64.56           O  
ANISOU 1800  O   HOH A 478     7018   9704   7809   -954    308   2139       O  
HETATM 1801  O   HOH A 479      18.751  24.277 -30.227  1.00 40.11           O  
ANISOU 1801  O   HOH A 479     5939   5763   3538    372   -329    675       O  
HETATM 1802  O   HOH A 480      22.112  31.713 -18.224  1.00 44.51           O  
ANISOU 1802  O   HOH A 480     6193   5462   5258   -510   -520    959       O  
HETATM 1803  O   HOH A 481      10.861  24.107 -11.051  1.00 44.56           O  
ANISOU 1803  O   HOH A 481     5903   5355   5673    187   -475    -83       O  
HETATM 1804  O   HOH A 482       8.769  22.690  -7.558  1.00 36.94           O  
ANISOU 1804  O   HOH A 482     4768   4421   4847    290   -377   -174       O  
HETATM 1805  O   HOH A 483      13.486  27.549  -8.588  1.00 44.14           O  
ANISOU 1805  O   HOH A 483     6084   5068   5619    111   -490    -24       O  
HETATM 1806  O   HOH A 484      14.157  29.529  -7.336  1.00 55.74           O  
ANISOU 1806  O   HOH A 484     7713   6370   7098     99   -560     -8       O  
HETATM 1807  O   HOH A 485      10.374  27.035 -19.853  1.00 42.70           O  
ANISOU 1807  O   HOH A 485     5948   5193   5083    218   -770    207       O  
HETATM 1808  O   HOH A 486       8.076  24.726 -16.955  1.00 33.35           O  
ANISOU 1808  O   HOH A 486     4542   4013   4118    278   -745     20       O  
HETATM 1809  O   HOH A 487      15.055  18.114 -25.917  1.00 47.78           O  
ANISOU 1809  O   HOH A 487     6830   6381   4943    429   -580    -40       O  
HETATM 1810  O   HOH A 488      16.855  10.426 -21.030  1.00 39.11           O  
ANISOU 1810  O   HOH A 488     5654   5124   4084    477   -490   -474       O  
HETATM 1811  O   HOH A 489      19.371   9.221 -21.187  1.00 48.52           O  
ANISOU 1811  O   HOH A 489     6883   6432   5122    625   -327   -487       O  
HETATM 1812  O   HOH A 490      30.255  11.565  -3.865  1.00 38.76           O  
ANISOU 1812  O   HOH A 490     4612   5320   4795    -64    148     45       O  
HETATM 1813  O   HOH A 491      27.697  13.447  16.185  1.00 49.58           O  
ANISOU 1813  O   HOH A 491     6710   6009   6117   -247   -287   -262       O  
HETATM 1814  O   HOH A 492      29.994  14.145  15.207  1.00 39.15           O  
ANISOU 1814  O   HOH A 492     5309   4701   4866   -384   -411   -183       O  
HETATM 1815  O   HOH A 493      37.745   7.403  12.357  1.00 35.96           O  
ANISOU 1815  O   HOH A 493     4127   4844   4692   -320   -316    195       O  
HETATM 1816  O   HOH A 494      30.372   5.017  15.173  1.00 37.91           O  
ANISOU 1816  O   HOH A 494     4825   4760   4820   -168   -126   -110       O  
HETATM 1817  O   HOH A 495      46.573  -1.987  21.481  1.00 52.02           O  
ANISOU 1817  O   HOH A 495     5855   7144   6766    114   -783    617       O  
HETATM 1818  O   HOH A 496      42.673  -3.596  22.529  1.00 44.50           O  
ANISOU 1818  O   HOH A 496     5321   5887   5700    155   -650    410       O  
HETATM 1819  O   HOH A 497      44.469 -18.911  16.648  1.00 45.01           O  
ANISOU 1819  O   HOH A 497     5905   5325   5871   1701   -577    212       O  
HETATM 1820  O   HOH A 498      38.658 -19.896   4.429  1.00 51.27           O  
ANISOU 1820  O   HOH A 498     7504   5650   6325   2077   -458   -588       O  
HETATM 1821  O   HOH A 499      13.185  15.489   9.316  1.00 37.63           O  
ANISOU 1821  O   HOH A 499     4837   4658   4802    270    212   -309       O  
HETATM 1822  O   HOH A 500      35.627  26.594  -8.640  1.00 34.66           O  
ANISOU 1822  O   HOH A 500     3890   4843   4435  -1191   -302   1371       O  
CONECT 1664 1665                                                                
CONECT 1665 1664 1666 1685                                                      
CONECT 1666 1665 1667 1696                                                      
CONECT 1667 1666 1668 1678 1699                                                 
CONECT 1668 1667 1669 1677                                                      
CONECT 1669 1668 1670 1676                                                      
CONECT 1670 1669 1671 1675                                                      
CONECT 1671 1670 1672 1705                                                      
CONECT 1672 1671 1673 1707                                                      
CONECT 1673 1672 1674 1708                                                      
CONECT 1674 1673 1675 1709                                                      
CONECT 1675 1670 1674 1706                                                      
CONECT 1676 1669 1702 1703 1704                                                 
CONECT 1677 1668                                                                
CONECT 1678 1667 1679 1700 1701                                                 
CONECT 1679 1678 1680 1684                                                      
CONECT 1680 1679 1681 1710                                                      
CONECT 1681 1680 1682 1712                                                      
CONECT 1682 1681 1683 1713                                                      
CONECT 1683 1682 1684 1714                                                      
CONECT 1684 1679 1683 1711                                                      
CONECT 1685 1665 1686 1697 1698                                                 
CONECT 1686 1685 1687 1694                                                      
CONECT 1687 1686 1688 1692                                                      
CONECT 1688 1687 1689 1715                                                      
CONECT 1689 1688 1690 1716                                                      
CONECT 1690 1689 1691 1717                                                      
CONECT 1691 1690 1692 1718                                                      
CONECT 1692 1687 1691 1693                                                      
CONECT 1693 1692 1694 1719                                                      
CONECT 1694 1686 1693 1695                                                      
CONECT 1695 1694 1720 1721 1722                                                 
CONECT 1696 1666                                                                
CONECT 1697 1685                                                                
CONECT 1698 1685                                                                
CONECT 1699 1667                                                                
CONECT 1700 1678                                                                
CONECT 1701 1678                                                                
CONECT 1702 1676                                                                
CONECT 1703 1676                                                                
CONECT 1704 1676                                                                
CONECT 1705 1671                                                                
CONECT 1706 1675                                                                
CONECT 1707 1672                                                                
CONECT 1708 1673                                                                
CONECT 1709 1674                                                                
CONECT 1710 1680                                                                
CONECT 1711 1684                                                                
CONECT 1712 1681                                                                
CONECT 1713 1682                                                                
CONECT 1714 1683                                                                
CONECT 1715 1688                                                                
CONECT 1716 1689                                                                
CONECT 1717 1690                                                                
CONECT 1718 1691                                                                
CONECT 1719 1693                                                                
CONECT 1720 1695                                                                
CONECT 1721 1695                                                                
CONECT 1722 1695                                                                
MASTER      305    0    1   12    2    0    3    6 1794    1   59   18          
END