HEADER    MEMBRANE PROTEIN                        11-SEP-18   6HLP              
TITLE     CRYSTAL STRUCTURE OF THE NEUROKININ 1 RECEPTOR IN COMPLEX WITH THE    
TITLE    2 SMALL MOLECULE ANTAGONIST NETUPITANT                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUBSTANCE-P RECEPTOR,SUBSTANCE-P RECEPTOR;                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: SPR,NK-1 RECEPTOR,NK-1R,TACHYKININ RECEPTOR 1,SPR,NK-1      
COMPND   5 RECEPTOR,NK-1R,TACHYKININ RECEPTOR 1;                                
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, PYROCOCCUS ABYSSI GE5;            
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606, 272844;                                        
SOURCE   5 GENE: TACR1, NK1R, TAC1R;                                            
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS                           
KEYWDS    7-TM; GPCR; SIGNALLING PROTEIN, MEMBRANE PROTEIN                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.SCHOPPE,J.EHRENMANN,C.KLENK,P.RUCKTOOA,M.SCHUTZ,A.S.DORE,           
AUTHOR   2 A.PLUCKTHUN                                                          
REVDAT   1   16-JAN-19 6HLP    0                                                
JRNL        AUTH   J.SCHOPPE,J.EHRENMANN,C.KLENK,P.RUCKTOOA,M.SCHUTZ,A.S.DORE,  
JRNL        AUTH 2 A.PLUCKTHUN                                                  
JRNL        TITL   CRYSTAL STRUCTURES OF THE HUMAN NEUROKININ 1 RECEPTOR IN     
JRNL        TITL 2 COMPLEX WITH CLINICALLY USED ANTAGONISTS.                    
JRNL        REF    NAT COMMUN                    V.  10    17 2019              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   30604743                                                     
JRNL        DOI    10.1038/S41467-018-07939-8                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.13_2998: ???)                              
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.24                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 40668                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.204                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.225                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.860                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1977                            
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 29.2390 -  5.2929    1.00     2950   162  0.1941 0.2238        
REMARK   3     2  5.2929 -  4.2051    1.00     2847   131  0.1801 0.1679        
REMARK   3     3  4.2051 -  3.6747    1.00     2784   141  0.1835 0.2104        
REMARK   3     4  3.6747 -  3.3393    1.00     2765   152  0.2008 0.2522        
REMARK   3     5  3.3393 -  3.1002    1.00     2742   166  0.2160 0.2285        
REMARK   3     6  3.1002 -  2.9176    1.00     2767   129  0.2070 0.2124        
REMARK   3     7  2.9176 -  2.7716    1.00     2758   144  0.2010 0.2461        
REMARK   3     8  2.7716 -  2.6510    1.00     2721   143  0.1984 0.2470        
REMARK   3     9  2.6510 -  2.5491    1.00     2742   145  0.2148 0.1930        
REMARK   3    10  2.5491 -  2.4611    1.00     2715   133  0.2290 0.2800        
REMARK   3    11  2.4611 -  2.3842    1.00     2739   137  0.2446 0.2662        
REMARK   3    12  2.3842 -  2.3161    1.00     2738   148  0.2650 0.3693        
REMARK   3    13  2.3161 -  2.2551    1.00     2726   123  0.2755 0.3124        
REMARK   3    14  2.2551 -  2.2001    1.00     2697   123  0.2985 0.3059        
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)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.980           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           4385                                  
REMARK   3   ANGLE     :  0.701           5810                                  
REMARK   3   CHIRALITY :  0.047            622                                  
REMARK   3   PLANARITY :  0.005            689                                  
REMARK   3   DIHEDRAL  : 16.564           2602                                  
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):   3.9767 -11.0651  57.5226              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4174 T22:   0.4087                                     
REMARK   3      T33:   0.4743 T12:   0.0011                                     
REMARK   3      T13:  -0.0092 T23:  -0.0310                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3916 L22:   1.1169                                     
REMARK   3      L33:   2.8662 L12:  -0.1394                                     
REMARK   3      L13:   0.3480 L23:  -1.5416                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0372 S12:  -0.0375 S13:   0.0181                       
REMARK   3      S21:  -0.0056 S22:   0.0042 S23:   0.0155                       
REMARK   3      S31:   0.0462 S32:   0.0605 S33:   0.0001                       
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 6HLP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-SEP-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200011874.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-MAY-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.06795                            
REMARK 200  MONOCHROMATOR                  : SI                                 
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40792                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 18.50                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.27                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 18.80                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 4ZJC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: STAR-SHAPED.                                                 
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.67                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.58                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CITRATE PH 6.0, 31%        
REMARK 280  (V/V) PEG400, 40-50 MM MG(HCO2)2 AND 50 UM NETUPITANT, LIPIDIC      
REMARK 280  CUBIC PHASE, TEMPERATURE 293K                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       30.82900            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       83.01750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.28550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       83.01750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       30.82900            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.28550            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 24330 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 66.0 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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     VAL A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     ASP A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     PRO A    13                                                      
REMARK 465     ASN A    14                                                      
REMARK 465     ILE A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     THR A    17                                                      
REMARK 465     ASN A    18                                                      
REMARK 465     THR A    19                                                      
REMARK 465     SER A    20                                                      
REMARK 465     GLU A    21                                                      
REMARK 465     PRO A    22                                                      
REMARK 465     ASN A    23                                                      
REMARK 465     GLN A    24                                                      
REMARK 465     PHE A    25                                                      
REMARK 465     VAL A    26                                                      
REMARK 465     TYR A   278                                                      
REMARK 465     ALA A   328                                                      
REMARK 465     GLY A   329                                                      
REMARK 465     ASP A   330                                                      
REMARK 465     TYR A   331                                                      
REMARK 465     GLU A   332                                                      
REMARK 465     GLY A   333                                                      
REMARK 465     LEU A   334                                                      
REMARK 465     GLU A   335                                                      
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  27    CG   CD   OE1  NE2                                  
REMARK 470     LEU A 279    CG   CD1  CD2                                       
REMARK 470     LYS A 281    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU A  1370     O    HOH A  1601              2.14            
REMARK 500   O6   CIT A  1502     O    HOH A  1602              2.14            
REMARK 500   OD2  ASP A  1266     O    HOH A  1603              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ILE A1354   C     PRO A1355   N       0.145                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    SER A 226   O   -  C   -  N   ANGL. DEV. = -11.2 DEGREES          
REMARK 500    PRO A1355   C   -  N   -  CA  ANGL. DEV. =  11.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  96       46.49    -81.14                                   
REMARK 500    HIS A 187     -159.82   -154.32                                   
REMARK 500    PRO A 188       80.87    -68.97                                   
REMARK 500    TYR A 205      -72.05   -137.44                                   
REMARK 500    GLN A1262      -80.66   -129.82                                   
REMARK 500    PRO A1335       42.82    -89.92                                   
REMARK 500    GLU A1339       80.41   -150.55                                   
REMARK 500    ASN A 274       88.67   -155.08                                   
REMARK 500    LYS A 280      -72.37    -57.53                                   
REMARK 500    PHE A 325      -59.22   -131.37                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     OLA A 1503                                                       
REMARK 610     OLA A 1504                                                       
REMARK 610     OLA A 1505                                                       
REMARK 610     OLA A 1506                                                       
REMARK 610     OLA A 1507                                                       
REMARK 610     OLA A 1508                                                       
REMARK 610     OLA A 1509                                                       
REMARK 610     OLA A 1510                                                       
REMARK 610     OLA A 1511                                                       
REMARK 610     OLC A 1512                                                       
REMARK 610     OLC A 1513                                                       
REMARK 610     OLC A 1514                                                       
REMARK 610     OLC A 1515                                                       
REMARK 610     OLC A 1516                                                       
REMARK 610     OLC A 1539                                                       
REMARK 610     OLC A 1540                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GAW A 1501                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CIT A 1502                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1503                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1504                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1505                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1506                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1507                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1508                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1509                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1510                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1511                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1512                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1513                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1514                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1515                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1516                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1517                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1518                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1519                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1520                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1521                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1522                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1523                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1524                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1526                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1527                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1528                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1529                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1530                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1531                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1532                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1533                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1536                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1537                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1538                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1539                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1540                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1541                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1542                
DBREF  6HLP A    1  1219  UNP    P25103   NK1R_HUMAN       1    228             
DBREF  6HLP A 1220  1413  UNP    Q9V2J8   Q9V2J8_PYRAB   220    413             
DBREF  6HLP A  238   335  UNP    P25103   NK1R_HUMAN     238    335             
SEQADV 6HLP ALA A   74  UNP  P25103    LEU    74 ENGINEERED MUTATION            
SEQADV 6HLP ILE A  116  UNP  P25103    VAL   116 ENGINEERED MUTATION            
SEQADV 6HLP LEU A  144  UNP  P25103    ALA   144 ENGINEERED MUTATION            
SEQADV 6HLP LYS A  181  UNP  P25103    MET   181 ENGINEERED MUTATION            
SEQADV 6HLP LEU A  215  UNP  P25103    ALA   215 ENGINEERED MUTATION            
SEQADV 6HLP ARG A  224  UNP  P25103    TRP   224 ENGINEERED MUTATION            
SEQADV 6HLP GLY A 1218  UNP  P25103    GLU   227 CONFLICT                       
SEQADV 6HLP ALA A  243  UNP  P25103    LYS   243 ENGINEERED MUTATION            
SEQRES   1 A  520  MET ASP ASN VAL LEU PRO VAL ASP SER ASP LEU SER PRO          
SEQRES   2 A  520  ASN ILE SER THR ASN THR SER GLU PRO ASN GLN PHE VAL          
SEQRES   3 A  520  GLN PRO ALA TRP GLN ILE VAL LEU TRP ALA ALA ALA TYR          
SEQRES   4 A  520  THR VAL ILE VAL VAL THR SER VAL VAL GLY ASN VAL VAL          
SEQRES   5 A  520  VAL MET TRP ILE ILE LEU ALA HIS LYS ARG MET ARG THR          
SEQRES   6 A  520  VAL THR ASN TYR PHE LEU VAL ASN ALA ALA PHE ALA GLU          
SEQRES   7 A  520  ALA SER MET ALA ALA PHE ASN THR VAL VAL ASN PHE THR          
SEQRES   8 A  520  TYR ALA VAL HIS ASN GLU TRP TYR TYR GLY LEU PHE TYR          
SEQRES   9 A  520  CYS LYS PHE HIS ASN PHE PHE PRO ILE ALA ALA ILE PHE          
SEQRES  10 A  520  ALA SER ILE TYR SER MET THR ALA VAL ALA PHE ASP ARG          
SEQRES  11 A  520  TYR MET ALA ILE ILE HIS PRO LEU GLN PRO ARG LEU SER          
SEQRES  12 A  520  LEU THR ALA THR LYS VAL VAL ILE CYS VAL ILE TRP VAL          
SEQRES  13 A  520  LEU ALA LEU LEU LEU ALA PHE PRO GLN GLY TYR TYR SER          
SEQRES  14 A  520  THR THR GLU THR MET PRO SER ARG VAL VAL CYS LYS ILE          
SEQRES  15 A  520  GLU TRP PRO GLU HIS PRO ASN LYS ILE TYR GLU LYS VAL          
SEQRES  16 A  520  TYR HIS ILE CYS VAL THR VAL LEU ILE TYR PHE LEU PRO          
SEQRES  17 A  520  LEU LEU VAL ILE GLY TYR LEU TYR THR VAL VAL GLY ILE          
SEQRES  18 A  520  THR LEU ARG ALA SER GLY ILE ASP YCM SER PHE TRP ASN          
SEQRES  19 A  520  GLU SER TYR LEU THR GLY SER ARG ASP GLU ARG LYS LYS          
SEQRES  20 A  520  SER LEU LEU SER LYS PHE GLY MET ASP GLU GLY VAL THR          
SEQRES  21 A  520  PHE MET PHE ILE GLY ARG PHE ASP ARG GLY GLN LYS GLY          
SEQRES  22 A  520  VAL ASP VAL LEU LEU LYS ALA ILE GLU ILE LEU SER SER          
SEQRES  23 A  520  LYS LYS GLU PHE GLN GLU MET ARG PHE ILE ILE ILE GLY          
SEQRES  24 A  520  LYS GLY ASP PRO GLU LEU GLU GLY TRP ALA ARG SER LEU          
SEQRES  25 A  520  GLU GLU LYS HIS GLY ASN VAL LYS VAL ILE THR GLU MET          
SEQRES  26 A  520  LEU SER ARG GLU PHE VAL ARG GLU LEU TYR GLY SER VAL          
SEQRES  27 A  520  ASP PHE VAL ILE ILE PRO SER TYR PHE GLU PRO PHE GLY          
SEQRES  28 A  520  LEU VAL ALA LEU GLU ALA MET CYS LEU GLY ALA ILE PRO          
SEQRES  29 A  520  ILE ALA SER ALA VAL GLY GLY LEU ARG ASP ILE ILE THR          
SEQRES  30 A  520  ASN GLU THR GLY ILE LEU VAL LYS ALA GLY ASP PRO GLY          
SEQRES  31 A  520  GLU LEU ALA ASN ALA ILE LEU LYS ALA LEU GLU LEU SER          
SEQRES  32 A  520  ARG SER ASP LEU SER LYS PHE ARG GLU ASN CYS LYS LYS          
SEQRES  33 A  520  ARG ALA MET SER PHE SER GLU GLN VAL SER ALA ALA ARG          
SEQRES  34 A  520  LYS VAL VAL LYS MET MET ILE VAL VAL VAL CYS THR PHE          
SEQRES  35 A  520  ALA ILE CYS TRP LEU PRO PHE HIS ILE PHE PHE LEU LEU          
SEQRES  36 A  520  PRO TYR ILE ASN PRO ASP LEU TYR LEU LYS LYS PHE ILE          
SEQRES  37 A  520  GLN GLN VAL TYR LEU ALA ILE MET TRP LEU ALA MET SER          
SEQRES  38 A  520  SER THR MET TYR ASN PRO ILE ILE TYR CYS CYS LEU ASN          
SEQRES  39 A  520  ASP ARG PHE ARG LEU GLY PHE LYS HIS ALA PHE ARG YCM          
SEQRES  40 A  520  CYS PRO PHE ILE SER ALA GLY ASP TYR GLU GLY LEU GLU          
MODRES 6HLP YCM A 1221  CYS  MODIFIED RESIDUE                                   
MODRES 6HLP YCM A  322  CYS  MODIFIED RESIDUE                                   
HET    YCM  A1221      10                                                       
HET    YCM  A 322      10                                                       
HET    GAW  A1501      41                                                       
HET    CIT  A1502      13                                                       
HET    OLA  A1503      11                                                       
HET    OLA  A1504      14                                                       
HET    OLA  A1505      17                                                       
HET    OLA  A1506       7                                                       
HET    OLA  A1507      11                                                       
HET    OLA  A1508      10                                                       
HET    OLA  A1509       6                                                       
HET    OLA  A1510      13                                                       
HET    OLA  A1511      10                                                       
HET    OLC  A1512      20                                                       
HET    OLC  A1513      23                                                       
HET    OLC  A1514      17                                                       
HET    OLC  A1515      17                                                       
HET    OLC  A1516      15                                                       
HET    PEG  A1517       7                                                       
HET    PEG  A1518       7                                                       
HET    PEG  A1519       7                                                       
HET    PEG  A1520       7                                                       
HET    PEG  A1521       7                                                       
HET    PEG  A1522       7                                                       
HET    PEG  A1523       7                                                       
HET    PEG  A1524       7                                                       
HET    PEG  A1525       7                                                       
HET    PEG  A1526       7                                                       
HET    PEG  A1527       7                                                       
HET    PEG  A1528       7                                                       
HET    PEG  A1529       7                                                       
HET    PEG  A1530       7                                                       
HET    PEG  A1531       7                                                       
HET    PEG  A1532       7                                                       
HET    PEG  A1533       7                                                       
HET    PEG  A1534       7                                                       
HET    PEG  A1535       7                                                       
HET    PEG  A1536       7                                                       
HET    PEG  A1537       7                                                       
HET    PEG  A1538       7                                                       
HET    OLC  A1539      17                                                       
HET    OLC  A1540      10                                                       
HET    PEG  A1541       7                                                       
HET    PEG  A1542       7                                                       
HETNAM     YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE                                
HETNAM     GAW 2-[3,5-BIS(TRIFLUOROMETHYL)PHENYL]-~{N},2-DIMETHYL-              
HETNAM   2 GAW  ~{N}-[4-(2-METHYLPHENYL)-6-(4-METHYLPIPERAZIN-1-YL)             
HETNAM   3 GAW  PYRIDIN-3-YL]PROPANAMIDE                                        
HETNAM     CIT CITRIC ACID                                                      
HETNAM     OLA OLEIC ACID                                                       
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETSYN     YCM CYSTEINE-S-ACETAMIDE                                             
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
FORMUL   1  YCM    2(C5 H10 N2 O3 S)                                            
FORMUL   2  GAW    C30 H32 F6 N4 O                                              
FORMUL   3  CIT    C6 H8 O7                                                     
FORMUL   4  OLA    9(C18 H34 O2)                                                
FORMUL  13  OLC    7(C21 H40 O4)                                                
FORMUL  18  PEG    24(C4 H10 O3)                                                
FORMUL  44  HOH   *74(H2 O)                                                     
HELIX    1 AA1 PRO A   28  ALA A   59  1                                  32    
HELIX    2 AA2 HIS A   60  ARG A   64  5                                   5    
HELIX    3 AA3 THR A   65  HIS A   95  1                                  31    
HELIX    4 AA4 GLY A  101  HIS A  136  1                                  36    
HELIX    5 AA5 SER A  143  TYR A  168  1                                  26    
HELIX    6 AA6 LYS A  190  TYR A  205  1                                  16    
HELIX    7 AA7 TYR A  205  SER A  226  1                                  22    
HELIX    8 AA8 ASN A 1225  LEU A 1229  5                                   5    
HELIX    9 AA9 SER A 1232  PHE A 1244  1                                  13    
HELIX   10 AB1 GLY A 1264  SER A 1276  1                                  13    
HELIX   11 AB2 SER A 1277  GLN A 1282  5                                   6    
HELIX   12 AB3 ASP A 1293  HIS A 1307  1                                  15    
HELIX   13 AB4 SER A 1318  GLY A 1327  1                                  10    
HELIX   14 AB5 GLY A 1342  LEU A 1351  1                                  10    
HELIX   15 AB6 VAL A 1360  ILE A 1367  1                                   8    
HELIX   16 AB7 ASP A 1379  ARG A 1395  1                                  17    
HELIX   17 AB8 LEU A 1398  ASN A  274  1                                  53    
HELIX   18 AB9 PHE A  282  ASN A  309  1                                  28    
HELIX   19 AC1 ASN A  309  PHE A  320  1                                  12    
SHEET    1 AA1 2 SER A 169  THR A 173  0                                        
SHEET    2 AA1 2 VAL A 178  ILE A 182 -1  O  LYS A 181   N  THR A 170           
SHEET    1 AA2 6 VAL A1310  ILE A1313  0                                        
SHEET    2 AA2 6 MET A1284  ILE A1289  1  N  ILE A1288   O  LYS A1311           
SHEET    3 AA2 6 VAL A1250  ILE A1255  1  N  PHE A1252   O  ARG A1285           
SHEET    4 AA2 6 PHE A1331  ILE A1334  1  O  ILE A1333   N  MET A1253           
SHEET    5 AA2 6 ILE A1354  SER A1358  1  O  ILE A1356   N  ILE A1334           
SHEET    6 AA2 6 ILE A1373  VAL A1375  1  O  ILE A1373   N  PRO A1355           
SSBOND   1 CYS A  105    CYS A  180                          1555   1555  2.06  
LINK         C   ASP A1220                 N   YCM A1221     1555   1555  1.33  
LINK         C   YCM A1221                 N   SER A1222     1555   1555  1.33  
LINK         C   ARG A 321                 N   YCM A 322     1555   1555  1.33  
LINK         C   YCM A 322                 N   CYS A 323     1555   1555  1.33  
CISPEP   1 MET A  174    PRO A  175          0        -4.51                     
SITE     1 AC1 16 ASN A  89  ASN A 109  PRO A 112  ILE A 113                    
SITE     2 AC1 16 ILE A 116  GLN A 165  HIS A 197  VAL A 200                    
SITE     3 AC1 16 ILE A 204  TRP A 261  PHE A 264  HIS A 265                    
SITE     4 AC1 16 PHE A 268  TYR A 272  MET A 295  HOH A1635                    
SITE     1 AC2 15 GLY A 101  LEU A 102  PHE A 103  THR A 171                    
SITE     2 AC2 15 ARG A 224  OLA A1503  PEG A1518  PEG A1523                    
SITE     3 AC2 15 PEG A1528  HOH A1602  HOH A1606  HOH A1607                    
SITE     4 AC2 15 HOH A1612  HOH A1630  HOH A1666                               
SITE     1 AC3  7 TYR A 100  GLY A 101  TYR A 104  CIT A1502                    
SITE     2 AC3  7 OLA A1504  OLC A1512  PEG A1524                               
SITE     1 AC4  7 GLY A 220  ILE A 221  ARG A 224  OLA A1503                    
SITE     2 AC4  7 OLC A1512  PEG A1519  PEG A1541                               
SITE     1 AC5  5 LYS A 106  PHE A 107  PHE A 110  PHE A 163                    
SITE     2 AC5  5 TYR A 167                                                     
SITE     1 AC6  4 ALA A 319  YCM A 322  PEG A1527  OLC A1540                    
SITE     1 AC7  1 THR A 124                                                     
SITE     1 AC8  5 TYR A 131  HIS A 136  TYR A 214  OLC A1513                    
SITE     2 AC8  5 OLC A1515                                                     
SITE     1 AC9  1 ASN A 274                                                     
SITE     1 AD1  3 THR A 256  TYR A 300  OLC A1512                               
SITE     1 AD2  1 CYS A 199                                                     
SITE     1 AD3 11 GLY A 220  ARG A 224  ARG A 244  LYS A 248                    
SITE     2 AD3 11 ILE A 251  THR A 256  ILE A 259  OLA A1503                    
SITE     3 AD3 11 OLA A1504  OLA A1510  PEG A1541                               
SITE     1 AD4  8 PHE A 128  MET A 132  HIS A 136  GLN A 139                    
SITE     2 AD4  8 TYR A 214  OLA A1508  OLC A1515  PEG A1536                    
SITE     1 AD5  5 ALA A  36  THR A  40  PHE A  90  HIS A  95                    
SITE     2 AD5  5 PHE A1338                                                     
SITE     1 AD6  5 ILE A 135  HIS A 136  OLA A1508  OLC A1513                    
SITE     2 AD6  5 OLC A1539                                                     
SITE     1 AD7  3 ASN A  73  PHE A  76  TRP A 155                               
SITE     1 AD8  8 MET A 174  PRO A 175  SER A 176  ARG A 177                    
SITE     2 AD8  8 VAL A 179  GLY A1256  HOH A1609  HOH A1610                    
SITE     1 AD9  2 LYS A 106  CIT A1502                                          
SITE     1 AE1  3 VAL A  88  TYR A 100  OLA A1504                               
SITE     1 AE2  1 PEG A1533                                                     
SITE     1 AE3  1 ILE A 290                                                     
SITE     1 AE4  5 YCM A1221  GLU A1382  ASN A1385  ALA A1386                    
SITE     2 AE4  5 HOH A1611                                                     
SITE     1 AE5  5 THR A 171  VAL A 178  CIT A1502  HOH A1607                    
SITE     2 AE5  5 HOH A1658                                                     
SITE     1 AE6  4 PHE A  84  PHE A 103  TYR A 104  OLA A1503                    
SITE     1 AE7  2 GLN A  31  TRP A  35                                          
SITE     1 AE8  1 OLA A1506                                                     
SITE     1 AE9  4 SER A 241  ARG A 244  GLU A1392  CIT A1502                    
SITE     1 AF1  2 ILE A 266  LEU A 270                                          
SITE     1 AF2  2 VAL A  48  PHE A 316                                          
SITE     1 AF3  2 GLY A 213  TYR A 214                                          
SITE     1 AF4  2 SER A1242  GLY A1245                                          
SITE     1 AF5  2 TYR A 192  PEG A1520                                          
SITE     1 AF6  2 LYS A1238  OLC A1513                                          
SITE     1 AF7  2 TYR A  92  ASN A  96                                          
SITE     1 AF8  1 LYS A1400                                                     
SITE     1 AF9  5 ILE A 135  PRO A 137  THR A 222  ASP A1365                    
SITE     2 AF9  5 OLC A1515                                                     
SITE     1 AG1  6 VAL A  51  TRP A  55  ILE A 273  ALA A 319                    
SITE     2 AG1  6 ARG A 321  OLA A1506                                          
SITE     1 AG2  5 CYS A 255  ALA A 258  ILE A 259  OLA A1504                    
SITE     2 AG2  5 OLC A1512                                                     
SITE     1 AG3  1 TRP A  30                                                     
CRYST1   61.658   76.571  166.035  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016219  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013060  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006023        0.00000                         
ATOM      1  N   GLN A  27     -16.752  -1.185  18.766  1.00116.46           N  
ANISOU    1  N   GLN A  27    14620  15145  14485  -1790  -1794   1829       N  
ATOM      2  CA  GLN A  27     -17.236  -1.241  20.140  1.00115.29           C  
ANISOU    2  CA  GLN A  27    14274  15102  14426  -1749  -1745   1906       C  
ATOM      3  C   GLN A  27     -18.217  -0.102  20.424  1.00114.38           C  
ANISOU    3  C   GLN A  27    13850  15198  14413  -1659  -1677   2102       C  
ATOM      4  O   GLN A  27     -17.906   1.065  20.178  1.00115.17           O  
ANISOU    4  O   GLN A  27    13882  15304  14573  -1486  -1546   2063       O  
ATOM      5  CB  GLN A  27     -16.068  -1.197  21.115  1.00113.08           C  
ANISOU    5  CB  GLN A  27    14050  14708  14208  -1563  -1580   1695       C  
ATOM      6  N   PRO A  28     -19.395  -0.444  20.947  1.00111.73           N  
ANISOU    6  N   PRO A  28    13330  15036  14087  -1769  -1766   2324       N  
ATOM      7  CA  PRO A  28     -20.430   0.573  21.172  1.00107.95           C  
ANISOU    7  CA  PRO A  28    12551  14781  13684  -1673  -1703   2547       C  
ATOM      8  C   PRO A  28     -20.010   1.613  22.200  1.00101.06           C  
ANISOU    8  C   PRO A  28    11560  13913  12923  -1381  -1472   2463       C  
ATOM      9  O   PRO A  28     -19.270   1.326  23.142  1.00100.19           O  
ANISOU    9  O   PRO A  28    11523  13700  12844  -1297  -1386   2303       O  
ATOM     10  CB  PRO A  28     -21.631  -0.247  21.659  1.00111.98           C  
ANISOU   10  CB  PRO A  28    12906  15472  14167  -1862  -1849   2794       C  
ATOM     11  CG  PRO A  28     -21.030  -1.474  22.249  1.00113.20           C  
ANISOU   11  CG  PRO A  28    13253  15478  14278  -1967  -1909   2649       C  
ATOM     12  CD  PRO A  28     -19.807  -1.773  21.429  1.00112.76           C  
ANISOU   12  CD  PRO A  28    13517  15171  14156  -1975  -1918   2390       C  
ATOM     13  N   ALA A  29     -20.500   2.841  21.999  1.00 95.03           N  
ANISOU   13  N   ALA A  29    10629  13266  12211  -1228  -1377   2578       N  
ATOM     14  CA  ALA A  29     -20.095   3.961  22.842  1.00 89.33           C  
ANISOU   14  CA  ALA A  29     9843  12523  11576   -946  -1163   2497       C  
ATOM     15  C   ALA A  29     -20.517   3.789  24.299  1.00 88.65           C  
ANISOU   15  C   ALA A  29     9615  12533  11533   -851  -1087   2567       C  
ATOM     16  O   ALA A  29     -19.852   4.327  25.193  1.00 86.34           O  
ANISOU   16  O   ALA A  29     9361  12153  11293   -656   -930   2425       O  
ATOM     17  CB  ALA A  29     -20.660   5.269  22.287  1.00 84.67           C  
ANISOU   17  CB  ALA A  29     9119  12037  11013   -803  -1090   2632       C  
ATOM     18  N   TRP A  30     -21.620   3.081  24.569  1.00 92.14           N  
ANISOU   18  N   TRP A  30     9894  13163  11951   -988  -1196   2796       N  
ATOM     19  CA  TRP A  30     -22.038   2.916  25.961  1.00 96.72           C  
ANISOU   19  CA  TRP A  30    10331  13850  12568   -889  -1117   2875       C  
ATOM     20  C   TRP A  30     -21.017   2.106  26.753  1.00 94.43           C  
ANISOU   20  C   TRP A  30    10219  13377  12282   -917  -1102   2641       C  
ATOM     21  O   TRP A  30     -20.763   2.395  27.930  1.00 93.70           O  
ANISOU   21  O   TRP A  30    10094  13272  12236   -741   -962   2577       O  
ATOM     22  CB  TRP A  30     -23.429   2.276  26.039  1.00103.26           C  
ANISOU   22  CB  TRP A  30    10933  14938  13363  -1053  -1250   3194       C  
ATOM     23  CG  TRP A  30     -23.568   0.925  25.390  1.00108.62           C  
ANISOU   23  CG  TRP A  30    11718  15589  13965  -1395  -1491   3228       C  
ATOM     24  CD1 TRP A  30     -23.839   0.673  24.078  1.00112.22           C  
ANISOU   24  CD1 TRP A  30    12239  16047  14354  -1604  -1660   3300       C  
ATOM     25  CD2 TRP A  30     -23.479  -0.356  26.033  1.00110.41           C  
ANISOU   25  CD2 TRP A  30    12019  15775  14159  -1571  -1596   3201       C  
ATOM     26  NE1 TRP A  30     -23.910  -0.683  23.859  1.00113.64           N  
ANISOU   26  NE1 TRP A  30    12552  16174  14453  -1899  -1868   3313       N  
ATOM     27  CE2 TRP A  30     -23.691  -1.336  25.043  1.00112.48           C  
ANISOU   27  CE2 TRP A  30    12413  15999  14327  -1885  -1833   3254       C  
ATOM     28  CE3 TRP A  30     -23.232  -0.768  27.347  1.00110.75           C  
ANISOU   28  CE3 TRP A  30    12046  15800  14235  -1495  -1517   3136       C  
ATOM     29  CZ2 TRP A  30     -23.665  -2.703  25.324  1.00113.05           C  
ANISOU   29  CZ2 TRP A  30    12614  16006  14335  -2121  -1994   3243       C  
ATOM     30  CZ3 TRP A  30     -23.205  -2.126  27.624  1.00111.15           C  
ANISOU   30  CZ3 TRP A  30    12200  15799  14232  -1729  -1672   3128       C  
ATOM     31  CH2 TRP A  30     -23.421  -3.076  26.617  1.00112.03           C  
ANISOU   31  CH2 TRP A  30    12455  15863  14247  -2038  -1909   3181       C  
ATOM     32  N   GLN A  31     -20.393   1.112  26.114  1.00 93.45           N  
ANISOU   32  N   GLN A  31    10302  13105  12101  -1123  -1239   2509       N  
ATOM     33  CA  GLN A  31     -19.304   0.395  26.765  1.00 92.34           C  
ANISOU   33  CA  GLN A  31    10347  12778  11958  -1126  -1214   2276       C  
ATOM     34  C   GLN A  31     -18.109   1.304  27.014  1.00 84.58           C  
ANISOU   34  C   GLN A  31     9469  11639  11027   -906  -1038   2046       C  
ATOM     35  O   GLN A  31     -17.423   1.159  28.033  1.00 83.93           O  
ANISOU   35  O   GLN A  31     9440  11474  10977   -813   -949   1908       O  
ATOM     36  CB  GLN A  31     -18.894  -0.811  25.922  1.00 98.90           C  
ANISOU   36  CB  GLN A  31    11403  13477  12698  -1365  -1391   2192       C  
ATOM     37  CG  GLN A  31     -19.999  -1.835  25.743  1.00107.19           C  
ANISOU   37  CG  GLN A  31    12393  14654  13681  -1625  -1594   2412       C  
ATOM     38  CD  GLN A  31     -19.561  -3.030  24.922  1.00113.55           C  
ANISOU   38  CD  GLN A  31    13479  15292  14373  -1854  -1773   2315       C  
ATOM     39  OE1 GLN A  31     -18.439  -3.075  24.417  1.00114.16           O  
ANISOU   39  OE1 GLN A  31    13783  15173  14419  -1799  -1733   2090       O  
ATOM     40  NE2 GLN A  31     -20.449  -4.009  24.782  1.00117.84           N  
ANISOU   40  NE2 GLN A  31    14017  15916  14843  -2112  -1974   2496       N  
ATOM     41  N   ILE A  32     -17.862   2.261  26.116  1.00 77.85           N  
ANISOU   41  N   ILE A  32     8645  10751  10182   -830   -993   2015       N  
ATOM     42  CA  ILE A  32     -16.780   3.213  26.338  1.00 72.24           C  
ANISOU   42  CA  ILE A  32     8026   9905   9517   -639   -839   1825       C  
ATOM     43  C   ILE A  32     -17.087   4.095  27.541  1.00 67.52           C  
ANISOU   43  C   ILE A  32     7301   9374   8982   -424   -686   1872       C  
ATOM     44  O   ILE A  32     -16.201   4.389  28.352  1.00 65.65           O  
ANISOU   44  O   ILE A  32     7148   9022   8775   -305   -579   1710       O  
ATOM     45  CB  ILE A  32     -16.538   4.053  25.071  1.00 73.08           C  
ANISOU   45  CB  ILE A  32     8185   9969   9611   -618   -835   1807       C  
ATOM     46  CG1 ILE A  32     -16.235   3.148  23.875  1.00 76.32           C  
ANISOU   46  CG1 ILE A  32     8748  10309   9942   -820   -984   1759       C  
ATOM     47  CG2 ILE A  32     -15.405   5.046  25.293  1.00 68.92           C  
ANISOU   47  CG2 ILE A  32     7754   9305   9126   -446   -691   1628       C  
ATOM     48  CD1 ILE A  32     -14.996   2.300  24.057  1.00 75.54           C  
ANISOU   48  CD1 ILE A  32     8852  10040   9811   -856   -987   1544       C  
ATOM     49  N   VAL A  33     -18.346   4.517  27.687  1.00 66.16           N  
ANISOU   49  N   VAL A  33     6928   9391   8817   -367   -674   2103       N  
ATOM     50  CA  VAL A  33     -18.718   5.353  28.827  1.00 66.74           C  
ANISOU   50  CA  VAL A  33     6897   9532   8928   -135   -518   2163       C  
ATOM     51  C   VAL A  33     -18.609   4.567  30.131  1.00 63.06           C  
ANISOU   51  C   VAL A  33     6420   9069   8471   -136   -498   2123       C  
ATOM     52  O   VAL A  33     -18.164   5.097  31.158  1.00 63.79           O  
ANISOU   52  O   VAL A  33     6556   9094   8588     40   -365   2026       O  
ATOM     53  CB  VAL A  33     -20.130   5.931  28.623  1.00 70.01           C  
ANISOU   53  CB  VAL A  33     7089  10175   9336    -57   -505   2446       C  
ATOM     54  CG1 VAL A  33     -20.567   6.720  29.847  1.00 72.20           C  
ANISOU   54  CG1 VAL A  33     7273  10527   9632    210   -335   2521       C  
ATOM     55  CG2 VAL A  33     -20.163   6.815  27.386  1.00 70.41           C  
ANISOU   55  CG2 VAL A  33     7163  10210   9382    -32   -510   2473       C  
ATOM     56  N   LEU A  34     -18.978   3.283  30.104  1.00 62.16           N  
ANISOU   56  N   LEU A  34     6270   9020   8330   -345   -638   2192       N  
ATOM     57  CA  LEU A  34     -18.837   2.458  31.300  1.00 64.85           C  
ANISOU   57  CA  LEU A  34     6609   9355   8675   -364   -630   2152       C  
ATOM     58  C   LEU A  34     -17.370   2.261  31.670  1.00 64.69           C  
ANISOU   58  C   LEU A  34     6804   9109   8668   -342   -584   1869       C  
ATOM     59  O   LEU A  34     -17.001   2.354  32.851  1.00 63.16           O  
ANISOU   59  O   LEU A  34     6623   8876   8497   -223   -485   1790       O  
ATOM     60  CB  LEU A  34     -19.522   1.108  31.091  1.00 68.29           C  
ANISOU   60  CB  LEU A  34     6987   9892   9068   -618   -810   2290       C  
ATOM     61  CG  LEU A  34     -21.043   1.112  30.922  1.00 74.20           C  
ANISOU   61  CG  LEU A  34     7486  10906   9799   -674   -875   2614       C  
ATOM     62  CD1 LEU A  34     -21.562  -0.312  30.787  1.00 75.23           C  
ANISOU   62  CD1 LEU A  34     7601  11104   9879   -964  -1076   2732       C  
ATOM     63  CD2 LEU A  34     -21.716   1.821  32.088  1.00 77.31           C  
ANISOU   63  CD2 LEU A  34     7688  11461  10225   -437   -715   2752       C  
ATOM     64  N   TRP A  35     -16.514   2.004  30.675  1.00 60.86           N  
ANISOU   64  N   TRP A  35     6483   8482   8160   -449   -652   1725       N  
ATOM     65  CA  TRP A  35     -15.094   1.849  30.972  1.00 56.47           C  
ANISOU   65  CA  TRP A  35     6108   7736   7611   -418   -603   1482       C  
ATOM     66  C   TRP A  35     -14.495   3.150  31.487  1.00 51.98           C  
ANISOU   66  C   TRP A  35     5565   7099   7086   -208   -446   1387       C  
ATOM     67  O   TRP A  35     -13.646   3.136  32.390  1.00 49.77           O  
ANISOU   67  O   TRP A  35     5363   6723   6824   -141   -377   1247       O  
ATOM     68  CB  TRP A  35     -14.336   1.374  29.730  1.00 54.87           C  
ANISOU   68  CB  TRP A  35     6069   7417   7362   -548   -694   1371       C  
ATOM     69  CG  TRP A  35     -14.386  -0.107  29.508  1.00 58.68           C  
ANISOU   69  CG  TRP A  35     6639   7874   7783   -742   -838   1370       C  
ATOM     70  CD1 TRP A  35     -14.898  -0.756  28.421  1.00 60.02           C  
ANISOU   70  CD1 TRP A  35     6857   8065   7885   -921   -988   1456       C  
ATOM     71  CD2 TRP A  35     -13.907  -1.126  30.397  1.00 58.40           C  
ANISOU   71  CD2 TRP A  35     6678   7774   7735   -781   -853   1282       C  
ATOM     72  NE1 TRP A  35     -14.764  -2.116  28.577  1.00 60.20           N  
ANISOU   72  NE1 TRP A  35     7001   8026   7847  -1070  -1099   1422       N  
ATOM     73  CE2 TRP A  35     -14.161  -2.369  29.781  1.00 59.25           C  
ANISOU   73  CE2 TRP A  35     6893   7856   7763   -982  -1015   1316       C  
ATOM     74  CE3 TRP A  35     -13.289  -1.108  31.652  1.00 55.04           C  
ANISOU   74  CE3 TRP A  35     6254   7305   7352   -670   -751   1179       C  
ATOM     75  CZ2 TRP A  35     -13.819  -3.580  30.378  1.00 59.08           C  
ANISOU   75  CZ2 TRP A  35     6981   7763   7704  -1063  -1072   1251       C  
ATOM     76  CZ3 TRP A  35     -12.952  -2.312  32.242  1.00 54.64           C  
ANISOU   76  CZ3 TRP A  35     6290   7199   7273   -751   -805   1118       C  
ATOM     77  CH2 TRP A  35     -13.217  -3.531  31.605  1.00 56.82           C  
ANISOU   77  CH2 TRP A  35     6673   7445   7470   -941   -961   1154       C  
ATOM     78  N   ALA A  36     -14.937   4.285  30.938  1.00 46.88           N  
ANISOU   78  N   ALA A  36     4865   6497   6451   -109   -396   1469       N  
ATOM     79  CA  ALA A  36     -14.418   5.565  31.397  1.00 48.07           C  
ANISOU   79  CA  ALA A  36     5072   6566   6628     81   -260   1389       C  
ATOM     80  C   ALA A  36     -14.835   5.834  32.835  1.00 48.25           C  
ANISOU   80  C   ALA A  36     5035   6636   6663    234   -158   1432       C  
ATOM     81  O   ALA A  36     -14.037   6.342  33.631  1.00 45.83           O  
ANISOU   81  O   ALA A  36     4837   6211   6365    338    -72   1299       O  
ATOM     82  CB  ALA A  36     -14.894   6.688  30.477  1.00 45.18           C  
ANISOU   82  CB  ALA A  36     4671   6234   6260    157   -234   1482       C  
ATOM     83  N   ALA A  37     -16.066   5.455  33.198  1.00 48.73           N  
ANISOU   83  N   ALA A  37     4925   6874   6715    242   -174   1626       N  
ATOM     84  CA  ALA A  37     -16.489   5.597  34.586  1.00 50.89           C  
ANISOU   84  CA  ALA A  37     5139   7208   6989    393    -73   1678       C  
ATOM     85  C   ALA A  37     -15.676   4.696  35.507  1.00 52.51           C  
ANISOU   85  C   ALA A  37     5427   7323   7202    324    -88   1528       C  
ATOM     86  O   ALA A  37     -15.310   5.103  36.618  1.00 56.09           O  
ANISOU   86  O   ALA A  37     5942   7714   7655    462     13   1452       O  
ATOM     87  CB  ALA A  37     -17.981   5.289  34.718  1.00 50.27           C  
ANISOU   87  CB  ALA A  37     4834   7371   6897    402    -94   1945       C  
ATOM     88  N   ALA A  38     -15.357   3.478  35.057  1.00 51.28           N  
ANISOU   88  N   ALA A  38     5296   7147   7042    114   -215   1482       N  
ATOM     89  CA  ALA A  38     -14.599   2.569  35.919  1.00 51.15           C  
ANISOU   89  CA  ALA A  38     5358   7048   7027     54   -230   1349       C  
ATOM     90  C   ALA A  38     -13.180   3.081  36.156  1.00 49.95           C  
ANISOU   90  C   ALA A  38     5378   6712   6888    118   -164   1131       C  
ATOM     91  O   ALA A  38     -12.684   3.080  37.296  1.00 51.01           O  
ANISOU   91  O   ALA A  38     5561   6792   7029    189   -100   1045       O  
ATOM     92  CB  ALA A  38     -14.576   1.168  35.307  1.00 50.02           C  
ANISOU   92  CB  ALA A  38     5237   6908   6861   -172   -382   1352       C  
ATOM     93  N   TYR A  39     -12.520   3.552  35.094  1.00 46.43           N  
ANISOU   93  N   TYR A  39     5022   6179   6442     87   -182   1052       N  
ATOM     94  CA  TYR A  39     -11.194   4.135  35.269  1.00 44.99           C  
ANISOU   94  CA  TYR A  39     4982   5845   6269    136   -126    878       C  
ATOM     95  C   TYR A  39     -11.244   5.410  36.107  1.00 45.91           C  
ANISOU   95  C   TYR A  39     5128   5925   6390    317     -8    875       C  
ATOM     96  O   TYR A  39     -10.317   5.675  36.889  1.00 45.59           O  
ANISOU   96  O   TYR A  39     5193   5780   6350    357     37    752       O  
ATOM     97  CB  TYR A  39     -10.555   4.399  33.904  1.00 42.66           C  
ANISOU   97  CB  TYR A  39     4759   5486   5965     67   -169    822       C  
ATOM     98  CG  TYR A  39      -9.962   3.159  33.255  1.00 45.36           C  
ANISOU   98  CG  TYR A  39     5158   5795   6280    -85   -264    754       C  
ATOM     99  CD1 TYR A  39     -10.772   2.215  32.632  1.00 46.34           C  
ANISOU   99  CD1 TYR A  39     5236   5994   6375   -206   -368    851       C  
ATOM    100  CD2 TYR A  39      -8.589   2.935  33.266  1.00 44.02           C  
ANISOU  100  CD2 TYR A  39     5102   5521   6103   -104   -253    605       C  
ATOM    101  CE1 TYR A  39     -10.231   1.082  32.038  1.00 44.97           C  
ANISOU  101  CE1 TYR A  39     5162   5767   6156   -331   -455    784       C  
ATOM    102  CE2 TYR A  39      -8.039   1.809  32.675  1.00 42.66           C  
ANISOU  102  CE2 TYR A  39     5003   5317   5891   -207   -324    548       C  
ATOM    103  CZ  TYR A  39      -8.865   0.888  32.060  1.00 43.37           C  
ANISOU  103  CZ  TYR A  39     5080   5457   5943   -315   -424    630       C  
ATOM    104  OH  TYR A  39      -8.323  -0.231  31.475  1.00 41.07           O  
ANISOU  104  OH  TYR A  39     4905   5109   5591   -404   -495    569       O  
ATOM    105  N   THR A  40     -12.322   6.196  35.990  1.00 47.52           N  
ANISOU  105  N   THR A  40     5252   6216   6587    433     39   1018       N  
ATOM    106  CA  THR A  40     -12.464   7.372  36.844  1.00 47.46           C  
ANISOU  106  CA  THR A  40     5306   6165   6563    630    157   1024       C  
ATOM    107  C   THR A  40     -12.604   6.971  38.307  1.00 48.38           C  
ANISOU  107  C   THR A  40     5414   6302   6668    702    210   1016       C  
ATOM    108  O   THR A  40     -12.094   7.659  39.204  1.00 51.08           O  
ANISOU  108  O   THR A  40     5886   6536   6986    813    285    931       O  
ATOM    109  CB  THR A  40     -13.677   8.196  36.406  1.00 50.15           C  
ANISOU  109  CB  THR A  40     5554   6614   6887    763    205   1201       C  
ATOM    110  OG1 THR A  40     -13.537   8.576  35.032  1.00 50.52           O  
ANISOU  110  OG1 THR A  40     5612   6640   6944    692    153   1207       O  
ATOM    111  CG2 THR A  40     -13.818   9.450  37.258  1.00 52.34           C  
ANISOU  111  CG2 THR A  40     5937   6823   7125    995    335   1204       C  
ATOM    112  N   VAL A  41     -13.285   5.850  38.564  1.00 48.25           N  
ANISOU  112  N   VAL A  41     5255   6419   6658    628    162   1109       N  
ATOM    113  CA  VAL A  41     -13.397   5.360  39.934  1.00 49.37           C  
ANISOU  113  CA  VAL A  41     5380   6589   6789    681    206   1106       C  
ATOM    114  C   VAL A  41     -12.021   5.009  40.472  1.00 48.79           C  
ANISOU  114  C   VAL A  41     5452   6363   6725    608    188    906       C  
ATOM    115  O   VAL A  41     -11.677   5.350  41.612  1.00 50.89           O  
ANISOU  115  O   VAL A  41     5803   6564   6970    708    259    841       O  
ATOM    116  CB  VAL A  41     -14.353   4.155  40.007  1.00 49.20           C  
ANISOU  116  CB  VAL A  41     5178   6742   6773    579    137   1255       C  
ATOM    117  CG1 VAL A  41     -14.216   3.455  41.357  1.00 49.95           C  
ANISOU  117  CG1 VAL A  41     5273   6845   6862    592    161   1220       C  
ATOM    118  CG2 VAL A  41     -15.790   4.597  39.787  1.00 47.88           C  
ANISOU  118  CG2 VAL A  41     4841   6763   6590    684    174   1490       C  
ATOM    119  N   ILE A  42     -11.190   4.376  39.639  1.00 46.28           N  
ANISOU  119  N   ILE A  42     5173   5984   6427    443     98    812       N  
ATOM    120  CA  ILE A  42      -9.816   4.109  40.062  1.00 44.53           C  
ANISOU  120  CA  ILE A  42     5075   5634   6210    385     87    641       C  
ATOM    121  C   ILE A  42      -9.123   5.407  40.450  1.00 46.74           C  
ANISOU  121  C   ILE A  42     5493   5791   6474    489    159    558       C  
ATOM    122  O   ILE A  42      -8.530   5.519  41.532  1.00 47.53           O  
ANISOU  122  O   ILE A  42     5679   5821   6560    526    194    477       O  
ATOM    123  CB  ILE A  42      -9.020   3.392  38.960  1.00 44.89           C  
ANISOU  123  CB  ILE A  42     5150   5641   6265    230     -3    569       C  
ATOM    124  CG1 ILE A  42      -9.503   1.960  38.757  1.00 46.69           C  
ANISOU  124  CG1 ILE A  42     5304   5946   6489    108    -90    622       C  
ATOM    125  CG2 ILE A  42      -7.532   3.421  39.316  1.00 43.00           C  
ANISOU  125  CG2 ILE A  42     5029   5283   6026    203      5    415       C  
ATOM    126  CD1 ILE A  42      -8.718   1.229  37.671  1.00 46.59           C  
ANISOU  126  CD1 ILE A  42     5360   5880   6463    -19   -171    548       C  
ATOM    127  N   VAL A  43      -9.199   6.414  39.575  1.00 42.83           N  
ANISOU  127  N   VAL A  43     5035   5264   5975    528    172    582       N  
ATOM    128  CA  VAL A  43      -8.437   7.641  39.806  1.00 43.07           C  
ANISOU  128  CA  VAL A  43     5226   5156   5982    592    216    501       C  
ATOM    129  C   VAL A  43      -8.856   8.294  41.118  1.00 44.15           C  
ANISOU  129  C   VAL A  43     5442   5258   6075    756    304    516       C  
ATOM    130  O   VAL A  43      -8.016   8.625  41.969  1.00 45.91           O  
ANISOU  130  O   VAL A  43     5806   5367   6271    760    317    417       O  
ATOM    131  CB  VAL A  43      -8.607   8.618  38.628  1.00 45.20           C  
ANISOU  131  CB  VAL A  43     5522   5402   6250    614    216    544       C  
ATOM    132  CG1 VAL A  43      -7.850   9.910  38.907  1.00 45.28           C  
ANISOU  132  CG1 VAL A  43     5721   5258   6225    667    249    471       C  
ATOM    133  CG2 VAL A  43      -8.131   7.982  37.338  1.00 43.47           C  
ANISOU  133  CG2 VAL A  43     5245   5211   6060    460    133    524       C  
ATOM    134  N   VAL A  44     -10.161   8.486  41.306  1.00 43.16           N  
ANISOU  134  N   VAL A  44     5232   5236   5931    896    366    652       N  
ATOM    135  CA  VAL A  44     -10.599   9.242  42.472  1.00 47.60           C  
ANISOU  135  CA  VAL A  44     5895   5761   6432   1092    468    676       C  
ATOM    136  C   VAL A  44     -10.351   8.447  43.748  1.00 46.68           C  
ANISOU  136  C   VAL A  44     5779   5652   6306   1079    476    624       C  
ATOM    137  O   VAL A  44      -9.874   8.997  44.752  1.00 46.24           O  
ANISOU  137  O   VAL A  44     5893   5477   6197   1154    520    546       O  
ATOM    138  CB  VAL A  44     -12.072   9.674  42.321  1.00 54.69           C  
ANISOU  138  CB  VAL A  44     6685   6792   7303   1274    546    859       C  
ATOM    139  CG1 VAL A  44     -12.260  10.428  41.008  1.00 52.43           C  
ANISOU  139  CG1 VAL A  44     6397   6496   7028   1276    529    908       C  
ATOM    140  CG2 VAL A  44     -13.015   8.485  42.385  1.00 61.43           C  
ANISOU  140  CG2 VAL A  44     7300   7854   8189   1231    524    992       C  
ATOM    141  N   THR A  45     -10.609   7.133  43.721  1.00 46.30           N  
ANISOU  141  N   THR A  45     5560   5729   6302    968    423    662       N  
ATOM    142  CA  THR A  45     -10.409   6.335  44.921  1.00 46.22           C  
ANISOU  142  CA  THR A  45     5544   5732   6285    953    429    621       C  
ATOM    143  C   THR A  45      -8.941   6.312  45.317  1.00 47.01           C  
ANISOU  143  C   THR A  45     5795   5681   6386    852    388    449       C  
ATOM    144  O   THR A  45      -8.606   6.528  46.491  1.00 43.29           O  
ANISOU  144  O   THR A  45     5435   5140   5872    914    428    391       O  
ATOM    145  CB  THR A  45     -10.931   4.918  44.692  1.00 46.13           C  
ANISOU  145  CB  THR A  45     5340   5870   6317    831    362    699       C  
ATOM    146  OG1 THR A  45     -12.264   4.983  44.168  1.00 46.70           O  
ANISOU  146  OG1 THR A  45     5257   6099   6389    893    380    882       O  
ATOM    147  CG2 THR A  45     -10.933   4.136  46.007  1.00 44.57           C  
ANISOU  147  CG2 THR A  45     5123   5704   6106    840    380    685       C  
ATOM    148  N   SER A  46      -8.046   6.122  44.342  1.00 48.29           N  
ANISOU  148  N   SER A  46     5966   5795   6586    702    310    377       N  
ATOM    149  CA  SER A  46      -6.625   6.082  44.658  1.00 45.45           C  
ANISOU  149  CA  SER A  46     5719   5323   6226    602    269    243       C  
ATOM    150  C   SER A  46      -6.141   7.422  45.190  1.00 45.67           C  
ANISOU  150  C   SER A  46     5946   5208   6197    675    306    190       C  
ATOM    151  O   SER A  46      -5.433   7.470  46.202  1.00 42.79           O  
ANISOU  151  O   SER A  46     5690   4768   5801    659    304    115       O  
ATOM    152  CB  SER A  46      -5.822   5.682  43.423  1.00 44.70           C  
ANISOU  152  CB  SER A  46     5587   5226   6172    455    193    203       C  
ATOM    153  OG  SER A  46      -4.432   5.795  43.683  1.00 45.99           O  
ANISOU  153  OG  SER A  46     5844   5301   6327    370    161    101       O  
ATOM    154  N   VAL A  47      -6.544   8.526  44.553  1.00 43.94           N  
ANISOU  154  N   VAL A  47     5794   4947   5956    755    336    233       N  
ATOM    155  CA  VAL A  47      -6.019   9.824  44.965  1.00 41.75           C  
ANISOU  155  CA  VAL A  47     5744   4506   5612    805    353    180       C  
ATOM    156  C   VAL A  47      -6.512  10.179  46.362  1.00 42.71           C  
ANISOU  156  C   VAL A  47     5990   4580   5657    964    429    183       C  
ATOM    157  O   VAL A  47      -5.719  10.528  47.246  1.00 42.91           O  
ANISOU  157  O   VAL A  47     6192   4483   5630    934    411    100       O  
ATOM    158  CB  VAL A  47      -6.385  10.912  43.938  1.00 46.25           C  
ANISOU  158  CB  VAL A  47     6371   5034   6170    863    367    230       C  
ATOM    159  CG1 VAL A  47      -6.048  12.288  44.486  1.00 43.56           C  
ANISOU  159  CG1 VAL A  47     6303   4508   5738    939    389    189       C  
ATOM    160  CG2 VAL A  47      -5.648  10.667  42.626  1.00 43.65           C  
ANISOU  160  CG2 VAL A  47     5959   4727   5901    694    287    210       C  
ATOM    161  N   VAL A  48      -7.820  10.048  46.599  1.00 43.67           N  
ANISOU  161  N   VAL A  48     6018   4811   5765   1132    513    290       N  
ATOM    162  CA  VAL A  48      -8.366  10.409  47.905  1.00 46.19           C  
ANISOU  162  CA  VAL A  48     6456   5098   5997   1317    604    308       C  
ATOM    163  C   VAL A  48      -7.801   9.505  48.998  1.00 47.37           C  
ANISOU  163  C   VAL A  48     6595   5254   6149   1237    577    237       C  
ATOM    164  O   VAL A  48      -7.329   9.984  50.040  1.00 49.80           O  
ANISOU  164  O   VAL A  48     7108   5434   6378   1278    592    165       O  
ATOM    165  CB  VAL A  48      -9.904  10.366  47.871  1.00 49.95           C  
ANISOU  165  CB  VAL A  48     6787   5732   6459   1517    704    470       C  
ATOM    166  CG1 VAL A  48     -10.473  10.476  49.279  1.00 53.49           C  
ANISOU  166  CG1 VAL A  48     7319   6187   6818   1713    807    501       C  
ATOM    167  CG2 VAL A  48     -10.443  11.485  46.977  1.00 49.52           C  
ANISOU  167  CG2 VAL A  48     6792   5647   6378   1637    746    541       C  
ATOM    168  N   GLY A  49      -7.811   8.186  48.775  1.00 47.75           N  
ANISOU  168  N   GLY A  49     6425   5439   6280   1114    530    254       N  
ATOM    169  CA  GLY A  49      -7.378   7.285  49.828  1.00 42.24           C  
ANISOU  169  CA  GLY A  49     5708   4758   5583   1055    512    200       C  
ATOM    170  C   GLY A  49      -5.899   7.402  50.140  1.00 45.56           C  
ANISOU  170  C   GLY A  49     6272   5043   5996    907    436     67       C  
ATOM    171  O   GLY A  49      -5.503   7.397  51.310  1.00 42.79           O  
ANISOU  171  O   GLY A  49     6036   4629   5592    922    444     12       O  
ATOM    172  N   ASN A  50      -5.058   7.558  49.111  1.00 40.97           N  
ANISOU  172  N   ASN A  50     5687   4422   5458    766    362     26       N  
ATOM    173  CA  ASN A  50      -3.631   7.664  49.378  1.00 40.56           C  
ANISOU  173  CA  ASN A  50     5743   4273   5397    618    286    -70       C  
ATOM    174  C   ASN A  50      -3.258   9.020  49.960  1.00 41.70           C  
ANISOU  174  C   ASN A  50     6155   4244   5445    659    289   -111       C  
ATOM    175  O   ASN A  50      -2.344   9.098  50.791  1.00 41.81           O  
ANISOU  175  O   ASN A  50     6291   4178   5417    574    240   -174       O  
ATOM    176  CB  ASN A  50      -2.837   7.375  48.109  1.00 42.18           C  
ANISOU  176  CB  ASN A  50     5850   4510   5668    465    213    -82       C  
ATOM    177  CG  ASN A  50      -2.728   5.883  47.822  1.00 45.56           C  
ANISOU  177  CG  ASN A  50     6082   5064   6164    386    185    -78       C  
ATOM    178  OD1 ASN A  50      -2.152   5.136  48.614  1.00 42.47           O  
ANISOU  178  OD1 ASN A  50     5676   4687   5774    333    163   -119       O  
ATOM    179  ND2 ASN A  50      -3.269   5.447  46.686  1.00 38.27           N  
ANISOU  179  ND2 ASN A  50     5028   4224   5289    377    179    -27       N  
ATOM    180  N   VAL A  51      -3.954  10.095  49.568  1.00 42.70           N  
ANISOU  180  N   VAL A  51     6392   4306   5525    787    339    -69       N  
ATOM    181  CA  VAL A  51      -3.689  11.388  50.190  1.00 45.85           C  
ANISOU  181  CA  VAL A  51     7093   4516   5810    842    341   -107       C  
ATOM    182  C   VAL A  51      -4.083  11.359  51.662  1.00 46.52           C  
ANISOU  182  C   VAL A  51     7309   4560   5808    975    402   -124       C  
ATOM    183  O   VAL A  51      -3.359  11.873  52.525  1.00 45.53           O  
ANISOU  183  O   VAL A  51     7416   4289   5595    925    358   -191       O  
ATOM    184  CB  VAL A  51      -4.417  12.509  49.423  1.00 46.82           C  
ANISOU  184  CB  VAL A  51     7316   4578   5896    975    391    -52       C  
ATOM    185  CG1 VAL A  51      -4.489  13.777  50.259  1.00 49.69           C  
ANISOU  185  CG1 VAL A  51     8028   4739   6114   1101    421    -80       C  
ATOM    186  CG2 VAL A  51      -3.707  12.785  48.114  1.00 45.43           C  
ANISOU  186  CG2 VAL A  51     7089   4391   5781    812    309    -56       C  
ATOM    187  N   VAL A  52      -5.214  10.721  51.979  1.00 48.70           N  
ANISOU  187  N   VAL A  52     7432   4972   6099   1133    498    -55       N  
ATOM    188  CA  VAL A  52      -5.609  10.594  53.379  1.00 50.20           C  
ANISOU  188  CA  VAL A  52     7721   5146   6205   1267    565    -61       C  
ATOM    189  C   VAL A  52      -4.640   9.697  54.144  1.00 48.57           C  
ANISOU  189  C   VAL A  52     7479   4951   6025   1098    489   -137       C  
ATOM    190  O   VAL A  52      -4.361   9.947  55.319  1.00 49.39           O  
ANISOU  190  O   VAL A  52     7775   4955   6034   1131    494   -186       O  
ATOM    191  CB  VAL A  52      -7.061  10.088  53.478  1.00 49.95           C  
ANISOU  191  CB  VAL A  52     7501   5291   6187   1467    683     60       C  
ATOM    192  CG1 VAL A  52      -7.394   9.677  54.900  1.00 48.81           C  
ANISOU  192  CG1 VAL A  52     7399   5172   5974   1580    747     62       C  
ATOM    193  CG2 VAL A  52      -8.029  11.170  53.004  1.00 47.40           C  
ANISOU  193  CG2 VAL A  52     7266   4942   5802   1684    776    145       C  
ATOM    194  N   VAL A  53      -4.078   8.671  53.497  1.00 43.20           N  
ANISOU  194  N   VAL A  53     6573   4381   5461    919    417   -146       N  
ATOM    195  CA  VAL A  53      -3.088   7.830  54.174  1.00 42.83           C  
ANISOU  195  CA  VAL A  53     6491   4347   5437    766    346   -209       C  
ATOM    196  C   VAL A  53      -1.837   8.638  54.501  1.00 47.57           C  
ANISOU  196  C   VAL A  53     7316   4787   5973    632    256   -283       C  
ATOM    197  O   VAL A  53      -1.279   8.542  55.608  1.00 48.59           O  
ANISOU  197  O   VAL A  53     7561   4859   6044    587    224   -330       O  
ATOM    198  CB  VAL A  53      -2.753   6.597  53.308  1.00 40.91           C  
ANISOU  198  CB  VAL A  53     5982   4246   5316    628    294   -196       C  
ATOM    199  CG1 VAL A  53      -1.401   5.996  53.700  1.00 40.22           C  
ANISOU  199  CG1 VAL A  53     5885   4150   5247    451    206   -259       C  
ATOM    200  CG2 VAL A  53      -3.846   5.554  53.422  1.00 40.57           C  
ANISOU  200  CG2 VAL A  53     5742   4354   5317    715    354   -127       C  
ATOM    201  N   MET A  54      -1.381   9.453  53.546  1.00 46.63           N  
ANISOU  201  N   MET A  54     7264   4596   5858    554    205   -283       N  
ATOM    202  CA  MET A  54      -0.212  10.286  53.799  1.00 49.12           C  
ANISOU  202  CA  MET A  54     7795   4764   6105    403    104   -329       C  
ATOM    203  C   MET A  54      -0.489  11.315  54.884  1.00 51.13           C  
ANISOU  203  C   MET A  54     8381   4837   6210    512    126   -360       C  
ATOM    204  O   MET A  54       0.400  11.622  55.684  1.00 54.22           O  
ANISOU  204  O   MET A  54     8956   5120   6525    388     41   -403       O  
ATOM    205  CB  MET A  54       0.238  10.972  52.507  1.00 49.31           C  
ANISOU  205  CB  MET A  54     7818   4757   6161    302     48   -307       C  
ATOM    206  CG  MET A  54       0.691   9.992  51.435  1.00 51.78           C  
ANISOU  206  CG  MET A  54     7839   5234   6600    187     18   -281       C  
ATOM    207  SD  MET A  54       1.322  10.759  49.923  1.00 53.97           S  
ANISOU  207  SD  MET A  54     8106   5491   6910     63    -47   -247       S  
ATOM    208  CE  MET A  54      -0.051  11.813  49.465  1.00 53.53           C  
ANISOU  208  CE  MET A  54     8180   5347   6811    268     41   -218       C  
ATOM    209  N   TRP A  55      -1.717  11.837  54.950  1.00 47.51           N  
ANISOU  209  N   TRP A  55     8011   4345   5696    748    241   -329       N  
ATOM    210  CA  TRP A  55      -2.048  12.755  56.035  1.00 51.97           C  
ANISOU  210  CA  TRP A  55     8914   4734   6097    894    281   -357       C  
ATOM    211  C   TRP A  55      -2.079  12.035  57.378  1.00 52.79           C  
ANISOU  211  C   TRP A  55     9026   4872   6161    933    308   -385       C  
ATOM    212  O   TRP A  55      -1.592  12.564  58.382  1.00 51.66           O  
ANISOU  212  O   TRP A  55     9168   4571   5891    905    262   -439       O  
ATOM    213  CB  TRP A  55      -3.389  13.437  55.766  1.00 53.36           C  
ANISOU  213  CB  TRP A  55     9163   4892   6218   1174    417   -297       C  
ATOM    214  CG  TRP A  55      -3.903  14.198  56.955  1.00 56.12           C  
ANISOU  214  CG  TRP A  55     9847   5087   6390   1386    494   -315       C  
ATOM    215  CD1 TRP A  55      -3.556  15.466  57.329  1.00 57.86           C  
ANISOU  215  CD1 TRP A  55    10480   5054   6451   1404    453   -363       C  
ATOM    216  CD2 TRP A  55      -4.850  13.739  57.930  1.00 58.69           C  
ANISOU  216  CD2 TRP A  55    10141   5495   6662   1615    624   -280       C  
ATOM    217  NE1 TRP A  55      -4.228  15.824  58.475  1.00 59.01           N  
ANISOU  217  NE1 TRP A  55    10873   5110   6440   1646    556   -369       N  
ATOM    218  CE2 TRP A  55      -5.032  14.784  58.862  1.00 59.48           C  
ANISOU  218  CE2 TRP A  55    10652   5383   6563   1785    668   -314       C  
ATOM    219  CE3 TRP A  55      -5.564  12.549  58.104  1.00 59.65           C  
ANISOU  219  CE3 TRP A  55     9939   5849   6876   1689    704   -216       C  
ATOM    220  CZ2 TRP A  55      -5.895  14.673  59.955  1.00 61.72           C  
ANISOU  220  CZ2 TRP A  55    11019   5692   6738   2046    804   -284       C  
ATOM    221  CZ3 TRP A  55      -6.422  12.439  59.192  1.00 60.08           C  
ANISOU  221  CZ3 TRP A  55    10057   5938   6831   1928    829   -177       C  
ATOM    222  CH2 TRP A  55      -6.578  13.494  60.104  1.00 61.18           C  
ANISOU  222  CH2 TRP A  55    10597   5877   6774   2113    885   -211       C  
ATOM    223  N   ILE A  56      -2.628  10.817  57.411  1.00 52.46           N  
ANISOU  223  N   ILE A  56     8684   5031   6219    983    371   -346       N  
ATOM    224  CA  ILE A  56      -2.729  10.079  58.668  1.00 51.59           C  
ANISOU  224  CA  ILE A  56     8561   4966   6074   1027    402   -364       C  
ATOM    225  C   ILE A  56      -1.344   9.803  59.228  1.00 49.64           C  
ANISOU  225  C   ILE A  56     8376   4663   5821    789    269   -433       C  
ATOM    226  O   ILE A  56      -1.107   9.929  60.434  1.00 53.47           O  
ANISOU  226  O   ILE A  56     9055   5059   6201    802    257   -475       O  
ATOM    227  CB  ILE A  56      -3.515   8.770  58.457  1.00 51.00           C  
ANISOU  227  CB  ILE A  56     8139   5122   6117   1086    472   -297       C  
ATOM    228  CG1 ILE A  56      -4.999   9.054  58.212  1.00 50.82           C  
ANISOU  228  CG1 ILE A  56     8064   5174   6072   1343    611   -200       C  
ATOM    229  CG2 ILE A  56      -3.314   7.812  59.643  1.00 48.38           C  
ANISOU  229  CG2 ILE A  56     7755   4850   5778   1059    469   -320       C  
ATOM    230  CD1 ILE A  56      -5.742   7.870  57.621  1.00 47.00           C  
ANISOU  230  CD1 ILE A  56     7225   4918   5716   1345    645   -111       C  
ATOM    231  N   ILE A  57      -0.394   9.474  58.356  1.00 47.77           N  
ANISOU  231  N   ILE A  57     7985   4479   5686    574    167   -437       N  
ATOM    232  CA  ILE A  57       0.949   9.169  58.835  1.00 46.99           C  
ANISOU  232  CA  ILE A  57     7906   4362   5586    348     42   -475       C  
ATOM    233  C   ILE A  57       1.729  10.447  59.145  1.00 53.80           C  
ANISOU  233  C   ILE A  57     9102   5017   6321    234    -61   -506       C  
ATOM    234  O   ILE A  57       2.259  10.612  60.248  1.00 59.49           O  
ANISOU  234  O   ILE A  57    10015   5645   6942    166   -122   -541       O  
ATOM    235  CB  ILE A  57       1.684   8.285  57.811  1.00 44.74           C  
ANISOU  235  CB  ILE A  57     7323   4230   5444    183    -17   -448       C  
ATOM    236  CG1 ILE A  57       0.994   6.921  57.707  1.00 45.48           C  
ANISOU  236  CG1 ILE A  57     7137   4503   5641    271     61   -424       C  
ATOM    237  CG2 ILE A  57       3.150   8.141  58.190  1.00 43.66           C  
ANISOU  237  CG2 ILE A  57     7205   4086   5297    -47   -148   -460       C  
ATOM    238  CD1 ILE A  57       1.569   6.003  56.635  1.00 48.54           C  
ANISOU  238  CD1 ILE A  57     7261   5028   6153    150     20   -399       C  
ATOM    239  N   LEU A  58       1.811  11.371  58.181  1.00 57.18           N  
ANISOU  239  N   LEU A  58     9618   5366   6743    200    -92   -488       N  
ATOM    240  CA  LEU A  58       2.710  12.517  58.314  1.00 57.67           C  
ANISOU  240  CA  LEU A  58     9978   5240   6695     33   -222   -503       C  
ATOM    241  C   LEU A  58       2.234  13.533  59.349  1.00 59.47           C  
ANISOU  241  C   LEU A  58    10620   5241   6734    165   -200   -547       C  
ATOM    242  O   LEU A  58       3.064  14.198  59.980  1.00 62.72           O  
ANISOU  242  O   LEU A  58    11311   5493   7026      3   -327   -570       O  
ATOM    243  CB  LEU A  58       2.893  13.198  56.954  1.00 56.91           C  
ANISOU  243  CB  LEU A  58     9854   5125   6645    -38   -259   -465       C  
ATOM    244  CG  LEU A  58       3.569  12.352  55.869  1.00 59.46           C  
ANISOU  244  CG  LEU A  58     9819   5646   7126   -190   -298   -419       C  
ATOM    245  CD1 LEU A  58       3.589  13.081  54.533  1.00 60.83           C  
ANISOU  245  CD1 LEU A  58     9981   5797   7334   -226   -317   -379       C  
ATOM    246  CD2 LEU A  58       4.979  11.958  56.289  1.00 59.95           C  
ANISOU  246  CD2 LEU A  58     9826   5760   7193   -442   -433   -401       C  
ATOM    247  N   ALA A  59       0.922  13.687  59.534  1.00 58.02           N  
ANISOU  247  N   ALA A  59    10496   5043   6509    457    -45   -547       N  
ATOM    248  CA  ALA A  59       0.402  14.714  60.430  1.00 59.97           C  
ANISOU  248  CA  ALA A  59    11161   5067   6557    630     -3   -582       C  
ATOM    249  C   ALA A  59       0.247  14.256  61.876  1.00 65.26           C  
ANISOU  249  C   ALA A  59    11935   5724   7136    714     35   -619       C  
ATOM    250  O   ALA A  59      -0.094  15.078  62.732  1.00 66.26           O  
ANISOU  250  O   ALA A  59    12446   5656   7076    857     66   -654       O  
ATOM    251  CB  ALA A  59      -0.949  15.232  59.925  1.00 57.14           C  
ANISOU  251  CB  ALA A  59    10837   4700   6175    936    158   -545       C  
ATOM    252  N   HIS A  60       0.479  12.982  62.180  1.00 65.22           N  
ANISOU  252  N   HIS A  60    11623   5913   7245    641     36   -613       N  
ATOM    253  CA  HIS A  60       0.317  12.467  63.539  1.00 64.89           C  
ANISOU  253  CA  HIS A  60    11652   5877   7126    719     75   -642       C  
ATOM    254  C   HIS A  60       1.639  11.858  63.989  1.00 61.40           C  
ANISOU  254  C   HIS A  60    11135   5473   6721    427    -80   -664       C  
ATOM    255  O   HIS A  60       2.079  10.842  63.441  1.00 57.29           O  
ANISOU  255  O   HIS A  60    10259   5144   6364    299   -108   -634       O  
ATOM    256  CB  HIS A  60      -0.824  11.452  63.606  1.00 65.24           C  
ANISOU  256  CB  HIS A  60    11396   6130   7260    942    240   -596       C  
ATOM    257  CG  HIS A  60      -2.149  12.017  63.196  1.00 68.42           C  
ANISOU  257  CG  HIS A  60    11841   6531   7624   1235    395   -546       C  
ATOM    258  ND1 HIS A  60      -2.608  11.969  61.897  1.00 67.56           N  
ANISOU  258  ND1 HIS A  60    11501   6531   7639   1264    434   -488       N  
ATOM    259  CD2 HIS A  60      -3.102  12.662  63.908  1.00 70.36           C  
ANISOU  259  CD2 HIS A  60    12337   6684   7712   1523    525   -534       C  
ATOM    260  CE1 HIS A  60      -3.791  12.553  61.830  1.00 69.11           C  
ANISOU  260  CE1 HIS A  60    11786   6712   7762   1549    576   -435       C  
ATOM    261  NE2 HIS A  60      -4.115  12.981  63.036  1.00 70.63           N  
ANISOU  261  NE2 HIS A  60    12268   6786   7781   1722    641   -459       N  
ATOM    262  N   LYS A  61       2.247  12.469  65.009  1.00 63.00           N  
ANISOU  262  N   LYS A  61    11684   5492   6761    332   -178   -708       N  
ATOM    263  CA  LYS A  61       3.617  12.136  65.390  1.00 69.33           C  
ANISOU  263  CA  LYS A  61    12456   6311   7574     24   -353   -709       C  
ATOM    264  C   LYS A  61       3.767  10.678  65.811  1.00 68.08           C  
ANISOU  264  C   LYS A  61    11956   6372   7537      0   -322   -696       C  
ATOM    265  O   LYS A  61       4.833  10.085  65.612  1.00 66.83           O  
ANISOU  265  O   LYS A  61    11597   6325   7468   -233   -435   -665       O  
ATOM    266  CB  LYS A  61       4.079  13.060  66.518  1.00 78.16           C  
ANISOU  266  CB  LYS A  61    14043   7182   8472    -56   -461   -754       C  
ATOM    267  CG  LYS A  61       3.765  14.538  66.284  1.00 85.56           C  
ANISOU  267  CG  LYS A  61    15401   7859   9249     15   -476   -776       C  
ATOM    268  CD  LYS A  61       4.310  15.413  67.408  1.00 92.12           C  
ANISOU  268  CD  LYS A  61    16731   8425   9844    -96   -609   -821       C  
ATOM    269  CE  LYS A  61       4.150  16.893  67.082  1.00 96.84           C  
ANISOU  269  CE  LYS A  61    17773   8745  10279    -66   -653   -839       C  
ATOM    270  NZ  LYS A  61       4.821  17.247  65.798  1.00 97.63           N  
ANISOU  270  NZ  LYS A  61    17727   8880  10490   -293   -766   -782       N  
ATOM    271  N   ARG A  62       2.722  10.081  66.391  1.00 68.36           N  
ANISOU  271  N   ARG A  62    11921   6480   7572    243   -171   -706       N  
ATOM    272  CA  ARG A  62       2.811   8.676  66.777  1.00 69.17           C  
ANISOU  272  CA  ARG A  62    11710   6783   7787    222   -144   -691       C  
ATOM    273  C   ARG A  62       2.927   7.759  65.566  1.00 63.82           C  
ANISOU  273  C   ARG A  62    10626   6310   7313    158   -132   -643       C  
ATOM    274  O   ARG A  62       3.455   6.647  65.682  1.00 62.83           O  
ANISOU  274  O   ARG A  62    10255   6334   7285     55   -164   -627       O  
ATOM    275  CB  ARG A  62       1.599   8.278  67.619  1.00 78.65           C  
ANISOU  275  CB  ARG A  62    12922   8023   8937    494     16   -695       C  
ATOM    276  CG  ARG A  62       1.547   8.943  68.981  1.00 89.19           C  
ANISOU  276  CG  ARG A  62    14648   9177  10063    568     12   -744       C  
ATOM    277  CD  ARG A  62       0.368   8.438  69.791  1.00 94.86           C  
ANISOU  277  CD  ARG A  62    15331   9974  10739    845    181   -728       C  
ATOM    278  NE  ARG A  62       0.314   9.055  71.111  1.00101.36           N  
ANISOU  278  NE  ARG A  62    16544  10621  11347    936    187   -776       N  
ATOM    279  CZ  ARG A  62      -0.578   8.739  72.043  1.00106.27           C  
ANISOU  279  CZ  ARG A  62    17203  11288  11889   1174    325   -763       C  
ATOM    280  NH1 ARG A  62      -1.493   7.811  71.796  1.00105.68           N  
ANISOU  280  NH1 ARG A  62    16782  11434  11937   1326    458   -693       N  
ATOM    281  NH2 ARG A  62      -0.556   9.349  73.221  1.00109.95           N  
ANISOU  281  NH2 ARG A  62    18057  11577  12141   1255    324   -811       N  
ATOM    282  N   MET A  63       2.432   8.194  64.407  1.00 59.16           N  
ANISOU  282  N   MET A  63     9975   5724   6778    226    -85   -620       N  
ATOM    283  CA  MET A  63       2.445   7.376  63.200  1.00 56.49           C  
ANISOU  283  CA  MET A  63     9285   5564   6615    183    -68   -577       C  
ATOM    284  C   MET A  63       3.769   7.431  62.449  1.00 55.62           C  
ANISOU  284  C   MET A  63     9090   5478   6565    -69   -205   -557       C  
ATOM    285  O   MET A  63       3.909   6.737  61.434  1.00 52.71           O  
ANISOU  285  O   MET A  63     8448   5251   6328   -108   -197   -523       O  
ATOM    286  CB  MET A  63       1.312   7.800  62.260  1.00 56.67           C  
ANISOU  286  CB  MET A  63     9270   5595   6669    366     40   -549       C  
ATOM    287  CG  MET A  63      -0.071   7.692  62.877  1.00 58.46           C  
ANISOU  287  CG  MET A  63     9523   5845   6844    633    190   -532       C  
ATOM    288  SD  MET A  63      -0.526   5.985  63.235  1.00 60.56           S  
ANISOU  288  SD  MET A  63     9450   6336   7224    670    251   -496       S  
ATOM    289  CE  MET A  63      -0.815   5.355  61.585  1.00 53.16           C  
ANISOU  289  CE  MET A  63     8189   5552   6457    632    261   -439       C  
ATOM    290  N   ARG A  64       4.727   8.249  62.889  1.00 56.51           N  
ANISOU  290  N   ARG A  64     9435   5459   6575   -241   -334   -567       N  
ATOM    291  CA  ARG A  64       5.972   8.438  62.142  1.00 59.74           C  
ANISOU  291  CA  ARG A  64     9765   5905   7030   -484   -466   -520       C  
ATOM    292  C   ARG A  64       6.968   7.357  62.547  1.00 59.34           C  
ANISOU  292  C   ARG A  64     9500   6007   7040   -631   -532   -487       C  
ATOM    293  O   ARG A  64       7.893   7.569  63.333  1.00 63.28           O  
ANISOU  293  O   ARG A  64    10118   6464   7461   -802   -652   -471       O  
ATOM    294  CB  ARG A  64       6.529   9.837  62.365  1.00 63.39           C  
ANISOU  294  CB  ARG A  64    10572   6163   7350   -623   -589   -522       C  
ATOM    295  CG  ARG A  64       5.607  10.941  61.879  1.00 64.51           C  
ANISOU  295  CG  ARG A  64    10940   6145   7426   -470   -524   -548       C  
ATOM    296  CD  ARG A  64       6.309  12.284  61.868  1.00 68.40           C  
ANISOU  296  CD  ARG A  64    11762   6437   7789   -649   -669   -537       C  
ATOM    297  NE  ARG A  64       5.345  13.375  61.794  1.00 72.74           N  
ANISOU  297  NE  ARG A  64    12620   6788   8228   -461   -599   -577       N  
ATOM    298  CZ  ARG A  64       5.144  14.260  62.763  1.00 73.15           C  
ANISOU  298  CZ  ARG A  64    13093   6610   8089   -411   -626   -625       C  
ATOM    299  NH1 ARG A  64       5.861  14.200  63.876  1.00 76.69           N  
ANISOU  299  NH1 ARG A  64    13704   6996   8438   -561   -736   -640       N  
ATOM    300  NH2 ARG A  64       4.236  15.214  62.612  1.00 71.38           N  
ANISOU  300  NH2 ARG A  64    13141   6215   7764   -206   -543   -653       N  
ATOM    301  N   THR A  65       6.763   6.172  61.986  1.00 51.38           N  
ANISOU  301  N   THR A  65     8179   5177   6166   -562   -457   -469       N  
ATOM    302  CA  THR A  65       7.627   5.023  62.190  1.00 48.58           C  
ANISOU  302  CA  THR A  65     7596   4983   5880   -660   -496   -431       C  
ATOM    303  C   THR A  65       8.316   4.656  60.881  1.00 47.98           C  
ANISOU  303  C   THR A  65     7279   5042   5908   -742   -518   -367       C  
ATOM    304  O   THR A  65       8.009   5.189  59.811  1.00 48.87           O  
ANISOU  304  O   THR A  65     7384   5133   6052   -715   -494   -358       O  
ATOM    305  CB  THR A  65       6.829   3.823  62.716  1.00 46.16           C  
ANISOU  305  CB  THR A  65     7152   4762   5625   -500   -389   -462       C  
ATOM    306  OG1 THR A  65       5.850   3.439  61.741  1.00 46.26           O  
ANISOU  306  OG1 THR A  65     7019   4832   5726   -353   -284   -465       O  
ATOM    307  CG2 THR A  65       6.128   4.174  64.019  1.00 43.65           C  
ANISOU  307  CG2 THR A  65     7063   4325   5195   -399   -354   -515       C  
ATOM    308  N   VAL A  66       9.269   3.731  60.989  1.00 44.97           N  
ANISOU  308  N   VAL A  66     6705   4807   5574   -833   -559   -315       N  
ATOM    309  CA  VAL A  66       9.966   3.216  59.814  1.00 48.47           C  
ANISOU  309  CA  VAL A  66     6912   5400   6105   -879   -563   -244       C  
ATOM    310  C   VAL A  66       8.971   2.615  58.827  1.00 48.37           C  
ANISOU  310  C   VAL A  66     6770   5427   6180   -708   -445   -278       C  
ATOM    311  O   VAL A  66       8.944   2.961  57.630  1.00 48.52           O  
ANISOU  311  O   VAL A  66     6734   5462   6237   -707   -433   -254       O  
ATOM    312  CB  VAL A  66      11.010   2.178  60.263  1.00 50.65           C  
ANISOU  312  CB  VAL A  66     7012   5830   6404   -950   -601   -182       C  
ATOM    313  CG1 VAL A  66      11.506   1.347  59.085  1.00 52.71           C  
ANISOU  313  CG1 VAL A  66     7021   6254   6751   -918   -561   -119       C  
ATOM    314  CG2 VAL A  66      12.149   2.867  61.012  1.00 51.31           C  
ANISOU  314  CG2 VAL A  66     7194   5901   6401  -1161   -742   -113       C  
ATOM    315  N   THR A  67       8.112   1.730  59.333  1.00 39.63           N  
ANISOU  315  N   THR A  67     5622   4335   5100   -572   -365   -327       N  
ATOM    316  CA  THR A  67       7.154   1.043  58.479  1.00 48.71           C  
ANISOU  316  CA  THR A  67     6650   5531   6325   -434   -272   -345       C  
ATOM    317  C   THR A  67       6.206   2.029  57.815  1.00 46.41           C  
ANISOU  317  C   THR A  67     6462   5147   6026   -365   -233   -365       C  
ATOM    318  O   THR A  67       5.948   1.944  56.606  1.00 46.35           O  
ANISOU  318  O   THR A  67     6357   5178   6074   -333   -203   -348       O  
ATOM    319  CB  THR A  67       6.378   0.023  59.313  1.00 47.61           C  
ANISOU  319  CB  THR A  67     6473   5417   6200   -327   -212   -378       C  
ATOM    320  OG1 THR A  67       7.193  -1.138  59.520  1.00 52.58           O  
ANISOU  320  OG1 THR A  67     6963   6155   6861   -365   -232   -351       O  
ATOM    321  CG2 THR A  67       5.073  -0.375  58.624  1.00 44.22           C  
ANISOU  321  CG2 THR A  67     5979   5001   5822   -194   -127   -389       C  
ATOM    322  N   ASN A  68       5.701   2.994  58.586  1.00 43.66           N  
ANISOU  322  N   ASN A  68     6323   4669   5597   -333   -231   -398       N  
ATOM    323  CA  ASN A  68       4.790   3.971  58.011  1.00 43.55           C  
ANISOU  323  CA  ASN A  68     6422   4563   5563   -245   -186   -410       C  
ATOM    324  C   ASN A  68       5.494   4.906  57.036  1.00 46.82           C  
ANISOU  324  C   ASN A  68     6877   4940   5973   -359   -252   -379       C  
ATOM    325  O   ASN A  68       4.848   5.412  56.117  1.00 45.47           O  
ANISOU  325  O   ASN A  68     6713   4741   5823   -291   -211   -374       O  
ATOM    326  CB  ASN A  68       4.093   4.759  59.113  1.00 44.91           C  
ANISOU  326  CB  ASN A  68     6835   4601   5630   -153   -156   -448       C  
ATOM    327  CG  ASN A  68       3.091   3.915  59.888  1.00 45.78           C  
ANISOU  327  CG  ASN A  68     6885   4763   5748     -2    -65   -461       C  
ATOM    328  OD1 ASN A  68       2.680   2.848  59.433  1.00 45.52           O  
ANISOU  328  OD1 ASN A  68     6642   4852   5802     42    -21   -439       O  
ATOM    329  ND2 ASN A  68       2.692   4.395  61.058  1.00 44.00           N  
ANISOU  329  ND2 ASN A  68     6857   4441   5418     75    -40   -489       N  
ATOM    330  N   TYR A  69       6.800   5.149  57.194  1.00 41.01           N  
ANISOU  330  N   TYR A  69     6159   4214   5210   -536   -356   -345       N  
ATOM    331  CA  TYR A  69       7.483   5.952  56.180  1.00 50.03           C  
ANISOU  331  CA  TYR A  69     7307   5348   6354   -655   -421   -295       C  
ATOM    332  C   TYR A  69       7.538   5.213  54.852  1.00 46.91           C  
ANISOU  332  C   TYR A  69     6672   5092   6061   -621   -375   -260       C  
ATOM    333  O   TYR A  69       7.280   5.804  53.790  1.00 46.01           O  
ANISOU  333  O   TYR A  69     6560   4956   5966   -608   -363   -244       O  
ATOM    334  CB  TYR A  69       8.894   6.332  56.626  1.00 49.73           C  
ANISOU  334  CB  TYR A  69     7313   5320   6262   -870   -552   -236       C  
ATOM    335  CG  TYR A  69       8.956   7.554  57.515  1.00 59.26           C  
ANISOU  335  CG  TYR A  69     8832   6341   7343   -954   -635   -257       C  
ATOM    336  CD1 TYR A  69       7.799   8.120  58.036  1.00 63.37           C  
ANISOU  336  CD1 TYR A  69     9576   6703   7800   -802   -570   -334       C  
ATOM    337  CD2 TYR A  69      10.171   8.144  57.832  1.00 64.43           C  
ANISOU  337  CD2 TYR A  69     9570   6981   7931  -1185   -781   -188       C  
ATOM    338  CE1 TYR A  69       7.853   9.237  58.855  1.00 65.42           C  
ANISOU  338  CE1 TYR A  69    10164   6770   7922   -861   -642   -359       C  
ATOM    339  CE2 TYR A  69      10.234   9.262  58.650  1.00 68.48           C  
ANISOU  339  CE2 TYR A  69    10409   7300   8310  -1278   -874   -208       C  
ATOM    340  CZ  TYR A  69       9.073   9.805  59.156  1.00 67.57           C  
ANISOU  340  CZ  TYR A  69    10544   7006   8124  -1108   -801   -302       C  
ATOM    341  OH  TYR A  69       9.131  10.919  59.963  1.00 69.80           O  
ANISOU  341  OH  TYR A  69    11193   7075   8252  -1182   -889   -327       O  
ATOM    342  N   PHE A  70       7.838   3.908  54.887  1.00 41.04           N  
ANISOU  342  N   PHE A  70     5737   4483   5373   -596   -348   -248       N  
ATOM    343  CA  PHE A  70       7.804   3.175  53.625  1.00 43.47           C  
ANISOU  343  CA  PHE A  70     5859   4901   5756   -544   -300   -223       C  
ATOM    344  C   PHE A  70       6.388   3.130  53.051  1.00 43.82           C  
ANISOU  344  C   PHE A  70     5911   4903   5835   -400   -218   -264       C  
ATOM    345  O   PHE A  70       6.201   3.232  51.828  1.00 43.97           O  
ANISOU  345  O   PHE A  70     5866   4950   5890   -380   -198   -244       O  
ATOM    346  CB  PHE A  70       8.370   1.771  53.812  1.00 42.59           C  
ANISOU  346  CB  PHE A  70     5583   4921   5681   -528   -286   -203       C  
ATOM    347  CG  PHE A  70       9.862   1.741  53.992  1.00 44.18           C  
ANISOU  347  CG  PHE A  70     5713   5215   5858   -659   -358   -124       C  
ATOM    348  CD1 PHE A  70      10.703   2.129  52.961  1.00 41.85           C  
ANISOU  348  CD1 PHE A  70     5337   4995   5568   -733   -389    -44       C  
ATOM    349  CD2 PHE A  70      10.427   1.315  55.188  1.00 45.46           C  
ANISOU  349  CD2 PHE A  70     5876   5406   5990   -709   -397   -114       C  
ATOM    350  CE1 PHE A  70      12.080   2.104  53.119  1.00 43.86           C  
ANISOU  350  CE1 PHE A  70     5500   5366   5797   -854   -455     59       C  
ATOM    351  CE2 PHE A  70      11.800   1.282  55.350  1.00 43.90           C  
ANISOU  351  CE2 PHE A  70     5593   5318   5769   -833   -467    -17       C  
ATOM    352  CZ  PHE A  70      12.629   1.679  54.317  1.00 43.54           C  
ANISOU  352  CZ  PHE A  70     5453   5361   5728   -906   -496     77       C  
ATOM    353  N   LEU A  71       5.376   3.025  53.920  1.00 40.91           N  
ANISOU  353  N   LEU A  71     5618   4476   5448   -302   -172   -309       N  
ATOM    354  CA  LEU A  71       3.997   3.014  53.437  1.00 39.47           C  
ANISOU  354  CA  LEU A  71     5427   4278   5293   -170    -97   -321       C  
ATOM    355  C   LEU A  71       3.606   4.361  52.832  1.00 41.85           C  
ANISOU  355  C   LEU A  71     5850   4485   5565   -153    -94   -313       C  
ATOM    356  O   LEU A  71       2.842   4.414  51.860  1.00 41.57           O  
ANISOU  356  O   LEU A  71     5758   4469   5566    -85    -53   -295       O  
ATOM    357  CB  LEU A  71       3.044   2.640  54.572  1.00 43.76           C  
ANISOU  357  CB  LEU A  71     6011   4803   5813    -64    -45   -346       C  
ATOM    358  CG  LEU A  71       3.209   1.241  55.171  1.00 42.87           C  
ANISOU  358  CG  LEU A  71     5779   4778   5729    -66    -41   -351       C  
ATOM    359  CD1 LEU A  71       2.136   0.969  56.210  1.00 42.78           C  
ANISOU  359  CD1 LEU A  71     5803   4756   5693     43     16   -360       C  
ATOM    360  CD2 LEU A  71       3.174   0.183  54.071  1.00 41.58           C  
ANISOU  360  CD2 LEU A  71     5452   4711   5636    -64    -33   -328       C  
ATOM    361  N   VAL A  72       4.127   5.459  53.382  1.00 39.34           N  
ANISOU  361  N   VAL A  72     5715   4058   5174   -222   -147   -322       N  
ATOM    362  CA  VAL A  72       3.857   6.772  52.810  1.00 44.27           C  
ANISOU  362  CA  VAL A  72     6485   4574   5760   -215   -154   -313       C  
ATOM    363  C   VAL A  72       4.501   6.886  51.439  1.00 43.43           C  
ANISOU  363  C   VAL A  72     6268   4529   5704   -306   -191   -270       C  
ATOM    364  O   VAL A  72       3.906   7.432  50.499  1.00 41.19           O  
ANISOU  364  O   VAL A  72     5994   4221   5437   -252   -161   -255       O  
ATOM    365  CB  VAL A  72       4.346   7.885  53.760  1.00 51.24           C  
ANISOU  365  CB  VAL A  72     7629   5306   6535   -288   -221   -332       C  
ATOM    366  CG1 VAL A  72       4.180   9.250  53.118  1.00 54.52           C  
ANISOU  366  CG1 VAL A  72     8150   5645   6920   -407   -295   -299       C  
ATOM    367  CG2 VAL A  72       3.571   7.850  55.053  1.00 50.96           C  
ANISOU  367  CG2 VAL A  72     7782   5155   6424   -119   -149   -368       C  
ATOM    368  N   ASN A  73       5.710   6.341  51.292  1.00 41.77           N  
ANISOU  368  N   ASN A  73     5941   4414   5517   -434   -249   -238       N  
ATOM    369  CA  ASN A  73       6.364   6.382  49.990  1.00 42.65           C  
ANISOU  369  CA  ASN A  73     5934   4604   5668   -505   -272   -184       C  
ATOM    370  C   ASN A  73       5.572   5.590  48.952  1.00 43.67           C  
ANISOU  370  C   ASN A  73     5917   4811   5866   -390   -197   -189       C  
ATOM    371  O   ASN A  73       5.390   6.041  47.808  1.00 40.08           O  
ANISOU  371  O   ASN A  73     5442   4358   5429   -385   -189   -164       O  
ATOM    372  CB  ASN A  73       7.787   5.838  50.103  1.00 42.06           C  
ANISOU  372  CB  ASN A  73     5741   4644   5595   -633   -333   -130       C  
ATOM    373  CG  ASN A  73       8.583   6.050  48.838  1.00 46.50           C  
ANISOU  373  CG  ASN A  73     6196   5294   6178   -708   -358    -54       C  
ATOM    374  OD1 ASN A  73       8.640   7.159  48.320  1.00 44.46           O  
ANISOU  374  OD1 ASN A  73     6031   4967   5896   -773   -397    -27       O  
ATOM    375  ND2 ASN A  73       9.183   4.985  48.321  1.00 39.18           N  
ANISOU  375  ND2 ASN A  73     5083   4516   5287   -688   -332    -15       N  
ATOM    376  N   ALA A  74       5.079   4.412  49.342  1.00 37.69           N  
ANISOU  376  N   ALA A  74     5070   4113   5139   -309   -151   -216       N  
ATOM    377  CA  ALA A  74       4.270   3.619  48.423  1.00 36.95           C  
ANISOU  377  CA  ALA A  74     4864   4079   5095   -221    -98   -214       C  
ATOM    378  C   ALA A  74       2.964   4.327  48.083  1.00 39.30           C  
ANISOU  378  C   ALA A  74     5226   4312   5393   -130    -57   -216       C  
ATOM    379  O   ALA A  74       2.506   4.281  46.933  1.00 38.49           O  
ANISOU  379  O   ALA A  74     5063   4241   5321   -102    -40   -192       O  
ATOM    380  CB  ALA A  74       3.995   2.240  49.019  1.00 36.34           C  
ANISOU  380  CB  ALA A  74     4705   4063   5038   -171    -73   -235       C  
ATOM    381  N   ALA A  75       2.357   5.001  49.066  1.00 37.69           N  
ANISOU  381  N   ALA A  75     5152   4021   5148    -74    -37   -235       N  
ATOM    382  CA  ALA A  75       1.129   5.743  48.802  1.00 45.15           C  
ANISOU  382  CA  ALA A  75     6160   4914   6080     39     15   -218       C  
ATOM    383  C   ALA A  75       1.380   6.897  47.840  1.00 42.92           C  
ANISOU  383  C   ALA A  75     5952   4569   5785      1     -9   -198       C  
ATOM    384  O   ALA A  75       0.541   7.194  46.983  1.00 40.17           O  
ANISOU  384  O   ALA A  75     5576   4230   5456     72     26   -166       O  
ATOM    385  CB  ALA A  75       0.534   6.263  50.113  1.00 38.85           C  
ANISOU  385  CB  ALA A  75     5511   4032   5219    131     51   -238       C  
ATOM    386  N   PHE A  76       2.542   7.542  47.957  1.00 42.33           N  
ANISOU  386  N   PHE A  76     5966   4440   5676   -123    -77   -203       N  
ATOM    387  CA  PHE A  76       2.860   8.651  47.069  1.00 46.45           C  
ANISOU  387  CA  PHE A  76     6566   4903   6182   -180   -112   -174       C  
ATOM    388  C   PHE A  76       3.048   8.159  45.643  1.00 43.00           C  
ANISOU  388  C   PHE A  76     5957   4573   5806   -209   -110   -138       C  
ATOM    389  O   PHE A  76       2.504   8.747  44.695  1.00 40.91           O  
ANISOU  389  O   PHE A  76     5705   4289   5552   -169    -92   -113       O  
ATOM    390  CB  PHE A  76       4.114   9.375  47.565  1.00 51.21           C  
ANISOU  390  CB  PHE A  76     7292   5436   6727   -338   -204   -167       C  
ATOM    391  CG  PHE A  76       4.734  10.277  46.539  1.00 55.88           C  
ANISOU  391  CG  PHE A  76     7915   6004   7311   -444   -260   -118       C  
ATOM    392  CD1 PHE A  76       4.230  11.551  46.325  1.00 58.76           C  
ANISOU  392  CD1 PHE A  76     8471   6229   7626   -413   -264   -115       C  
ATOM    393  CD2 PHE A  76       5.819   9.853  45.785  1.00 56.52           C  
ANISOU  393  CD2 PHE A  76     7839   6209   7428   -564   -302    -66       C  
ATOM    394  CE1 PHE A  76       4.793  12.386  45.372  1.00 61.48           C  
ANISOU  394  CE1 PHE A  76     8847   6549   7962   -520   -321    -64       C  
ATOM    395  CE2 PHE A  76       6.386  10.683  44.830  1.00 59.57           C  
ANISOU  395  CE2 PHE A  76     8241   6588   7804   -664   -352     -7       C  
ATOM    396  CZ  PHE A  76       5.873  11.951  44.623  1.00 60.94           C  
ANISOU  396  CZ  PHE A  76     8605   6614   7934   -652   -367     -7       C  
ATOM    397  N   ALA A  77       3.773   7.047  45.486  1.00 40.96           N  
ANISOU  397  N   ALA A  77     5551   4430   5583   -261   -123   -134       N  
ATOM    398  CA  ALA A  77       3.980   6.478  44.157  1.00 43.55           C  
ANISOU  398  CA  ALA A  77     5740   4855   5951   -270   -115   -103       C  
ATOM    399  C   ALA A  77       2.665   6.038  43.526  1.00 45.47           C  
ANISOU  399  C   ALA A  77     5930   5118   6226   -160    -62   -105       C  
ATOM    400  O   ALA A  77       2.420   6.286  42.335  1.00 37.29           O  
ANISOU  400  O   ALA A  77     4862   4102   5205   -154    -58    -76       O  
ATOM    401  CB  ALA A  77       4.944   5.297  44.246  1.00 37.34           C  
ANISOU  401  CB  ALA A  77     4833   4179   5177   -311   -125    -97       C  
ATOM    402  N   GLU A  78       1.788   5.407  44.311  1.00 37.05           N  
ANISOU  402  N   GLU A  78     4853   4057   5168    -82    -29   -127       N  
ATOM    403  CA  GLU A  78       0.555   4.886  43.731  1.00 36.76           C  
ANISOU  403  CA  GLU A  78     4746   4063   5159     -3      5   -104       C  
ATOM    404  C   GLU A  78      -0.419   6.009  43.397  1.00 39.90           C  
ANISOU  404  C   GLU A  78     5208   4407   5547     70     34    -70       C  
ATOM    405  O   GLU A  78      -1.059   5.990  42.334  1.00 37.72           O  
ANISOU  405  O   GLU A  78     4873   4169   5291     92     40    -29       O  
ATOM    406  CB  GLU A  78      -0.076   3.866  44.680  1.00 43.48           C  
ANISOU  406  CB  GLU A  78     5553   4951   6018     46     26   -116       C  
ATOM    407  CG  GLU A  78       0.732   2.580  44.784  1.00 49.24           C  
ANISOU  407  CG  GLU A  78     6213   5739   6756     -9      1   -141       C  
ATOM    408  CD  GLU A  78       0.365   1.736  45.993  1.00 60.25           C  
ANISOU  408  CD  GLU A  78     7592   7149   8149     21     13   -158       C  
ATOM    409  OE1 GLU A  78      -0.639   2.047  46.672  1.00 63.86           O  
ANISOU  409  OE1 GLU A  78     8072   7591   8600     90     46   -141       O  
ATOM    410  OE2 GLU A  78       1.094   0.760  46.271  1.00 63.60           O  
ANISOU  410  OE2 GLU A  78     7982   7608   8574    -14     -5   -181       O  
ATOM    411  N   ALA A  79      -0.530   7.011  44.276  1.00 38.05           N  
ANISOU  411  N   ALA A  79     5109   4079   5271    112     50    -82       N  
ATOM    412  CA  ALA A  79      -1.385   8.150  43.971  1.00 45.95           C  
ANISOU  412  CA  ALA A  79     6196   5016   6247    203     85    -45       C  
ATOM    413  C   ALA A  79      -0.879   8.904  42.752  1.00 42.66           C  
ANISOU  413  C   ALA A  79     5801   4572   5836    136     51    -26       C  
ATOM    414  O   ALA A  79      -1.677   9.375  41.936  1.00 39.25           O  
ANISOU  414  O   ALA A  79     5357   4146   5411    200     76     20       O  
ATOM    415  CB  ALA A  79      -1.467   9.089  45.175  1.00 39.74           C  
ANISOU  415  CB  ALA A  79     5601   4109   5392    269    107    -69       C  
ATOM    416  N   SER A  80       0.447   8.997  42.589  1.00 42.18           N  
ANISOU  416  N   SER A  80     5757   4499   5770      5     -7    -48       N  
ATOM    417  CA  SER A  80       0.988   9.710  41.437  1.00 42.41           C  
ANISOU  417  CA  SER A  80     5798   4516   5801    -68    -41    -17       C  
ATOM    418  C   SER A  80       0.704   8.966  40.141  1.00 41.65           C  
ANISOU  418  C   SER A  80     5548   4526   5749    -62    -31     12       C  
ATOM    419  O   SER A  80       0.285   9.580  39.150  1.00 39.64           O  
ANISOU  419  O   SER A  80     5300   4263   5500    -42    -26     49       O  
ATOM    420  CB  SER A  80       2.491   9.925  41.611  1.00 41.24           C  
ANISOU  420  CB  SER A  80     5679   4359   5631   -216   -108    -20       C  
ATOM    421  OG  SER A  80       2.743  10.803  42.694  1.00 43.52           O  
ANISOU  421  OG  SER A  80     6149   4525   5861   -245   -139    -39       O  
ATOM    422  N   MET A  81       0.906   7.644  40.129  1.00 42.50           N  
ANISOU  422  N   MET A  81     5539   4728   5882    -77    -31     -4       N  
ATOM    423  CA  MET A  81       0.616   6.898  38.910  1.00 45.43           C  
ANISOU  423  CA  MET A  81     5806   5181   6276    -72    -29     19       C  
ATOM    424  C   MET A  81      -0.862   6.980  38.564  1.00 45.00           C  
ANISOU  424  C   MET A  81     5730   5133   6234     12     -3     57       C  
ATOM    425  O   MET A  81      -1.221   7.174  37.395  1.00 41.28           O  
ANISOU  425  O   MET A  81     5229   4686   5769     12     -9     95       O  
ATOM    426  CB  MET A  81       1.049   5.438  39.045  1.00 46.32           C  
ANISOU  426  CB  MET A  81     5837   5368   6394    -91    -35     -7       C  
ATOM    427  CG  MET A  81       1.081   4.720  37.703  1.00 52.60           C  
ANISOU  427  CG  MET A  81     6572   6227   7185   -100    -44     12       C  
ATOM    428  SD  MET A  81       1.556   2.984  37.775  1.00 57.06           S  
ANISOU  428  SD  MET A  81     7093   6855   7733    -99    -50    -18       S  
ATOM    429  CE  MET A  81      -0.001   2.228  38.223  1.00 60.01           C  
ANISOU  429  CE  MET A  81     7452   7225   8123    -63    -57    -13       C  
ATOM    430  N   ALA A  82      -1.735   6.912  39.572  1.00 42.54           N  
ANISOU  430  N   ALA A  82     5432   4809   5923     88     28     60       N  
ATOM    431  CA  ALA A  82      -3.160   7.005  39.280  1.00 43.52           C  
ANISOU  431  CA  ALA A  82     5512   4970   6055    174     56    126       C  
ATOM    432  C   ALA A  82      -3.529   8.389  38.755  1.00 44.33           C  
ANISOU  432  C   ALA A  82     5687   5013   6143    229     77    167       C  
ATOM    433  O   ALA A  82      -4.280   8.508  37.781  1.00 42.49           O  
ANISOU  433  O   ALA A  82     5396   4826   5920    253     77    230       O  
ATOM    434  CB  ALA A  82      -3.976   6.670  40.528  1.00 41.07           C  
ANISOU  434  CB  ALA A  82     5190   4677   5739    258     94    140       C  
ATOM    435  N   ALA A  83      -3.005   9.446  39.383  1.00 44.01           N  
ANISOU  435  N   ALA A  83     5789   4864   6069    244     87    135       N  
ATOM    436  CA  ALA A  83      -3.357  10.803  38.985  1.00 45.51           C  
ANISOU  436  CA  ALA A  83     6088   4974   6231    306    106    172       C  
ATOM    437  C   ALA A  83      -2.795  11.177  37.619  1.00 46.32           C  
ANISOU  437  C   ALA A  83     6172   5079   6347    217     65    187       C  
ATOM    438  O   ALA A  83      -3.405  11.984  36.907  1.00 40.50           O  
ANISOU  438  O   ALA A  83     5464   4321   5603    275     81    240       O  
ATOM    439  CB  ALA A  83      -2.873  11.802  40.037  1.00 40.79           C  
ANISOU  439  CB  ALA A  83     5689   4234   5575    326    111    130       C  
ATOM    440  N   PHE A  84      -1.641  10.628  37.233  1.00 43.88           N  
ANISOU  440  N   PHE A  84     5816   4804   6052     91     17    152       N  
ATOM    441  CA  PHE A  84      -0.943  11.127  36.057  1.00 43.26           C  
ANISOU  441  CA  PHE A  84     5738   4726   5973      9    -17    173       C  
ATOM    442  C   PHE A  84      -0.845  10.142  34.899  1.00 46.44           C  
ANISOU  442  C   PHE A  84     6006   5239   6400    -32    -31    188       C  
ATOM    443  O   PHE A  84      -0.329  10.526  33.841  1.00 46.02           O  
ANISOU  443  O   PHE A  84     5946   5199   6341    -86    -52    213       O  
ATOM    444  CB  PHE A  84       0.465  11.602  36.450  1.00 43.17           C  
ANISOU  444  CB  PHE A  84     5804   4662   5937   -105    -62    148       C  
ATOM    445  CG  PHE A  84       0.458  12.684  37.494  1.00 49.58           C  
ANISOU  445  CG  PHE A  84     6799   5335   6703    -88    -67    133       C  
ATOM    446  CD1 PHE A  84      -0.333  13.809  37.330  1.00 53.04           C  
ANISOU  446  CD1 PHE A  84     7364   5675   7113     -2    -45    161       C  
ATOM    447  CD2 PHE A  84       1.206  12.558  38.656  1.00 51.61           C  
ANISOU  447  CD2 PHE A  84     7119   5555   6936   -147    -95     93       C  
ATOM    448  CE1 PHE A  84      -0.358  14.800  38.288  1.00 57.72           C  
ANISOU  448  CE1 PHE A  84     8168   6119   7643     31    -49    143       C  
ATOM    449  CE2 PHE A  84       1.185  13.544  39.623  1.00 53.34           C  
ANISOU  449  CE2 PHE A  84     7543   5629   7095   -134   -108     75       C  
ATOM    450  CZ  PHE A  84       0.400  14.665  39.441  1.00 59.12           C  
ANISOU  450  CZ  PHE A  84     8426   6248   7789    -40    -84     97       C  
ATOM    451  N   ASN A  85      -1.342   8.906  35.035  1.00 43.38           N  
ANISOU  451  N   ASN A  85     5529   4925   6028     -9    -25    178       N  
ATOM    452  CA  ASN A  85      -1.206   7.969  33.926  1.00 42.84           C  
ANISOU  452  CA  ASN A  85     5381   4937   5959    -48    -46    186       C  
ATOM    453  C   ASN A  85      -2.533   7.367  33.477  1.00 46.15           C  
ANISOU  453  C   ASN A  85     5740   5408   6387     -9    -52    231       C  
ATOM    454  O   ASN A  85      -2.691   7.046  32.290  1.00 47.92           O  
ANISOU  454  O   ASN A  85     5935   5673   6599    -38    -78    258       O  
ATOM    455  CB  ASN A  85      -0.241   6.839  34.305  1.00 43.38           C  
ANISOU  455  CB  ASN A  85     5419   5045   6018    -90    -56    137       C  
ATOM    456  CG  ASN A  85       1.193   7.311  34.419  1.00 49.28           C  
ANISOU  456  CG  ASN A  85     6189   5784   6750   -151    -62    126       C  
ATOM    457  OD1 ASN A  85       1.707   7.510  35.519  1.00 54.87           O  
ANISOU  457  OD1 ASN A  85     6931   6460   7458   -171    -63    102       O  
ATOM    458  ND2 ASN A  85       1.847   7.496  33.279  1.00 47.53           N  
ANISOU  458  ND2 ASN A  85     5948   5601   6509   -187    -70    156       N  
ATOM    459  N   THR A  86      -3.478   7.209  34.415  1.00 42.65           N  
ANISOU  459  N   THR A  86     5277   4970   5957     51    -32    250       N  
ATOM    460  CA  THR A  86      -4.648   6.366  34.174  1.00 45.31           C  
ANISOU  460  CA  THR A  86     5534   5383   6298     59    -53    308       C  
ATOM    461  C   THR A  86      -5.511   6.899  33.041  1.00 43.76           C  
ANISOU  461  C   THR A  86     5305   5222   6101     72    -67    393       C  
ATOM    462  O   THR A  86      -5.963   6.132  32.179  1.00 45.45           O  
ANISOU  462  O   THR A  86     5473   5493   6302     16   -117    432       O  
ATOM    463  CB  THR A  86      -5.500   6.260  35.445  1.00 45.59           C  
ANISOU  463  CB  THR A  86     5541   5436   6344    131    -20    337       C  
ATOM    464  OG1 THR A  86      -4.683   5.886  36.555  1.00 45.38           O  
ANISOU  464  OG1 THR A  86     5555   5371   6317    122     -7    257       O  
ATOM    465  CG2 THR A  86      -6.600   5.221  35.264  1.00 45.87           C  
ANISOU  465  CG2 THR A  86     5480   5569   6382    107    -59    413       C  
ATOM    466  N   VAL A  87      -5.748   8.213  33.023  1.00 43.89           N  
ANISOU  466  N   VAL A  87     5360   5196   6121    143    -27    426       N  
ATOM    467  CA  VAL A  87      -6.684   8.780  32.056  1.00 44.84           C  
ANISOU  467  CA  VAL A  87     5440   5357   6241    174    -32    522       C  
ATOM    468  C   VAL A  87      -6.158   8.588  30.638  1.00 41.78           C  
ANISOU  468  C   VAL A  87     5056   4980   5840     83    -82    512       C  
ATOM    469  O   VAL A  87      -6.874   8.106  29.751  1.00 43.40           O  
ANISOU  469  O   VAL A  87     5201   5254   6035     45   -127    578       O  
ATOM    470  CB  VAL A  87      -6.947  10.265  32.368  1.00 48.03           C  
ANISOU  470  CB  VAL A  87     5916   5693   6639    287     26    553       C  
ATOM    471  CG1 VAL A  87      -7.697  10.932  31.215  1.00 48.29           C  
ANISOU  471  CG1 VAL A  87     5916   5762   6669    317     21    649       C  
ATOM    472  CG2 VAL A  87      -7.727  10.408  33.676  1.00 47.24           C  
ANISOU  472  CG2 VAL A  87     5814   5599   6533    410     86    587       C  
ATOM    473  N   VAL A  88      -4.893   8.944  30.408  1.00 40.91           N  
ANISOU  473  N   VAL A  88     5014   4808   5721     42    -79    441       N  
ATOM    474  CA  VAL A  88      -4.348   8.816  29.061  1.00 44.79           C  
ANISOU  474  CA  VAL A  88     5512   5318   6190    -25   -112    440       C  
ATOM    475  C   VAL A  88      -4.138   7.355  28.685  1.00 43.79           C  
ANISOU  475  C   VAL A  88     5365   5238   6034    -86   -154    410       C  
ATOM    476  O   VAL A  88      -4.311   6.989  27.519  1.00 40.79           O  
ANISOU  476  O   VAL A  88     4987   4890   5622   -127   -193    437       O  
ATOM    477  CB  VAL A  88      -3.057   9.639  28.928  1.00 51.17           C  
ANISOU  477  CB  VAL A  88     6384   6069   6991    -53    -96    399       C  
ATOM    478  CG1 VAL A  88      -2.471   9.501  27.525  1.00 50.59           C  
ANISOU  478  CG1 VAL A  88     6306   6030   6886   -107   -119    410       C  
ATOM    479  CG2 VAL A  88      -3.362  11.090  29.213  1.00 55.59           C  
ANISOU  479  CG2 VAL A  88     7003   6557   7563      1    -69    433       C  
ATOM    480  N   ASN A  89      -3.809   6.483  29.647  1.00 44.40           N  
ANISOU  480  N   ASN A  89     5443   5313   6113    -91   -150    356       N  
ATOM    481  CA  ASN A  89      -3.706   5.068  29.308  1.00 45.99           C  
ANISOU  481  CA  ASN A  89     5657   5543   6275   -139   -193    331       C  
ATOM    482  C   ASN A  89      -5.040   4.554  28.799  1.00 42.49           C  
ANISOU  482  C   ASN A  89     5181   5146   5818   -173   -252    408       C  
ATOM    483  O   ASN A  89      -5.102   3.866  27.770  1.00 44.66           O  
ANISOU  483  O   ASN A  89     5500   5431   6040   -228   -307    417       O  
ATOM    484  CB  ASN A  89      -3.256   4.248  30.522  1.00 53.07           C  
ANISOU  484  CB  ASN A  89     6559   6428   7177   -132   -180    271       C  
ATOM    485  CG  ASN A  89      -1.804   4.483  30.890  1.00 59.10           C  
ANISOU  485  CG  ASN A  89     7350   7168   7938   -122   -139    208       C  
ATOM    486  OD1 ASN A  89      -1.051   5.110  30.145  1.00 60.90           O  
ANISOU  486  OD1 ASN A  89     7592   7396   8151   -130   -125    213       O  
ATOM    487  ND2 ASN A  89      -1.401   3.967  32.045  1.00 63.68           N  
ANISOU  487  ND2 ASN A  89     7928   7738   8528   -112   -124    163       N  
ATOM    488  N   PHE A  90      -6.130   4.976  29.441  1.00 39.01           N  
ANISOU  488  N   PHE A  90     4669   4737   5416   -138   -244    479       N  
ATOM    489  CA  PHE A  90      -7.453   4.574  28.980  1.00 42.60           C  
ANISOU  489  CA  PHE A  90     5063   5264   5859   -180   -306    586       C  
ATOM    490  C   PHE A  90      -7.759   5.139  27.596  1.00 43.92           C  
ANISOU  490  C   PHE A  90     5233   5450   6006   -205   -337    646       C  
ATOM    491  O   PHE A  90      -8.144   4.399  26.676  1.00 42.45           O  
ANISOU  491  O   PHE A  90     5068   5291   5770   -293   -418    684       O  
ATOM    492  CB  PHE A  90      -8.511   5.026  29.983  1.00 42.70           C  
ANISOU  492  CB  PHE A  90     4979   5332   5913   -109   -271    673       C  
ATOM    493  CG  PHE A  90      -9.902   4.892  29.472  1.00 43.50           C  
ANISOU  493  CG  PHE A  90     4984   5538   6006   -143   -327    823       C  
ATOM    494  CD1 PHE A  90     -10.479   3.643  29.336  1.00 47.88           C  
ANISOU  494  CD1 PHE A  90     5516   6148   6529   -258   -422    875       C  
ATOM    495  CD2 PHE A  90     -10.628   6.006  29.101  1.00 45.84           C  
ANISOU  495  CD2 PHE A  90     5217   5880   6319    -67   -294    924       C  
ATOM    496  CE1 PHE A  90     -11.761   3.507  28.846  1.00 50.76           C  
ANISOU  496  CE1 PHE A  90     5781   6625   6880   -315   -491   1037       C  
ATOM    497  CE2 PHE A  90     -11.914   5.877  28.609  1.00 49.79           C  
ANISOU  497  CE2 PHE A  90     5607   6502   6809   -101   -349   1086       C  
ATOM    498  CZ  PHE A  90     -12.481   4.624  28.486  1.00 50.67           C  
ANISOU  498  CZ  PHE A  90     5681   6681   6891   -235   -452   1148       C  
ATOM    499  N   THR A  91      -7.600   6.457  27.429  1.00 42.90           N  
ANISOU  499  N   THR A  91     5097   5298   5904   -133   -279    658       N  
ATOM    500  CA  THR A  91      -8.038   7.077  26.180  1.00 43.32           C  
ANISOU  500  CA  THR A  91     5140   5379   5943   -148   -305    731       C  
ATOM    501  C   THR A  91      -7.195   6.601  25.004  1.00 42.41           C  
ANISOU  501  C   THR A  91     5108   5235   5772   -221   -345    674       C  
ATOM    502  O   THR A  91      -7.720   6.381  23.906  1.00 41.14           O  
ANISOU  502  O   THR A  91     4952   5109   5571   -280   -408    734       O  
ATOM    503  CB  THR A  91      -7.993   8.605  26.286  1.00 46.97           C  
ANISOU  503  CB  THR A  91     5603   5806   6439    -50   -234    752       C  
ATOM    504  OG1 THR A  91      -6.634   9.045  26.378  1.00 52.04           O  
ANISOU  504  OG1 THR A  91     6328   6364   7081    -48   -196    650       O  
ATOM    505  CG2 THR A  91      -8.762   9.086  27.511  1.00 43.40           C  
ANISOU  505  CG2 THR A  91     5100   5369   6021     56   -178    803       C  
ATOM    506  N   TYR A  92      -5.887   6.429  25.214  1.00 40.01           N  
ANISOU  506  N   TYR A  92     4870   4875   5456   -213   -308    569       N  
ATOM    507  CA  TYR A  92      -5.028   5.889  24.173  1.00 46.28           C  
ANISOU  507  CA  TYR A  92     5745   5655   6184   -253   -328    522       C  
ATOM    508  C   TYR A  92      -5.350   4.431  23.878  1.00 45.06           C  
ANISOU  508  C   TYR A  92     5652   5506   5962   -317   -402    513       C  
ATOM    509  O   TYR A  92      -5.237   4.000  22.723  1.00 48.65           O  
ANISOU  509  O   TYR A  92     6189   5955   6342   -357   -446    515       O  
ATOM    510  CB  TYR A  92      -3.565   6.051  24.580  1.00 39.48           C  
ANISOU  510  CB  TYR A  92     4916   4761   5325   -217   -264    439       C  
ATOM    511  CG  TYR A  92      -2.561   5.821  23.473  1.00 39.65           C  
ANISOU  511  CG  TYR A  92     5002   4788   5277   -222   -256    414       C  
ATOM    512  CD1 TYR A  92      -2.744   6.372  22.206  1.00 40.12           C  
ANISOU  512  CD1 TYR A  92     5076   4862   5306   -238   -273    462       C  
ATOM    513  CD2 TYR A  92      -1.415   5.072  23.703  1.00 39.45           C  
ANISOU  513  CD2 TYR A  92     5019   4762   5209   -197   -224    352       C  
ATOM    514  CE1 TYR A  92      -1.816   6.170  21.194  1.00 43.26           C  
ANISOU  514  CE1 TYR A  92     5534   5274   5631   -228   -256    447       C  
ATOM    515  CE2 TYR A  92      -0.484   4.865  22.705  1.00 39.80           C  
ANISOU  515  CE2 TYR A  92     5116   4828   5178   -174   -200    345       C  
ATOM    516  CZ  TYR A  92      -0.686   5.415  21.451  1.00 43.83           C  
ANISOU  516  CZ  TYR A  92     5645   5353   5656   -189   -215    391       C  
ATOM    517  OH  TYR A  92       0.249   5.204  20.462  1.00 40.72           O  
ANISOU  517  OH  TYR A  92     5305   4990   5177   -152   -183    392       O  
ATOM    518  N   ALA A  93      -5.759   3.653  24.885  1.00 43.35           N  
ANISOU  518  N   ALA A  93     5418   5293   5762   -333   -422    505       N  
ATOM    519  CA  ALA A  93      -6.191   2.293  24.584  1.00 43.56           C  
ANISOU  519  CA  ALA A  93     5523   5312   5715   -415   -512    511       C  
ATOM    520  C   ALA A  93      -7.475   2.283  23.763  1.00 44.61           C  
ANISOU  520  C   ALA A  93     5631   5494   5823   -502   -607    627       C  
ATOM    521  O   ALA A  93      -7.664   1.399  22.922  1.00 46.38           O  
ANISOU  521  O   ALA A  93     5970   5696   5958   -588   -697    636       O  
ATOM    522  CB  ALA A  93      -6.372   1.498  25.878  1.00 41.83           C  
ANISOU  522  CB  ALA A  93     5285   5090   5521   -421   -518    490       C  
ATOM    523  N   VAL A  94      -8.353   3.266  23.976  1.00 46.91           N  
ANISOU  523  N   VAL A  94     5787   5852   6184   -478   -589    724       N  
ATOM    524  CA  VAL A  94      -9.631   3.300  23.268  1.00 46.95           C  
ANISOU  524  CA  VAL A  94     5735   5933   6171   -558   -679    864       C  
ATOM    525  C   VAL A  94      -9.483   3.933  21.886  1.00 49.36           C  
ANISOU  525  C   VAL A  94     6083   6233   6440   -568   -691    882       C  
ATOM    526  O   VAL A  94     -10.109   3.488  20.917  1.00 49.47           O  
ANISOU  526  O   VAL A  94     6139   6271   6388   -672   -795    953       O  
ATOM    527  CB  VAL A  94     -10.681   4.036  24.123  1.00 47.73           C  
ANISOU  527  CB  VAL A  94     5662   6126   6349   -501   -643    981       C  
ATOM    528  CG1 VAL A  94     -11.837   4.513  23.264  1.00 53.04           C  
ANISOU  528  CG1 VAL A  94     6245   6896   7014   -544   -704   1142       C  
ATOM    529  CG2 VAL A  94     -11.193   3.122  25.222  1.00 46.47           C  
ANISOU  529  CG2 VAL A  94     5455   6003   6199   -540   -675   1011       C  
ATOM    530  N   HIS A  95      -8.660   4.972  21.770  1.00 48.32           N  
ANISOU  530  N   HIS A  95     5949   6068   6345   -471   -596    825       N  
ATOM    531  CA  HIS A  95      -8.474   5.712  20.519  1.00 47.48           C  
ANISOU  531  CA  HIS A  95     5870   5959   6211   -470   -596    847       C  
ATOM    532  C   HIS A  95      -6.975   5.754  20.256  1.00 46.43           C  
ANISOU  532  C   HIS A  95     5834   5757   6048   -423   -530    727       C  
ATOM    533  O   HIS A  95      -6.253   6.544  20.871  1.00 46.14           O  
ANISOU  533  O   HIS A  95     5763   5699   6068   -348   -444    683       O  
ATOM    534  CB  HIS A  95      -9.070   7.112  20.610  1.00 48.58           C  
ANISOU  534  CB  HIS A  95     5894   6142   6423   -397   -546    935       C  
ATOM    535  CG  HIS A  95      -8.973   7.898  19.340  1.00 51.98           C  
ANISOU  535  CG  HIS A  95     6348   6575   6829   -400   -551    970       C  
ATOM    536  ND1 HIS A  95      -9.797   7.669  18.259  1.00 53.57           N  
ANISOU  536  ND1 HIS A  95     6547   6829   6979   -483   -643   1066       N  
ATOM    537  CD2 HIS A  95      -8.154   8.915  18.981  1.00 51.94           C  
ANISOU  537  CD2 HIS A  95     6368   6526   6840   -340   -483    931       C  
ATOM    538  CE1 HIS A  95      -9.488   8.510  17.288  1.00 53.04           C  
ANISOU  538  CE1 HIS A  95     6502   6751   6899   -462   -623   1077       C  
ATOM    539  NE2 HIS A  95      -8.494   9.277  17.700  1.00 51.68           N  
ANISOU  539  NE2 HIS A  95     6346   6521   6768   -377   -526    998       N  
ATOM    540  N   ASN A  96      -6.517   4.909  19.336  1.00 45.10           N  
ANISOU  540  N   ASN A  96     5795   5561   5781   -468   -574    686       N  
ATOM    541  CA  ASN A  96      -5.102   4.589  19.201  1.00 47.21           C  
ANISOU  541  CA  ASN A  96     6155   5784   6000   -412   -511    585       C  
ATOM    542  C   ASN A  96      -4.326   5.642  18.421  1.00 45.82           C  
ANISOU  542  C   ASN A  96     5966   5619   5825   -363   -449    588       C  
ATOM    543  O   ASN A  96      -3.545   5.300  17.525  1.00 46.37           O  
ANISOU  543  O   ASN A  96     6133   5680   5806   -344   -435    557       O  
ATOM    544  CB  ASN A  96      -4.945   3.228  18.522  1.00 55.77           C  
ANISOU  544  CB  ASN A  96     7410   6827   6955   -453   -575    546       C  
ATOM    545  CG  ASN A  96      -5.768   2.149  19.189  1.00 63.80           C  
ANISOU  545  CG  ASN A  96     8459   7826   7958   -529   -660    557       C  
ATOM    546  OD1 ASN A  96      -5.817   2.054  20.413  1.00 65.71           O  
ANISOU  546  OD1 ASN A  96     8621   8075   8272   -509   -631    540       O  
ATOM    547  ND2 ASN A  96      -6.433   1.330  18.379  1.00 67.02           N  
ANISOU  547  ND2 ASN A  96     8992   8209   8264   -629   -775    593       N  
ATOM    548  N   GLU A  97      -4.532   6.920  18.742  1.00 41.81           N  
ANISOU  548  N   GLU A  97     5352   5129   5407   -338   -410    632       N  
ATOM    549  CA  GLU A  97      -3.741   8.008  18.184  1.00 41.81           C  
ANISOU  549  CA  GLU A  97     5337   5132   5417   -304   -353    640       C  
ATOM    550  C   GLU A  97      -3.269   8.896  19.322  1.00 42.88           C  
ANISOU  550  C   GLU A  97     5408   5246   5639   -263   -290    623       C  
ATOM    551  O   GLU A  97      -4.032   9.189  20.246  1.00 41.61           O  
ANISOU  551  O   GLU A  97     5195   5072   5541   -248   -291    642       O  
ATOM    552  CB  GLU A  97      -4.535   8.831  17.158  1.00 42.38           C  
ANISOU  552  CB  GLU A  97     5388   5227   5489   -329   -389    728       C  
ATOM    553  CG  GLU A  97      -4.697   8.142  15.820  1.00 51.38           C  
ANISOU  553  CG  GLU A  97     6618   6380   6523   -376   -449    743       C  
ATOM    554  CD  GLU A  97      -5.509   8.955  14.828  1.00 54.01           C  
ANISOU  554  CD  GLU A  97     6921   6743   6857   -406   -490    838       C  
ATOM    555  OE1 GLU A  97      -5.055  10.050  14.426  1.00 54.93           O  
ANISOU  555  OE1 GLU A  97     7009   6862   6999   -375   -443    861       O  
ATOM    556  OE2 GLU A  97      -6.605   8.493  14.449  1.00 54.61           O  
ANISOU  556  OE2 GLU A  97     7001   6843   6904   -471   -577    900       O  
ATOM    557  N   TRP A  98      -2.012   9.324  19.246  1.00 41.21           N  
ANISOU  557  N   TRP A  98     5204   5034   5418   -247   -238    597       N  
ATOM    558  CA  TRP A  98      -1.361  10.049  20.330  1.00 40.88           C  
ANISOU  558  CA  TRP A  98     5129   4965   5438   -234   -194    578       C  
ATOM    559  C   TRP A  98      -1.460  11.552  20.067  1.00 44.56           C  
ANISOU  559  C   TRP A  98     5586   5403   5943   -240   -187    636       C  
ATOM    560  O   TRP A  98      -0.847  12.066  19.128  1.00 41.61           O  
ANISOU  560  O   TRP A  98     5221   5052   5538   -262   -180    670       O  
ATOM    561  CB  TRP A  98       0.095   9.616  20.473  1.00 40.77           C  
ANISOU  561  CB  TRP A  98     5120   4984   5388   -229   -153    541       C  
ATOM    562  CG  TRP A  98       0.712  10.195  21.697  1.00 40.52           C  
ANISOU  562  CG  TRP A  98     5060   4925   5411   -239   -128    525       C  
ATOM    563  CD1 TRP A  98       1.458  11.338  21.783  1.00 40.83           C  
ANISOU  563  CD1 TRP A  98     5090   4954   5470   -276   -117    563       C  
ATOM    564  CD2 TRP A  98       0.597   9.687  23.028  1.00 40.04           C  
ANISOU  564  CD2 TRP A  98     4991   4836   5385   -225   -124    474       C  
ATOM    565  NE1 TRP A  98       1.828  11.561  23.089  1.00 40.62           N  
ANISOU  565  NE1 TRP A  98     5062   4889   5482   -292   -112    536       N  
ATOM    566  CE2 TRP A  98       1.316  10.558  23.872  1.00 42.19           C  
ANISOU  566  CE2 TRP A  98     5257   5079   5692   -253   -110    478       C  
ATOM    567  CE3 TRP A  98      -0.031   8.566  23.588  1.00 41.06           C  
ANISOU  567  CE3 TRP A  98     5127   4961   5513   -202   -138    429       C  
ATOM    568  CZ2 TRP A  98       1.418  10.347  25.254  1.00 39.73           C  
ANISOU  568  CZ2 TRP A  98     4948   4735   5415   -249   -105    434       C  
ATOM    569  CZ3 TRP A  98       0.078   8.354  24.958  1.00 39.26           C  
ANISOU  569  CZ3 TRP A  98     4885   4707   5324   -193   -125    388       C  
ATOM    570  CH2 TRP A  98       0.794   9.243  25.773  1.00 43.15           C  
ANISOU  570  CH2 TRP A  98     5373   5171   5850   -212   -106    388       C  
ATOM    571  N   TYR A  99      -2.222  12.256  20.903  1.00 41.24           N  
ANISOU  571  N   TYR A  99     5159   4931   5580   -214   -185    652       N  
ATOM    572  CA  TYR A  99      -2.433  13.689  20.738  1.00 47.78           C  
ANISOU  572  CA  TYR A  99     6012   5708   6434   -202   -178    706       C  
ATOM    573  C   TYR A  99      -1.765  14.520  21.832  1.00 48.82           C  
ANISOU  573  C   TYR A  99     6194   5762   6594   -206   -157    682       C  
ATOM    574  O   TYR A  99      -1.958  15.739  21.873  1.00 42.34           O  
ANISOU  574  O   TYR A  99     5433   4870   5786   -192   -155    721       O  
ATOM    575  CB  TYR A  99      -3.930  14.004  20.709  1.00 42.09           C  
ANISOU  575  CB  TYR A  99     5271   4984   5738   -144   -189    766       C  
ATOM    576  CG  TYR A  99      -4.741  13.268  19.663  1.00 47.00           C  
ANISOU  576  CG  TYR A  99     5848   5681   6328   -164   -233    810       C  
ATOM    577  CD1 TYR A  99      -4.309  13.179  18.341  1.00 42.48           C  
ANISOU  577  CD1 TYR A  99     5292   5142   5705   -211   -255    825       C  
ATOM    578  CD2 TYR A  99      -5.951  12.672  19.999  1.00 43.72           C  
ANISOU  578  CD2 TYR A  99     5379   5307   5924   -141   -258    849       C  
ATOM    579  CE1 TYR A  99      -5.064  12.520  17.386  1.00 46.41           C  
ANISOU  579  CE1 TYR A  99     5777   5696   6160   -241   -307    867       C  
ATOM    580  CE2 TYR A  99      -6.707  12.008  19.055  1.00 49.06           C  
ANISOU  580  CE2 TYR A  99     6027   6052   6564   -187   -318    904       C  
ATOM    581  CZ  TYR A  99      -6.263  11.933  17.751  1.00 50.24           C  
ANISOU  581  CZ  TYR A  99     6216   6216   6658   -239   -346    907       C  
ATOM    582  OH  TYR A  99      -7.028  11.269  16.819  1.00 52.64           O  
ANISOU  582  OH  TYR A  99     6516   6575   6911   -297   -419    962       O  
ATOM    583  N   TYR A 100      -0.982  13.900  22.712  1.00 41.35           N  
ANISOU  583  N   TYR A 100     5241   4821   5649   -228   -146    623       N  
ATOM    584  CA  TYR A 100      -0.675  14.490  24.011  1.00 45.18           C  
ANISOU  584  CA  TYR A 100     5783   5225   6158   -228   -138    596       C  
ATOM    585  C   TYR A 100       0.747  15.038  24.139  1.00 43.31           C  
ANISOU  585  C   TYR A 100     5576   4976   5904   -319   -151    603       C  
ATOM    586  O   TYR A 100       1.128  15.486  25.227  1.00 45.11           O  
ANISOU  586  O   TYR A 100     5867   5133   6139   -344   -159    582       O  
ATOM    587  CB  TYR A 100      -0.976  13.453  25.094  1.00 40.82           C  
ANISOU  587  CB  TYR A 100     5200   4686   5622   -191   -124    538       C  
ATOM    588  CG  TYR A 100      -2.288  12.761  24.797  1.00 40.67           C  
ANISOU  588  CG  TYR A 100     5130   4712   5611   -134   -127    556       C  
ATOM    589  CD1 TYR A 100      -3.495  13.407  25.017  1.00 41.11           C  
ANISOU  589  CD1 TYR A 100     5195   4737   5687    -59   -117    606       C  
ATOM    590  CD2 TYR A 100      -2.319  11.486  24.237  1.00 42.25           C  
ANISOU  590  CD2 TYR A 100     5280   4988   5786   -156   -146    539       C  
ATOM    591  CE1 TYR A 100      -4.698  12.796  24.718  1.00 48.11           C  
ANISOU  591  CE1 TYR A 100     6012   5690   6578    -24   -129    653       C  
ATOM    592  CE2 TYR A 100      -3.518  10.863  23.933  1.00 42.43           C  
ANISOU  592  CE2 TYR A 100     5264   5051   5806   -136   -171    573       C  
ATOM    593  CZ  TYR A 100      -4.706  11.523  24.178  1.00 47.77           C  
ANISOU  593  CZ  TYR A 100     5919   5718   6512    -79   -166    638       C  
ATOM    594  OH  TYR A 100      -5.906  10.918  23.885  1.00 49.33           O  
ANISOU  594  OH  TYR A 100     6056   5983   6706    -74   -200    700       O  
ATOM    595  N   GLY A 101       1.532  15.037  23.068  1.00 41.94           N  
ANISOU  595  N   GLY A 101     5361   4874   5700   -373   -157    645       N  
ATOM    596  CA  GLY A 101       2.844  15.653  23.092  1.00 42.48           C  
ANISOU  596  CA  GLY A 101     5436   4955   5748   -472   -177    687       C  
ATOM    597  C   GLY A 101       3.962  14.675  23.419  1.00 42.23           C  
ANISOU  597  C   GLY A 101     5322   5027   5696   -500   -161    676       C  
ATOM    598  O   GLY A 101       3.745  13.563  23.896  1.00 41.58           O  
ANISOU  598  O   GLY A 101     5207   4975   5619   -441   -137    615       O  
ATOM    599  N   LEU A 102       5.191  15.117  23.136  1.00 42.89           N  
ANISOU  599  N   LEU A 102     5371   5174   5751   -591   -177    750       N  
ATOM    600  CA  LEU A 102       6.353  14.240  23.251  1.00 43.50           C  
ANISOU  600  CA  LEU A 102     5346   5384   5796   -602   -151    773       C  
ATOM    601  C   LEU A 102       6.767  14.028  24.705  1.00 44.00           C  
ANISOU  601  C   LEU A 102     5418   5421   5881   -639   -169    739       C  
ATOM    602  O   LEU A 102       7.056  12.893  25.115  1.00 45.83           O  
ANISOU  602  O   LEU A 102     5588   5721   6103   -583   -134    702       O  
ATOM    603  CB  LEU A 102       7.517  14.810  22.437  1.00 43.91           C  
ANISOU  603  CB  LEU A 102     5332   5544   5806   -687   -161    895       C  
ATOM    604  CG  LEU A 102       8.874  14.113  22.572  1.00 52.58           C  
ANISOU  604  CG  LEU A 102     6307   6808   6863   -700   -132    962       C  
ATOM    605  CD1 LEU A 102       8.794  12.672  22.088  1.00 43.83           C  
ANISOU  605  CD1 LEU A 102     5152   5787   5715   -551    -54    914       C  
ATOM    606  CD2 LEU A 102       9.960  14.880  21.815  1.00 45.54           C  
ANISOU  606  CD2 LEU A 102     5339   6033   5931   -801   -149   1114       C  
ATOM    607  N   PHE A 103       6.801  15.097  25.506  1.00 43.22           N  
ANISOU  607  N   PHE A 103     5411   5212   5799   -731   -227    751       N  
ATOM    608  CA  PHE A 103       7.183  14.905  26.903  1.00 43.15           C  
ANISOU  608  CA  PHE A 103     5424   5170   5800   -771   -250    718       C  
ATOM    609  C   PHE A 103       6.219  13.961  27.596  1.00 42.13           C  
ANISOU  609  C   PHE A 103     5310   4997   5701   -651   -209    608       C  
ATOM    610  O   PHE A 103       6.640  13.085  28.361  1.00 41.77           O  
ANISOU  610  O   PHE A 103     5212   5003   5656   -636   -194    577       O  
ATOM    611  CB  PHE A 103       7.235  16.233  27.664  1.00 43.96           C  
ANISOU  611  CB  PHE A 103     5676   5128   5898   -884   -326    737       C  
ATOM    612  CG  PHE A 103       7.277  16.060  29.164  1.00 54.61           C  
ANISOU  612  CG  PHE A 103     7092   6404   7252   -901   -349    679       C  
ATOM    613  CD1 PHE A 103       8.472  15.782  29.810  1.00 53.38           C  
ANISOU  613  CD1 PHE A 103     6871   6334   7078  -1007   -386    729       C  
ATOM    614  CD2 PHE A 103       6.117  16.150  29.923  1.00 55.89           C  
ANISOU  614  CD2 PHE A 103     7374   6427   7434   -804   -330    586       C  
ATOM    615  CE1 PHE A 103       8.513  15.607  31.188  1.00 54.52           C  
ANISOU  615  CE1 PHE A 103     7082   6412   7222  -1027   -411    676       C  
ATOM    616  CE2 PHE A 103       6.150  15.975  31.303  1.00 55.33           C  
ANISOU  616  CE2 PHE A 103     7372   6291   7360   -811   -346    533       C  
ATOM    617  CZ  PHE A 103       7.350  15.705  31.934  1.00 53.24           C  
ANISOU  617  CZ  PHE A 103     7055   6098   7076   -928   -390    572       C  
ATOM    618  N   TYR A 104       4.920  14.106  27.327  1.00 41.76           N  
ANISOU  618  N   TYR A 104     5322   4868   5676   -565   -191    561       N  
ATOM    619  CA  TYR A 104       3.975  13.211  27.975  1.00 47.36           C  
ANISOU  619  CA  TYR A 104     6031   5554   6411   -464   -159    480       C  
ATOM    620  C   TYR A 104       4.072  11.792  27.424  1.00 49.04           C  
ANISOU  620  C   TYR A 104     6144   5880   6610   -406   -122    459       C  
ATOM    621  O   TYR A 104       3.777  10.840  28.146  1.00 39.81           O  
ANISOU  621  O   TYR A 104     4959   4716   5451   -357   -106    401       O  
ATOM    622  CB  TYR A 104       2.546  13.735  27.865  1.00 40.92           C  
ANISOU  622  CB  TYR A 104     5286   4646   5618   -387   -151    464       C  
ATOM    623  CG  TYR A 104       1.653  12.988  28.820  1.00 51.57           C  
ANISOU  623  CG  TYR A 104     6633   5972   6989   -303   -127    403       C  
ATOM    624  CD1 TYR A 104       1.722  13.224  30.187  1.00 52.88           C  
ANISOU  624  CD1 TYR A 104     6869   6063   7160   -304   -131    367       C  
ATOM    625  CD2 TYR A 104       0.793  12.003  28.368  1.00 52.85           C  
ANISOU  625  CD2 TYR A 104     6728   6192   7161   -237   -107    389       C  
ATOM    626  CE1 TYR A 104       0.931  12.525  31.077  1.00 49.19           C  
ANISOU  626  CE1 TYR A 104     6391   5588   6710   -225   -105    321       C  
ATOM    627  CE2 TYR A 104       0.005  11.295  29.247  1.00 52.42           C  
ANISOU  627  CE2 TYR A 104     6661   6131   7125   -177    -93    351       C  
ATOM    628  CZ  TYR A 104       0.075  11.562  30.603  1.00 52.19           C  
ANISOU  628  CZ  TYR A 104     6688   6038   7106   -164    -85    318       C  
ATOM    629  OH  TYR A 104      -0.717  10.859  31.482  1.00 55.21           O  
ANISOU  629  OH  TYR A 104     7049   6425   7504   -101    -66    289       O  
ATOM    630  N   CYS A 105       4.509  11.624  26.172  1.00 43.98           N  
ANISOU  630  N   CYS A 105     5452   5324   5934   -407   -109    506       N  
ATOM    631  CA  CYS A 105       4.756  10.278  25.652  1.00 40.33           C  
ANISOU  631  CA  CYS A 105     4936   4956   5433   -342    -73    487       C  
ATOM    632  C   CYS A 105       5.899   9.604  26.407  1.00 40.37           C  
ANISOU  632  C   CYS A 105     4885   5034   5419   -349    -54    490       C  
ATOM    633  O   CYS A 105       5.794   8.433  26.822  1.00 39.92           O  
ANISOU  633  O   CYS A 105     4823   4995   5351   -285    -32    436       O  
ATOM    634  CB  CYS A 105       5.050  10.368  24.148  1.00 40.81           C  
ANISOU  634  CB  CYS A 105     4975   5088   5444   -332    -57    545       C  
ATOM    635  SG  CYS A 105       5.812   8.937  23.360  1.00 41.49           S  
ANISOU  635  SG  CYS A 105     5026   5296   5442   -243     -2    549       S  
ATOM    636  N   LYS A 106       6.978  10.354  26.649  1.00 41.00           N  
ANISOU  636  N   LYS A 106     4926   5158   5494   -435    -71    562       N  
ATOM    637  CA  LYS A 106       8.073   9.824  27.454  1.00 46.77           C  
ANISOU  637  CA  LYS A 106     5589   5973   6210   -453    -62    587       C  
ATOM    638  C   LYS A 106       7.619   9.522  28.878  1.00 45.20           C  
ANISOU  638  C   LYS A 106     5435   5689   6051   -453    -80    506       C  
ATOM    639  O   LYS A 106       7.934   8.458  29.419  1.00 45.37           O  
ANISOU  639  O   LYS A 106     5418   5760   6061   -399    -52    477       O  
ATOM    640  CB  LYS A 106       9.248  10.806  27.463  1.00 42.20           C  
ANISOU  640  CB  LYS A 106     4956   5461   5616   -579    -99    704       C  
ATOM    641  CG  LYS A 106       9.845  11.059  26.072  1.00 46.45           C  
ANISOU  641  CG  LYS A 106     5426   6115   6106   -578    -73    806       C  
ATOM    642  CD  LYS A 106      11.084  11.949  26.136  1.00 44.12           C  
ANISOU  642  CD  LYS A 106     5056   5915   5792   -721   -118    949       C  
ATOM    643  CE  LYS A 106      11.746  12.101  24.762  1.00 48.99           C  
ANISOU  643  CE  LYS A 106     5581   6677   6354   -707    -81   1068       C  
ATOM    644  NZ  LYS A 106      12.374  10.831  24.280  1.00 45.15           N  
ANISOU  644  NZ  LYS A 106     4995   6355   5804   -557     13   1098       N  
ATOM    645  N   PHE A 107       6.856  10.436  29.491  1.00 44.73           N  
ANISOU  645  N   PHE A 107     5466   5497   6031   -498   -121    473       N  
ATOM    646  CA  PHE A 107       6.384  10.220  30.859  1.00 41.59           C  
ANISOU  646  CA  PHE A 107     5122   5019   5663   -486   -132    401       C  
ATOM    647  C   PHE A 107       5.453   9.016  30.932  1.00 43.22           C  
ANISOU  647  C   PHE A 107     5319   5222   5881   -376    -94    326       C  
ATOM    648  O   PHE A 107       5.525   8.216  31.872  1.00 42.11           O  
ANISOU  648  O   PHE A 107     5166   5088   5747   -351    -85    282       O  
ATOM    649  CB  PHE A 107       5.675  11.480  31.367  1.00 40.34           C  
ANISOU  649  CB  PHE A 107     5088   4716   5525   -523   -169    388       C  
ATOM    650  CG  PHE A 107       5.147  11.367  32.780  1.00 46.08           C  
ANISOU  650  CG  PHE A 107     5886   5354   6268   -495   -173    320       C  
ATOM    651  CD1 PHE A 107       5.930  11.754  33.859  1.00 43.80           C  
ANISOU  651  CD1 PHE A 107     5647   5033   5963   -584   -216    329       C  
ATOM    652  CD2 PHE A 107       3.864  10.888  33.027  1.00 45.60           C  
ANISOU  652  CD2 PHE A 107     5843   5251   6232   -387   -138    262       C  
ATOM    653  CE1 PHE A 107       5.453  11.659  35.165  1.00 42.70           C  
ANISOU  653  CE1 PHE A 107     5587   4809   5829   -552   -217    266       C  
ATOM    654  CE2 PHE A 107       3.377  10.793  34.332  1.00 46.22           C  
ANISOU  654  CE2 PHE A 107     5981   5260   6318   -351   -133    211       C  
ATOM    655  CZ  PHE A 107       4.173  11.179  35.401  1.00 40.85           C  
ANISOU  655  CZ  PHE A 107     5364   4537   5619   -426   -168    206       C  
ATOM    656  N   HIS A 108       4.616   8.847  29.910  1.00 44.63           N  
ANISOU  656  N   HIS A 108     5505   5396   6057   -322    -80    320       N  
ATOM    657  CA  HIS A 108       3.672   7.745  29.831  1.00 43.88           C  
ANISOU  657  CA  HIS A 108     5413   5298   5963   -246    -65    269       C  
ATOM    658  C   HIS A 108       4.388   6.406  29.773  1.00 41.53           C  
ANISOU  658  C   HIS A 108     5079   5078   5623   -206    -40    251       C  
ATOM    659  O   HIS A 108       3.919   5.427  30.363  1.00 38.60           O  
ANISOU  659  O   HIS A 108     4722   4690   5254   -167    -39    201       O  
ATOM    660  CB  HIS A 108       2.782   7.992  28.602  1.00 45.47           C  
ANISOU  660  CB  HIS A 108     5632   5489   6157   -225    -72    291       C  
ATOM    661  CG  HIS A 108       2.192   6.764  27.983  1.00 45.58           C  
ANISOU  661  CG  HIS A 108     5651   5529   6138   -179    -73    268       C  
ATOM    662  ND1 HIS A 108       0.933   6.301  28.303  1.00 45.73           N  
ANISOU  662  ND1 HIS A 108     5684   5513   6177   -160    -95    248       N  
ATOM    663  CD2 HIS A 108       2.660   5.941  27.014  1.00 46.09           C  
ANISOU  663  CD2 HIS A 108     5726   5648   6138   -151    -61    272       C  
ATOM    664  CE1 HIS A 108       0.664   5.227  27.583  1.00 45.38           C  
ANISOU  664  CE1 HIS A 108     5667   5491   6083   -146   -111    238       C  
ATOM    665  NE2 HIS A 108       1.697   4.984  26.796  1.00 46.75           N  
ANISOU  665  NE2 HIS A 108     5854   5709   6200   -131    -88    244       N  
ATOM    666  N   ASN A 109       5.543   6.345  29.108  1.00 39.89           N  
ANISOU  666  N   ASN A 109     4828   4960   5370   -207    -17    303       N  
ATOM    667  CA  ASN A 109       6.284   5.085  29.118  1.00 42.52           C  
ANISOU  667  CA  ASN A 109     5139   5368   5650   -138     21    295       C  
ATOM    668  C   ASN A 109       7.313   4.976  30.242  1.00 41.90           C  
ANISOU  668  C   ASN A 109     5000   5341   5579   -162     29    314       C  
ATOM    669  O   ASN A 109       7.832   3.882  30.482  1.00 43.28           O  
ANISOU  669  O   ASN A 109     5161   5570   5715    -91     62    304       O  
ATOM    670  CB  ASN A 109       6.966   4.866  27.771  1.00 42.30           C  
ANISOU  670  CB  ASN A 109     5097   5429   5547    -86     60    351       C  
ATOM    671  CG  ASN A 109       5.974   4.524  26.684  1.00 44.53           C  
ANISOU  671  CG  ASN A 109     5460   5661   5796    -48     50    321       C  
ATOM    672  OD1 ASN A 109       5.070   3.718  26.892  1.00 48.27           O  
ANISOU  672  OD1 ASN A 109     6002   6069   6268    -25     27    258       O  
ATOM    673  ND2 ASN A 109       6.116   5.158  25.533  1.00 40.85           N  
ANISOU  673  ND2 ASN A 109     4990   5229   5303    -56     57    374       N  
ATOM    674  N   PHE A 110       7.607   6.063  30.945  1.00 39.39           N  
ANISOU  674  N   PHE A 110     4662   5002   5303   -260     -7    345       N  
ATOM    675  CA  PHE A 110       8.643   6.077  31.968  1.00 39.51           C  
ANISOU  675  CA  PHE A 110     4620   5073   5318   -310    -17    381       C  
ATOM    676  C   PHE A 110       8.078   5.889  33.370  1.00 42.70           C  
ANISOU  676  C   PHE A 110     5072   5387   5763   -324    -41    306       C  
ATOM    677  O   PHE A 110       8.513   4.994  34.102  1.00 42.29           O  
ANISOU  677  O   PHE A 110     4989   5378   5702   -290    -25    290       O  
ATOM    678  CB  PHE A 110       9.413   7.404  31.861  1.00 40.32           C  
ANISOU  678  CB  PHE A 110     4693   5205   5423   -436    -60    477       C  
ATOM    679  CG  PHE A 110      10.376   7.675  32.990  1.00 41.80           C  
ANISOU  679  CG  PHE A 110     4838   5432   5610   -535   -102    528       C  
ATOM    680  CD1 PHE A 110       9.954   8.324  34.143  1.00 44.06           C  
ANISOU  680  CD1 PHE A 110     5218   5594   5928   -615   -159    480       C  
ATOM    681  CD2 PHE A 110      11.718   7.345  32.869  1.00 42.99           C  
ANISOU  681  CD2 PHE A 110     4862   5753   5719   -550    -85    641       C  
ATOM    682  CE1 PHE A 110      10.843   8.601  35.172  1.00 47.41           C  
ANISOU  682  CE1 PHE A 110     5624   6048   6342   -724   -212    531       C  
ATOM    683  CE2 PHE A 110      12.615   7.620  33.893  1.00 45.74           C  
ANISOU  683  CE2 PHE A 110     5162   6153   6064   -662   -138    708       C  
ATOM    684  CZ  PHE A 110      12.176   8.248  35.047  1.00 47.56           C  
ANISOU  684  CZ  PHE A 110     5502   6244   6326   -760   -208    649       C  
ATOM    685  N   PHE A 111       7.110   6.717  33.754  1.00 39.20           N  
ANISOU  685  N   PHE A 111     4710   4823   5360   -359    -74    265       N  
ATOM    686  CA  PHE A 111       6.689   6.760  35.149  1.00 39.42           C  
ANISOU  686  CA  PHE A 111     4791   4771   5415   -373    -94    210       C  
ATOM    687  C   PHE A 111       6.134   5.450  35.690  1.00 40.48           C  
ANISOU  687  C   PHE A 111     4917   4907   5558   -290    -66    143       C  
ATOM    688  O   PHE A 111       6.446   5.131  36.847  1.00 37.94           O  
ANISOU  688  O   PHE A 111     4594   4581   5241   -304    -74    122       O  
ATOM    689  CB  PHE A 111       5.686   7.890  35.387  1.00 38.80           C  
ANISOU  689  CB  PHE A 111     4816   4565   5361   -389   -117    187       C  
ATOM    690  CG  PHE A 111       5.534   8.232  36.841  1.00 41.38           C  
ANISOU  690  CG  PHE A 111     5220   4808   5693   -413   -139    149       C  
ATOM    691  CD1 PHE A 111       6.609   8.745  37.553  1.00 39.16           C  
ANISOU  691  CD1 PHE A 111     4961   4529   5390   -520   -186    184       C  
ATOM    692  CD2 PHE A 111       4.346   8.003  37.507  1.00 39.49           C  
ANISOU  692  CD2 PHE A 111     5031   4500   5474   -333   -116     92       C  
ATOM    693  CE1 PHE A 111       6.489   9.045  38.903  1.00 39.68           C  
ANISOU  693  CE1 PHE A 111     5123   4507   5446   -545   -212    147       C  
ATOM    694  CE2 PHE A 111       4.221   8.307  38.859  1.00 39.78           C  
ANISOU  694  CE2 PHE A 111     5151   4461   5503   -339   -128     59       C  
ATOM    695  CZ  PHE A 111       5.295   8.828  39.553  1.00 38.89           C  
ANISOU  695  CZ  PHE A 111     5084   4330   5362   -444   -177     78       C  
ATOM    696  N   PRO A 112       5.266   4.706  34.990  1.00 40.83           N  
ANISOU  696  N   PRO A 112     4969   4946   5600   -217    -45    113       N  
ATOM    697  CA  PRO A 112       4.681   3.520  35.639  1.00 39.06           C  
ANISOU  697  CA  PRO A 112     4754   4707   5379   -163    -37     58       C  
ATOM    698  C   PRO A 112       5.719   2.531  36.135  1.00 43.08           C  
ANISOU  698  C   PRO A 112     5225   5285   5860   -141    -19     57       C  
ATOM    699  O   PRO A 112       5.546   1.950  37.214  1.00 36.54           O  
ANISOU  699  O   PRO A 112     4403   4435   5044   -130    -22     18       O  
ATOM    700  CB  PRO A 112       3.808   2.912  34.529  1.00 42.86           C  
ANISOU  700  CB  PRO A 112     5258   5184   5842   -119    -36     52       C  
ATOM    701  CG  PRO A 112       3.474   4.060  33.647  1.00 41.60           C  
ANISOU  701  CG  PRO A 112     5106   5005   5693   -146    -44     89       C  
ATOM    702  CD  PRO A 112       4.702   4.918  33.642  1.00 39.57           C  
ANISOU  702  CD  PRO A 112     4821   4784   5429   -196    -41    132       C  
ATOM    703  N   ILE A 113       6.832   2.377  35.417  1.00 40.88           N  
ANISOU  703  N   ILE A 113     4899   5096   5538   -126      4    109       N  
ATOM    704  CA  ILE A 113       7.867   1.451  35.860  1.00 37.55           C  
ANISOU  704  CA  ILE A 113     4432   4756   5081    -82     32    127       C  
ATOM    705  C   ILE A 113       8.514   1.955  37.146  1.00 43.21           C  
ANISOU  705  C   ILE A 113     5105   5488   5824   -159      6    148       C  
ATOM    706  O   ILE A 113       8.667   1.204  38.120  1.00 40.73           O  
ANISOU  706  O   ILE A 113     4786   5179   5511   -136      9    120       O  
ATOM    707  CB  ILE A 113       8.903   1.239  34.742  1.00 44.43           C  
ANISOU  707  CB  ILE A 113     5254   5741   5888    -27     75    202       C  
ATOM    708  CG1 ILE A 113       8.264   0.497  33.563  1.00 45.15           C  
ANISOU  708  CG1 ILE A 113     5426   5800   5930     62     98    169       C  
ATOM    709  CG2 ILE A 113      10.116   0.491  35.261  1.00 38.77           C  
ANISOU  709  CG2 ILE A 113     4467   5135   5130     27    111    253       C  
ATOM    710  CD1 ILE A 113       9.160   0.383  32.354  1.00 45.73           C  
ANISOU  710  CD1 ILE A 113     5473   5975   5927    135    150    241       C  
ATOM    711  N   ALA A 114       8.876   3.242  37.175  1.00 40.22           N  
ANISOU  711  N   ALA A 114     4714   5108   5461   -260    -30    198       N  
ATOM    712  CA  ALA A 114       9.512   3.808  38.362  1.00 43.97           C  
ANISOU  712  CA  ALA A 114     5176   5584   5945   -358    -74    225       C  
ATOM    713  C   ALA A 114       8.571   3.787  39.557  1.00 41.43           C  
ANISOU  713  C   ALA A 114     4939   5145   5657   -359    -93    138       C  
ATOM    714  O   ALA A 114       8.990   3.496  40.683  1.00 38.73           O  
ANISOU  714  O   ALA A 114     4590   4814   5313   -385   -110    132       O  
ATOM    715  CB  ALA A 114       9.975   5.238  38.077  1.00 39.18           C  
ANISOU  715  CB  ALA A 114     4579   4972   5336   -482   -125    297       C  
ATOM    716  N   ALA A 115       7.283   4.035  39.320  1.00 39.10           N  
ANISOU  716  N   ALA A 115     4718   4752   5387   -321    -86     80       N  
ATOM    717  CA  ALA A 115       6.323   4.096  40.411  1.00 39.54           C  
ANISOU  717  CA  ALA A 115     4846   4712   5466   -304    -92     16       C  
ATOM    718  C   ALA A 115       6.065   2.711  40.988  1.00 38.93           C  
ANISOU  718  C   ALA A 115     4740   4660   5393   -236    -68    -27       C  
ATOM    719  O   ALA A 115       6.048   2.536  42.213  1.00 38.04           O  
ANISOU  719  O   ALA A 115     4649   4522   5284   -246    -77    -56       O  
ATOM    720  CB  ALA A 115       5.019   4.738  39.933  1.00 36.91           C  
ANISOU  720  CB  ALA A 115     4576   4296   5153   -267    -84     -4       C  
ATOM    721  N   ILE A 116       5.859   1.710  40.125  1.00 37.83           N  
ANISOU  721  N   ILE A 116     4570   4562   5242   -171    -43    -33       N  
ATOM    722  CA  ILE A 116       5.639   0.360  40.632  1.00 38.69           C  
ANISOU  722  CA  ILE A 116     4677   4681   5343   -116    -30    -70       C  
ATOM    723  C   ILE A 116       6.890  -0.160  41.327  1.00 41.13           C  
ANISOU  723  C   ILE A 116     4938   5059   5630   -119    -24    -49       C  
ATOM    724  O   ILE A 116       6.800  -0.828  42.366  1.00 45.75           O  
ANISOU  724  O   ILE A 116     5530   5634   6221   -105    -26    -81       O  
ATOM    725  CB  ILE A 116       5.182  -0.578  39.502  1.00 39.98           C  
ANISOU  725  CB  ILE A 116     4859   4852   5479    -57    -18    -77       C  
ATOM    726  CG1 ILE A 116       3.856  -0.087  38.919  1.00 40.79           C  
ANISOU  726  CG1 ILE A 116     4995   4899   5605    -67    -35    -81       C  
ATOM    727  CG2 ILE A 116       5.017  -2.003  40.024  1.00 35.61           C  
ANISOU  727  CG2 ILE A 116     4332   4293   4904    -10    -16   -111       C  
ATOM    728  CD1 ILE A 116       2.796   0.167  39.975  1.00 45.28           C  
ANISOU  728  CD1 ILE A 116     5575   5418   6214    -75    -45   -100       C  
ATOM    729  N   PHE A 117       8.074   0.173  40.803  1.00 37.94           N  
ANISOU  729  N   PHE A 117     4475   4740   5199   -139    -17     17       N  
ATOM    730  CA  PHE A 117       9.308  -0.229  41.467  1.00 37.09           C  
ANISOU  730  CA  PHE A 117     4299   4727   5068   -145    -13     66       C  
ATOM    731  C   PHE A 117       9.392   0.378  42.863  1.00 40.86           C  
ANISOU  731  C   PHE A 117     4791   5164   5568   -236    -58     55       C  
ATOM    732  O   PHE A 117       9.618  -0.336  43.849  1.00 39.77           O  
ANISOU  732  O   PHE A 117     4641   5042   5427   -220    -58     39       O  
ATOM    733  CB  PHE A 117      10.516   0.180  40.615  1.00 37.92           C  
ANISOU  733  CB  PHE A 117     4317   4952   5137   -160      0    170       C  
ATOM    734  CG  PHE A 117      11.848  -0.273  41.168  1.00 43.64           C  
ANISOU  734  CG  PHE A 117     4941   5812   5830   -156     10    254       C  
ATOM    735  CD1 PHE A 117      12.447   0.400  42.222  1.00 43.03           C  
ANISOU  735  CD1 PHE A 117     4827   5757   5764   -279    -48    300       C  
ATOM    736  CD2 PHE A 117      12.510  -1.360  40.617  1.00 44.08           C  
ANISOU  736  CD2 PHE A 117     4947   5971   5831    -23     75    298       C  
ATOM    737  CE1 PHE A 117      13.671  -0.008  42.725  1.00 45.03           C  
ANISOU  737  CE1 PHE A 117     4970   6154   5987   -285    -47    398       C  
ATOM    738  CE2 PHE A 117      13.735  -1.771  41.117  1.00 43.90           C  
ANISOU  738  CE2 PHE A 117     4815   6091   5774     -1     92    396       C  
ATOM    739  CZ  PHE A 117      14.315  -1.092  42.171  1.00 43.61           C  
ANISOU  739  CZ  PHE A 117     4715   6094   5759   -139     28    452       C  
ATOM    740  N   ALA A 118       9.188   1.697  42.971  1.00 38.11           N  
ANISOU  740  N   ALA A 118     4491   4753   5234   -329   -100     63       N  
ATOM    741  CA  ALA A 118       9.303   2.347  44.273  1.00 38.36           C  
ANISOU  741  CA  ALA A 118     4579   4729   5267   -417   -150     52       C  
ATOM    742  C   ALA A 118       8.277   1.801  45.254  1.00 37.61           C  
ANISOU  742  C   ALA A 118     4548   4552   5191   -358   -134    -34       C  
ATOM    743  O   ALA A 118       8.588   1.574  46.431  1.00 37.41           O  
ANISOU  743  O   ALA A 118     4533   4525   5155   -386   -154    -44       O  
ATOM    744  CB  ALA A 118       9.140   3.857  44.119  1.00 38.56           C  
ANISOU  744  CB  ALA A 118     4692   4671   5287   -511   -196     68       C  
ATOM    745  N   SER A 119       7.072   1.501  44.765  1.00 38.43           N  
ANISOU  745  N   SER A 119     4681   4605   5317   -278    -99    -83       N  
ATOM    746  CA  SER A 119       6.020   0.998  45.640  1.00 41.78           C  
ANISOU  746  CA  SER A 119     5148   4971   5757   -224    -84   -141       C  
ATOM    747  C   SER A 119       6.336  -0.408  46.150  1.00 41.15           C  
ANISOU  747  C   SER A 119     5017   4947   5672   -184    -70   -154       C  
ATOM    748  O   SER A 119       6.298  -0.672  47.365  1.00 38.69           O  
ANISOU  748  O   SER A 119     4724   4618   5358   -189    -78   -178       O  
ATOM    749  CB  SER A 119       4.690   1.016  44.884  1.00 43.64           C  
ANISOU  749  CB  SER A 119     5403   5166   6014   -165    -60   -158       C  
ATOM    750  OG  SER A 119       3.665   0.416  45.649  1.00 51.77           O  
ANISOU  750  OG  SER A 119     6446   6170   7056   -115    -45   -188       O  
ATOM    751  N   ILE A 120       6.640  -1.330  45.233  1.00 40.68           N  
ANISOU  751  N   ILE A 120     4911   4946   5601   -135    -50   -139       N  
ATOM    752  CA  ILE A 120       6.842  -2.711  45.646  1.00 35.36           C  
ANISOU  752  CA  ILE A 120     4220   4304   4912    -80    -36   -153       C  
ATOM    753  C   ILE A 120       8.115  -2.848  46.469  1.00 44.09           C  
ANISOU  753  C   ILE A 120     5273   5480   5998   -105    -43   -118       C  
ATOM    754  O   ILE A 120       8.165  -3.657  47.403  1.00 42.08           O  
ANISOU  754  O   ILE A 120     5020   5230   5740    -83    -42   -137       O  
ATOM    755  CB  ILE A 120       6.834  -3.668  44.435  1.00 35.39           C  
ANISOU  755  CB  ILE A 120     4232   4331   4885     -7    -12   -148       C  
ATOM    756  CG1 ILE A 120       6.714  -5.121  44.911  1.00 38.21           C  
ANISOU  756  CG1 ILE A 120     4620   4680   5219     51     -7   -175       C  
ATOM    757  CG2 ILE A 120       8.092  -3.496  43.577  1.00 35.96           C  
ANISOU  757  CG2 ILE A 120     4250   4493   4921     13     11    -86       C  
ATOM    758  CD1 ILE A 120       5.479  -5.401  45.751  1.00 34.85           C  
ANISOU  758  CD1 ILE A 120     4231   4187   4824     28    -31   -215       C  
ATOM    759  N   TYR A 121       9.152  -2.048  46.188  1.00 41.07           N  
ANISOU  759  N   TYR A 121     4840   5162   5602   -163    -57    -53       N  
ATOM    760  CA  TYR A 121      10.329  -2.159  47.039  1.00 42.31           C  
ANISOU  760  CA  TYR A 121     4935   5403   5739   -205    -76      3       C  
ATOM    761  C   TYR A 121      10.152  -1.465  48.382  1.00 44.59           C  
ANISOU  761  C   TYR A 121     5278   5626   6036   -298   -126    -23       C  
ATOM    762  O   TYR A 121      10.813  -1.861  49.351  1.00 43.05           O  
ANISOU  762  O   TYR A 121     5051   5480   5827   -322   -145      1       O  
ATOM    763  CB  TYR A 121      11.576  -1.664  46.309  1.00 39.99           C  
ANISOU  763  CB  TYR A 121     4548   5230   5418   -244    -81    112       C  
ATOM    764  CG  TYR A 121      12.097  -2.756  45.412  1.00 42.34           C  
ANISOU  764  CG  TYR A 121     4785   5623   5679   -113    -16    152       C  
ATOM    765  CD1 TYR A 121      12.930  -3.756  45.905  1.00 43.85           C  
ANISOU  765  CD1 TYR A 121     4912   5910   5838    -42     11    199       C  
ATOM    766  CD2 TYR A 121      11.691  -2.838  44.091  1.00 40.80           C  
ANISOU  766  CD2 TYR A 121     4618   5412   5474    -44     21    140       C  
ATOM    767  CE1 TYR A 121      13.378  -4.785  45.084  1.00 42.90           C  
ANISOU  767  CE1 TYR A 121     4771   5864   5666    109     81    234       C  
ATOM    768  CE2 TYR A 121      12.130  -3.851  43.271  1.00 44.14           C  
ANISOU  768  CE2 TYR A 121     5026   5903   5843     92     84    169       C  
ATOM    769  CZ  TYR A 121      12.969  -4.822  43.765  1.00 46.68           C  
ANISOU  769  CZ  TYR A 121     5299   6312   6124    177    117    215       C  
ATOM    770  OH  TYR A 121      13.391  -5.826  42.921  1.00 46.48           O  
ANISOU  770  OH  TYR A 121     5291   6341   6028    340    189    245       O  
ATOM    771  N   SER A 122       9.234  -0.495  48.492  1.00 43.64           N  
ANISOU  771  N   SER A 122     5253   5395   5931   -335   -144    -70       N  
ATOM    772  CA  SER A 122       8.876  -0.015  49.823  1.00 43.09           C  
ANISOU  772  CA  SER A 122     5274   5245   5854   -382   -176   -110       C  
ATOM    773  C   SER A 122       8.185  -1.109  50.633  1.00 44.17           C  
ANISOU  773  C   SER A 122     5416   5365   6003   -302   -144   -165       C  
ATOM    774  O   SER A 122       8.468  -1.289  51.831  1.00 47.16           O  
ANISOU  774  O   SER A 122     5813   5740   6364   -332   -166   -173       O  
ATOM    775  CB  SER A 122       7.985   1.218  49.702  1.00 37.66           C  
ANISOU  775  CB  SER A 122     4704   4439   5165   -400   -185   -142       C  
ATOM    776  OG  SER A 122       8.702   2.289  49.123  1.00 38.98           O  
ANISOU  776  OG  SER A 122     4887   4609   5313   -497   -230    -86       O  
ATOM    777  N   MET A 123       7.292  -1.868  49.988  1.00 37.95           N  
ANISOU  777  N   MET A 123     4613   4567   5239   -214   -102   -196       N  
ATOM    778  CA  MET A 123       6.657  -2.981  50.694  1.00 40.04           C  
ANISOU  778  CA  MET A 123     4880   4823   5512   -155    -83   -233       C  
ATOM    779  C   MET A 123       7.682  -4.049  51.069  1.00 41.16           C  
ANISOU  779  C   MET A 123     4960   5042   5635   -141    -84   -209       C  
ATOM    780  O   MET A 123       7.582  -4.686  52.132  1.00 39.91           O  
ANISOU  780  O   MET A 123     4811   4880   5474   -130    -86   -229       O  
ATOM    781  CB  MET A 123       5.538  -3.587  49.842  1.00 38.55           C  
ANISOU  781  CB  MET A 123     4693   4611   5341    -92    -58   -250       C  
ATOM    782  CG  MET A 123       4.398  -2.628  49.532  1.00 43.24           C  
ANISOU  782  CG  MET A 123     5329   5146   5952    -88    -50   -257       C  
ATOM    783  SD  MET A 123       3.769  -1.788  50.995  1.00 51.36           S  
ANISOU  783  SD  MET A 123     6432   6112   6971    -86    -44   -279       S  
ATOM    784  CE  MET A 123       2.366  -0.900  50.332  1.00 53.93           C  
ANISOU  784  CE  MET A 123     6790   6393   7308    -35    -15   -264       C  
ATOM    785  N   THR A 124       8.683  -4.253  50.209  1.00 39.15           N  
ANISOU  785  N   THR A 124     4644   4867   5364   -129    -76   -157       N  
ATOM    786  CA  THR A 124       9.736  -5.214  50.518  1.00 39.10           C  
ANISOU  786  CA  THR A 124     4575   4951   5332    -91    -65   -115       C  
ATOM    787  C   THR A 124      10.567  -4.758  51.714  1.00 42.84           C  
ANISOU  787  C   THR A 124     5017   5466   5793   -176   -107    -78       C  
ATOM    788  O   THR A 124      10.948  -5.577  52.563  1.00 42.21           O  
ANISOU  788  O   THR A 124     4913   5423   5700   -152   -106    -70       O  
ATOM    789  CB  THR A 124      10.622  -5.424  49.290  1.00 38.25           C  
ANISOU  789  CB  THR A 124     4404   4934   5195    -38    -35    -48       C  
ATOM    790  OG1 THR A 124       9.818  -5.891  48.201  1.00 40.19           O  
ANISOU  790  OG1 THR A 124     4706   5126   5438     35     -6    -88       O  
ATOM    791  CG2 THR A 124      11.698  -6.455  49.575  1.00 40.53           C  
ANISOU  791  CG2 THR A 124     4628   5328   5445     36     -9     11       C  
ATOM    792  N   ALA A 125      10.836  -3.451  51.812  1.00 39.15           N  
ANISOU  792  N   ALA A 125     4567   4986   5323   -285   -152    -52       N  
ATOM    793  CA  ALA A 125      11.551  -2.943  52.979  1.00 42.93           C  
ANISOU  793  CA  ALA A 125     5050   5484   5778   -393   -212    -16       C  
ATOM    794  C   ALA A 125      10.732  -3.121  54.251  1.00 45.65           C  
ANISOU  794  C   ALA A 125     5486   5735   6123   -387   -218    -94       C  
ATOM    795  O   ALA A 125      11.288  -3.416  55.318  1.00 43.51           O  
ANISOU  795  O   ALA A 125     5203   5499   5830   -426   -249    -74       O  
ATOM    796  CB  ALA A 125      11.912  -1.472  52.783  1.00 40.24           C  
ANISOU  796  CB  ALA A 125     4751   5118   5419   -525   -274     25       C  
ATOM    797  N   VAL A 126       9.407  -2.962  54.158  1.00 45.62           N  
ANISOU  797  N   VAL A 126     5566   5627   6141   -334   -188   -171       N  
ATOM    798  CA  VAL A 126       8.570  -3.178  55.338  1.00 44.77           C  
ANISOU  798  CA  VAL A 126     5533   5450   6028   -308   -180   -229       C  
ATOM    799  C   VAL A 126       8.639  -4.637  55.775  1.00 45.25           C  
ANISOU  799  C   VAL A 126     5530   5564   6097   -243   -156   -233       C  
ATOM    800  O   VAL A 126       8.768  -4.943  56.972  1.00 41.80           O  
ANISOU  800  O   VAL A 126     5112   5126   5642   -259   -172   -243       O  
ATOM    801  CB  VAL A 126       7.117  -2.752  55.059  1.00 43.90           C  
ANISOU  801  CB  VAL A 126     5495   5249   5935   -248   -143   -280       C  
ATOM    802  CG1 VAL A 126       6.188  -3.281  56.149  1.00 35.63           C  
ANISOU  802  CG1 VAL A 126     4486   4167   4883   -192   -117   -319       C  
ATOM    803  CG2 VAL A 126       7.016  -1.248  54.956  1.00 36.40           C  
ANISOU  803  CG2 VAL A 126     4648   4223   4960   -301   -167   -282       C  
ATOM    804  N   ALA A 127       8.565  -5.558  54.811  1.00 35.50           N  
ANISOU  804  N   ALA A 127     4240   4367   4882   -169   -122   -226       N  
ATOM    805  CA  ALA A 127       8.631  -6.974  55.152  1.00 43.39           C  
ANISOU  805  CA  ALA A 127     5211   5397   5877   -103   -104   -228       C  
ATOM    806  C   ALA A 127       9.974  -7.324  55.777  1.00 43.26           C  
ANISOU  806  C   ALA A 127     5131   5473   5835   -122   -122   -172       C  
ATOM    807  O   ALA A 127      10.036  -8.099  56.738  1.00 42.36           O  
ANISOU  807  O   ALA A 127     5016   5367   5711   -104   -125   -179       O  
ATOM    808  CB  ALA A 127       8.387  -7.830  53.910  1.00 41.30           C  
ANISOU  808  CB  ALA A 127     4940   5137   5615    -23    -72   -228       C  
ATOM    809  N   PHE A 128      11.057  -6.734  55.264  1.00 42.18           N  
ANISOU  809  N   PHE A 128     4929   5416   5682   -165   -138   -101       N  
ATOM    810  CA  PHE A 128      12.375  -6.999  55.829  1.00 45.28           C  
ANISOU  810  CA  PHE A 128     5235   5925   6045   -192   -160    -17       C  
ATOM    811  C   PHE A 128      12.496  -6.439  57.241  1.00 47.95           C  
ANISOU  811  C   PHE A 128     5612   6239   6369   -301   -220    -22       C  
ATOM    812  O   PHE A 128      13.112  -7.063  58.113  1.00 46.12           O  
ANISOU  812  O   PHE A 128     5337   6070   6118   -303   -235     14       O  
ATOM    813  CB  PHE A 128      13.453  -6.410  54.923  1.00 51.47           C  
ANISOU  813  CB  PHE A 128     5924   6819   6811   -226   -168     85       C  
ATOM    814  CG  PHE A 128      14.829  -6.919  55.212  1.00 60.51           C  
ANISOU  814  CG  PHE A 128     6943   8127   7923   -215   -171    206       C  
ATOM    815  CD1 PHE A 128      15.304  -8.055  54.580  1.00 65.52           C  
ANISOU  815  CD1 PHE A 128     7514   8846   8534    -59   -101    253       C  
ATOM    816  CD2 PHE A 128      15.653  -6.259  56.113  1.00 65.16           C  
ANISOU  816  CD2 PHE A 128     7485   8783   8490   -356   -248    285       C  
ATOM    817  CE1 PHE A 128      16.576  -8.529  54.843  1.00 69.99           C  
ANISOU  817  CE1 PHE A 128     7952   9581   9062    -23    -92    383       C  
ATOM    818  CE2 PHE A 128      16.928  -6.727  56.382  1.00 66.86           C  
ANISOU  818  CE2 PHE A 128     7559   9173   8671   -349   -255    421       C  
ATOM    819  CZ  PHE A 128      17.390  -7.865  55.747  1.00 69.20           C  
ANISOU  819  CZ  PHE A 128     7771   9570   8950   -172   -169    475       C  
ATOM    820  N   ASP A 129      11.907  -5.268  57.490  1.00 47.16           N  
ANISOU  820  N   ASP A 129     5610   6041   6267   -386   -256    -67       N  
ATOM    821  CA  ASP A 129      11.966  -4.694  58.828  1.00 44.37           C  
ANISOU  821  CA  ASP A 129     5339   5641   5880   -483   -315    -80       C  
ATOM    822  C   ASP A 129      11.216  -5.566  59.828  1.00 47.74           C  
ANISOU  822  C   ASP A 129     5806   6022   6310   -412   -285   -145       C  
ATOM    823  O   ASP A 129      11.690  -5.786  60.954  1.00 44.86           O  
ANISOU  823  O   ASP A 129     5447   5683   5916   -458   -322   -127       O  
ATOM    824  CB  ASP A 129      11.395  -3.277  58.803  1.00 42.61           C  
ANISOU  824  CB  ASP A 129     5252   5300   5638   -556   -347   -121       C  
ATOM    825  CG  ASP A 129      11.494  -2.579  60.149  1.00 49.06           C  
ANISOU  825  CG  ASP A 129     6200   6046   6395   -656   -414   -136       C  
ATOM    826  OD1 ASP A 129      12.618  -2.201  60.550  1.00 50.73           O  
ANISOU  826  OD1 ASP A 129     6394   6316   6564   -789   -498    -58       O  
ATOM    827  OD2 ASP A 129      10.442  -2.394  60.801  1.00 49.27           O  
ANISOU  827  OD2 ASP A 129     6351   5962   6405   -601   -385   -216       O  
ATOM    828  N   ARG A 130      10.064  -6.108  59.422  1.00 45.12           N  
ANISOU  828  N   ARG A 130     5497   5635   6013   -309   -224   -207       N  
ATOM    829  CA  ARG A 130       9.342  -7.005  60.322  1.00 47.86           C  
ANISOU  829  CA  ARG A 130     5868   5953   6363   -250   -200   -250       C  
ATOM    830  C   ARG A 130      10.110  -8.303  60.540  1.00 45.62           C  
ANISOU  830  C   ARG A 130     5500   5756   6078   -208   -195   -210       C  
ATOM    831  O   ARG A 130      10.183  -8.812  61.669  1.00 44.27           O  
ANISOU  831  O   ARG A 130     5339   5593   5891   -212   -207   -214       O  
ATOM    832  CB  ARG A 130       7.945  -7.288  59.773  1.00 54.23           C  
ANISOU  832  CB  ARG A 130     6704   6698   7202   -171   -150   -298       C  
ATOM    833  CG  ARG A 130       7.064  -6.048  59.633  1.00 61.93           C  
ANISOU  833  CG  ARG A 130     7764   7595   8174   -182   -141   -329       C  
ATOM    834  CD  ARG A 130       6.739  -5.435  60.992  1.00 64.68           C  
ANISOU  834  CD  ARG A 130     8213   7887   8476   -201   -151   -355       C  
ATOM    835  NE  ARG A 130       7.803  -4.554  61.467  1.00 67.45           N  
ANISOU  835  NE  ARG A 130     8620   8228   8779   -304   -213   -338       N  
ATOM    836  CZ  ARG A 130       8.019  -4.257  62.744  1.00 70.89           C  
ANISOU  836  CZ  ARG A 130     9146   8632   9159   -348   -246   -349       C  
ATOM    837  NH1 ARG A 130       7.246  -4.773  63.690  1.00 72.26           N  
ANISOU  837  NH1 ARG A 130     9353   8785   9319   -281   -210   -380       N  
ATOM    838  NH2 ARG A 130       9.015  -3.448  63.075  1.00 74.91           N  
ANISOU  838  NH2 ARG A 130     9715   9131   9617   -469   -323   -320       N  
ATOM    839  N   TYR A 131      10.711  -8.835  59.475  1.00 43.97           N  
ANISOU  839  N   TYR A 131     5216   5612   5878   -156   -172   -167       N  
ATOM    840  CA  TYR A 131      11.502 -10.050  59.607  1.00 44.26           C  
ANISOU  840  CA  TYR A 131     5188   5730   5899    -87   -157   -119       C  
ATOM    841  C   TYR A 131      12.669  -9.840  60.557  1.00 46.93           C  
ANISOU  841  C   TYR A 131     5463   6160   6207   -158   -202    -47       C  
ATOM    842  O   TYR A 131      13.003 -10.728  61.345  1.00 49.55           O  
ANISOU  842  O   TYR A 131     5772   6531   6523   -123   -201    -27       O  
ATOM    843  CB  TYR A 131      12.005 -10.481  58.232  1.00 38.87           C  
ANISOU  843  CB  TYR A 131     4456   5101   5211     -1   -117    -76       C  
ATOM    844  CG  TYR A 131      12.854 -11.729  58.203  1.00 37.10           C  
ANISOU  844  CG  TYR A 131     4185   4959   4954    109    -84    -17       C  
ATOM    845  CD1 TYR A 131      14.227 -11.672  58.430  1.00 43.32           C  
ANISOU  845  CD1 TYR A 131     4859   5889   5712    105    -91     93       C  
ATOM    846  CD2 TYR A 131      12.293 -12.960  57.900  1.00 40.33           C  
ANISOU  846  CD2 TYR A 131     4669   5304   5351    218    -49    -58       C  
ATOM    847  CE1 TYR A 131      15.011 -12.812  58.383  1.00 41.77           C  
ANISOU  847  CE1 TYR A 131     4618   5778   5476    236    -48    160       C  
ATOM    848  CE2 TYR A 131      13.068 -14.104  57.844  1.00 42.99           C  
ANISOU  848  CE2 TYR A 131     4993   5698   5642    341    -14     -5       C  
ATOM    849  CZ  TYR A 131      14.425 -14.023  58.089  1.00 46.41           C  
ANISOU  849  CZ  TYR A 131     5307   6280   6047    364     -5    104       C  
ATOM    850  OH  TYR A 131      15.193 -15.160  58.034  1.00 52.79           O  
ANISOU  850  OH  TYR A 131     6104   7154   6802    514     43    168       O  
ATOM    851  N   MET A 132      13.294  -8.664  60.511  1.00 46.17           N  
ANISOU  851  N   MET A 132     5346   6100   6097   -271   -251      1       N  
ATOM    852  CA  MET A 132      14.400  -8.411  61.425  1.00 44.62           C  
ANISOU  852  CA  MET A 132     5094   5998   5864   -370   -315     87       C  
ATOM    853  C   MET A 132      13.899  -8.276  62.853  1.00 47.90           C  
ANISOU  853  C   MET A 132     5608   6333   6260   -431   -355     27       C  
ATOM    854  O   MET A 132      14.504  -8.828  63.779  1.00 48.84           O  
ANISOU  854  O   MET A 132     5686   6517   6355   -447   -380     72       O  
ATOM    855  CB  MET A 132      15.171  -7.163  61.004  1.00 45.99           C  
ANISOU  855  CB  MET A 132     5235   6223   6017   -505   -378    166       C  
ATOM    856  CG  MET A 132      15.893  -7.307  59.674  1.00 54.21           C  
ANISOU  856  CG  MET A 132     6149   7382   7065   -446   -339    257       C  
ATOM    857  SD  MET A 132      17.097  -8.653  59.654  1.00 63.03           S  
ANISOU  857  SD  MET A 132     7098   8693   8159   -321   -293    387       S  
ATOM    858  CE  MET A 132      18.326  -8.023  60.800  1.00 63.06           C  
ANISOU  858  CE  MET A 132     7014   8828   8118   -511   -407    527       C  
ATOM    859  N   ALA A 133      12.779  -7.575  63.052  1.00 46.11           N  
ANISOU  859  N   ALA A 133     5514   5970   6036   -450   -352    -68       N  
ATOM    860  CA  ALA A 133      12.292  -7.382  64.412  1.00 45.02           C  
ANISOU  860  CA  ALA A 133     5485   5757   5864   -490   -379   -120       C  
ATOM    861  C   ALA A 133      11.873  -8.696  65.058  1.00 46.51           C  
ANISOU  861  C   ALA A 133     5648   5955   6067   -393   -336   -146       C  
ATOM    862  O   ALA A 133      12.031  -8.867  66.271  1.00 50.88           O  
ANISOU  862  O   ALA A 133     6236   6511   6585   -430   -367   -146       O  
ATOM    863  CB  ALA A 133      11.126  -6.397  64.420  1.00 41.03           C  
ANISOU  863  CB  ALA A 133     5126   5113   5348   -489   -364   -204       C  
ATOM    864  N   ILE A 134      11.353  -9.638  64.281  1.00 46.44           N  
ANISOU  864  N   ILE A 134     5595   5948   6102   -280   -273   -166       N  
ATOM    865  CA  ILE A 134      10.812 -10.865  64.846  1.00 47.16           C  
ANISOU  865  CA  ILE A 134     5689   6028   6202   -201   -241   -191       C  
ATOM    866  C   ILE A 134      11.831 -12.001  64.843  1.00 50.52           C  
ANISOU  866  C   ILE A 134     6023   6551   6621   -148   -237   -124       C  
ATOM    867  O   ILE A 134      11.899 -12.774  65.798  1.00 53.43           O  
ANISOU  867  O   ILE A 134     6392   6933   6975   -130   -242   -119       O  
ATOM    868  CB  ILE A 134       9.519 -11.253  64.099  1.00 48.15           C  
ANISOU  868  CB  ILE A 134     5849   6081   6364   -125   -190   -245       C  
ATOM    869  CG1 ILE A 134       8.393 -10.298  64.495  1.00 51.49           C  
ANISOU  869  CG1 ILE A 134     6358   6424   6783   -149   -182   -297       C  
ATOM    870  CG2 ILE A 134       9.115 -12.691  64.385  1.00 46.40           C  
ANISOU  870  CG2 ILE A 134     5624   5856   6149    -54   -170   -249       C  
ATOM    871  CD1 ILE A 134       7.149 -10.450  63.655  1.00 57.36           C  
ANISOU  871  CD1 ILE A 134     7114   7121   7561    -93   -142   -322       C  
ATOM    872  N   ILE A 135      12.644 -12.111  63.794  1.00 50.99           N  
ANISOU  872  N   ILE A 135     6005   6684   6683   -110   -222    -64       N  
ATOM    873  CA  ILE A 135      13.573 -13.227  63.663  1.00 50.28           C  
ANISOU  873  CA  ILE A 135     5839   6691   6576    -18   -198      9       C  
ATOM    874  C   ILE A 135      14.954 -12.915  64.243  1.00 52.61           C  
ANISOU  874  C   ILE A 135     6027   7126   6838    -83   -243    121       C  
ATOM    875  O   ILE A 135      15.639 -13.826  64.721  1.00 55.93           O  
ANISOU  875  O   ILE A 135     6389   7627   7235    -19   -233    185       O  
ATOM    876  CB  ILE A 135      13.673 -13.646  62.183  1.00 47.02           C  
ANISOU  876  CB  ILE A 135     5411   6289   6166     93   -144     25       C  
ATOM    877  CG1 ILE A 135      12.288 -13.989  61.637  1.00 46.99           C  
ANISOU  877  CG1 ILE A 135     5517   6151   6188    131   -119    -72       C  
ATOM    878  CG2 ILE A 135      14.592 -14.846  62.012  1.00 47.67           C  
ANISOU  878  CG2 ILE A 135     5443   6459   6211    228   -103    102       C  
ATOM    879  CD1 ILE A 135      11.596 -15.094  62.414  1.00 47.91           C  
ANISOU  879  CD1 ILE A 135     5702   6202   6301    169   -119   -112       C  
ATOM    880  N   HIS A 136      15.397 -11.657  64.201  1.00 49.69           N  
ANISOU  880  N   HIS A 136     5632   6790   6460   -213   -298    159       N  
ATOM    881  CA  HIS A 136      16.673 -11.248  64.794  1.00 48.30           C  
ANISOU  881  CA  HIS A 136     5356   6750   6245   -319   -366    284       C  
ATOM    882  C   HIS A 136      16.484  -9.968  65.594  1.00 47.71           C  
ANISOU  882  C   HIS A 136     5375   6605   6146   -503   -456    253       C  
ATOM    883  O   HIS A 136      16.999  -8.909  65.219  1.00 47.33           O  
ANISOU  883  O   HIS A 136     5312   6591   6082   -624   -514    311       O  
ATOM    884  CB  HIS A 136      17.740 -11.043  63.720  1.00 53.76           C  
ANISOU  884  CB  HIS A 136     5908   7592   6927   -300   -354    414       C  
ATOM    885  CG  HIS A 136      17.810 -12.148  62.717  1.00 58.16           C  
ANISOU  885  CG  HIS A 136     6421   8188   7491    -97   -253    429       C  
ATOM    886  ND1 HIS A 136      17.215 -12.063  61.477  1.00 60.23           N  
ANISOU  886  ND1 HIS A 136     6731   8380   7775    -22   -198    370       N  
ATOM    887  CD2 HIS A 136      18.399 -13.365  62.770  1.00 59.99           C  
ANISOU  887  CD2 HIS A 136     6588   8509   7697     55   -198    497       C  
ATOM    888  CE1 HIS A 136      17.442 -13.178  60.806  1.00 59.53           C  
ANISOU  888  CE1 HIS A 136     6624   8327   7666    161   -118    397       C  
ATOM    889  NE2 HIS A 136      18.156 -13.986  61.569  1.00 60.89           N  
ANISOU  889  NE2 HIS A 136     6734   8593   7808    220   -112    473       N  
ATOM    890  N   PRO A 137      15.776 -10.037  66.724  1.00 50.06           N  
ANISOU  890  N   PRO A 137     5786   6803   6430   -527   -473    169       N  
ATOM    891  CA  PRO A 137      15.517  -8.810  67.501  1.00 49.95           C  
ANISOU  891  CA  PRO A 137     5910   6696   6373   -679   -552    129       C  
ATOM    892  C   PRO A 137      16.775  -8.090  67.965  1.00 54.94           C  
ANISOU  892  C   PRO A 137     6502   7426   6948   -858   -667    251       C  
ATOM    893  O   PRO A 137      16.755  -6.860  68.098  1.00 56.44           O  
ANISOU  893  O   PRO A 137     6811   7540   7095  -1000   -743    240       O  
ATOM    894  CB  PRO A 137      14.681  -9.317  68.687  1.00 51.07           C  
ANISOU  894  CB  PRO A 137     6153   6750   6500   -636   -534     42       C  
ATOM    895  CG  PRO A 137      14.934 -10.793  68.753  1.00 50.04           C  
ANISOU  895  CG  PRO A 137     5909   6705   6399   -515   -482     76       C  
ATOM    896  CD  PRO A 137      15.166 -11.228  67.340  1.00 50.38           C  
ANISOU  896  CD  PRO A 137     5850   6806   6485   -414   -422    112       C  
ATOM    897  N   LEU A 138      17.859  -8.817  68.246  1.00 57.21           N  
ANISOU  897  N   LEU A 138     6633   7879   7225   -860   -688    377       N  
ATOM    898  CA  LEU A 138      19.078  -8.177  68.737  1.00 59.10           C  
ANISOU  898  CA  LEU A 138     6814   8238   7405  -1050   -811    522       C  
ATOM    899  C   LEU A 138      19.759  -7.321  67.673  1.00 61.27           C  
ANISOU  899  C   LEU A 138     7007   8594   7679  -1144   -852    627       C  
ATOM    900  O   LEU A 138      20.480  -6.375  68.013  1.00 62.23           O  
ANISOU  900  O   LEU A 138     7147   8755   7742  -1356   -980    723       O  
ATOM    901  CB  LEU A 138      20.050  -9.233  69.261  1.00 60.31           C  
ANISOU  901  CB  LEU A 138     6794   8572   7548  -1008   -813    651       C  
ATOM    902  CG  LEU A 138      20.081  -9.440  70.778  1.00 62.54           C  
ANISOU  902  CG  LEU A 138     7152   8829   7781  -1086   -880    638       C  
ATOM    903  CD1 LEU A 138      18.691  -9.742  71.316  1.00 62.03           C  
ANISOU  903  CD1 LEU A 138     7266   8571   7732   -986   -814    450       C  
ATOM    904  CD2 LEU A 138      21.065 -10.543  71.154  1.00 60.40           C  
ANISOU  904  CD2 LEU A 138     6691   8754   7505  -1020   -869    781       C  
ATOM    905  N   GLN A 139      19.571  -7.644  66.396  1.00 58.99           N  
ANISOU  905  N   GLN A 139     6635   8334   7445  -1000   -753    619       N  
ATOM    906  CA  GLN A 139      20.307  -6.949  65.347  1.00 62.58           C  
ANISOU  906  CA  GLN A 139     6984   8897   7898  -1072   -781    739       C  
ATOM    907  C   GLN A 139      19.709  -5.564  65.091  1.00 60.22           C  
ANISOU  907  C   GLN A 139     6861   8435   7584  -1210   -842    658       C  
ATOM    908  O   GLN A 139      18.488  -5.402  65.105  1.00 55.84           O  
ANISOU  908  O   GLN A 139     6473   7693   7051  -1139   -793    491       O  
ATOM    909  CB  GLN A 139      20.313  -7.776  64.063  1.00 65.79           C  
ANISOU  909  CB  GLN A 139     7262   9383   8353   -859   -650    757       C  
ATOM    910  CG  GLN A 139      21.066  -9.091  64.220  1.00 71.92           C  
ANISOU  910  CG  GLN A 139     7873  10329   9123   -709   -588    863       C  
ATOM    911  CD  GLN A 139      21.136  -9.904  62.942  1.00 78.72           C  
ANISOU  911  CD  GLN A 139     8644  11257  10006   -485   -459    885       C  
ATOM    912  OE1 GLN A 139      21.060  -9.362  61.835  1.00 82.16           O  
ANISOU  912  OE1 GLN A 139     9070  11692  10456   -478   -434    890       O  
ATOM    913  NE2 GLN A 139      21.287 -11.216  63.089  1.00 80.19           N  
ANISOU  913  NE2 GLN A 139     8786  11496  10188   -297   -378    900       N  
ATOM    914  N   PRO A 140      20.550  -4.554  64.870  1.00 64.93           N  
ANISOU  914  N   PRO A 140     7426   9105   8139  -1406   -953    787       N  
ATOM    915  CA  PRO A 140      20.032  -3.199  64.651  1.00 67.39           C  
ANISOU  915  CA  PRO A 140     7934   9248   8424  -1543  -1021    717       C  
ATOM    916  C   PRO A 140      19.176  -3.112  63.394  1.00 66.24           C  
ANISOU  916  C   PRO A 140     7808   9020   8341  -1394   -911    618       C  
ATOM    917  O   PRO A 140      19.434  -3.776  62.386  1.00 64.14           O  
ANISOU  917  O   PRO A 140     7370   8877   8123  -1258   -820    671       O  
ATOM    918  CB  PRO A 140      21.306  -2.354  64.519  1.00 69.39           C  
ANISOU  918  CB  PRO A 140     8099   9645   8622  -1783  -1165    919       C  
ATOM    919  CG  PRO A 140      22.334  -3.317  64.017  1.00 69.03           C  
ANISOU  919  CG  PRO A 140     7751   9873   8605  -1690  -1109   1095       C  
ATOM    920  CD  PRO A 140      22.011  -4.624  64.689  1.00 67.72           C  
ANISOU  920  CD  PRO A 140     7551   9713   8465  -1503  -1016   1022       C  
ATOM    921  N   ARG A 141      18.148  -2.274  63.462  1.00 66.32           N  
ANISOU  921  N   ARG A 141     8042   8817   8339  -1414   -918    478       N  
ATOM    922  CA  ARG A 141      17.289  -1.982  62.325  1.00 67.05           C  
ANISOU  922  CA  ARG A 141     8176   8819   8481  -1305   -833    390       C  
ATOM    923  C   ARG A 141      17.484  -0.527  61.908  1.00 64.71           C  
ANISOU  923  C   ARG A 141     7995   8450   8141  -1480   -930    427       C  
ATOM    924  O   ARG A 141      18.274   0.217  62.496  1.00 64.44           O  
ANISOU  924  O   ARG A 141     8019   8431   8035  -1693  -1068    520       O  
ATOM    925  CB  ARG A 141      15.827  -2.293  62.658  1.00 69.41           C  
ANISOU  925  CB  ARG A 141     8620   8946   8805  -1150   -743    212       C  
ATOM    926  CG  ARG A 141      15.548  -3.785  62.770  1.00 70.73           C  
ANISOU  926  CG  ARG A 141     8669   9181   9024   -971   -642    180       C  
ATOM    927  CD  ARG A 141      14.092  -4.092  63.091  1.00 72.71           C  
ANISOU  927  CD  ARG A 141     9046   9284   9298   -839   -563     31       C  
ATOM    928  NE  ARG A 141      13.746  -3.779  64.475  1.00 77.36           N  
ANISOU  928  NE  ARG A 141     9791   9775   9828   -893   -607    -23       N  
ATOM    929  CZ  ARG A 141      12.777  -2.943  64.833  1.00 79.47           C  
ANISOU  929  CZ  ARG A 141    10254   9881  10059   -886   -602   -115       C  
ATOM    930  NH1 ARG A 141      12.531  -2.721  66.118  1.00 79.85           N  
ANISOU  930  NH1 ARG A 141    10452   9848  10038   -919   -636   -158       N  
ATOM    931  NH2 ARG A 141      12.045  -2.341  63.905  1.00 80.58           N  
ANISOU  931  NH2 ARG A 141    10445   9947  10225   -833   -558   -160       N  
ATOM    932  N   LEU A 142      16.774  -0.127  60.859  1.00 61.28           N  
ANISOU  932  N   LEU A 142     7600   7937   7745  -1400   -866    362       N  
ATOM    933  CA  LEU A 142      16.941   1.218  60.331  1.00 59.14           C  
ANISOU  933  CA  LEU A 142     7437   7596   7436  -1551   -950    399       C  
ATOM    934  C   LEU A 142      16.459   2.275  61.319  1.00 55.68           C  
ANISOU  934  C   LEU A 142     7298   6945   6911  -1667  -1040    319       C  
ATOM    935  O   LEU A 142      15.386   2.153  61.913  1.00 53.65           O  
ANISOU  935  O   LEU A 142     7193   6543   6649  -1544   -977    179       O  
ATOM    936  CB  LEU A 142      16.184   1.365  59.015  1.00 57.79           C  
ANISOU  936  CB  LEU A 142     7252   7380   7326  -1420   -852    337       C  
ATOM    937  CG  LEU A 142      16.669   0.547  57.822  1.00 56.10           C  
ANISOU  937  CG  LEU A 142     6790   7351   7175  -1312   -769    419       C  
ATOM    938  CD1 LEU A 142      15.771   0.806  56.632  1.00 54.69           C  
ANISOU  938  CD1 LEU A 142     6646   7090   7042  -1198   -687    340       C  
ATOM    939  CD2 LEU A 142      18.116   0.889  57.497  1.00 55.77           C  
ANISOU  939  CD2 LEU A 142     6592   7497   7102  -1475   -859    618       C  
ATOM    940  N   SER A 143      17.265   3.322  61.479  1.00 55.32           N  
ANISOU  940  N   SER A 143     7346   6885   6789  -1905  -1192    419       N  
ATOM    941  CA  SER A 143      16.813   4.589  62.034  1.00 55.09           C  
ANISOU  941  CA  SER A 143     7650   6622   6661  -2019  -1283    349       C  
ATOM    942  C   SER A 143      15.947   5.322  61.011  1.00 58.25           C  
ANISOU  942  C   SER A 143     8155   6892   7086  -1928  -1219    271       C  
ATOM    943  O   SER A 143      15.974   5.022  59.815  1.00 56.84           O  
ANISOU  943  O   SER A 143     7782   6823   6990  -1848  -1144    307       O  
ATOM    944  CB  SER A 143      18.005   5.457  62.423  1.00 57.50           C  
ANISOU  944  CB  SER A 143     8027   6952   6867  -2329  -1485    499       C  
ATOM    945  OG  SER A 143      18.802   5.737  61.284  1.00 58.67           O  
ANISOU  945  OG  SER A 143     7989   7253   7051  -2432  -1523    647       O  
ATOM    946  N   LEU A 144      15.151   6.281  61.496  1.00 60.32           N  
ANISOU  946  N   LEU A 144     8739   6914   7265  -1926  -1242    166       N  
ATOM    947  CA  LEU A 144      14.251   7.009  60.603  1.00 64.39           C  
ANISOU  947  CA  LEU A 144     9371   7297   7795  -1821  -1176     93       C  
ATOM    948  C   LEU A 144      15.011   7.726  59.488  1.00 64.37           C  
ANISOU  948  C   LEU A 144     9299   7357   7803  -1981  -1256    211       C  
ATOM    949  O   LEU A 144      14.574   7.726  58.327  1.00 62.72           O  
ANISOU  949  O   LEU A 144     8988   7176   7668  -1869  -1167    197       O  
ATOM    950  CB  LEU A 144      13.422   8.019  61.400  1.00 67.64           C  
ANISOU  950  CB  LEU A 144    10170   7442   8089  -1797  -1200    -16       C  
ATOM    951  CG  LEU A 144      12.473   7.519  62.485  1.00 72.54           C  
ANISOU  951  CG  LEU A 144    10905   7977   8681  -1613  -1106   -137       C  
ATOM    952  CD1 LEU A 144      13.182   7.439  63.833  1.00 78.20           C  
ANISOU  952  CD1 LEU A 144    11735   8678   9301  -1765  -1223   -110       C  
ATOM    953  CD2 LEU A 144      11.257   8.429  62.568  1.00 73.53           C  
ANISOU  953  CD2 LEU A 144    11330   7874   8733  -1462  -1040   -245       C  
ATOM    954  N   THR A 145      16.155   8.338  59.814  1.00 64.90           N  
ANISOU  954  N   THR A 145     9416   7453   7791  -2253  -1431    341       N  
ATOM    955  CA  THR A 145      16.962   8.974  58.777  1.00 65.98           C  
ANISOU  955  CA  THR A 145     9457   7679   7935  -2424  -1515    482       C  
ATOM    956  C   THR A 145      17.514   7.942  57.803  1.00 64.38           C  
ANISOU  956  C   THR A 145     8857   7754   7849  -2340  -1424    582       C  
ATOM    957  O   THR A 145      17.606   8.200  56.593  1.00 65.71           O  
ANISOU  957  O   THR A 145     8916   7988   8064  -2328  -1393    636       O  
ATOM    958  CB  THR A 145      18.106   9.768  59.406  1.00 70.69           C  
ANISOU  958  CB  THR A 145    10173   8270   8414  -2757  -1737    627       C  
ATOM    959  OG1 THR A 145      19.048   8.861  59.991  1.00 77.19           O  
ANISOU  959  OG1 THR A 145    10762   9313   9253  -2834  -1776    742       O  
ATOM    960  CG2 THR A 145      17.579  10.705  60.480  1.00 66.85           C  
ANISOU  960  CG2 THR A 145    10124   7488   7788  -2828  -1830    519       C  
ATOM    961  N   ALA A 146      17.859   6.755  58.307  1.00 59.54           N  
ANISOU  961  N   ALA A 146     8043   7302   7277  -2265  -1374    606       N  
ATOM    962  CA  ALA A 146      18.289   5.685  57.421  1.00 56.62           C  
ANISOU  962  CA  ALA A 146     7334   7176   7003  -2138  -1267    685       C  
ATOM    963  C   ALA A 146      17.161   5.244  56.501  1.00 57.00           C  
ANISOU  963  C   ALA A 146     7352   7169   7135  -1880  -1097    551       C  
ATOM    964  O   ALA A 146      17.406   4.903  55.340  1.00 57.93           O  
ANISOU  964  O   ALA A 146     7276   7425   7311  -1806  -1029    614       O  
ATOM    965  CB  ALA A 146      18.807   4.502  58.236  1.00 55.77           C  
ANISOU  965  CB  ALA A 146     7058   7223   6909  -2091  -1244    727       C  
ATOM    966  N   THR A 147      15.918   5.262  56.988  1.00 55.79           N  
ANISOU  966  N   THR A 147     7391   6824   6984  -1743  -1031    379       N  
ATOM    967  CA  THR A 147      14.802   4.920  56.114  1.00 57.71           C  
ANISOU  967  CA  THR A 147     7609   7019   7300  -1524   -889    271       C  
ATOM    968  C   THR A 147      14.581   5.988  55.052  1.00 55.58           C  
ANISOU  968  C   THR A 147     7419   6674   7027  -1567   -905    283       C  
ATOM    969  O   THR A 147      14.240   5.666  53.912  1.00 54.56           O  
ANISOU  969  O   THR A 147     7164   6603   6964  -1445   -814    275       O  
ATOM    970  CB  THR A 147      13.528   4.710  56.924  1.00 59.85           C  
ANISOU  970  CB  THR A 147     8046   7130   7566  -1373   -816    114       C  
ATOM    971  OG1 THR A 147      13.103   5.959  57.475  1.00 69.77           O  
ANISOU  971  OG1 THR A 147     9595   8180   8735  -1450   -885     63       O  
ATOM    972  CG2 THR A 147      13.789   3.751  58.037  1.00 54.93           C  
ANISOU  972  CG2 THR A 147     7363   6571   6936  -1354   -814    108       C  
ATOM    973  N   LYS A 148      14.776   7.264  55.395  1.00 57.46           N  
ANISOU  973  N   LYS A 148     7878   6773   7179  -1743  -1027    304       N  
ATOM    974  CA  LYS A 148      14.669   8.292  54.362  1.00 60.80           C  
ANISOU  974  CA  LYS A 148     8375   7130   7596  -1798  -1053    332       C  
ATOM    975  C   LYS A 148      15.764   8.127  53.311  1.00 59.14           C  
ANISOU  975  C   LYS A 148     7908   7138   7423  -1892  -1079    494       C  
ATOM    976  O   LYS A 148      15.520   8.299  52.106  1.00 59.79           O  
ANISOU  976  O   LYS A 148     7918   7248   7550  -1826  -1020    503       O  
ATOM    977  CB  LYS A 148      14.721   9.683  54.993  1.00 67.41           C  
ANISOU  977  CB  LYS A 148     9537   7759   8317  -1978  -1193    329       C  
ATOM    978  CG  LYS A 148      13.449  10.071  55.736  1.00 73.61           C  
ANISOU  978  CG  LYS A 148    10611   8304   9051  -1832  -1138    168       C  
ATOM    979  CD  LYS A 148      13.501  11.517  56.208  1.00 83.42           C  
ANISOU  979  CD  LYS A 148    12218   9318  10160  -1993  -1272    165       C  
ATOM    980  CE  LYS A 148      12.236  11.904  56.967  1.00 89.11           C  
ANISOU  980  CE  LYS A 148    13239   9806  10813  -1810  -1200     14       C  
ATOM    981  NZ  LYS A 148      12.336  13.262  57.584  1.00 93.47           N  
ANISOU  981  NZ  LYS A 148    14200  10111  11205  -1955  -1335      6       N  
ATOM    982  N   VAL A 149      16.964   7.731  53.743  1.00 58.37           N  
ANISOU  982  N   VAL A 149     7656   7217   7306  -2031  -1156    632       N  
ATOM    983  CA  VAL A 149      18.034   7.450  52.788  1.00 56.46           C  
ANISOU  983  CA  VAL A 149     7137   7221   7093  -2087  -1160    808       C  
ATOM    984  C   VAL A 149      17.660   6.268  51.899  1.00 55.27           C  
ANISOU  984  C   VAL A 149     6776   7194   7031  -1828   -986    765       C  
ATOM    985  O   VAL A 149      17.869   6.296  50.678  1.00 53.49           O  
ANISOU  985  O   VAL A 149     6419   7070   6836  -1786   -937    831       O  
ATOM    986  CB  VAL A 149      19.360   7.199  53.530  1.00 56.96           C  
ANISOU  986  CB  VAL A 149     7063   7469   7111  -2269  -1271    983       C  
ATOM    987  CG1 VAL A 149      20.422   6.692  52.566  1.00 57.60           C  
ANISOU  987  CG1 VAL A 149     6818   7844   7222  -2265  -1237   1178       C  
ATOM    988  CG2 VAL A 149      19.827   8.469  54.221  1.00 59.79           C  
ANISOU  988  CG2 VAL A 149     7641   7709   7366  -2569  -1471   1053       C  
ATOM    989  N   VAL A 150      17.084   5.221  52.491  1.00 51.64           N  
ANISOU  989  N   VAL A 150     6301   6715   6605  -1656   -894    654       N  
ATOM    990  CA  VAL A 150      16.694   4.052  51.709  1.00 48.92           C  
ANISOU  990  CA  VAL A 150     5799   6461   6328  -1422   -745    608       C  
ATOM    991  C   VAL A 150      15.596   4.412  50.718  1.00 48.85           C  
ANISOU  991  C   VAL A 150     5878   6325   6356  -1310   -672    501       C  
ATOM    992  O   VAL A 150      15.563   3.905  49.592  1.00 50.73           O  
ANISOU  992  O   VAL A 150     5989   6655   6632  -1190   -586    520       O  
ATOM    993  CB  VAL A 150      16.267   2.908  52.647  1.00 46.23           C  
ANISOU  993  CB  VAL A 150     5453   6106   6006  -1289   -683    514       C  
ATOM    994  CG1 VAL A 150      15.591   1.788  51.861  1.00 45.39           C  
ANISOU  994  CG1 VAL A 150     5260   6028   5959  -1056   -542    438       C  
ATOM    995  CG2 VAL A 150      17.475   2.377  53.393  1.00 47.19           C  
ANISOU  995  CG2 VAL A 150     5432   6400   6097  -1372   -736    645       C  
ATOM    996  N   ILE A 151      14.700   5.318  51.106  1.00 48.57           N  
ANISOU  996  N   ILE A 151     6071   6081   6302  -1343   -705    398       N  
ATOM    997  CA  ILE A 151      13.639   5.739  50.200  1.00 46.99           C  
ANISOU  997  CA  ILE A 151     5953   5768   6133  -1239   -641    313       C  
ATOM    998  C   ILE A 151      14.222   6.495  49.012  1.00 48.92           C  
ANISOU  998  C   ILE A 151     6138   6076   6372  -1331   -676    419       C  
ATOM    999  O   ILE A 151      13.834   6.267  47.853  1.00 49.49           O  
ANISOU  999  O   ILE A 151     6133   6184   6486  -1219   -597    406       O  
ATOM   1000  CB  ILE A 151      12.603   6.577  50.972  1.00 45.09           C  
ANISOU 1000  CB  ILE A 151     5976   5299   5857  -1235   -663    199       C  
ATOM   1001  CG1 ILE A 151      11.782   5.662  51.889  1.00 43.64           C  
ANISOU 1001  CG1 ILE A 151     5815   5075   5692  -1090   -591     92       C  
ATOM   1002  CG2 ILE A 151      11.709   7.360  50.013  1.00 44.01           C  
ANISOU 1002  CG2 ILE A 151     5935   5052   5734  -1171   -625    153       C  
ATOM   1003  CD1 ILE A 151      10.948   6.389  52.914  1.00 43.55           C  
ANISOU 1003  CD1 ILE A 151     6055   4868   5624  -1078   -610      1       C  
ATOM   1004  N   CYS A 152      15.191   7.378  49.274  1.00 48.75           N  
ANISOU 1004  N   CYS A 152     6151   6077   6294  -1549   -803    537       N  
ATOM   1005  CA  CYS A 152      15.846   8.077  48.172  1.00 52.30           C  
ANISOU 1005  CA  CYS A 152     6526   6612   6736  -1656   -845    663       C  
ATOM   1006  C   CYS A 152      16.591   7.107  47.262  1.00 50.49           C  
ANISOU 1006  C   CYS A 152     6012   6630   6541  -1566   -766    771       C  
ATOM   1007  O   CYS A 152      16.578   7.260  46.035  1.00 51.10           O  
ANISOU 1007  O   CYS A 152     6015   6764   6638  -1518   -718    809       O  
ATOM   1008  CB  CYS A 152      16.802   9.138  48.712  1.00 60.82           C  
ANISOU 1008  CB  CYS A 152     7691   7680   7737  -1935  -1016    791       C  
ATOM   1009  SG  CYS A 152      15.968  10.533  49.483  1.00 67.59           S  
ANISOU 1009  SG  CYS A 152     8946   8214   8523  -2039  -1115    676       S  
ATOM   1010  N   VAL A 153      17.227   6.088  47.842  1.00 49.15           N  
ANISOU 1010  N   VAL A 153     5695   6608   6372  -1525   -743    821       N  
ATOM   1011  CA  VAL A 153      17.947   5.116  47.025  1.00 49.70           C  
ANISOU 1011  CA  VAL A 153     5517   6909   6456  -1405   -653    927       C  
ATOM   1012  C   VAL A 153      16.974   4.321  46.166  1.00 50.28           C  
ANISOU 1012  C   VAL A 153     5592   6934   6577  -1164   -513    798       C  
ATOM   1013  O   VAL A 153      17.244   4.036  44.990  1.00 50.01           O  
ANISOU 1013  O   VAL A 153     5440   7017   6545  -1071   -443    860       O  
ATOM   1014  CB  VAL A 153      18.791   4.192  47.921  1.00 48.92           C  
ANISOU 1014  CB  VAL A 153     5281   6966   6340  -1397   -657   1008       C  
ATOM   1015  CG1 VAL A 153      19.264   2.974  47.133  1.00 48.67           C  
ANISOU 1015  CG1 VAL A 153     5041   7134   6316  -1191   -528   1076       C  
ATOM   1016  CG2 VAL A 153      19.971   4.954  48.513  1.00 49.66           C  
ANISOU 1016  CG2 VAL A 153     5321   7169   6378  -1656   -805   1192       C  
ATOM   1017  N   ILE A 154      15.818   3.968  46.735  1.00 47.52           N  
ANISOU 1017  N   ILE A 154     5383   6415   6257  -1067   -476    626       N  
ATOM   1018  CA  ILE A 154      14.812   3.232  45.981  1.00 47.18           C  
ANISOU 1018  CA  ILE A 154     5357   6317   6253   -869   -366    512       C  
ATOM   1019  C   ILE A 154      14.345   4.056  44.796  1.00 50.79           C  
ANISOU 1019  C   ILE A 154     5860   6717   6720   -876   -357    505       C  
ATOM   1020  O   ILE A 154      14.209   3.542  43.679  1.00 41.23           O  
ANISOU 1020  O   ILE A 154     4581   5565   5518   -753   -280    508       O  
ATOM   1021  CB  ILE A 154      13.630   2.852  46.892  1.00 46.75           C  
ANISOU 1021  CB  ILE A 154     5439   6101   6224   -796   -345    356       C  
ATOM   1022  CG1 ILE A 154      14.014   1.722  47.848  1.00 44.88           C  
ANISOU 1022  CG1 ILE A 154     5136   5935   5981   -743   -327    355       C  
ATOM   1023  CG2 ILE A 154      12.418   2.471  46.060  1.00 46.75           C  
ANISOU 1023  CG2 ILE A 154     5485   6017   6259   -649   -265    252       C  
ATOM   1024  CD1 ILE A 154      12.922   1.386  48.831  1.00 39.54           C  
ANISOU 1024  CD1 ILE A 154     4584   5116   5325   -688   -313    220       C  
ATOM   1025  N   TRP A 155      14.108   5.352  45.014  1.00 42.06           N  
ANISOU 1025  N   TRP A 155     4890   5489   5604  -1016   -440    498       N  
ATOM   1026  CA  TRP A 155      13.675   6.183  43.898  1.00 45.30           C  
ANISOU 1026  CA  TRP A 155     5349   5841   6021  -1024   -435    498       C  
ATOM   1027  C   TRP A 155      14.777   6.366  42.862  1.00 46.83           C  
ANISOU 1027  C   TRP A 155     5386   6214   6194  -1081   -441    656       C  
ATOM   1028  O   TRP A 155      14.493   6.399  41.660  1.00 47.51           O  
ANISOU 1028  O   TRP A 155     5439   6320   6291  -1004   -386    657       O  
ATOM   1029  CB  TRP A 155      13.167   7.530  44.408  1.00 45.18           C  
ANISOU 1029  CB  TRP A 155     5543   5637   5985  -1147   -519    456       C  
ATOM   1030  CG  TRP A 155      11.706   7.486  44.722  1.00 43.07           C  
ANISOU 1030  CG  TRP A 155     5421   5199   5744  -1018   -466    305       C  
ATOM   1031  CD1 TRP A 155      11.128   7.469  45.957  1.00 41.38           C  
ANISOU 1031  CD1 TRP A 155     5338   4868   5518   -999   -477    220       C  
ATOM   1032  CD2 TRP A 155      10.634   7.423  43.775  1.00 42.34           C  
ANISOU 1032  CD2 TRP A 155     5344   5055   5688   -885   -390    240       C  
ATOM   1033  NE1 TRP A 155       9.760   7.412  45.839  1.00 41.24           N  
ANISOU 1033  NE1 TRP A 155     5402   4740   5526   -856   -407    116       N  
ATOM   1034  CE2 TRP A 155       9.431   7.385  44.509  1.00 42.50           C  
ANISOU 1034  CE2 TRP A 155     5490   4939   5718   -792   -359    130       C  
ATOM   1035  CE3 TRP A 155      10.574   7.406  42.376  1.00 42.46           C  
ANISOU 1035  CE3 TRP A 155     5278   5134   5723   -837   -349    274       C  
ATOM   1036  CZ2 TRP A 155       8.181   7.329  43.893  1.00 43.17           C  
ANISOU 1036  CZ2 TRP A 155     5604   4963   5834   -663   -293     67       C  
ATOM   1037  CZ3 TRP A 155       9.332   7.344  41.765  1.00 42.18           C  
ANISOU 1037  CZ3 TRP A 155     5289   5021   5717   -716   -289    198       C  
ATOM   1038  CH2 TRP A 155       8.152   7.306  42.524  1.00 43.55           C  
ANISOU 1038  CH2 TRP A 155     5571   5072   5903   -635   -265    102       C  
ATOM   1039  N   VAL A 156      16.038   6.444  43.289  1.00 46.50           N  
ANISOU 1039  N   VAL A 156     5232   6319   6116  -1210   -506    801       N  
ATOM   1040  CA  VAL A 156      17.119   6.564  42.315  1.00 49.25           C  
ANISOU 1040  CA  VAL A 156     5402   6874   6439  -1251   -503    979       C  
ATOM   1041  C   VAL A 156      17.170   5.323  41.436  1.00 49.51           C  
ANISOU 1041  C   VAL A 156     5295   7038   6476  -1023   -364    980       C  
ATOM   1042  O   VAL A 156      17.264   5.412  40.204  1.00 50.39           O  
ANISOU 1042  O   VAL A 156     5346   7222   6579   -962   -312   1030       O  
ATOM   1043  CB  VAL A 156      18.467   6.809  43.017  1.00 52.93           C  
ANISOU 1043  CB  VAL A 156     5751   7500   6860  -1437   -602   1162       C  
ATOM   1044  CG1 VAL A 156      19.599   6.716  42.006  1.00 54.04           C  
ANISOU 1044  CG1 VAL A 156     5662   7902   6970  -1438   -573   1371       C  
ATOM   1045  CG2 VAL A 156      18.481   8.168  43.702  1.00 53.03           C  
ANISOU 1045  CG2 VAL A 156     5938   7367   6845  -1690   -759   1178       C  
ATOM   1046  N   LEU A 157      17.082   4.144  42.056  1.00 49.68           N  
ANISOU 1046  N   LEU A 157     5290   7083   6505   -891   -305    919       N  
ATOM   1047  CA  LEU A 157      17.103   2.908  41.281  1.00 48.53           C  
ANISOU 1047  CA  LEU A 157     5062   7033   6346   -665   -178    910       C  
ATOM   1048  C   LEU A 157      15.880   2.795  40.378  1.00 48.72           C  
ANISOU 1048  C   LEU A 157     5206   6911   6394   -549   -120    769       C  
ATOM   1049  O   LEU A 157      15.986   2.321  39.241  1.00 42.70           O  
ANISOU 1049  O   LEU A 157     4397   6225   5603   -418    -40    797       O  
ATOM   1050  CB  LEU A 157      17.192   1.702  42.216  1.00 48.83           C  
ANISOU 1050  CB  LEU A 157     5079   7094   6380   -560   -140    867       C  
ATOM   1051  CG  LEU A 157      18.445   1.651  43.093  1.00 50.41           C  
ANISOU 1051  CG  LEU A 157     5138   7466   6550   -655   -190   1023       C  
ATOM   1052  CD1 LEU A 157      18.500   0.365  43.889  1.00 46.52           C  
ANISOU 1052  CD1 LEU A 157     4626   6999   6051   -519   -136    979       C  
ATOM   1053  CD2 LEU A 157      19.691   1.809  42.237  1.00 54.10           C  
ANISOU 1053  CD2 LEU A 157     5409   8181   6967   -658   -167   1240       C  
ATOM   1054  N   ALA A 158      14.719   3.260  40.850  1.00 44.35           N  
ANISOU 1054  N   ALA A 158     4811   6156   5885   -595   -160    629       N  
ATOM   1055  CA  ALA A 158      13.509   3.178  40.040  1.00 42.80           C  
ANISOU 1055  CA  ALA A 158     4715   5835   5712   -498   -115    514       C  
ATOM   1056  C   ALA A 158      13.607   4.074  38.814  1.00 42.72           C  
ANISOU 1056  C   ALA A 158     4691   5847   5692   -542   -120    578       C  
ATOM   1057  O   ALA A 158      13.247   3.664  37.700  1.00 43.82           O  
ANISOU 1057  O   ALA A 158     4831   5999   5820   -427    -57    557       O  
ATOM   1058  CB  ALA A 158      12.291   3.560  40.882  1.00 39.87           C  
ANISOU 1058  CB  ALA A 158     4494   5272   5384   -533   -152    383       C  
ATOM   1059  N   LEU A 159      14.108   5.298  38.998  1.00 43.90           N  
ANISOU 1059  N   LEU A 159     4842   6000   5839   -715   -203    660       N  
ATOM   1060  CA  LEU A 159      14.254   6.205  37.868  1.00 43.79           C  
ANISOU 1060  CA  LEU A 159     4816   6010   5814   -772   -217    732       C  
ATOM   1061  C   LEU A 159      15.305   5.699  36.889  1.00 46.90           C  
ANISOU 1061  C   LEU A 159     5038   6621   6161   -702   -155    871       C  
ATOM   1062  O   LEU A 159      15.115   5.784  35.669  1.00 45.59           O  
ANISOU 1062  O   LEU A 159     4863   6478   5982   -634   -107    884       O  
ATOM   1063  CB  LEU A 159      14.593   7.607  38.371  1.00 43.50           C  
ANISOU 1063  CB  LEU A 159     4843   5913   5771   -989   -335    796       C  
ATOM   1064  CG  LEU A 159      13.545   8.169  39.340  1.00 49.39           C  
ANISOU 1064  CG  LEU A 159     5790   6434   6542  -1030   -384    661       C  
ATOM   1065  CD1 LEU A 159      14.002   9.483  39.977  1.00 48.85           C  
ANISOU 1065  CD1 LEU A 159     5828   6290   6443  -1248   -512    726       C  
ATOM   1066  CD2 LEU A 159      12.194   8.336  38.657  1.00 45.53           C  
ANISOU 1066  CD2 LEU A 159     5408   5807   6085   -919   -334    546       C  
ATOM   1067  N   LEU A 160      16.397   5.119  37.396  1.00 48.40           N  
ANISOU 1067  N   LEU A 160     5091   6979   6319   -698   -145    981       N  
ATOM   1068  CA  LEU A 160      17.391   4.564  36.484  1.00 49.15           C  
ANISOU 1068  CA  LEU A 160     5019   7298   6356   -590    -65   1127       C  
ATOM   1069  C   LEU A 160      16.831   3.381  35.704  1.00 48.08           C  
ANISOU 1069  C   LEU A 160     4928   7141   6197   -348     54   1030       C  
ATOM   1070  O   LEU A 160      17.113   3.235  34.509  1.00 44.95           O  
ANISOU 1070  O   LEU A 160     4485   6842   5753   -245    124   1095       O  
ATOM   1071  CB  LEU A 160      18.647   4.152  37.253  1.00 52.49           C  
ANISOU 1071  CB  LEU A 160     5279   7919   6746   -619    -75   1279       C  
ATOM   1072  CG  LEU A 160      19.584   5.291  37.656  1.00 54.62           C  
ANISOU 1072  CG  LEU A 160     5456   8292   7007   -870   -196   1455       C  
ATOM   1073  CD1 LEU A 160      20.676   4.789  38.592  1.00 55.18           C  
ANISOU 1073  CD1 LEU A 160     5372   8547   7048   -905   -217   1596       C  
ATOM   1074  CD2 LEU A 160      20.187   5.940  36.421  1.00 53.26           C  
ANISOU 1074  CD2 LEU A 160     5172   8265   6797   -907   -185   1616       C  
ATOM   1075  N   LEU A 161      16.024   2.534  36.351  1.00 45.96           N  
ANISOU 1075  N   LEU A 161     4767   6742   5952   -261     73    879       N  
ATOM   1076  CA  LEU A 161      15.453   1.391  35.643  1.00 47.07           C  
ANISOU 1076  CA  LEU A 161     4985   6841   6059    -56    165    788       C  
ATOM   1077  C   LEU A 161      14.463   1.841  34.575  1.00 46.88           C  
ANISOU 1077  C   LEU A 161     5067   6699   6048    -50    165    710       C  
ATOM   1078  O   LEU A 161      14.424   1.273  33.477  1.00 42.44           O  
ANISOU 1078  O   LEU A 161     4532   6168   5427     89    236    712       O  
ATOM   1079  CB  LEU A 161      14.774   0.440  36.630  1.00 43.41           C  
ANISOU 1079  CB  LEU A 161     4615   6261   5619      3    165    656       C  
ATOM   1080  CG  LEU A 161      14.199  -0.847  36.024  1.00 44.12           C  
ANISOU 1080  CG  LEU A 161     4812   6291   5661    193    239    566       C  
ATOM   1081  CD1 LEU A 161      15.296  -1.658  35.346  1.00 44.24           C  
ANISOU 1081  CD1 LEU A 161     4756   6477   5577    368    336    678       C  
ATOM   1082  CD2 LEU A 161      13.475  -1.693  37.070  1.00 42.10           C  
ANISOU 1082  CD2 LEU A 161     4648   5914   5434    216    221    447       C  
ATOM   1083  N   ALA A 162      13.663   2.866  34.875  1.00 45.75           N  
ANISOU 1083  N   ALA A 162     4996   6418   5970   -192     88    646       N  
ATOM   1084  CA  ALA A 162      12.676   3.326  33.910  1.00 41.12           C  
ANISOU 1084  CA  ALA A 162     4502   5723   5398   -186     85    582       C  
ATOM   1085  C   ALA A 162      13.284   4.198  32.821  1.00 44.62           C  
ANISOU 1085  C   ALA A 162     4877   6264   5814   -234     88    699       C  
ATOM   1086  O   ALA A 162      12.646   4.396  31.779  1.00 45.31           O  
ANISOU 1086  O   ALA A 162     5024   6298   5894   -196    104    666       O  
ATOM   1087  CB  ALA A 162      11.563   4.095  34.623  1.00 40.30           C  
ANISOU 1087  CB  ALA A 162     4504   5444   5365   -289     16    483       C  
ATOM   1088  N   PHE A 163      14.510   4.687  33.019  1.00 43.09           N  
ANISOU 1088  N   PHE A 163     4552   6221   5600   -320     68    847       N  
ATOM   1089  CA  PHE A 163      15.090   5.665  32.100  1.00 44.06           C  
ANISOU 1089  CA  PHE A 163     4602   6437   5700   -402     51    977       C  
ATOM   1090  C   PHE A 163      15.097   5.237  30.636  1.00 47.63           C  
ANISOU 1090  C   PHE A 163     5043   6962   6093   -252    140   1002       C  
ATOM   1091  O   PHE A 163      14.720   6.058  29.786  1.00 48.24           O  
ANISOU 1091  O   PHE A 163     5155   6995   6178   -307    119   1010       O  
ATOM   1092  CB  PHE A 163      16.507   6.030  32.559  1.00 48.25           C  
ANISOU 1092  CB  PHE A 163     4967   7159   6205   -513     17   1163       C  
ATOM   1093  CG  PHE A 163      17.175   7.053  31.680  1.00 51.44           C  
ANISOU 1093  CG  PHE A 163     5283   7678   6583   -623    -13   1323       C  
ATOM   1094  CD1 PHE A 163      18.100   6.668  30.725  1.00 51.49           C  
ANISOU 1094  CD1 PHE A 163     5138   7907   6517   -516     72   1476       C  
ATOM   1095  CD2 PHE A 163      16.859   8.397  31.795  1.00 52.67           C  
ANISOU 1095  CD2 PHE A 163     5519   7716   6778   -824   -121   1324       C  
ATOM   1096  CE1 PHE A 163      18.705   7.606  29.910  1.00 54.38           C  
ANISOU 1096  CE1 PHE A 163     5412   8392   6859   -622     45   1636       C  
ATOM   1097  CE2 PHE A 163      17.458   9.338  30.981  1.00 55.23           C  
ANISOU 1097  CE2 PHE A 163     5771   8139   7077   -938   -157   1476       C  
ATOM   1098  CZ  PHE A 163      18.381   8.942  30.039  1.00 54.89           C  
ANISOU 1098  CZ  PHE A 163     5554   8332   6968   -844    -75   1635       C  
ATOM   1099  N   PRO A 164      15.483   4.016  30.257  1.00 46.62           N  
ANISOU 1099  N   PRO A 164     4883   6936   5895    -60    238   1019       N  
ATOM   1100  CA  PRO A 164      15.561   3.680  28.857  1.00 48.14           C  
ANISOU 1100  CA  PRO A 164     5088   7193   6008     82    321   1053       C  
ATOM   1101  C   PRO A 164      14.225   3.859  28.136  1.00 48.88           C  
ANISOU 1101  C   PRO A 164     5343   7104   6124     89    302    916       C  
ATOM   1102  O   PRO A 164      14.234   4.282  27.051  1.00 46.91           O  
ANISOU 1102  O   PRO A 164     5096   6887   5839    104    322    962       O  
ATOM   1103  CB  PRO A 164      15.935   2.203  28.858  1.00 47.38           C  
ANISOU 1103  CB  PRO A 164     4997   7180   5825    305    424   1057       C  
ATOM   1104  CG  PRO A 164      16.566   1.978  30.187  1.00 45.84           C  
ANISOU 1104  CG  PRO A 164     4699   7060   5658    256    402   1109       C  
ATOM   1105  CD  PRO A 164      15.911   2.955  31.126  1.00 47.02           C  
ANISOU 1105  CD  PRO A 164     4897   7049   5917     46    283   1019       C  
ATOM   1106  N   GLN A 165      13.125   3.498  28.777  1.00 49.75           N  
ANISOU 1106  N   GLN A 165     5577   7035   6291     71    260    762       N  
ATOM   1107  CA  GLN A 165      11.798   3.641  28.143  1.00 47.51           C  
ANISOU 1107  CA  GLN A 165     5428   6598   6027     71    235    654       C  
ATOM   1108  C   GLN A 165      11.495   5.118  27.905  1.00 46.36           C  
ANISOU 1108  C   GLN A 165     5275   6393   5946    -84    166    674       C  
ATOM   1109  O   GLN A 165      10.873   5.433  26.933  1.00 49.34           O  
ANISOU 1109  O   GLN A 165     5714   6716   6317    -78    162    652       O  
ATOM   1110  CB  GLN A 165      10.748   2.827  28.888  1.00 45.97           C  
ANISOU 1110  CB  GLN A 165     5345   6255   5868     93    208    514       C  
ATOM   1111  CG  GLN A 165      10.916   1.338  28.669  1.00 48.18           C  
ANISOU 1111  CG  GLN A 165     5699   6545   6063    257    269    474       C  
ATOM   1112  CD  GLN A 165       9.592   0.691  28.390  1.00 50.36           C  
ANISOU 1112  CD  GLN A 165     6131   6666   6338    277    235    353       C  
ATOM   1113  OE1 GLN A 165       8.558   1.201  28.767  1.00 47.67           O  
ANISOU 1113  OE1 GLN A 165     5813   6221   6078    176    171    295       O  
ATOM   1114  NE2 GLN A 165       9.622  -0.435  27.721  1.00 41.17           N  
ANISOU 1114  NE2 GLN A 165     5083   5488   5071    410    276    326       N  
ATOM   1115  N   GLY A 166      11.858   5.966  28.842  1.00 43.73           N  
ANISOU 1115  N   GLY A 166     4886   6063   5667   -224    107    719       N  
ATOM   1116  CA  GLY A 166      11.656   7.401  28.648  1.00 43.58           C  
ANISOU 1116  CA  GLY A 166     4882   5989   5688   -364     43    756       C  
ATOM   1117  C   GLY A 166      12.531   7.933  27.534  1.00 45.24           C  
ANISOU 1117  C   GLY A 166     4997   6343   5848   -389     62    899       C  
ATOM   1118  O   GLY A 166      12.047   8.704  26.738  1.00 45.84           O  
ANISOU 1118  O   GLY A 166     5112   6372   5933   -443     37    915       O  
ATOM   1119  N   TYR A 167      13.761   7.444  27.457  1.00 44.50           N  
ANISOU 1119  N   TYR A 167     4774   6438   5695   -338    113   1016       N  
ATOM   1120  CA  TYR A 167      14.753   7.971  26.528  1.00 45.80           C  
ANISOU 1120  CA  TYR A 167     4818   6777   5806   -364    135   1186       C  
ATOM   1121  C   TYR A 167      14.422   7.602  25.084  1.00 45.89           C  
ANISOU 1121  C   TYR A 167     4871   6809   5757   -221    211   1172       C  
ATOM   1122  O   TYR A 167      14.576   8.428  24.177  1.00 46.51           O  
ANISOU 1122  O   TYR A 167     4920   6931   5820   -278    201   1255       O  
ATOM   1123  CB  TYR A 167      16.134   7.454  26.928  1.00 46.92           C  
ANISOU 1123  CB  TYR A 167     4792   7139   5897   -332    176   1335       C  
ATOM   1124  CG  TYR A 167      17.280   8.017  26.122  1.00 51.93           C  
ANISOU 1124  CG  TYR A 167     5263   7994   6473   -373    195   1551       C  
ATOM   1125  CD1 TYR A 167      17.824   7.303  25.062  1.00 55.01           C  
ANISOU 1125  CD1 TYR A 167     5584   8551   6767   -178    316   1634       C  
ATOM   1126  CD2 TYR A 167      17.824   9.256  26.427  1.00 53.57           C  
ANISOU 1126  CD2 TYR A 167     5398   8244   6712   -606     90   1680       C  
ATOM   1127  CE1 TYR A 167      18.877   7.813  24.318  1.00 59.99           C  
ANISOU 1127  CE1 TYR A 167     6047   9407   7339   -205    342   1851       C  
ATOM   1128  CE2 TYR A 167      18.877   9.774  25.691  1.00 58.75           C  
ANISOU 1128  CE2 TYR A 167     5890   9119   7313   -662     99   1900       C  
ATOM   1129  CZ  TYR A 167      19.400   9.048  24.640  1.00 62.56           C  
ANISOU 1129  CZ  TYR A 167     6277   9789   7706   -456    230   1990       C  
ATOM   1130  OH  TYR A 167      20.449   9.562  23.910  1.00 67.89           O  
ANISOU 1130  OH  TYR A 167     6771  10703   8320   -501    247   2227       O  
ATOM   1131  N   TYR A 168      13.968   6.371  24.849  1.00 45.40           N  
ANISOU 1131  N   TYR A 168     4892   6708   5649    -42    280   1071       N  
ATOM   1132  CA  TYR A 168      13.682   5.907  23.497  1.00 46.83           C  
ANISOU 1132  CA  TYR A 168     5145   6898   5750     99    348   1055       C  
ATOM   1133  C   TYR A 168      12.244   6.149  23.052  1.00 46.42           C  
ANISOU 1133  C   TYR A 168     5245   6653   5738     66    298    921       C  
ATOM   1134  O   TYR A 168      11.912   5.833  21.907  1.00 45.89           O  
ANISOU 1134  O   TYR A 168     5255   6579   5604    159    336    904       O  
ATOM   1135  CB  TYR A 168      14.019   4.418  23.370  1.00 47.45           C  
ANISOU 1135  CB  TYR A 168     5268   7033   5729    314    445   1031       C  
ATOM   1136  CG  TYR A 168      15.498   4.118  23.499  1.00 51.22           C  
ANISOU 1136  CG  TYR A 168     5581   7742   6138    398    522   1198       C  
ATOM   1137  CD1 TYR A 168      16.415   4.628  22.587  1.00 56.46           C  
ANISOU 1137  CD1 TYR A 168     6119   8597   6737    421    574   1371       C  
ATOM   1138  CD2 TYR A 168      15.973   3.312  24.518  1.00 49.71           C  
ANISOU 1138  CD2 TYR A 168     5351   7594   5942    460    547   1197       C  
ATOM   1139  CE1 TYR A 168      17.769   4.349  22.703  1.00 58.11           C  
ANISOU 1139  CE1 TYR A 168     6152   9048   6877    506    650   1552       C  
ATOM   1140  CE2 TYR A 168      17.318   3.031  24.640  1.00 51.47           C  
ANISOU 1140  CE2 TYR A 168     5408   8049   6099    546    621   1370       C  
ATOM   1141  CZ  TYR A 168      18.210   3.549  23.734  1.00 56.10           C  
ANISOU 1141  CZ  TYR A 168     5857   8837   6620    570    673   1553       C  
ATOM   1142  OH  TYR A 168      19.547   3.259  23.868  1.00 58.66           O  
ANISOU 1142  OH  TYR A 168     5993   9421   6875    663    751   1751       O  
ATOM   1143  N   SER A 169      11.375   6.655  23.923  1.00 43.65           N  
ANISOU 1143  N   SER A 169     4944   6155   5487    -51    217    833       N  
ATOM   1144  CA  SER A 169      10.019   6.975  23.503  1.00 42.89           C  
ANISOU 1144  CA  SER A 169     4964   5904   5429    -80    172    738       C  
ATOM   1145  C   SER A 169      10.014   8.202  22.601  1.00 43.85           C  
ANISOU 1145  C   SER A 169     5063   6038   5558   -163    147    813       C  
ATOM   1146  O   SER A 169      10.772   9.153  22.815  1.00 43.96           O  
ANISOU 1146  O   SER A 169     4992   6116   5595   -272    120    913       O  
ATOM   1147  CB  SER A 169       9.120   7.211  24.716  1.00 44.58           C  
ANISOU 1147  CB  SER A 169     5226   5975   5735   -158    108    644       C  
ATOM   1148  OG  SER A 169       8.822   5.991  25.371  1.00 45.54           O  
ANISOU 1148  OG  SER A 169     5393   6062   5847    -77    126    559       O  
ATOM   1149  N   THR A 170       9.141   8.183  21.595  1.00 44.50           N  
ANISOU 1149  N   THR A 170     5231   6058   5620   -125    145    771       N  
ATOM   1150  CA  THR A 170       9.029   9.292  20.659  1.00 43.62           C  
ANISOU 1150  CA  THR A 170     5111   5950   5513   -192    122    836       C  
ATOM   1151  C   THR A 170       7.641   9.254  20.037  1.00 43.35           C  
ANISOU 1151  C   THR A 170     5187   5795   5489   -173     92    755       C  
ATOM   1152  O   THR A 170       6.970   8.217  20.033  1.00 42.63           O  
ANISOU 1152  O   THR A 170     5174   5652   5371    -98     97    671       O  
ATOM   1153  CB  THR A 170      10.121   9.237  19.574  1.00 47.55           C  
ANISOU 1153  CB  THR A 170     5536   6615   5917   -134    187    956       C  
ATOM   1154  OG1 THR A 170      10.144  10.470  18.851  1.00 48.51           O  
ANISOU 1154  OG1 THR A 170     5631   6746   6054   -231    154   1036       O  
ATOM   1155  CG2 THR A 170       9.867   8.104  18.583  1.00 44.96           C  
ANISOU 1155  CG2 THR A 170     5297   6300   5484     25    249    911       C  
ATOM   1156  N   THR A 171       7.206  10.405  19.532  1.00 43.19           N  
ANISOU 1156  N   THR A 171     5176   5731   5505   -251     52    791       N  
ATOM   1157  CA  THR A 171       5.985  10.492  18.743  1.00 42.93           C  
ANISOU 1157  CA  THR A 171     5224   5616   5473   -236     25    750       C  
ATOM   1158  C   THR A 171       6.332  10.481  17.259  1.00 43.74           C  
ANISOU 1158  C   THR A 171     5332   5800   5489   -194     57    812       C  
ATOM   1159  O   THR A 171       7.312  11.102  16.837  1.00 44.43           O  
ANISOU 1159  O   THR A 171     5347   5984   5552   -223     82    911       O  
ATOM   1160  CB  THR A 171       5.193  11.757  19.080  1.00 46.96           C  
ANISOU 1160  CB  THR A 171     5753   6021   6067   -323    -33    755       C  
ATOM   1161  OG1 THR A 171       5.983  12.915  18.779  1.00 45.74           O  
ANISOU 1161  OG1 THR A 171     5557   5905   5917   -405    -43    851       O  
ATOM   1162  CG2 THR A 171       4.811  11.768  20.548  1.00 42.10           C  
ANISOU 1162  CG2 THR A 171     5152   5323   5523   -346    -57    694       C  
ATOM   1163  N   GLU A 172       5.528   9.769  16.471  1.00 43.63           N  
ANISOU 1163  N   GLU A 172     5408   5749   5419   -134     52    764       N  
ATOM   1164  CA  GLU A 172       5.809   9.668  15.041  1.00 47.44           C  
ANISOU 1164  CA  GLU A 172     5924   6298   5802    -81     84    814       C  
ATOM   1165  C   GLU A 172       4.579   9.132  14.324  1.00 44.30           C  
ANISOU 1165  C   GLU A 172     5648   5819   5365    -65     38    756       C  
ATOM   1166  O   GLU A 172       3.799   8.376  14.906  1.00 43.77           O  
ANISOU 1166  O   GLU A 172     5641   5676   5315    -62      1    680       O  
ATOM   1167  CB  GLU A 172       7.017   8.756  14.775  1.00 45.16           C  
ANISOU 1167  CB  GLU A 172     5627   6128   5403     35    169    844       C  
ATOM   1168  CG  GLU A 172       6.755   7.289  15.105  1.00 56.12           C  
ANISOU 1168  CG  GLU A 172     7125   7468   6729    131    182    751       C  
ATOM   1169  CD  GLU A 172       8.022   6.487  15.346  1.00 57.93           C  
ANISOU 1169  CD  GLU A 172     7325   7810   6878    254    273    784       C  
ATOM   1170  OE1 GLU A 172       7.944   5.467  16.053  1.00 60.02           O  
ANISOU 1170  OE1 GLU A 172     7651   8030   7125    311    279    712       O  
ATOM   1171  OE2 GLU A 172       9.092   6.869  14.836  1.00 62.65           O  
ANISOU 1171  OE2 GLU A 172     7832   8548   7425    296    339    893       O  
ATOM   1172  N   THR A 173       4.394   9.557  13.072  1.00 44.88           N  
ANISOU 1172  N   THR A 173     5754   5912   5386    -68     32    803       N  
ATOM   1173  CA  THR A 173       3.394   8.929  12.213  1.00 48.04           C  
ANISOU 1173  CA  THR A 173     6283   6254   5717    -54    -15    765       C  
ATOM   1174  C   THR A 173       3.874   7.549  11.774  1.00 47.88           C  
ANISOU 1174  C   THR A 173     6390   6252   5552     58     27    725       C  
ATOM   1175  O   THR A 173       5.055   7.355  11.473  1.00 47.85           O  
ANISOU 1175  O   THR A 173     6367   6342   5469    152    113    766       O  
ATOM   1176  CB  THR A 173       3.099   9.803  10.995  1.00 45.60           C  
ANISOU 1176  CB  THR A 173     5976   5962   5386    -90    -35    832       C  
ATOM   1177  OG1 THR A 173       4.292   9.968  10.219  1.00 48.47           O  
ANISOU 1177  OG1 THR A 173     6316   6435   5667    -28     42    900       O  
ATOM   1178  CG2 THR A 173       2.588  11.169  11.428  1.00 45.15           C  
ANISOU 1178  CG2 THR A 173     5824   5870   5461   -184    -75    873       C  
ATOM   1179  N   MET A 174       2.956   6.583  11.731  1.00 48.62           N  
ANISOU 1179  N   MET A 174     6620   6256   5598     52    -36    657       N  
ATOM   1180  CA  MET A 174       3.321   5.180  11.514  1.00 50.95           C  
ANISOU 1180  CA  MET A 174     7081   6529   5750    158    -10    604       C  
ATOM   1181  C   MET A 174       2.392   4.510  10.507  1.00 49.17           C  
ANISOU 1181  C   MET A 174     7056   6220   5408    133    -91    577       C  
ATOM   1182  O   MET A 174       1.680   3.557  10.839  1.00 46.95           O  
ANISOU 1182  O   MET A 174     6899   5846   5092     99   -164    518       O  
ATOM   1183  CB  MET A 174       3.297   4.425  12.846  1.00 54.71           C  
ANISOU 1183  CB  MET A 174     7550   6961   6276    163    -16    539       C  
ATOM   1184  CG  MET A 174       4.327   3.317  12.973  1.00 63.27           C  
ANISOU 1184  CG  MET A 174     8727   8071   7241    312     67    511       C  
ATOM   1185  SD  MET A 174       6.009   3.958  13.068  1.00 72.14           S  
ANISOU 1185  SD  MET A 174     9674   9367   8370    414    204    603       S  
ATOM   1186  CE  MET A 174       6.904   2.469  13.512  1.00 75.48           C  
ANISOU 1186  CE  MET A 174    10209   9804   8666    596    288    565       C  
ATOM   1187  N   PRO A 175       2.436   4.928   9.229  1.00 47.73           N  
ANISOU 1187  N   PRO A 175     6924   6067   5144    146    -86    625       N  
ATOM   1188  CA  PRO A 175       3.184   6.016   8.594  1.00 48.00           C  
ANISOU 1188  CA  PRO A 175     6837   6209   5194    173    -14    708       C  
ATOM   1189  C   PRO A 175       2.425   7.343   8.507  1.00 47.44           C  
ANISOU 1189  C   PRO A 175     6631   6138   5256     43    -75    762       C  
ATOM   1190  O   PRO A 175       3.053   8.369   8.243  1.00 47.53           O  
ANISOU 1190  O   PRO A 175     6521   6230   5309     42    -24    834       O  
ATOM   1191  CB  PRO A 175       3.445   5.469   7.190  1.00 49.35           C  
ANISOU 1191  CB  PRO A 175     7195   6385   5170    267     12    718       C  
ATOM   1192  CG  PRO A 175       2.234   4.649   6.909  1.00 49.58           C  
ANISOU 1192  CG  PRO A 175     7421   6283   5133    193   -111    657       C  
ATOM   1193  CD  PRO A 175       1.765   4.081   8.226  1.00 48.70           C  
ANISOU 1193  CD  PRO A 175     7284   6106   5112    139   -160    596       C  
ATOM   1194  N   SER A 176       1.106   7.334   8.708  1.00 47.02           N  
ANISOU 1194  N   SER A 176     6600   6005   5262    -62   -181    741       N  
ATOM   1195  CA  SER A 176       0.311   8.541   8.513  1.00 51.29           C  
ANISOU 1195  CA  SER A 176     7034   6547   5907   -157   -233    802       C  
ATOM   1196  C   SER A 176      -0.294   9.121   9.787  1.00 45.76           C  
ANISOU 1196  C   SER A 176     6201   5817   5368   -220   -260    800       C  
ATOM   1197  O   SER A 176      -0.530  10.330   9.835  1.00 45.56           O  
ANISOU 1197  O   SER A 176     6073   5802   5436   -259   -262    855       O  
ATOM   1198  CB  SER A 176      -0.816   8.282   7.499  1.00 47.36           C  
ANISOU 1198  CB  SER A 176     6651   6008   5337   -223   -333    822       C  
ATOM   1199  OG  SER A 176      -1.712   7.288   7.959  1.00 48.99           O  
ANISOU 1199  OG  SER A 176     6943   6146   5526   -276   -420    778       O  
ATOM   1200  N   ARG A 177      -0.556   8.316  10.813  1.00 45.26           N  
ANISOU 1200  N   ARG A 177     6152   5713   5333   -221   -279    740       N  
ATOM   1201  CA  ARG A 177      -1.180   8.808  12.037  1.00 44.47           C  
ANISOU 1201  CA  ARG A 177     5939   5586   5371   -264   -299    739       C  
ATOM   1202  C   ARG A 177      -0.207   8.729  13.208  1.00 43.88           C  
ANISOU 1202  C   ARG A 177     5805   5521   5347   -220   -229    696       C  
ATOM   1203  O   ARG A 177       0.617   7.814  13.282  1.00 44.02           O  
ANISOU 1203  O   ARG A 177     5882   5555   5290   -159   -187    652       O  
ATOM   1204  CB  ARG A 177      -2.469   8.037  12.340  1.00 44.45           C  
ANISOU 1204  CB  ARG A 177     5979   5540   5370   -323   -392    729       C  
ATOM   1205  CG  ARG A 177      -3.576   8.371  11.351  1.00 51.08           C  
ANISOU 1205  CG  ARG A 177     6834   6386   6187   -391   -474    803       C  
ATOM   1206  CD  ARG A 177      -4.774   7.448  11.474  1.00 49.36           C  
ANISOU 1206  CD  ARG A 177     6667   6145   5941   -470   -583    817       C  
ATOM   1207  NE  ARG A 177      -5.704   7.653  10.367  1.00 46.22           N  
ANISOU 1207  NE  ARG A 177     6298   5768   5496   -546   -671    900       N  
ATOM   1208  CZ  ARG A 177      -6.754   8.468  10.405  1.00 50.22           C  
ANISOU 1208  CZ  ARG A 177     6682   6316   6084   -587   -712    998       C  
ATOM   1209  NH1 ARG A 177      -7.538   8.591   9.337  1.00 47.22           N  
ANISOU 1209  NH1 ARG A 177     6328   5964   5649   -659   -796   1082       N  
ATOM   1210  NH2 ARG A 177      -7.019   9.165  11.503  1.00 45.73           N  
ANISOU 1210  NH2 ARG A 177     5972   5761   5641   -547   -665   1018       N  
ATOM   1211  N   VAL A 178      -0.286   9.725  14.098  1.00 43.37           N  
ANISOU 1211  N   VAL A 178     5633   5444   5399   -244   -217    715       N  
ATOM   1212  CA  VAL A 178       0.663   9.844  15.203  1.00 42.93           C  
ANISOU 1212  CA  VAL A 178     5519   5398   5393   -223   -163    687       C  
ATOM   1213  C   VAL A 178       0.464   8.724  16.218  1.00 42.44           C  
ANISOU 1213  C   VAL A 178     5482   5307   5337   -204   -171    616       C  
ATOM   1214  O   VAL A 178      -0.658   8.441  16.657  1.00 44.19           O  
ANISOU 1214  O   VAL A 178     5710   5486   5595   -232   -224    604       O  
ATOM   1215  CB  VAL A 178       0.526  11.219  15.882  1.00 42.69           C  
ANISOU 1215  CB  VAL A 178     5415   5337   5470   -263   -163    723       C  
ATOM   1216  CG1 VAL A 178       1.558  11.370  17.013  1.00 42.40           C  
ANISOU 1216  CG1 VAL A 178     5333   5307   5472   -265   -123    703       C  
ATOM   1217  CG2 VAL A 178       0.660  12.345  14.857  1.00 43.26           C  
ANISOU 1217  CG2 VAL A 178     5477   5426   5534   -289   -163    798       C  
ATOM   1218  N   VAL A 179       1.574   8.139  16.659  1.00 42.39           N  
ANISOU 1218  N   VAL A 179     5474   5336   5298   -156   -117    585       N  
ATOM   1219  CA  VAL A 179       1.601   7.199  17.766  1.00 42.01           C  
ANISOU 1219  CA  VAL A 179     5438   5262   5262   -135   -114    521       C  
ATOM   1220  C   VAL A 179       2.753   7.594  18.679  1.00 41.71           C  
ANISOU 1220  C   VAL A 179     5315   5265   5268   -123    -58    527       C  
ATOM   1221  O   VAL A 179       3.699   8.280  18.278  1.00 42.13           O  
ANISOU 1221  O   VAL A 179     5315   5382   5309   -124    -20    585       O  
ATOM   1222  CB  VAL A 179       1.770   5.723  17.323  1.00 43.20           C  
ANISOU 1222  CB  VAL A 179     5713   5408   5293    -74   -113    475       C  
ATOM   1223  CG1 VAL A 179       0.655   5.291  16.375  1.00 42.75           C  
ANISOU 1223  CG1 VAL A 179     5765   5305   5175   -113   -190    478       C  
ATOM   1224  CG2 VAL A 179       3.145   5.514  16.701  1.00 42.97           C  
ANISOU 1224  CG2 VAL A 179     5699   5457   5171     16    -31    498       C  
ATOM   1225  N   CYS A 180       2.640   7.168  19.931  1.00 41.15           N  
ANISOU 1225  N   CYS A 180     5226   5162   5247   -125    -63    479       N  
ATOM   1226  CA  CYS A 180       3.745   7.187  20.875  1.00 44.25           C  
ANISOU 1226  CA  CYS A 180     5555   5595   5662   -114    -19    478       C  
ATOM   1227  C   CYS A 180       4.353   5.791  20.880  1.00 43.32           C  
ANISOU 1227  C   CYS A 180     5488   5514   5458    -28     18    442       C  
ATOM   1228  O   CYS A 180       3.671   4.820  21.224  1.00 46.13           O  
ANISOU 1228  O   CYS A 180     5916   5812   5799    -11    -10    381       O  
ATOM   1229  CB  CYS A 180       3.259   7.592  22.269  1.00 42.42           C  
ANISOU 1229  CB  CYS A 180     5289   5301   5527   -160    -45    447       C  
ATOM   1230  SG  CYS A 180       4.464   7.403  23.624  1.00 41.71           S  
ANISOU 1230  SG  CYS A 180     5138   5250   5461   -161    -12    437       S  
ATOM   1231  N   LYS A 181       5.621   5.688  20.490  1.00 45.95           N  
ANISOU 1231  N   LYS A 181     5785   5946   5727     31     83    492       N  
ATOM   1232  CA  LYS A 181       6.277   4.395  20.359  1.00 47.71           C  
ANISOU 1232  CA  LYS A 181     6072   6210   5847    149    136    472       C  
ATOM   1233  C   LYS A 181       7.679   4.463  20.946  1.00 47.35           C  
ANISOU 1233  C   LYS A 181     5910   6282   5797    188    202    535       C  
ATOM   1234  O   LYS A 181       8.374   5.476  20.805  1.00 50.95           O  
ANISOU 1234  O   LYS A 181     6254   6822   6281    136    215    624       O  
ATOM   1235  CB  LYS A 181       6.339   3.950  18.888  1.00 54.20           C  
ANISOU 1235  CB  LYS A 181     7002   7051   6540    232    163    489       C  
ATOM   1236  CG  LYS A 181       6.964   2.578  18.668  1.00 58.67           C  
ANISOU 1236  CG  LYS A 181     7684   7638   6971    384    224    466       C  
ATOM   1237  CD  LYS A 181       6.819   2.134  17.219  1.00 66.05           C  
ANISOU 1237  CD  LYS A 181     8776   8556   7763    464    237    469       C  
ATOM   1238  CE  LYS A 181       7.520   0.801  16.970  1.00 71.11           C  
ANISOU 1238  CE  LYS A 181     9566   9206   8244    644    311    451       C  
ATOM   1239  NZ  LYS A 181       7.094  -0.238  17.953  1.00 74.17           N  
ANISOU 1239  NZ  LYS A 181    10048   9493   8640    646    271    364       N  
ATOM   1240  N   ILE A 182       8.083   3.383  21.610  1.00 44.10           N  
ANISOU 1240  N   ILE A 182     5527   5881   5348    271    235    500       N  
ATOM   1241  CA  ILE A 182       9.444   3.246  22.120  1.00 46.46           C  
ANISOU 1241  CA  ILE A 182     5715   6314   5625    329    303    574       C  
ATOM   1242  C   ILE A 182      10.315   2.746  20.973  1.00 47.47           C  
ANISOU 1242  C   ILE A 182     5869   6555   5612    483    394    646       C  
ATOM   1243  O   ILE A 182      10.163   1.612  20.514  1.00 47.42           O  
ANISOU 1243  O   ILE A 182     6016   6504   5496    616    427    594       O  
ATOM   1244  CB  ILE A 182       9.502   2.291  23.316  1.00 48.90           C  
ANISOU 1244  CB  ILE A 182     6043   6589   5947    368    305    513       C  
ATOM   1245  CG1 ILE A 182       8.441   2.674  24.345  1.00 46.64           C  
ANISOU 1245  CG1 ILE A 182     5760   6180   5782    238    220    435       C  
ATOM   1246  CG2 ILE A 182      10.893   2.301  23.952  1.00 49.85           C  
ANISOU 1246  CG2 ILE A 182     6018   6862   6059    406    364    610       C  
ATOM   1247  CD1 ILE A 182       8.280   1.661  25.427  1.00 46.84           C  
ANISOU 1247  CD1 ILE A 182     5827   6155   5816    272    214    365       C  
ATOM   1248  N   GLU A 183      11.179   3.628  20.484  1.00 48.24           N  
ANISOU 1248  N   GLU A 183     5831   6797   5701    467    432    774       N  
ATOM   1249  CA  GLU A 183      12.086   3.291  19.364  1.00 50.59           C  
ANISOU 1249  CA  GLU A 183     6132   7229   5861    622    530    867       C  
ATOM   1250  C   GLU A 183      13.413   2.782  19.923  1.00 51.77           C  
ANISOU 1250  C   GLU A 183     6162   7552   5958    738    619    971       C  
ATOM   1251  O   GLU A 183      14.343   3.566  20.033  1.00 53.39           O  
ANISOU 1251  O   GLU A 183     6179   7932   6177    698    646   1122       O  
ATOM   1252  CB  GLU A 183      12.300   4.510  18.473  1.00 50.98           C  
ANISOU 1252  CB  GLU A 183     6095   7352   5922    540    522    966       C  
ATOM   1253  CG  GLU A 183      11.145   4.792  17.540  1.00 58.22           C  
ANISOU 1253  CG  GLU A 183     7152   8130   6838    495    465    885       C  
ATOM   1254  CD  GLU A 183      10.925   3.783  16.431  1.00 65.64           C  
ANISOU 1254  CD  GLU A 183     8266   9056   7616    669    526    857       C  
ATOM   1255  OE1 GLU A 183      10.011   3.975  15.641  1.00 66.08           O  
ANISOU 1255  OE1 GLU A 183     8442   9012   7654    632    477    805       O  
ATOM   1256  OE2 GLU A 183      11.674   2.814  16.367  1.00 68.98           O  
ANISOU 1256  OE2 GLU A 183     8720   9568   7923    848    622    893       O  
ATOM   1257  N   TRP A 184      13.487   1.485  20.191  1.00 50.45           N  
ANISOU 1257  N   TRP A 184     6110   7338   5720    883    661    902       N  
ATOM   1258  CA  TRP A 184      14.725   0.843  20.685  1.00 53.78           C  
ANISOU 1258  CA  TRP A 184     6440   7925   6069   1038    761   1003       C  
ATOM   1259  C   TRP A 184      15.725   0.801  19.535  1.00 58.73           C  
ANISOU 1259  C   TRP A 184     7031   8733   6550   1217    882   1146       C  
ATOM   1260  O   TRP A 184      15.283   0.661  18.399  1.00 57.32           O  
ANISOU 1260  O   TRP A 184     6994   8496   6287   1280    898   1112       O  
ATOM   1261  CB  TRP A 184      14.410  -0.575  21.148  1.00 54.07           C  
ANISOU 1261  CB  TRP A 184     6652   7850   6042   1175    783    891       C  
ATOM   1262  CG  TRP A 184      13.502  -0.641  22.333  1.00 53.32           C  
ANISOU 1262  CG  TRP A 184     6577   7605   6078   1022    679    770       C  
ATOM   1263  CD1 TRP A 184      12.157  -0.848  22.330  1.00 52.22           C  
ANISOU 1263  CD1 TRP A 184     6596   7259   5985    928    586    624       C  
ATOM   1264  CD2 TRP A 184      13.884  -0.497  23.705  1.00 53.76           C  
ANISOU 1264  CD2 TRP A 184     6482   7716   6226    947    658    799       C  
ATOM   1265  NE1 TRP A 184      11.684  -0.865  23.609  1.00 53.23           N  
ANISOU 1265  NE1 TRP A 184     6679   7318   6228    814    519    561       N  
ATOM   1266  CE2 TRP A 184      12.716  -0.638  24.470  1.00 52.80           C  
ANISOU 1266  CE2 TRP A 184     6447   7411   6202    823    561    658       C  
ATOM   1267  CE3 TRP A 184      15.095  -0.273  24.352  1.00 56.87           C  
ANISOU 1267  CE3 TRP A 184     6675   8309   6626    969    709    944       C  
ATOM   1268  CZ2 TRP A 184      12.724  -0.558  25.855  1.00 54.30           C  
ANISOU 1268  CZ2 TRP A 184     6544   7597   6490    731    519    643       C  
ATOM   1269  CZ3 TRP A 184      15.105  -0.193  25.722  1.00 57.23           C  
ANISOU 1269  CZ3 TRP A 184     6630   8345   6769    860    655    929       C  
ATOM   1270  CH2 TRP A 184      13.934  -0.335  26.458  1.00 55.68           C  
ANISOU 1270  CH2 TRP A 184     6541   7952   6665    748    564    773       C  
ATOM   1271  N   PRO A 185      17.043   0.837  19.792  1.00 66.86           N  
ANISOU 1271  N   PRO A 185     7865   9996   7541   1302    967   1320       N  
ATOM   1272  CA  PRO A 185      18.015   0.801  18.718  1.00 73.02           C  
ANISOU 1272  CA  PRO A 185     8601  10975   8167   1504   1100   1476       C  
ATOM   1273  C   PRO A 185      17.734  -0.508  17.984  1.00 80.35           C  
ANISOU 1273  C   PRO A 185     9802  11810   8917   1779   1194   1387       C  
ATOM   1274  O   PRO A 185      17.562  -1.501  18.626  1.00 77.29           O  
ANISOU 1274  O   PRO A 185     9554  11310   8501   1870   1199   1285       O  
ATOM   1275  CB  PRO A 185      19.348   0.731  19.461  1.00 71.63           C  
ANISOU 1275  CB  PRO A 185     8158  11067   7989   1545   1166   1682       C  
ATOM   1276  CG  PRO A 185      19.055   1.396  20.770  1.00 70.40           C  
ANISOU 1276  CG  PRO A 185     7889  10849   8012   1284   1034   1640       C  
ATOM   1277  CD  PRO A 185      17.658   0.926  21.106  1.00 67.93           C  
ANISOU 1277  CD  PRO A 185     7812  10237   7760   1225    948   1394       C  
ATOM   1278  N   GLU A 186      17.693  -0.451  16.655  1.00 89.87           N  
ANISOU 1278  N   GLU A 186    11101  13054   9992   1909   1265   1430       N  
ATOM   1279  CA  GLU A 186      17.387  -1.662  15.857  1.00102.20           C  
ANISOU 1279  CA  GLU A 186    12963  14514  11354   2176   1353   1351       C  
ATOM   1280  C   GLU A 186      18.517  -2.648  16.123  1.00112.60           C  
ANISOU 1280  C   GLU A 186    14244  16008  12533   2467   1511   1475       C  
ATOM   1281  O   GLU A 186      19.677  -2.224  16.087  1.00113.15           O  
ANISOU 1281  O   GLU A 186    14040  16358  12594   2526   1600   1687       O  
ATOM   1282  CB  GLU A 186      17.270  -1.277  14.384  1.00105.94           C  
ANISOU 1282  CB  GLU A 186    13549  14992  11711   2246   1391   1375       C  
ATOM   1283  CG  GLU A 186      16.079  -0.391  14.065  1.00107.81           C  
ANISOU 1283  CG  GLU A 186    13899  15016  12048   2004   1239   1230       C  
ATOM   1284  CD  GLU A 186      15.933   0.092  12.630  1.00110.63           C  
ANISOU 1284  CD  GLU A 186    14544  15089  12403   1963   1140   1019       C  
ATOM   1285  OE1 GLU A 186      16.883  -0.100  11.846  1.00112.84           O  
ANISOU 1285  OE1 GLU A 186    15031  15302  12540   2168   1202    969       O  
ATOM   1286  OE2 GLU A 186      14.877   0.672  12.302  1.00109.93           O  
ANISOU 1286  OE2 GLU A 186    14474  14847  12447   1727    999    914       O  
ATOM   1287  N   HIS A 187      18.184  -3.912  16.365  1.00123.46           N  
ANISOU 1287  N   HIS A 187    15897  17222  13790   2650   1543   1353       N  
ATOM   1288  CA  HIS A 187      19.242  -4.898  16.699  1.00135.97           C  
ANISOU 1288  CA  HIS A 187    17465  18933  15264   2915   1676   1444       C  
ATOM   1289  C   HIS A 187      18.819  -6.314  16.332  1.00142.42           C  
ANISOU 1289  C   HIS A 187    18695  19504  15912   3118   1697   1279       C  
ATOM   1290  O   HIS A 187      17.881  -6.478  15.540  1.00144.72           O  
ANISOU 1290  O   HIS A 187    19254  19550  16184   3019   1597   1113       O  
ATOM   1291  CB  HIS A 187      19.725  -4.805  18.151  1.00138.78           C  
ANISOU 1291  CB  HIS A 187    17547  19379  15803   2740   1614   1490       C  
ATOM   1292  CG  HIS A 187      20.306  -3.474  18.503  1.00142.94           C  
ANISOU 1292  CG  HIS A 187    17705  20254  16353   2765   1699   1752       C  
ATOM   1293  ND1 HIS A 187      21.501  -3.035  17.982  1.00142.81           N  
ANISOU 1293  ND1 HIS A 187    17399  20351  16513   2537   1617   1831       N  
ATOM   1294  CD2 HIS A 187      19.869  -2.493  19.321  1.00145.70           C  
ANISOU 1294  CD2 HIS A 187    17928  20871  16562   2985   1853   1968       C  
ATOM   1295  CE1 HIS A 187      21.774  -1.836  18.455  1.00144.47           C  
ANISOU 1295  CE1 HIS A 187    17316  20884  16692   2594   1704   2089       C  
ATOM   1296  NE2 HIS A 187      20.788  -1.481  19.277  1.00146.12           N  
ANISOU 1296  NE2 HIS A 187    17603  21203  16712   2869   1853   2184       N  
ATOM   1297  N   PRO A 188      19.470  -7.323  16.940  1.00146.99           N  
ANISOU 1297  N   PRO A 188    19359  20139  16354   3405   1823   1329       N  
ATOM   1298  CA  PRO A 188      19.260  -8.710  16.567  1.00147.76           C  
ANISOU 1298  CA  PRO A 188    19903  19987  16252   3620   1848   1182       C  
ATOM   1299  C   PRO A 188      17.864  -9.184  16.965  1.00142.51           C  
ANISOU 1299  C   PRO A 188    19478  18992  15678   3371   1654    947       C  
ATOM   1300  O   PRO A 188      17.720  -9.876  17.930  1.00142.04           O  
ANISOU 1300  O   PRO A 188    19501  18811  15655   3347   1604    862       O  
ATOM   1301  CB  PRO A 188      20.303  -9.448  17.412  1.00150.10           C  
ANISOU 1301  CB  PRO A 188    20168  20403  16458   3892   1981   1277       C  
ATOM   1302  CG  PRO A 188      20.479  -8.584  18.627  1.00149.20           C  
ANISOU 1302  CG  PRO A 188    19591  20552  16548   3727   1970   1430       C  
ATOM   1303  CD  PRO A 188      20.279  -7.165  18.147  1.00148.98           C  
ANISOU 1303  CD  PRO A 188    19322  20675  16608   3551   1944   1529       C  
ATOM   1304  N   ASN A 189      16.894  -8.838  16.127  1.00137.32           N  
ANISOU 1304  N   ASN A 189    18927  18201  15049   3187   1546    858       N  
ATOM   1305  CA  ASN A 189      15.485  -9.217  16.378  1.00128.97           C  
ANISOU 1305  CA  ASN A 189    18080  16855  14068   2937   1357    664       C  
ATOM   1306  C   ASN A 189      15.029  -8.730  17.752  1.00115.79           C  
ANISOU 1306  C   ASN A 189    16188  15169  12639   2682   1242    618       C  
ATOM   1307  O   ASN A 189      14.550  -9.553  18.548  1.00115.08           O  
ANISOU 1307  O   ASN A 189    16247  14925  12552   2664   1183    519       O  
ATOM   1308  CB  ASN A 189      15.175 -10.649  15.958  1.00133.40           C  
ANISOU 1308  CB  ASN A 189    19117  17163  14404   3109   1348    541       C  
ATOM   1309  CG  ASN A 189      14.623 -10.635  14.552  1.00136.24           C  
ANISOU 1309  CG  ASN A 189    19772  17406  14586   3166   1338    500       C  
ATOM   1310  OD1 ASN A 189      14.727  -9.619  13.867  1.00135.99           O  
ANISOU 1310  OD1 ASN A 189    19575  17507  14589   3117   1363    576       O  
ATOM   1311  ND2 ASN A 189      14.003 -11.726  14.134  1.00138.41           N  
ANISOU 1311  ND2 ASN A 189    20503  17425  14663   3261   1293    382       N  
ATOM   1312  N   LYS A 190      15.273  -7.440  18.001  1.00102.86           N  
ANISOU 1312  N   LYS A 190    14200  13691  11192   2484   1210    698       N  
ATOM   1313  CA  LYS A 190      14.789  -6.718  19.200  1.00 88.93           C  
ANISOU 1313  CA  LYS A 190    12234  11894   9660   2205   1084    648       C  
ATOM   1314  C   LYS A 190      15.257  -7.374  20.493  1.00 82.09           C  
ANISOU 1314  C   LYS A 190    11297  11065   8829   2269   1114    658       C  
ATOM   1315  O   LYS A 190      14.447  -7.470  21.404  1.00 80.29           O  
ANISOU 1315  O   LYS A 190    11062  10716   8730   2092   1004    561       O  
ATOM   1316  CB  LYS A 190      13.265  -6.662  19.125  1.00 83.11           C  
ANISOU 1316  CB  LYS A 190    11688  10905   8984   1988    918    484       C  
ATOM   1317  CG  LYS A 190      12.746  -6.139  17.796  1.00 81.15           C  
ANISOU 1317  CG  LYS A 190    11604  10581   8649   1966    886    459       C  
ATOM   1318  CD  LYS A 190      11.342  -5.600  17.833  1.00 78.23           C  
ANISOU 1318  CD  LYS A 190    11115  10152   8457   1672    745    414       C  
ATOM   1319  CE  LYS A 190      10.989  -4.838  16.576  1.00 78.66           C  
ANISOU 1319  CE  LYS A 190    11355  10117   8415   1646    701    385       C  
ATOM   1320  NZ  LYS A 190       9.556  -4.476  16.529  1.00 78.04           N  
ANISOU 1320  NZ  LYS A 190    11143  10004   8507   1382    578    364       N  
ATOM   1321  N   ILE A 191      16.510  -7.809  20.555  1.00 80.79           N  
ANISOU 1321  N   ILE A 191    11073  11078   8546   2530   1268    787       N  
ATOM   1322  CA  ILE A 191      17.011  -8.446  21.806  1.00 83.14           C  
ANISOU 1322  CA  ILE A 191    11314  11413   8861   2610   1302    804       C  
ATOM   1323  C   ILE A 191      17.010  -7.436  22.957  1.00 81.66           C  
ANISOU 1323  C   ILE A 191    10789  11339   8899   2365   1227    852       C  
ATOM   1324  O   ILE A 191      16.714  -7.841  24.073  1.00 81.39           O  
ANISOU 1324  O   ILE A 191    10740  11242   8941   2303   1178    795       O  
ATOM   1325  CB  ILE A 191      18.346  -9.198  21.620  1.00 85.20           C  
ANISOU 1325  CB  ILE A 191    11571  11866   8936   2966   1494    957       C  
ATOM   1326  CG1 ILE A 191      18.379 -10.462  22.476  1.00 86.78           C  
ANISOU 1326  CG1 ILE A 191    11838  12029   9106   3093   1524    936       C  
ATOM   1327  CG2 ILE A 191      19.565  -8.334  21.884  1.00 85.10           C  
ANISOU 1327  CG2 ILE A 191    11173  12182   8978   2969   1578   1180       C  
ATOM   1328  CD1 ILE A 191      17.302 -11.459  22.134  1.00 87.12           C  
ANISOU 1328  CD1 ILE A 191    12268  11749   9084   3083   1433    733       C  
ATOM   1329  N   TYR A 192      17.323  -6.171  22.691  1.00 81.51           N  
ANISOU 1329  N   TYR A 192    10516  11472   8982   2214   1210    953       N  
ATOM   1330  CA  TYR A 192      17.417  -5.189  23.792  1.00 80.77           C  
ANISOU 1330  CA  TYR A 192    10133  11481   9077   1988   1137   1009       C  
ATOM   1331  C   TYR A 192      16.064  -4.965  24.464  1.00 71.37           C  
ANISOU 1331  C   TYR A 192     9007  10069   8040   1729    979    839       C  
ATOM   1332  O   TYR A 192      16.011  -4.984  25.684  1.00 68.12           O  
ANISOU 1332  O   TYR A 192     8510   9638   7735   1623    924    810       O  
ATOM   1333  CB  TYR A 192      18.186  -3.959  23.321  1.00 90.36           C  
ANISOU 1333  CB  TYR A 192    11086  12910  10338   1895   1155   1176       C  
ATOM   1334  CG  TYR A 192      19.673  -4.195  23.381  1.00101.19           C  
ANISOU 1334  CG  TYR A 192    12239  14580  11630   2069   1285   1403       C  
ATOM   1335  CD1 TYR A 192      20.208  -4.993  24.374  1.00104.61           C  
ANISOU 1335  CD1 TYR A 192    12626  15087  12034   2197   1339   1449       C  
ATOM   1336  CD2 TYR A 192      20.543  -3.651  22.452  1.00106.03           C  
ANISOU 1336  CD2 TYR A 192    12680  15415  12192   2108   1354   1588       C  
ATOM   1337  CE1 TYR A 192      21.566  -5.237  24.461  1.00108.94           C  
ANISOU 1337  CE1 TYR A 192    12953  15933  12505   2363   1460   1681       C  
ATOM   1338  CE2 TYR A 192      21.905  -3.885  22.522  1.00109.93           C  
ANISOU 1338  CE2 TYR A 192    12948  16212  12608   2266   1474   1825       C  
ATOM   1339  CZ  TYR A 192      22.418  -4.682  23.529  1.00112.03           C  
ANISOU 1339  CZ  TYR A 192    13163  16558  12847   2396   1527   1875       C  
ATOM   1340  OH  TYR A 192      23.756  -4.926  23.610  1.00115.61           O  
ANISOU 1340  OH  TYR A 192    13371  17337  13219   2560   1648   2135       O  
ATOM   1341  N   GLU A 193      15.003  -4.807  23.687  1.00 65.00           N  
ANISOU 1341  N   GLU A 193     8352   9103   7242   1633    908    734       N  
ATOM   1342  CA  GLU A 193      13.686  -4.605  24.327  1.00 62.17           C  
ANISOU 1342  CA  GLU A 193     8057   8549   7015   1414    768    590       C  
ATOM   1343  C   GLU A 193      13.256  -5.877  25.057  1.00 59.84           C  
ANISOU 1343  C   GLU A 193     7966   8092   6679   1473    740    472       C  
ATOM   1344  O   GLU A 193      12.588  -5.746  26.064  1.00 56.01           O  
ANISOU 1344  O   GLU A 193     7450   7516   6315   1318    650    397       O  
ATOM   1345  CB  GLU A 193      12.643  -4.033  23.376  1.00 59.44           C  
ANISOU 1345  CB  GLU A 193     7813   8093   6679   1306    700    530       C  
ATOM   1346  CG  GLU A 193      12.355  -4.907  22.193  1.00 69.12           C  
ANISOU 1346  CG  GLU A 193     9326   9199   7737   1450    721    466       C  
ATOM   1347  CD  GLU A 193      11.975  -4.118  20.959  1.00 77.45           C  
ANISOU 1347  CD  GLU A 193    10415  10243   8770   1393    698    478       C  
ATOM   1348  OE1 GLU A 193      12.891  -3.668  20.243  1.00 76.69           O  
ANISOU 1348  OE1 GLU A 193    10223  10306   8611   1494    790    594       O  
ATOM   1349  OE2 GLU A 193      10.768  -3.974  20.713  1.00 81.53           O  
ANISOU 1349  OE2 GLU A 193    11045  10603   9330   1248    587    384       O  
ATOM   1350  N   LYS A 194      13.535  -7.050  24.490  1.00 59.16           N  
ANISOU 1350  N   LYS A 194     8095   7969   6415   1704    819    462       N  
ATOM   1351  CA  LYS A 194      13.140  -8.314  25.157  1.00 60.74           C  
ANISOU 1351  CA  LYS A 194     8502   8014   6564   1762    790    362       C  
ATOM   1352  C   LYS A 194      13.897  -8.473  26.477  1.00 58.53           C  
ANISOU 1352  C   LYS A 194     8047   7835   6358   1778    820    409       C  
ATOM   1353  O   LYS A 194      13.265  -8.773  27.469  1.00 56.18           O  
ANISOU 1353  O   LYS A 194     7776   7426   6146   1660    736    323       O  
ATOM   1354  CB  LYS A 194      13.394  -9.512  24.245  1.00 67.41           C  
ANISOU 1354  CB  LYS A 194     9647   8787   7177   2025    873    349       C  
ATOM   1355  CG  LYS A 194      12.518  -9.577  23.009  1.00 74.76           C  
ANISOU 1355  CG  LYS A 194    10847   9545   8014   1988    806    265       C  
ATOM   1356  CD  LYS A 194      12.868 -10.722  22.092  1.00 82.21           C  
ANISOU 1356  CD  LYS A 194    12117  10416   8703   2271    898    259       C  
ATOM   1357  CE  LYS A 194      11.954 -10.819  20.890  1.00 85.08           C  
ANISOU 1357  CE  LYS A 194    12780  10592   8954   2220    815    175       C  
ATOM   1358  NZ  LYS A 194      11.568  -9.476  20.406  1.00 86.61           N  
ANISOU 1358  NZ  LYS A 194    12801  10884   9221   2102    803    224       N  
ATOM   1359  N   VAL A 195      15.196  -8.212  26.493  1.00 57.60           N  
ANISOU 1359  N   VAL A 195     7742   7942   6203   1921    937    558       N  
ATOM   1360  CA  VAL A 195      15.937  -8.373  27.740  1.00 57.37           C  
ANISOU 1360  CA  VAL A 195     7534   8029   6235   1934    963    624       C  
ATOM   1361  C   VAL A 195      15.473  -7.350  28.765  1.00 55.49           C  
ANISOU 1361  C   VAL A 195     7095   7789   6201   1648    847    599       C  
ATOM   1362  O   VAL A 195      15.298  -7.668  29.948  1.00 56.63           O  
ANISOU 1362  O   VAL A 195     7214   7886   6418   1580    800    552       O  
ATOM   1363  CB  VAL A 195      17.451  -8.265  27.476  1.00 60.69           C  
ANISOU 1363  CB  VAL A 195     7763   8725   6573   2130   1106    824       C  
ATOM   1364  CG1 VAL A 195      18.218  -8.164  28.785  1.00 58.21           C  
ANISOU 1364  CG1 VAL A 195     7210   8561   6345   2085   1108    918       C  
ATOM   1365  CG2 VAL A 195      17.934  -9.454  26.656  1.00 64.81           C  
ANISOU 1365  CG2 VAL A 195     8515   9238   6872   2464   1238    847       C  
ATOM   1366  N   TYR A 196      15.215  -6.119  28.319  1.00 53.45           N  
ANISOU 1366  N   TYR A 196     6718   7566   6027   1483    798    624       N  
ATOM   1367  CA  TYR A 196      14.748  -5.087  29.231  1.00 49.74           C  
ANISOU 1367  CA  TYR A 196     6096   7074   5730   1228    692    599       C  
ATOM   1368  C   TYR A 196      13.369  -5.419  29.780  1.00 48.82           C  
ANISOU 1368  C   TYR A 196     6134   6734   5682   1109    589    434       C  
ATOM   1369  O   TYR A 196      13.126  -5.272  30.983  1.00 48.76           O  
ANISOU 1369  O   TYR A 196     6055   6696   5776    991    531    399       O  
ATOM   1370  CB  TYR A 196      14.729  -3.732  28.523  1.00 46.04           C  
ANISOU 1370  CB  TYR A 196     5506   6669   5316   1095    664    661       C  
ATOM   1371  CG  TYR A 196      14.157  -2.621  29.368  1.00 45.98           C  
ANISOU 1371  CG  TYR A 196     5395   6607   5467    847    554    626       C  
ATOM   1372  CD1 TYR A 196      12.816  -2.267  29.272  1.00 44.44           C  
ANISOU 1372  CD1 TYR A 196     5311   6234   5341    722    468    503       C  
ATOM   1373  CD2 TYR A 196      14.956  -1.930  30.269  1.00 44.58           C  
ANISOU 1373  CD2 TYR A 196     5021   6559   5359    742    534    725       C  
ATOM   1374  CE1 TYR A 196      12.291  -1.260  30.051  1.00 42.15           C  
ANISOU 1374  CE1 TYR A 196     4947   5891   5179    529    383    476       C  
ATOM   1375  CE2 TYR A 196      14.443  -0.914  31.045  1.00 43.43           C  
ANISOU 1375  CE2 TYR A 196     4822   6342   5336    528    434    689       C  
ATOM   1376  CZ  TYR A 196      13.111  -0.580  30.933  1.00 44.00           C  
ANISOU 1376  CZ  TYR A 196     5017   6232   5470    437    367    562       C  
ATOM   1377  OH  TYR A 196      12.600   0.431  31.718  1.00 41.54           O  
ANISOU 1377  OH  TYR A 196     4672   5847   5264    256    281    530       O  
ATOM   1378  N   HIS A 197      12.456  -5.882  28.921  1.00 46.11           N  
ANISOU 1378  N   HIS A 197     6004   6241   5275   1135    563    343       N  
ATOM   1379  CA  HIS A 197      11.120  -6.223  29.391  1.00 46.49           C  
ANISOU 1379  CA  HIS A 197     6184   6100   5380   1013    459    214       C  
ATOM   1380  C   HIS A 197      11.177  -7.356  30.408  1.00 47.15           C  
ANISOU 1380  C   HIS A 197     6344   6128   5443   1076    459    169       C  
ATOM   1381  O   HIS A 197      10.513  -7.297  31.453  1.00 44.74           O  
ANISOU 1381  O   HIS A 197     6003   5754   5240    944    386    112       O  
ATOM   1382  CB  HIS A 197      10.236  -6.595  28.196  1.00 47.50           C  
ANISOU 1382  CB  HIS A 197     6531   6095   5421   1028    423    151       C  
ATOM   1383  CG  HIS A 197       8.891  -7.133  28.575  1.00 49.17           C  
ANISOU 1383  CG  HIS A 197     6890   6130   5664    911    313     47       C  
ATOM   1384  ND1 HIS A 197       8.203  -8.029  27.786  1.00 50.03           N  
ANISOU 1384  ND1 HIS A 197     7257   6097   5654    943    269    -11       N  
ATOM   1385  CD2 HIS A 197       8.104  -6.899  29.652  1.00 47.54           C  
ANISOU 1385  CD2 HIS A 197     6608   5871   5583    758    235      3       C  
ATOM   1386  CE1 HIS A 197       7.052  -8.328  28.363  1.00 50.39           C  
ANISOU 1386  CE1 HIS A 197     7363   6025   5759    799    161    -74       C  
ATOM   1387  NE2 HIS A 197       6.969  -7.657  29.498  1.00 47.56           N  
ANISOU 1387  NE2 HIS A 197     6798   5724   5549    698    147    -65       N  
ATOM   1388  N   ILE A 198      12.018  -8.362  30.154  1.00 47.12           N  
ANISOU 1388  N   ILE A 198     6440   6162   5302   1289    549    203       N  
ATOM   1389  CA  ILE A 198      12.117  -9.489  31.079  1.00 50.30           C  
ANISOU 1389  CA  ILE A 198     6934   6506   5672   1364    553    164       C  
ATOM   1390  C   ILE A 198      12.699  -9.036  32.413  1.00 49.32           C  
ANISOU 1390  C   ILE A 198     6571   6501   5665   1293    555    216       C  
ATOM   1391  O   ILE A 198      12.186  -9.385  33.486  1.00 51.03           O  
ANISOU 1391  O   ILE A 198     6802   6638   5950   1207    494    153       O  
ATOM   1392  CB  ILE A 198      12.955 -10.623  30.460  1.00 53.92           C  
ANISOU 1392  CB  ILE A 198     7567   6981   5941   1640    662    201       C  
ATOM   1393  CG1 ILE A 198      12.265 -11.199  29.223  1.00 59.05           C  
ANISOU 1393  CG1 ILE A 198     8516   7468   6454   1698    639    131       C  
ATOM   1394  CG2 ILE A 198      13.210 -11.715  31.486  1.00 51.89           C  
ANISOU 1394  CG2 ILE A 198     7383   6682   5652   1730    676    179       C  
ATOM   1395  CD1 ILE A 198      10.890 -11.754  29.506  1.00 59.72           C  
ANISOU 1395  CD1 ILE A 198     8797   7331   6561   1541    502      6       C  
ATOM   1396  N   CYS A 199      13.777  -8.246  32.367  1.00 51.22           N  
ANISOU 1396  N   CYS A 199     6593   6940   5927   1316    619    342       N  
ATOM   1397  CA  CYS A 199      14.407  -7.799  33.605  1.00 51.57           C  
ANISOU 1397  CA  CYS A 199     6423   7104   6067   1233    609    407       C  
ATOM   1398  C   CYS A 199      13.475  -6.911  34.411  1.00 49.61           C  
ANISOU 1398  C   CYS A 199     6110   6767   5971    989    495    333       C  
ATOM   1399  O   CYS A 199      13.431  -7.008  35.642  1.00 51.92           O  
ANISOU 1399  O   CYS A 199     6348   7048   6331    917    457    311       O  
ATOM   1400  CB  CYS A 199      15.708  -7.059  33.302  1.00 56.00           C  
ANISOU 1400  CB  CYS A 199     6762   7902   6612   1274    679    579       C  
ATOM   1401  SG  CYS A 199      17.012  -8.111  32.648  1.00 64.87           S  
ANISOU 1401  SG  CYS A 199     7907   9187   7553   1600    838    709       S  
ATOM   1402  N   VAL A 200      12.701  -6.055  33.741  1.00 48.11           N  
ANISOU 1402  N   VAL A 200     5939   6514   5828    872    445    297       N  
ATOM   1403  CA  VAL A 200      11.768  -5.215  34.482  1.00 48.25           C  
ANISOU 1403  CA  VAL A 200     5915   6445   5975    673    351    233       C  
ATOM   1404  C   VAL A 200      10.677  -6.066  35.115  1.00 46.24           C  
ANISOU 1404  C   VAL A 200     5799   6032   5737    649    297    118       C  
ATOM   1405  O   VAL A 200      10.304  -5.850  36.274  1.00 49.32           O  
ANISOU 1405  O   VAL A 200     6138   6389   6211    547    249     85       O  
ATOM   1406  CB  VAL A 200      11.174  -4.120  33.578  1.00 45.68           C  
ANISOU 1406  CB  VAL A 200     5581   6090   5687    574    316    231       C  
ATOM   1407  CG1 VAL A 200      10.064  -3.382  34.322  1.00 39.32           C  
ANISOU 1407  CG1 VAL A 200     4768   5177   4995    407    230    161       C  
ATOM   1408  CG2 VAL A 200      12.257  -3.145  33.147  1.00 43.26           C  
ANISOU 1408  CG2 VAL A 200     5116   5944   5377    558    353    357       C  
ATOM   1409  N   THR A 201      10.160  -7.059  34.381  1.00 45.07           N  
ANISOU 1409  N   THR A 201     5841   5785   5499    737    299     65       N  
ATOM   1410  CA  THR A 201       9.116  -7.901  34.954  1.00 44.90           C  
ANISOU 1410  CA  THR A 201     5952   5620   5486    693    233    -25       C  
ATOM   1411  C   THR A 201       9.637  -8.689  36.147  1.00 41.87           C  
ANISOU 1411  C   THR A 201     5551   5255   5101    746    252    -27       C  
ATOM   1412  O   THR A 201       8.893  -8.929  37.104  1.00 41.61           O  
ANISOU 1412  O   THR A 201     5531   5148   5129    657    192    -80       O  
ATOM   1413  CB  THR A 201       8.549  -8.851  33.898  1.00 45.83           C  
ANISOU 1413  CB  THR A 201     6304   5621   5487    761    216    -69       C  
ATOM   1414  OG1 THR A 201       8.081  -8.098  32.773  1.00 45.09           O  
ANISOU 1414  OG1 THR A 201     6222   5519   5393    709    196    -61       O  
ATOM   1415  CG2 THR A 201       7.379  -9.640  34.474  1.00 47.53           C  
ANISOU 1415  CG2 THR A 201     6649   5694   5715    673    124   -142       C  
ATOM   1416  N   VAL A 202      10.913  -9.075  36.124  1.00 43.19           N  
ANISOU 1416  N   VAL A 202     5677   5535   5199    895    338     44       N  
ATOM   1417  CA  VAL A 202      11.496  -9.756  37.278  1.00 40.93           C  
ANISOU 1417  CA  VAL A 202     5353   5286   4913    950    359     58       C  
ATOM   1418  C   VAL A 202      11.649  -8.791  38.449  1.00 43.50           C  
ANISOU 1418  C   VAL A 202     5478   5686   5365    802    324     83       C  
ATOM   1419  O   VAL A 202      11.284  -9.109  39.589  1.00 45.96           O  
ANISOU 1419  O   VAL A 202     5788   5947   5727    743    283     39       O  
ATOM   1420  CB  VAL A 202      12.841 -10.402  36.899  1.00 44.73           C  
ANISOU 1420  CB  VAL A 202     5830   5889   5276   1168    469    149       C  
ATOM   1421  CG1 VAL A 202      13.537 -10.941  38.136  1.00 46.79           C  
ANISOU 1421  CG1 VAL A 202     6011   6219   5548   1216    492    186       C  
ATOM   1422  CG2 VAL A 202      12.635 -11.517  35.865  1.00 47.14           C  
ANISOU 1422  CG2 VAL A 202     6398   6083   5430   1335    503    108       C  
ATOM   1423  N   LEU A 203      12.187  -7.593  38.188  1.00 40.19           N  
ANISOU 1423  N   LEU A 203     4903   5378   4988    736    333    157       N  
ATOM   1424  CA  LEU A 203      12.484  -6.659  39.273  1.00 41.55           C  
ANISOU 1424  CA  LEU A 203     4916   5616   5256    597    293    192       C  
ATOM   1425  C   LEU A 203      11.231  -6.102  39.936  1.00 41.35           C  
ANISOU 1425  C   LEU A 203     4927   5460   5325    442    211     99       C  
ATOM   1426  O   LEU A 203      11.247  -5.825  41.141  1.00 44.23           O  
ANISOU 1426  O   LEU A 203     5233   5825   5747    359    176     91       O  
ATOM   1427  CB  LEU A 203      13.356  -5.514  38.759  1.00 44.56           C  
ANISOU 1427  CB  LEU A 203     5147   6138   5645    547    308    305       C  
ATOM   1428  CG  LEU A 203      14.795  -5.922  38.448  1.00 48.02           C  
ANISOU 1428  CG  LEU A 203     5481   6764   5999    688    392    444       C  
ATOM   1429  CD1 LEU A 203      15.549  -4.810  37.741  1.00 48.24           C  
ANISOU 1429  CD1 LEU A 203     5366   6937   6027    631    401    570       C  
ATOM   1430  CD2 LEU A 203      15.498  -6.319  39.736  1.00 48.19           C  
ANISOU 1430  CD2 LEU A 203     5410   6866   6033    686    388    492       C  
ATOM   1431  N   ILE A 204      10.171  -5.902  39.176  1.00 39.71           N  
ANISOU 1431  N   ILE A 204     4813   5148   5128    408    182     38       N  
ATOM   1432  CA  ILE A 204       8.960  -5.295  39.779  1.00 38.77           C  
ANISOU 1432  CA  ILE A 204     4708   4931   5092    282    117    -25       C  
ATOM   1433  C   ILE A 204       7.888  -6.340  40.066  1.00 36.87           C  
ANISOU 1433  C   ILE A 204     4585   4578   4846    290     84    -99       C  
ATOM   1434  O   ILE A 204       6.854  -5.957  40.524  1.00 36.28           O  
ANISOU 1434  O   ILE A 204     4516   4437   4831    204     38   -136       O  
ATOM   1435  CB  ILE A 204       8.440  -4.147  38.908  1.00 38.53           C  
ANISOU 1435  CB  ILE A 204     4667   4878   5094    211     97    -18       C  
ATOM   1436  CG1 ILE A 204       7.788  -4.663  37.633  1.00 37.29           C  
ANISOU 1436  CG1 ILE A 204     4620   4666   4881    266     99    -42       C  
ATOM   1437  CG2 ILE A 204       9.534  -3.142  38.617  1.00 37.61           C  
ANISOU 1437  CG2 ILE A 204     4438   4871   4980    180    117     67       C  
ATOM   1438  CD1 ILE A 204       6.898  -3.669  36.981  1.00 37.92           C  
ANISOU 1438  CD1 ILE A 204     4696   4714   4998    194     72    -40       C  
ATOM   1439  N   TYR A 205       8.120  -7.607  39.775  1.00 37.34           N  
ANISOU 1439  N   TYR A 205     4745   4616   4826    394    105   -112       N  
ATOM   1440  CA  TYR A 205       7.055  -8.582  40.092  1.00 42.72           C  
ANISOU 1440  CA  TYR A 205     5549   5186   5495    375     55   -170       C  
ATOM   1441  C   TYR A 205       7.597  -9.871  40.713  1.00 46.62           C  
ANISOU 1441  C   TYR A 205     6110   5673   5931    468     76   -177       C  
ATOM   1442  O   TYR A 205       7.429 -10.052  41.891  1.00 48.29           O  
ANISOU 1442  O   TYR A 205     6282   5878   6188    427     56   -193       O  
ATOM   1443  CB  TYR A 205       6.165  -8.866  38.885  1.00 37.46           C  
ANISOU 1443  CB  TYR A 205     5021   4439   4771    374     21   -188       C  
ATOM   1444  CG  TYR A 205       4.937  -9.676  39.184  1.00 38.55           C  
ANISOU 1444  CG  TYR A 205     5269   4472   4907    302    -57   -225       C  
ATOM   1445  CD1 TYR A 205       3.832  -9.098  39.757  1.00 38.48           C  
ANISOU 1445  CD1 TYR A 205     5181   4452   4987    183   -107   -226       C  
ATOM   1446  CD2 TYR A 205       4.879 -11.023  38.899  1.00 44.08           C  
ANISOU 1446  CD2 TYR A 205     6159   5086   5505    354    -83   -247       C  
ATOM   1447  CE1 TYR A 205       2.698  -9.825  40.042  1.00 41.90           C  
ANISOU 1447  CE1 TYR A 205     5686   4817   5416    108   -182   -231       C  
ATOM   1448  CE2 TYR A 205       3.759 -11.773  39.190  1.00 48.24           C  
ANISOU 1448  CE2 TYR A 205     6785   5521   6024    260   -173   -263       C  
ATOM   1449  CZ  TYR A 205       2.660 -11.172  39.765  1.00 46.27           C  
ANISOU 1449  CZ  TYR A 205     6419   5288   5873    131   -222   -247       C  
ATOM   1450  OH  TYR A 205       1.551 -11.883  40.044  1.00 42.60           O  
ANISOU 1450  OH  TYR A 205     6027   4759   5400     29   -314   -236       O  
ATOM   1451  N   PHE A 206       8.259 -10.713  39.931  1.00 46.91           N  
ANISOU 1451  N   PHE A 206     6257   5709   5859    606    121   -162       N  
ATOM   1452  CA  PHE A 206       8.673 -12.043  40.434  1.00 46.70           C  
ANISOU 1452  CA  PHE A 206     6345   5641   5757    708    136   -175       C  
ATOM   1453  C   PHE A 206       9.669 -12.002  41.585  1.00 44.82           C  
ANISOU 1453  C   PHE A 206     5964   5511   5556    744    180   -134       C  
ATOM   1454  O   PHE A 206       9.399 -12.603  42.593  1.00 45.51           O  
ANISOU 1454  O   PHE A 206     6072   5557   5662    721    151   -161       O  
ATOM   1455  CB  PHE A 206       9.210 -12.867  39.275  1.00 43.68           C  
ANISOU 1455  CB  PHE A 206     6137   5231   5230    877    188   -163       C  
ATOM   1456  CG  PHE A 206       8.157 -13.131  38.247  1.00 48.17           C  
ANISOU 1456  CG  PHE A 206     6895   5666   5742    830    124   -209       C  
ATOM   1457  CD1 PHE A 206       7.115 -13.987  38.521  1.00 48.98           C  
ANISOU 1457  CD1 PHE A 206     7169   5625   5818    754     33   -261       C  
ATOM   1458  CD2 PHE A 206       8.187 -12.492  37.030  1.00 48.31           C  
ANISOU 1458  CD2 PHE A 206     6916   5708   5730    844    144   -191       C  
ATOM   1459  CE1 PHE A 206       6.129 -14.220  37.590  1.00 49.33           C  
ANISOU 1459  CE1 PHE A 206     7387   5552   5803    683    -45   -287       C  
ATOM   1460  CE2 PHE A 206       7.195 -12.723  36.102  1.00 50.72           C  
ANISOU 1460  CE2 PHE A 206     7398   5894   5979    787     74   -227       C  
ATOM   1461  CZ  PHE A 206       6.170 -13.586  36.383  1.00 50.38           C  
ANISOU 1461  CZ  PHE A 206     7526   5708   5906    700    -24   -272       C  
ATOM   1462  N   LEU A 207      10.732 -11.239  41.459  1.00 43.31           N  
ANISOU 1462  N   LEU A 207     5623   5465   5369    793    242    -56       N  
ATOM   1463  CA  LEU A 207      11.717 -11.202  42.539  1.00 48.20           C  
ANISOU 1463  CA  LEU A 207     6099   6202   6013    813    271      3       C  
ATOM   1464  C   LEU A 207      11.177 -10.608  43.837  1.00 47.77           C  
ANISOU 1464  C   LEU A 207     5955   6126   6067    650    206    -31       C  
ATOM   1465  O   LEU A 207      11.333 -11.248  44.895  1.00 45.60           O  
ANISOU 1465  O   LEU A 207     5679   5850   5798    663    199    -38       O  
ATOM   1466  CB  LEU A 207      12.975 -10.458  42.074  1.00 50.35           C  
ANISOU 1466  CB  LEU A 207     6211   6651   6268    863    334    119       C  
ATOM   1467  CG  LEU A 207      13.971 -10.170  43.205  1.00 52.21           C  
ANISOU 1467  CG  LEU A 207     6269   7027   6540    832    340    204       C  
ATOM   1468  CD1 LEU A 207      14.549 -11.470  43.760  1.00 51.22           C  
ANISOU 1468  CD1 LEU A 207     6191   6926   6345    987    388    227       C  
ATOM   1469  CD2 LEU A 207      15.077  -9.236  42.738  1.00 53.30           C  
ANISOU 1469  CD2 LEU A 207     6230   7350   6672    824    374    338       C  
ATOM   1470  N   PRO A 208      10.583  -9.405  43.854  1.00 48.13           N  
ANISOU 1470  N   PRO A 208     5935   6158   6193    509    162    -48       N  
ATOM   1471  CA  PRO A 208      10.046  -8.902  45.133  1.00 44.83           C  
ANISOU 1471  CA  PRO A 208     5467   5710   5858    384    110    -83       C  
ATOM   1472  C   PRO A 208       8.986  -9.806  45.732  1.00 45.47           C  
ANISOU 1472  C   PRO A 208     5653   5678   5945    372     74   -154       C  
ATOM   1473  O   PRO A 208       8.932  -9.958  46.957  1.00 43.51           O  
ANISOU 1473  O   PRO A 208     5374   5428   5729    333     55   -166       O  
ATOM   1474  CB  PRO A 208       9.491  -7.517  44.765  1.00 42.62           C  
ANISOU 1474  CB  PRO A 208     5146   5411   5636    272     80    -90       C  
ATOM   1475  CG  PRO A 208       9.257  -7.565  43.291  1.00 41.32           C  
ANISOU 1475  CG  PRO A 208     5043   5226   5430    324     99    -88       C  
ATOM   1476  CD  PRO A 208      10.337  -8.455  42.749  1.00 43.99           C  
ANISOU 1476  CD  PRO A 208     5397   5637   5681    468    161    -38       C  
ATOM   1477  N   LEU A 209       8.159 -10.444  44.902  1.00 42.65           N  
ANISOU 1477  N   LEU A 209     5425   5229   5551    396     56   -191       N  
ATOM   1478  CA  LEU A 209       7.150 -11.339  45.450  1.00 43.58           C  
ANISOU 1478  CA  LEU A 209     5641   5250   5668    362      7   -237       C  
ATOM   1479  C   LEU A 209       7.786 -12.564  46.088  1.00 46.89           C  
ANISOU 1479  C   LEU A 209     6119   5666   6033    452     25   -235       C  
ATOM   1480  O   LEU A 209       7.345 -13.007  47.150  1.00 48.05           O  
ANISOU 1480  O   LEU A 209     6270   5780   6206    407     -7   -254       O  
ATOM   1481  CB  LEU A 209       6.152 -11.753  44.371  1.00 42.47           C  
ANISOU 1481  CB  LEU A 209     5634   5015   5488    342    -35   -260       C  
ATOM   1482  CG  LEU A 209       5.169 -10.653  43.968  1.00 44.77           C  
ANISOU 1482  CG  LEU A 209     5867   5299   5843    238    -67   -259       C  
ATOM   1483  CD1 LEU A 209       4.111 -11.204  43.046  1.00 47.18           C  
ANISOU 1483  CD1 LEU A 209     6301   5519   6106    198   -128   -266       C  
ATOM   1484  CD2 LEU A 209       4.539 -10.023  45.197  1.00 40.89           C  
ANISOU 1484  CD2 LEU A 209     5275   4824   5437    154    -86   -262       C  
ATOM   1485  N   LEU A 210       8.842 -13.107  45.480  1.00 47.69           N  
ANISOU 1485  N   LEU A 210     6262   5807   6052    591     83   -201       N  
ATOM   1486  CA  LEU A 210       9.502 -14.256  46.092  1.00 48.87           C  
ANISOU 1486  CA  LEU A 210     6471   5958   6141    700    110   -189       C  
ATOM   1487  C   LEU A 210      10.167 -13.867  47.403  1.00 48.05           C  
ANISOU 1487  C   LEU A 210     6203   5955   6097    668    122   -155       C  
ATOM   1488  O   LEU A 210      10.091 -14.610  48.392  1.00 47.77           O  
ANISOU 1488  O   LEU A 210     6198   5892   6062    672    105   -169       O  
ATOM   1489  CB  LEU A 210      10.526 -14.858  45.129  1.00 49.97           C  
ANISOU 1489  CB  LEU A 210     6689   6132   6165    889    186   -145       C  
ATOM   1490  CG  LEU A 210       9.938 -15.415  43.834  1.00 57.84           C  
ANISOU 1490  CG  LEU A 210     7899   7006   7070    936    171   -183       C  
ATOM   1491  CD1 LEU A 210      11.036 -15.875  42.883  1.00 59.29           C  
ANISOU 1491  CD1 LEU A 210     8159   7240   7128   1151    266   -131       C  
ATOM   1492  CD2 LEU A 210       8.971 -16.549  44.139  1.00 62.29           C  
ANISOU 1492  CD2 LEU A 210     8666   7407   7595    893     94   -243       C  
ATOM   1493  N   VAL A 211      10.771 -12.678  47.446  1.00 46.06           N  
ANISOU 1493  N   VAL A 211     5789   5816   5895    619    140   -107       N  
ATOM   1494  CA  VAL A 211      11.451 -12.237  48.660  1.00 44.44           C  
ANISOU 1494  CA  VAL A 211     5443   5707   5735    567    135    -65       C  
ATOM   1495  C   VAL A 211      10.442 -11.989  49.777  1.00 46.53           C  
ANISOU 1495  C   VAL A 211     5714   5896   6071    438     75   -129       C  
ATOM   1496  O   VAL A 211      10.611 -12.460  50.912  1.00 46.90           O  
ANISOU 1496  O   VAL A 211     5744   5952   6124    433     64   -129       O  
ATOM   1497  CB  VAL A 211      12.295 -10.985  48.367  1.00 42.72           C  
ANISOU 1497  CB  VAL A 211     5076   5616   5541    517    148     11       C  
ATOM   1498  CG1 VAL A 211      12.829 -10.381  49.660  1.00 42.23           C  
ANISOU 1498  CG1 VAL A 211     4895   5629   5524    415    115     50       C  
ATOM   1499  CG2 VAL A 211      13.429 -11.329  47.423  1.00 43.38           C  
ANISOU 1499  CG2 VAL A 211     5124   5812   5545    665    221    102       C  
ATOM   1500  N   ILE A 212       9.372 -11.252  49.470  1.00 44.32           N  
ANISOU 1500  N   ILE A 212     5456   5547   5838    345     40   -174       N  
ATOM   1501  CA  ILE A 212       8.341 -10.976  50.461  1.00 41.10           C  
ANISOU 1501  CA  ILE A 212     5052   5079   5486    248     -3   -220       C  
ATOM   1502  C   ILE A 212       7.634 -12.259  50.878  1.00 44.83           C  
ANISOU 1502  C   ILE A 212     5621   5476   5937    271    -25   -252       C  
ATOM   1503  O   ILE A 212       7.259 -12.415  52.047  1.00 47.13           O  
ANISOU 1503  O   ILE A 212     5898   5756   6255    227    -46   -266       O  
ATOM   1504  CB  ILE A 212       7.348  -9.931  49.910  1.00 37.26           C  
ANISOU 1504  CB  ILE A 212     4566   4549   5043    173    -22   -242       C  
ATOM   1505  CG1 ILE A 212       8.041  -8.585  49.695  1.00 42.12           C  
ANISOU 1505  CG1 ILE A 212     5099   5225   5679    130    -13   -209       C  
ATOM   1506  CG2 ILE A 212       6.179  -9.742  50.850  1.00 36.63           C  
ANISOU 1506  CG2 ILE A 212     4494   4417   5005    107    -52   -273       C  
ATOM   1507  CD1 ILE A 212       7.173  -7.580  48.943  1.00 42.86           C  
ANISOU 1507  CD1 ILE A 212     5207   5274   5803     81    -24   -224       C  
ATOM   1508  N   GLY A 213       7.474 -13.210  49.957  1.00 40.35           N  
ANISOU 1508  N   GLY A 213     5170   4852   5310    337    -25   -259       N  
ATOM   1509  CA  GLY A 213       6.834 -14.458  50.319  1.00 41.48           C  
ANISOU 1509  CA  GLY A 213     5431   4911   5420    341    -63   -280       C  
ATOM   1510  C   GLY A 213       7.684 -15.275  51.267  1.00 43.06           C  
ANISOU 1510  C   GLY A 213     5630   5140   5591    411    -41   -266       C  
ATOM   1511  O   GLY A 213       7.174 -15.815  52.250  1.00 40.51           O  
ANISOU 1511  O   GLY A 213     5327   4782   5283    368    -75   -279       O  
ATOM   1512  N   TYR A 214       9.002 -15.307  51.038  1.00 40.89           N  
ANISOU 1512  N   TYR A 214     5313   4947   5277    520     17   -225       N  
ATOM   1513  CA  TYR A 214       9.885 -15.955  52.003  1.00 43.94           C  
ANISOU 1513  CA  TYR A 214     5667   5387   5640    589     41   -193       C  
ATOM   1514  C   TYR A 214       9.801 -15.268  53.361  1.00 43.80           C  
ANISOU 1514  C   TYR A 214     5525   5421   5697    480     16   -193       C  
ATOM   1515  O   TYR A 214       9.627 -15.928  54.399  1.00 41.85           O  
ANISOU 1515  O   TYR A 214     5299   5151   5452    469     -4   -203       O  
ATOM   1516  CB  TYR A 214      11.334 -15.952  51.508  1.00 46.59           C  
ANISOU 1516  CB  TYR A 214     5940   5840   5921    725    113   -118       C  
ATOM   1517  CG  TYR A 214      12.304 -16.250  52.637  1.00 46.21           C  
ANISOU 1517  CG  TYR A 214     5796   5893   5870    766    133    -60       C  
ATOM   1518  CD1 TYR A 214      12.572 -17.559  53.018  1.00 49.72           C  
ANISOU 1518  CD1 TYR A 214     6340   6301   6250    884    151    -53       C  
ATOM   1519  CD2 TYR A 214      12.919 -15.223  53.348  1.00 45.31           C  
ANISOU 1519  CD2 TYR A 214     5504   5901   5811    677    124    -10       C  
ATOM   1520  CE1 TYR A 214      13.433 -17.838  54.065  1.00 53.03           C  
ANISOU 1520  CE1 TYR A 214     6665   6819   6667    922    168      8       C  
ATOM   1521  CE2 TYR A 214      13.779 -15.490  54.396  1.00 47.98           C  
ANISOU 1521  CE2 TYR A 214     5753   6336   6143    696    129     52       C  
ATOM   1522  CZ  TYR A 214      14.035 -16.800  54.752  1.00 51.91           C  
ANISOU 1522  CZ  TYR A 214     6331   6810   6582    823    155     63       C  
ATOM   1523  OH  TYR A 214      14.893 -17.076  55.795  1.00 51.26           O  
ANISOU 1523  OH  TYR A 214     6151   6832   6492    846    161    133       O  
ATOM   1524  N   LEU A 215       9.918 -13.935  53.368  1.00 42.47           N  
ANISOU 1524  N   LEU A 215     5245   5312   5581    398     13   -182       N  
ATOM   1525  CA  LEU A 215       9.978 -13.204  54.629  1.00 38.58           C  
ANISOU 1525  CA  LEU A 215     4664   4860   5137    303    -12   -179       C  
ATOM   1526  C   LEU A 215       8.706 -13.407  55.441  1.00 38.53           C  
ANISOU 1526  C   LEU A 215     4710   4767   5161    236    -48   -234       C  
ATOM   1527  O   LEU A 215       8.759 -13.729  56.635  1.00 40.86           O  
ANISOU 1527  O   LEU A 215     4992   5072   5461    217    -61   -235       O  
ATOM   1528  CB  LEU A 215      10.220 -11.715  54.365  1.00 39.02           C  
ANISOU 1528  CB  LEU A 215     4638   4962   5225    221    -19   -161       C  
ATOM   1529  CG  LEU A 215      11.549 -11.323  53.705  1.00 42.07           C  
ANISOU 1529  CG  LEU A 215     4935   5466   5583    257      8    -79       C  
ATOM   1530  CD1 LEU A 215      11.569  -9.839  53.293  1.00 40.28           C  
ANISOU 1530  CD1 LEU A 215     4661   5257   5388    156    -13    -65       C  
ATOM   1531  CD2 LEU A 215      12.738 -11.658  54.606  1.00 40.58           C  
ANISOU 1531  CD2 LEU A 215     4659   5389   5370    276     10     -3       C  
ATOM   1532  N   TYR A 216       7.547 -13.246  54.805  1.00 38.89           N  
ANISOU 1532  N   TYR A 216     4810   4741   5225    202    -64   -267       N  
ATOM   1533  CA  TYR A 216       6.296 -13.400  55.531  1.00 39.17           C  
ANISOU 1533  CA  TYR A 216     4873   4724   5288    142    -94   -291       C  
ATOM   1534  C   TYR A 216       5.924 -14.855  55.791  1.00 39.00           C  
ANISOU 1534  C   TYR A 216     4936   4649   5232    165   -119   -292       C  
ATOM   1535  O   TYR A 216       5.186 -15.112  56.738  1.00 38.35           O  
ANISOU 1535  O   TYR A 216     4852   4554   5167    119   -141   -293       O  
ATOM   1536  CB  TYR A 216       5.164 -12.677  54.797  1.00 36.69           C  
ANISOU 1536  CB  TYR A 216     4565   4375   5003     93   -105   -300       C  
ATOM   1537  CG  TYR A 216       5.186 -11.177  55.044  1.00 38.34           C  
ANISOU 1537  CG  TYR A 216     4710   4612   5246     55    -89   -304       C  
ATOM   1538  CD1 TYR A 216       5.621 -10.658  56.264  1.00 38.10           C  
ANISOU 1538  CD1 TYR A 216     4647   4610   5221     31    -85   -307       C  
ATOM   1539  CD2 TYR A 216       4.788 -10.284  54.058  1.00 37.35           C  
ANISOU 1539  CD2 TYR A 216     4580   4475   5137     39    -83   -303       C  
ATOM   1540  CE1 TYR A 216       5.650  -9.286  56.491  1.00 39.27           C  
ANISOU 1540  CE1 TYR A 216     4782   4758   5381     -8    -80   -313       C  
ATOM   1541  CE2 TYR A 216       4.815  -8.920  54.270  1.00 37.69           C  
ANISOU 1541  CE2 TYR A 216     4595   4525   5200      8    -72   -306       C  
ATOM   1542  CZ  TYR A 216       5.245  -8.424  55.484  1.00 40.03           C  
ANISOU 1542  CZ  TYR A 216     4883   4835   5492    -16    -73   -313       C  
ATOM   1543  OH  TYR A 216       5.267  -7.063  55.673  1.00 40.55           O  
ANISOU 1543  OH  TYR A 216     4964   4883   5559    -50    -71   -318       O  
ATOM   1544  N   THR A 217       6.450 -15.817  55.032  1.00 37.75           N  
ANISOU 1544  N   THR A 217     4865   4460   5017    242   -115   -286       N  
ATOM   1545  CA  THR A 217       6.233 -17.208  55.400  1.00 41.65           C  
ANISOU 1545  CA  THR A 217     5468   4890   5465    266   -144   -286       C  
ATOM   1546  C   THR A 217       6.960 -17.526  56.697  1.00 43.78           C  
ANISOU 1546  C   THR A 217     5685   5211   5738    294   -128   -273       C  
ATOM   1547  O   THR A 217       6.376 -18.095  57.631  1.00 45.66           O  
ANISOU 1547  O   THR A 217     5945   5422   5983    249   -160   -274       O  
ATOM   1548  CB  THR A 217       6.702 -18.138  54.277  1.00 42.94           C  
ANISOU 1548  CB  THR A 217     5778   4993   5546    365   -138   -285       C  
ATOM   1549  OG1 THR A 217       5.834 -18.012  53.145  1.00 43.24           O  
ANISOU 1549  OG1 THR A 217     5892   4964   5572    316   -174   -296       O  
ATOM   1550  CG2 THR A 217       6.696 -19.589  54.745  1.00 46.35           C  
ANISOU 1550  CG2 THR A 217     6350   5347   5915    405   -167   -282       C  
ATOM   1551  N   VAL A 218       8.224 -17.105  56.794  1.00 39.79           N  
ANISOU 1551  N   VAL A 218     5097   4794   5227    357    -83   -249       N  
ATOM   1552  CA  VAL A 218       8.987 -17.367  58.009  1.00 40.91           C  
ANISOU 1552  CA  VAL A 218     5179   4998   5367    376    -73   -223       C  
ATOM   1553  C   VAL A 218       8.364 -16.635  59.192  1.00 43.81           C  
ANISOU 1553  C   VAL A 218     5476   5380   5788    266    -99   -242       C  
ATOM   1554  O   VAL A 218       8.131 -17.224  60.259  1.00 44.40           O  
ANISOU 1554  O   VAL A 218     5565   5444   5861    249   -117   -243       O  
ATOM   1555  CB  VAL A 218      10.462 -16.979  57.804  1.00 41.07           C  
ANISOU 1555  CB  VAL A 218     5104   5136   5367    449    -29   -166       C  
ATOM   1556  CG1 VAL A 218      11.211 -17.007  59.117  1.00 40.80           C  
ANISOU 1556  CG1 VAL A 218     4982   5183   5337    435    -33   -127       C  
ATOM   1557  CG2 VAL A 218      11.111 -17.917  56.792  1.00 43.11           C  
ANISOU 1557  CG2 VAL A 218     5446   5385   5549    602     14   -137       C  
ATOM   1558  N   VAL A 219       8.030 -15.352  59.006  1.00 40.79           N  
ANISOU 1558  N   VAL A 219     5038   5014   5446    198    -99   -255       N  
ATOM   1559  CA  VAL A 219       7.470 -14.581  60.112  1.00 42.39           C  
ANISOU 1559  CA  VAL A 219     5204   5223   5680    120   -113   -272       C  
ATOM   1560  C   VAL A 219       6.096 -15.110  60.512  1.00 41.42           C  
ANISOU 1560  C   VAL A 219     5128   5042   5568     90   -131   -286       C  
ATOM   1561  O   VAL A 219       5.791 -15.227  61.706  1.00 43.26           O  
ANISOU 1561  O   VAL A 219     5351   5284   5803     65   -138   -286       O  
ATOM   1562  CB  VAL A 219       7.418 -13.085  59.748  1.00 43.29           C  
ANISOU 1562  CB  VAL A 219     5281   5350   5819     70   -107   -281       C  
ATOM   1563  CG1 VAL A 219       6.453 -12.348  60.666  1.00 34.66           C  
ANISOU 1563  CG1 VAL A 219     4199   4229   4741     18   -111   -305       C  
ATOM   1564  CG2 VAL A 219       8.810 -12.470  59.834  1.00 39.00           C  
ANISOU 1564  CG2 VAL A 219     4674   4882   5260     57   -108   -245       C  
ATOM   1565  N   GLY A 220       5.247 -15.455  59.539  1.00 40.72           N  
ANISOU 1565  N   GLY A 220     5088   4902   5480     85   -145   -287       N  
ATOM   1566  CA  GLY A 220       3.900 -15.869  59.877  1.00 41.83           C  
ANISOU 1566  CA  GLY A 220     5250   5012   5630     36   -173   -272       C  
ATOM   1567  C   GLY A 220       3.871 -17.224  60.549  1.00 43.58           C  
ANISOU 1567  C   GLY A 220     5528   5209   5823     38   -203   -256       C  
ATOM   1568  O   GLY A 220       3.110 -17.437  61.499  1.00 45.76           O  
ANISOU 1568  O   GLY A 220     5783   5497   6106     -4   -216   -233       O  
ATOM   1569  N   ILE A 221       4.743 -18.138  60.113  1.00 43.85           N  
ANISOU 1569  N   ILE A 221     5635   5210   5815     98   -208   -260       N  
ATOM   1570  CA  ILE A 221       4.842 -19.414  60.807  1.00 41.02           C  
ANISOU 1570  CA  ILE A 221     5347   4818   5422    113   -235   -246       C  
ATOM   1571  C   ILE A 221       5.375 -19.211  62.219  1.00 40.20           C  
ANISOU 1571  C   ILE A 221     5163   4779   5331    119   -213   -243       C  
ATOM   1572  O   ILE A 221       4.849 -19.790  63.179  1.00 39.19           O  
ANISOU 1572  O   ILE A 221     5046   4645   5201     82   -237   -226       O  
ATOM   1573  CB  ILE A 221       5.708 -20.395  59.997  1.00 41.68           C  
ANISOU 1573  CB  ILE A 221     5550   4846   5441    208   -233   -248       C  
ATOM   1574  CG1 ILE A 221       4.983 -20.774  58.697  1.00 37.69           C  
ANISOU 1574  CG1 ILE A 221     5167   4250   4902    183   -275   -251       C  
ATOM   1575  CG2 ILE A 221       6.046 -21.622  60.841  1.00 45.40           C  
ANISOU 1575  CG2 ILE A 221     6096   5286   5870    246   -250   -232       C  
ATOM   1576  CD1 ILE A 221       5.803 -21.602  57.715  1.00 39.71           C  
ANISOU 1576  CD1 ILE A 221     5576   4438   5075    300   -262   -259       C  
ATOM   1577  N   THR A 222       6.393 -18.355  62.383  1.00 39.12           N  
ANISOU 1577  N   THR A 222     4947   4709   5205    151   -175   -251       N  
ATOM   1578  CA  THR A 222       6.946 -18.142  63.718  1.00 40.25           C  
ANISOU 1578  CA  THR A 222     5030   4912   5351    141   -168   -244       C  
ATOM   1579  C   THR A 222       5.911 -17.535  64.657  1.00 38.79           C  
ANISOU 1579  C   THR A 222     4817   4732   5190     71   -173   -252       C  
ATOM   1580  O   THR A 222       5.798 -17.945  65.819  1.00 37.66           O  
ANISOU 1580  O   THR A 222     4671   4603   5037     58   -181   -242       O  
ATOM   1581  CB  THR A 222       8.184 -17.246  63.644  1.00 40.83           C  
ANISOU 1581  CB  THR A 222     5028   5061   5425    157   -146   -233       C  
ATOM   1582  OG1 THR A 222       9.196 -17.895  62.864  1.00 44.21           O  
ANISOU 1582  OG1 THR A 222     5467   5511   5820    248   -128   -202       O  
ATOM   1583  CG2 THR A 222       8.733 -16.961  65.045  1.00 38.75           C  
ANISOU 1583  CG2 THR A 222     4714   4855   5154    122   -156   -219       C  
ATOM   1584  N   LEU A 223       5.109 -16.598  64.160  1.00 36.22           N  
ANISOU 1584  N   LEU A 223     4475   4398   4889     40   -162   -264       N  
ATOM   1585  CA  LEU A 223       4.122 -15.965  65.023  1.00 34.97           C  
ANISOU 1585  CA  LEU A 223     4294   4253   4739      7   -149   -260       C  
ATOM   1586  C   LEU A 223       2.978 -16.916  65.352  1.00 37.38           C  
ANISOU 1586  C   LEU A 223     4613   4549   5042    -17   -170   -220       C  
ATOM   1587  O   LEU A 223       2.541 -16.988  66.508  1.00 37.63           O  
ANISOU 1587  O   LEU A 223     4626   4609   5062    -25   -161   -201       O  
ATOM   1588  CB  LEU A 223       3.598 -14.686  64.371  1.00 39.13           C  
ANISOU 1588  CB  LEU A 223     4806   4777   5285      1   -125   -273       C  
ATOM   1589  CG  LEU A 223       4.607 -13.539  64.270  1.00 37.86           C  
ANISOU 1589  CG  LEU A 223     4641   4626   5120     -1   -114   -302       C  
ATOM   1590  CD1 LEU A 223       4.011 -12.369  63.511  1.00 34.72           C  
ANISOU 1590  CD1 LEU A 223     4247   4208   4736     -3    -93   -312       C  
ATOM   1591  CD2 LEU A 223       5.068 -13.104  65.673  1.00 36.25           C  
ANISOU 1591  CD2 LEU A 223     4450   4440   4883    -17   -114   -312       C  
ATOM   1592  N   ARG A 224       2.484 -17.666  64.361  1.00 35.27           N  
ANISOU 1592  N   ARG A 224     4383   4242   4777    -37   -205   -198       N  
ATOM   1593  CA  ARG A 224       1.399 -18.599  64.648  1.00 39.37           C  
ANISOU 1593  CA  ARG A 224     4917   4755   5287    -90   -245   -139       C  
ATOM   1594  C   ARG A 224       1.850 -19.703  65.602  1.00 36.88           C  
ANISOU 1594  C   ARG A 224     4641   4426   4944    -87   -268   -131       C  
ATOM   1595  O   ARG A 224       1.094 -20.106  66.492  1.00 37.59           O  
ANISOU 1595  O   ARG A 224     4708   4546   5028   -126   -282    -82       O  
ATOM   1596  CB  ARG A 224       0.859 -19.196  63.343  1.00 40.06           C  
ANISOU 1596  CB  ARG A 224     5067   4786   5367   -134   -299   -114       C  
ATOM   1597  CG  ARG A 224      -0.378 -20.092  63.514  1.00 45.58           C  
ANISOU 1597  CG  ARG A 224     5781   5484   6052   -226   -364    -29       C  
ATOM   1598  CD  ARG A 224      -1.013 -20.427  62.155  1.00 52.14           C  
ANISOU 1598  CD  ARG A 224     6678   6265   6870   -293   -428      4       C  
ATOM   1599  NE  ARG A 224       0.034 -20.650  61.169  1.00 56.12           N  
ANISOU 1599  NE  ARG A 224     7291   6684   7348   -234   -429    -67       N  
ATOM   1600  CZ  ARG A 224       0.214 -19.947  60.056  1.00 47.16           C  
ANISOU 1600  CZ  ARG A 224     6157   5537   6223   -208   -410    -98       C  
ATOM   1601  NH1 ARG A 224      -0.611 -18.966  59.713  1.00 47.58           N  
ANISOU 1601  NH1 ARG A 224     6116   5649   6314   -241   -394    -67       N  
ATOM   1602  NH2 ARG A 224       1.231 -20.251  59.272  1.00 45.43           N  
ANISOU 1602  NH2 ARG A 224     6038   5254   5969   -137   -401   -151       N  
ATOM   1603  N   ALA A 225       3.087 -20.184  65.455  1.00 35.88           N  
ANISOU 1603  N   ALA A 225     4567   4269   4799    -33   -268   -167       N  
ATOM   1604  CA  ALA A 225       3.572 -21.234  66.341  1.00 37.95           C  
ANISOU 1604  CA  ALA A 225     4869   4519   5031    -17   -287   -155       C  
ATOM   1605  C   ALA A 225       3.870 -20.710  67.741  1.00 41.35           C  
ANISOU 1605  C   ALA A 225     5224   5018   5467    -11   -255   -160       C  
ATOM   1606  O   ALA A 225       3.967 -21.507  68.678  1.00 41.02           O  
ANISOU 1606  O   ALA A 225     5201   4980   5406    -14   -272   -138       O  
ATOM   1607  CB  ALA A 225       4.815 -21.897  65.750  1.00 36.42           C  
ANISOU 1607  CB  ALA A 225     4751   4284   4804     66   -285   -175       C  
ATOM   1608  N   SER A 226       4.021 -19.397  67.897  1.00 41.58           N  
ANISOU 1608  N   SER A 226     5191   5093   5514     -5   -215   -186       N  
ATOM   1609  CA  SER A 226       4.217 -18.771  69.200  1.00 39.94           C  
ANISOU 1609  CA  SER A 226     4946   4935   5295     -7   -192   -194       C  
ATOM   1610  C   SER A 226       2.875 -18.305  69.752  1.00 44.58           C  
ANISOU 1610  C   SER A 226     5508   5547   5882    -28   -169   -167       C  
ATOM   1611  O   SER A 226       2.780 -17.830  70.883  1.00 47.15           O  
ANISOU 1611  O   SER A 226     5826   5906   6183    -20   -144   -169       O  
ATOM   1612  CB  SER A 226       5.185 -17.589  69.096  1.00 41.54           C  
ANISOU 1612  CB  SER A 226     5127   5159   5496      3   -173   -231       C  
ATOM   1613  OG  SER A 226       6.390 -17.962  68.449  1.00 45.76           O  
ANISOU 1613  OG  SER A 226     5658   5699   6029     33   -185   -231       O  
ATOM   1614  N   GLY A1218       1.707 -18.631  69.258  1.00 44.54           N  
ANISOU 1614  N   GLY A1218     5492   5542   5891    -55   -180   -120       N  
ATOM   1615  CA  GLY A1218       0.361 -18.292  69.674  1.00 44.62           C  
ANISOU 1615  CA  GLY A1218     5452   5604   5897    -64   -154    -60       C  
ATOM   1616  C   GLY A1218      -0.208 -19.294  70.657  1.00 49.27           C  
ANISOU 1616  C   GLY A1218     6027   6229   6466    -95   -175      6       C  
ATOM   1617  O   GLY A1218       0.071 -20.489  70.579  1.00 50.50           O  
ANISOU 1617  O   GLY A1218     6225   6345   6618   -136   -231     20       O  
ATOM   1618  N   ILE A1219      -1.014 -18.809  71.594  1.00 50.07           N  
ANISOU 1618  N   ILE A1219     6079   6402   6544    -68   -125     53       N  
ATOM   1619  CA  ILE A1219      -1.677 -19.668  72.567  1.00 46.00           C  
ANISOU 1619  CA  ILE A1219     5532   5942   6005    -97   -138    135       C  
ATOM   1620  C   ILE A1219      -3.108 -19.174  72.713  1.00 45.98           C  
ANISOU 1620  C   ILE A1219     5440   6040   5990    -77    -91    240       C  
ATOM   1621  O   ILE A1219      -3.370 -17.971  72.626  1.00 49.40           O  
ANISOU 1621  O   ILE A1219     5859   6498   6412      2    -21    224       O  
ATOM   1622  CB  ILE A1219      -0.918 -19.681  73.917  1.00 45.90           C  
ANISOU 1622  CB  ILE A1219     5552   5933   5956    -59   -115     93       C  
ATOM   1623  CG1 ILE A1219      -1.533 -20.678  74.904  1.00 49.47           C  
ANISOU 1623  CG1 ILE A1219     5974   6440   6384    -94   -133    180       C  
ATOM   1624  CG2 ILE A1219      -0.866 -18.293  74.542  1.00 45.41           C  
ANISOU 1624  CG2 ILE A1219     5505   5894   5856     24    -37     51       C  
ATOM   1625  CD1 ILE A1219      -0.748 -20.798  76.203  1.00 46.02           C  
ANISOU 1625  CD1 ILE A1219     5574   6002   5907    -63   -119    140       C  
ATOM   1626  N   ASP A1220      -4.038 -20.106  72.889  1.00 45.77           N  
ANISOU 1626  N   ASP A1220     5356   6076   5960   -148   -132    360       N  
ATOM   1627  CA  ASP A1220      -5.423 -19.749  73.179  1.00 46.57           C  
ANISOU 1627  CA  ASP A1220     5342   6312   6041   -125    -83    498       C  
ATOM   1628  C   ASP A1220      -5.583 -19.381  74.663  1.00 49.82           C  
ANISOU 1628  C   ASP A1220     5733   6799   6397    -28      2    519       C  
ATOM   1629  O   ASP A1220      -5.693 -20.259  75.525  1.00 47.74           O  
ANISOU 1629  O   ASP A1220     5455   6572   6113    -70    -24    574       O  
ATOM   1630  CB  ASP A1220      -6.352 -20.903  72.797  1.00 48.74           C  
ANISOU 1630  CB  ASP A1220     5556   6638   6326   -263   -175    643       C  
ATOM   1631  CG  ASP A1220      -7.819 -20.554  72.953  1.00 54.32           C  
ANISOU 1631  CG  ASP A1220     6110   7516   7014   -249   -132    821       C  
ATOM   1632  OD1 ASP A1220      -8.134 -19.409  73.340  1.00 57.36           O  
ANISOU 1632  OD1 ASP A1220     6447   7973   7373   -106    -17    825       O  
ATOM   1633  OD2 ASP A1220      -8.665 -21.435  72.686  1.00 58.44           O  
ANISOU 1633  OD2 ASP A1220     6565   8103   7537   -382   -217    968       O  
HETATM 1634  N   YCM A1221      -5.607 -18.080  74.947  1.00 53.70           N  
ANISOU 1634  N   YCM A1221     6244   7307   6854    104    101    476       N  
HETATM 1635  CA  YCM A1221      -5.741 -17.568  76.350  1.00 54.94           C  
ANISOU 1635  CA  YCM A1221     6423   7518   6935    221    193    484       C  
HETATM 1636  CB  YCM A1221      -5.362 -16.092  76.425  1.00 60.10           C  
ANISOU 1636  CB  YCM A1221     7178   8114   7544    350    274    385       C  
HETATM 1637  SG  YCM A1221      -3.625 -15.898  76.195  1.00 61.80           S  
ANISOU 1637  SG  YCM A1221     7533   8167   7783    291    208    201       S  
HETATM 1638  CD  YCM A1221      -3.171 -16.929  77.553  1.00 64.03           C  
ANISOU 1638  CD  YCM A1221     7830   8464   8033    252    178    207       C  
HETATM 1639  CE  YCM A1221      -3.381 -16.210  78.866  1.00 65.87           C  
ANISOU 1639  CE  YCM A1221     8133   8728   8166    367    263    206       C  
HETATM 1640  OZ1 YCM A1221      -3.085 -15.033  78.974  1.00 69.19           O  
ANISOU 1640  OZ1 YCM A1221     8666   9090   8534    444    307    134       O  
HETATM 1641  NZ2 YCM A1221      -3.906 -16.920  79.868  1.00 61.06           N  
ANISOU 1641  NZ2 YCM A1221     7475   8205   7520    378    282    292       N  
HETATM 1642  C   YCM A1221      -7.129 -17.736  76.892  1.00 54.11           C  
ANISOU 1642  C   YCM A1221     6189   7580   6790    266    249    664       C  
HETATM 1643  O   YCM A1221      -7.349 -17.591  78.096  1.00 54.32           O  
ANISOU 1643  O   YCM A1221     6224   7670   6746    356    320    697       O  
ATOM   1644  N   SER A1222      -8.086 -18.035  76.021  1.00 53.94           N  
ANISOU 1644  N   SER A1222     6046   7644   6806    203    218    794       N  
ATOM   1645  CA  SER A1222      -9.450 -18.269  76.482  1.00 56.59           C  
ANISOU 1645  CA  SER A1222     6225   8172   7106    228    262   1004       C  
ATOM   1646  C   SER A1222      -9.591 -19.685  77.034  1.00 54.61           C  
ANISOU 1646  C   SER A1222     5924   7963   6861     86    173   1094       C  
ATOM   1647  O   SER A1222     -10.607 -20.019  77.644  1.00 57.17           O  
ANISOU 1647  O   SER A1222     6117   8457   7148     91    202   1277       O  
ATOM   1648  CB  SER A1222     -10.461 -18.027  75.357  1.00 60.13           C  
ANISOU 1648  CB  SER A1222     6546   8716   7584    200    251   1137       C  
ATOM   1649  OG  SER A1222     -10.552 -19.145  74.491  1.00 62.62           O  
ANISOU 1649  OG  SER A1222     6828   9006   7960     -9    105   1188       O  
ATOM   1650  N   PHE A1223      -8.571 -20.520  76.825  1.00 51.85           N  
ANISOU 1650  N   PHE A1223     5682   7466   6552    -35     67    976       N  
ATOM   1651  CA  PHE A1223      -8.543 -21.855  77.410  1.00 54.10           C  
ANISOU 1651  CA  PHE A1223     5962   7757   6835   -160    -18   1038       C  
ATOM   1652  C   PHE A1223      -7.430 -22.014  78.440  1.00 43.18           C  
ANISOU 1652  C   PHE A1223     4694   6284   5427   -113     -2    904       C  
ATOM   1653  O   PHE A1223      -7.701 -22.406  79.577  1.00 43.83           O  
ANISOU 1653  O   PHE A1223     4743   6446   5464    -96     24    975       O  
ATOM   1654  CB  PHE A1223      -8.406 -22.935  76.328  1.00 43.53           C  
ANISOU 1654  CB  PHE A1223     4666   6326   5549   -348   -169   1047       C  
ATOM   1655  CG  PHE A1223      -8.304 -24.314  76.894  1.00 43.91           C  
ANISOU 1655  CG  PHE A1223     4749   6350   5586   -476   -266   1101       C  
ATOM   1656  CD1 PHE A1223      -9.445 -25.020  77.231  1.00 47.93           C  
ANISOU 1656  CD1 PHE A1223     5140   6999   6072   -583   -313   1310       C  
ATOM   1657  CD2 PHE A1223      -7.069 -24.893  77.129  1.00 43.09           C  
ANISOU 1657  CD2 PHE A1223     4790   6093   5488   -486   -308    956       C  
ATOM   1658  CE1 PHE A1223      -9.356 -26.286  77.781  1.00 47.65           C  
ANISOU 1658  CE1 PHE A1223     5152   6933   6020   -708   -408   1364       C  
ATOM   1659  CE2 PHE A1223      -6.975 -26.155  77.679  1.00 43.91           C  
ANISOU 1659  CE2 PHE A1223     4940   6167   5575   -590   -393   1007       C  
ATOM   1660  CZ  PHE A1223      -8.119 -26.853  78.005  1.00 46.78           C  
ANISOU 1660  CZ  PHE A1223     5206   6653   5916   -706   -446   1205       C  
ATOM   1661  N   TRP A1224      -6.178 -21.738  78.068  1.00 42.04           N  
ANISOU 1661  N   TRP A1224     4677   5988   5309    -96    -20    725       N  
ATOM   1662  CA  TRP A1224      -5.037 -21.913  78.969  1.00 46.38           C  
ANISOU 1662  CA  TRP A1224     5328   6458   5836    -68    -20    609       C  
ATOM   1663  C   TRP A1224      -5.004 -20.714  79.913  1.00 45.00           C  
ANISOU 1663  C   TRP A1224     5180   6323   5594     83     97    567       C  
ATOM   1664  O   TRP A1224      -4.271 -19.739  79.727  1.00 44.68           O  
ANISOU 1664  O   TRP A1224     5227   6204   5545    149    130    445       O  
ATOM   1665  CB  TRP A1224      -3.739 -22.062  78.181  1.00 40.48           C  
ANISOU 1665  CB  TRP A1224     4685   5561   5134   -106    -83    466       C  
ATOM   1666  CG  TRP A1224      -3.725 -23.243  77.244  1.00 45.06           C  
ANISOU 1666  CG  TRP A1224     5286   6077   5757   -231   -193    497       C  
ATOM   1667  CD1 TRP A1224      -3.878 -23.216  75.878  1.00 40.16           C  
ANISOU 1667  CD1 TRP A1224     4675   5407   5175   -279   -237    492       C  
ATOM   1668  CD2 TRP A1224      -3.556 -24.624  77.599  1.00 40.68           C  
ANISOU 1668  CD2 TRP A1224     4774   5487   5197   -321   -276    538       C  
ATOM   1669  NE1 TRP A1224      -3.810 -24.489  75.372  1.00 40.35           N  
ANISOU 1669  NE1 TRP A1224     4763   5360   5210   -391   -343    523       N  
ATOM   1670  CE2 TRP A1224      -3.612 -25.372  76.404  1.00 42.21           C  
ANISOU 1670  CE2 TRP A1224     5023   5597   5417   -418   -370    552       C  
ATOM   1671  CE3 TRP A1224      -3.357 -25.300  78.812  1.00 42.41           C  
ANISOU 1671  CE3 TRP A1224     5003   5728   5382   -327   -282    565       C  
ATOM   1672  CZ2 TRP A1224      -3.479 -26.760  76.385  1.00 42.94           C  
ANISOU 1672  CZ2 TRP A1224     5203   5616   5498   -516   -470    590       C  
ATOM   1673  CZ3 TRP A1224      -3.227 -26.681  78.791  1.00 42.48           C  
ANISOU 1673  CZ3 TRP A1224     5076   5674   5389   -427   -381    606       C  
ATOM   1674  CH2 TRP A1224      -3.290 -27.396  77.583  1.00 43.87           C  
ANISOU 1674  CH2 TRP A1224     5328   5755   5586   -519   -474    617       C  
ATOM   1675  N   ASN A1225      -5.833 -20.795  80.948  1.00 44.98           N  
ANISOU 1675  N   ASN A1225     5114   6444   5531    137    158    680       N  
ATOM   1676  CA  ASN A1225      -6.111 -19.651  81.803  1.00 45.13           C  
ANISOU 1676  CA  ASN A1225     5169   6514   5463    304    282    672       C  
ATOM   1677  C   ASN A1225      -6.474 -20.175  83.181  1.00 49.57           C  
ANISOU 1677  C   ASN A1225     5704   7173   5956    335    318    758       C  
ATOM   1678  O   ASN A1225      -7.350 -21.034  83.305  1.00 45.03           O  
ANISOU 1678  O   ASN A1225     5000   6717   5392    272    297    916       O  
ATOM   1679  CB  ASN A1225      -7.248 -18.803  81.211  1.00 47.22           C  
ANISOU 1679  CB  ASN A1225     5349   6879   5714    400    366    770       C  
ATOM   1680  CG  ASN A1225      -7.399 -17.455  81.894  1.00 50.26           C  
ANISOU 1680  CG  ASN A1225     5826   7273   5996    601    499    733       C  
ATOM   1681  OD1 ASN A1225      -7.277 -17.343  83.108  1.00 50.47           O  
ANISOU 1681  OD1 ASN A1225     5923   7316   5936    682    554    723       O  
ATOM   1682  ND2 ASN A1225      -7.668 -16.423  81.105  1.00 52.44           N  
ANISOU 1682  ND2 ASN A1225     6122   7531   6272    685    551    713       N  
ATOM   1683  N   GLU A1226      -5.801 -19.654  84.210  1.00 49.67           N  
ANISOU 1683  N   GLU A1226     5843   7135   5894    421    365    661       N  
ATOM   1684  CA  GLU A1226      -6.009 -20.146  85.564  1.00 53.78           C  
ANISOU 1684  CA  GLU A1226     6358   7734   6343    452    397    727       C  
ATOM   1685  C   GLU A1226      -7.409 -19.836  86.081  1.00 51.83           C  
ANISOU 1685  C   GLU A1226     6006   7667   6019    583    515    899       C  
ATOM   1686  O   GLU A1226      -7.868 -20.489  87.023  1.00 52.51           O  
ANISOU 1686  O   GLU A1226     6029   7862   6061    586    535   1009       O  
ATOM   1687  CB  GLU A1226      -4.952 -19.565  86.505  1.00 59.98           C  
ANISOU 1687  CB  GLU A1226     7322   8417   7052    510    413    583       C  
ATOM   1688  CG  GLU A1226      -4.824 -20.325  87.819  1.00 69.99           C  
ANISOU 1688  CG  GLU A1226     8598   9731   8264    496    407    622       C  
ATOM   1689  CD  GLU A1226      -3.684 -19.828  88.689  1.00 77.12           C  
ANISOU 1689  CD  GLU A1226     9681  10526   9093    520    396    483       C  
ATOM   1690  OE1 GLU A1226      -2.899 -18.976  88.222  1.00 79.48           O  
ANISOU 1690  OE1 GLU A1226    10096  10710   9394    521    375    358       O  
ATOM   1691  OE2 GLU A1226      -3.575 -20.294  89.844  1.00 80.65           O  
ANISOU 1691  OE2 GLU A1226    10154  11010   9478    527    400    509       O  
ATOM   1692  N   SER A1227      -8.105 -18.875  85.469  1.00 49.80           N  
ANISOU 1692  N   SER A1227     5722   7456   5744    697    598    938       N  
ATOM   1693  CA  SER A1227      -9.428 -18.493  85.945  1.00 50.49           C  
ANISOU 1693  CA  SER A1227     5703   7733   5747    857    729   1118       C  
ATOM   1694  C   SER A1227     -10.424 -19.642  85.892  1.00 51.31           C  
ANISOU 1694  C   SER A1227     5581   8020   5894    746    688   1339       C  
ATOM   1695  O   SER A1227     -11.444 -19.589  86.585  1.00 52.70           O  
ANISOU 1695  O   SER A1227     5647   8386   5990    862    790   1518       O  
ATOM   1696  CB  SER A1227      -9.961 -17.316  85.131  1.00 54.15           C  
ANISOU 1696  CB  SER A1227     6169   8210   6195    993    815   1128       C  
ATOM   1697  OG  SER A1227      -9.089 -16.206  85.226  1.00 58.59           O  
ANISOU 1697  OG  SER A1227     6959   8599   6702   1089    848    936       O  
ATOM   1698  N   TYR A1228     -10.179 -20.660  85.071  1.00 48.62           N  
ANISOU 1698  N   TYR A1228     5178   7630   5665    527    540   1344       N  
ATOM   1699  CA  TYR A1228     -11.089 -21.793  84.988  1.00 49.45           C  
ANISOU 1699  CA  TYR A1228     5098   7887   5803    385    472   1557       C  
ATOM   1700  C   TYR A1228     -10.805 -22.882  86.014  1.00 49.61           C  
ANISOU 1700  C   TYR A1228     5128   7917   5806    293    416   1586       C  
ATOM   1701  O   TYR A1228     -11.577 -23.842  86.095  1.00 54.24           O  
ANISOU 1701  O   TYR A1228     5571   8633   6405    167    355   1778       O  
ATOM   1702  CB  TYR A1228     -11.073 -22.358  83.564  1.00 48.72           C  
ANISOU 1702  CB  TYR A1228     4964   7727   5820    192    333   1562       C  
ATOM   1703  CG  TYR A1228     -11.601 -21.331  82.601  1.00 48.86           C  
ANISOU 1703  CG  TYR A1228     4933   7783   5849    282    395   1584       C  
ATOM   1704  CD1 TYR A1228     -12.947 -21.008  82.597  1.00 50.43           C  
ANISOU 1704  CD1 TYR A1228     4946   8208   6006    361    477   1811       C  
ATOM   1705  CD2 TYR A1228     -10.754 -20.631  81.756  1.00 47.57           C  
ANISOU 1705  CD2 TYR A1228     4901   7445   5729    303    382   1389       C  
ATOM   1706  CE1 TYR A1228     -13.447 -20.050  81.755  1.00 50.67           C  
ANISOU 1706  CE1 TYR A1228     4930   8282   6042    460    541   1841       C  
ATOM   1707  CE2 TYR A1228     -11.250 -19.662  80.900  1.00 47.76           C  
ANISOU 1707  CE2 TYR A1228     4884   7502   5759    392    441   1412       C  
ATOM   1708  CZ  TYR A1228     -12.603 -19.381  80.911  1.00 49.30           C  
ANISOU 1708  CZ  TYR A1228     4901   7918   5915    474    522   1636       C  
ATOM   1709  OH  TYR A1228     -13.138 -18.430  80.089  1.00 49.63           O  
ANISOU 1709  OH  TYR A1228     4894   8004   5957    574    586   1674       O  
ATOM   1710  N   LEU A1229      -9.724 -22.773  86.782  1.00 48.87           N  
ANISOU 1710  N   LEU A1229     5198   7690   5681    338    423   1413       N  
ATOM   1711  CA  LEU A1229      -9.496 -23.673  87.905  1.00 49.19           C  
ANISOU 1711  CA  LEU A1229     5249   7754   5687    286    393   1446       C  
ATOM   1712  C   LEU A1229     -10.245 -23.189  89.144  1.00 55.09           C  
ANISOU 1712  C   LEU A1229     5950   8670   6310    467    540   1563       C  
ATOM   1713  O   LEU A1229     -10.522 -21.997  89.300  1.00 56.17           O  
ANISOU 1713  O   LEU A1229     6131   8840   6371    667    673   1541       O  
ATOM   1714  CB  LEU A1229      -8.004 -23.785  88.208  1.00 54.70           C  
ANISOU 1714  CB  LEU A1229     6132   8253   6400    254    334   1228       C  
ATOM   1715  CG  LEU A1229      -7.106 -24.113  87.014  1.00 57.35           C  
ANISOU 1715  CG  LEU A1229     6534   8417   6839    123    213   1098       C  
ATOM   1716  CD1 LEU A1229      -5.659 -23.898  87.393  1.00 58.74           C  
ANISOU 1716  CD1 LEU A1229     6873   8436   7008    141    190    902       C  
ATOM   1717  CD2 LEU A1229      -7.330 -25.537  86.528  1.00 58.10           C  
ANISOU 1717  CD2 LEU A1229     6566   8509   7002    -71     80   1196       C  
ATOM   1718  N   THR A1230     -10.569 -24.123  90.033  1.00 52.63           N  
ANISOU 1718  N   THR A1230     5565   8462   5969    406    519   1690       N  
ATOM   1719  CA  THR A1230     -11.285 -23.801  91.259  1.00 56.37           C  
ANISOU 1719  CA  THR A1230     5989   9112   6318    577    659   1819       C  
ATOM   1720  C   THR A1230     -10.453 -24.180  92.476  1.00 55.81           C  
ANISOU 1720  C   THR A1230     6050   8964   6192    581    648   1719       C  
ATOM   1721  O   THR A1230      -9.627 -25.098  92.428  1.00 52.55           O  
ANISOU 1721  O   THR A1230     5691   8427   5849    410    514   1637       O  
ATOM   1722  CB  THR A1230     -12.642 -24.514  91.334  1.00 59.82           C  
ANISOU 1722  CB  THR A1230     6180   9802   6749    515    662   2118       C  
ATOM   1723  OG1 THR A1230     -12.436 -25.929  91.410  1.00 63.19           O  
ANISOU 1723  OG1 THR A1230     6569  10201   7241    276    506   2171       O  
ATOM   1724  CG2 THR A1230     -13.491 -24.182  90.113  1.00 55.94           C  
ANISOU 1724  CG2 THR A1230     5542   9401   6311    492    659   2239       C  
ATOM   1725  N   GLY A1231     -10.675 -23.453  93.571  1.00 57.01           N  
ANISOU 1725  N   GLY A1231     6266   9189   6207    790    792   1731       N  
ATOM   1726  CA  GLY A1231      -9.972 -23.715  94.808  1.00 54.90           C  
ANISOU 1726  CA  GLY A1231     6128   8866   5867    809    793   1650       C  
ATOM   1727  C   GLY A1231      -8.585 -23.101  94.806  1.00 58.05           C  
ANISOU 1727  C   GLY A1231     6765   9028   6262    816    751   1386       C  
ATOM   1728  O   GLY A1231      -8.140 -22.470  93.845  1.00 58.00           O  
ANISOU 1728  O   GLY A1231     6825   8899   6312    806    724   1263       O  
ATOM   1729  N   SER A1232      -7.895 -23.287  95.924  1.00 52.68           N  
ANISOU 1729  N   SER A1232     6210   8295   5510    826    743   1312       N  
ATOM   1730  CA  SER A1232      -6.513 -22.861  96.058  1.00 51.63           C  
ANISOU 1730  CA  SER A1232     6287   7959   5370    796    679   1090       C  
ATOM   1731  C   SER A1232      -5.585 -23.832  95.335  1.00 57.99           C  
ANISOU 1731  C   SER A1232     7060   8650   6323    578    514   1018       C  
ATOM   1732  O   SER A1232      -5.925 -24.995  95.094  1.00 49.99           O  
ANISOU 1732  O   SER A1232     5907   7698   5390    449    443   1130       O  
ATOM   1733  CB  SER A1232      -6.114 -22.767  97.528  1.00 52.41           C  
ANISOU 1733  CB  SER A1232     6529   8051   5333    871    718   1053       C  
ATOM   1734  OG  SER A1232      -5.867 -24.060  98.044  1.00 54.33           O  
ANISOU 1734  OG  SER A1232     6690   8330   5624    731    630   1113       O  
ATOM   1735  N   ARG A1233      -4.399 -23.335  94.975  1.00 49.05           N  
ANISOU 1735  N   ARG A1233     6070   7351   5216    542    452    838       N  
ATOM   1736  CA  ARG A1233      -3.433 -24.194  94.300  1.00 51.01           C  
ANISOU 1736  CA  ARG A1233     6299   7495   5588    371    312    771       C  
ATOM   1737  C   ARG A1233      -2.973 -25.342  95.194  1.00 51.39           C  
ANISOU 1737  C   ARG A1233     6338   7553   5632    284    244    804       C  
ATOM   1738  O   ARG A1233      -2.706 -26.442  94.694  1.00 47.23           O  
ANISOU 1738  O   ARG A1233     5747   6997   5203    156    145    832       O  
ATOM   1739  CB  ARG A1233      -2.231 -23.372  93.824  1.00 49.85           C  
ANISOU 1739  CB  ARG A1233     6290   7196   5454    359    268    595       C  
ATOM   1740  CG  ARG A1233      -1.356 -24.115  92.826  1.00 47.75           C  
ANISOU 1740  CG  ARG A1233     5985   6839   5317    220    148    543       C  
ATOM   1741  CD  ARG A1233      -0.128 -23.333  92.398  1.00 44.91           C  
ANISOU 1741  CD  ARG A1233     5738   6358   4967    202    102    396       C  
ATOM   1742  NE  ARG A1233       0.507 -23.999  91.265  1.00 45.87           N  
ANISOU 1742  NE  ARG A1233     5803   6417   5209    104     14    369       N  
ATOM   1743  CZ  ARG A1233       0.210 -23.747  89.995  1.00 47.60           C  
ANISOU 1743  CZ  ARG A1233     5976   6610   5500     96     14    360       C  
ATOM   1744  NH1 ARG A1233      -0.698 -22.828  89.698  1.00 43.72           N  
ANISOU 1744  NH1 ARG A1233     5477   6154   4980    177     96    378       N  
ATOM   1745  NH2 ARG A1233       0.817 -24.414  89.021  1.00 42.59           N  
ANISOU 1745  NH2 ARG A1233     5310   5914   4958     20    -63    338       N  
ATOM   1746  N   ASP A1234      -2.893 -25.115  96.513  1.00 52.90           N  
ANISOU 1746  N   ASP A1234     6612   7782   5706    359    295    804       N  
ATOM   1747  CA  ASP A1234      -2.462 -26.169  97.432  1.00 56.33           C  
ANISOU 1747  CA  ASP A1234     7041   8231   6129    284    234    839       C  
ATOM   1748  C   ASP A1234      -3.489 -27.290  97.525  1.00 52.04           C  
ANISOU 1748  C   ASP A1234     6338   7814   5620    228    230   1020       C  
ATOM   1749  O   ASP A1234      -3.127 -28.474  97.534  1.00 50.69           O  
ANISOU 1749  O   ASP A1234     6130   7616   5512    104    131   1053       O  
ATOM   1750  CB  ASP A1234      -2.198 -25.585  98.821  1.00 68.05           C  
ANISOU 1750  CB  ASP A1234     8663   9728   7465    380    292    801       C  
ATOM   1751  CG  ASP A1234      -0.781 -25.071  98.981  1.00 79.40           C  
ANISOU 1751  CG  ASP A1234    10259  11028   8880    341    220    641       C  
ATOM   1752  OD1 ASP A1234       0.011 -25.190  98.023  1.00 84.50           O  
ANISOU 1752  OD1 ASP A1234    10890  11584   9631    250    134    569       O  
ATOM   1753  OD2 ASP A1234      -0.457 -24.550 100.068  1.00 85.51           O  
ANISOU 1753  OD2 ASP A1234    11176  11790   9526    397    245    599       O  
ATOM   1754  N   GLU A1235      -4.776 -26.944  97.593  1.00 52.11           N  
ANISOU 1754  N   GLU A1235     6253   7967   5582    318    333   1151       N  
ATOM   1755  CA  GLU A1235      -5.803 -27.979  97.591  1.00 55.88           C  
ANISOU 1755  CA  GLU A1235     6559   8581   6091    239    315   1351       C  
ATOM   1756  C   GLU A1235      -5.796 -28.750  96.277  1.00 55.61           C  
ANISOU 1756  C   GLU A1235     6453   8482   6194     77    197   1371       C  
ATOM   1757  O   GLU A1235      -5.943 -29.978  96.270  1.00 50.53           O  
ANISOU 1757  O   GLU A1235     5752   7849   5597    -65    102   1468       O  
ATOM   1758  CB  GLU A1235      -7.177 -27.359  97.842  1.00 59.88           C  
ANISOU 1758  CB  GLU A1235     6957   9278   6515    380    456   1509       C  
ATOM   1759  CG  GLU A1235      -7.323 -26.718  99.213  1.00 63.92           C  
ANISOU 1759  CG  GLU A1235     7554   9866   6867    559    584   1516       C  
ATOM   1760  CD  GLU A1235      -8.614 -25.934  99.356  1.00 68.73           C  
ANISOU 1760  CD  GLU A1235     8076  10658   7380    748    747   1663       C  
ATOM   1761  OE1 GLU A1235      -9.031 -25.281  98.371  1.00 68.07           O  
ANISOU 1761  OE1 GLU A1235     7949  10579   7335    795    782   1666       O  
ATOM   1762  OE2 GLU A1235      -9.212 -25.973 100.453  1.00 74.53           O  
ANISOU 1762  OE2 GLU A1235     8783  11540   7996    861    845   1785       O  
ATOM   1763  N   ARG A1236      -5.572 -28.053  95.158  1.00 49.51           N  
ANISOU 1763  N   ARG A1236     5709   7625   5479     92    193   1273       N  
ATOM   1764  CA  ARG A1236      -5.515 -28.748  93.877  1.00 49.09           C  
ANISOU 1764  CA  ARG A1236     5616   7495   5543    -53     81   1280       C  
ATOM   1765  C   ARG A1236      -4.320 -29.693  93.816  1.00 47.93           C  
ANISOU 1765  C   ARG A1236     5565   7197   5449   -161    -40   1184       C  
ATOM   1766  O   ARG A1236      -4.462 -30.846  93.393  1.00 51.67           O  
ANISOU 1766  O   ARG A1236     6017   7640   5978   -296   -143   1259       O  
ATOM   1767  CB  ARG A1236      -5.473 -27.743  92.721  1.00 49.48           C  
ANISOU 1767  CB  ARG A1236     5680   7486   5633     -2    111   1191       C  
ATOM   1768  CG  ARG A1236      -6.748 -26.925  92.545  1.00 49.04           C  
ANISOU 1768  CG  ARG A1236     5514   7582   5536    101    223   1311       C  
ATOM   1769  CD  ARG A1236      -6.831 -26.296  91.150  1.00 48.36           C  
ANISOU 1769  CD  ARG A1236     5416   7438   5519     98    214   1257       C  
ATOM   1770  NE  ARG A1236      -5.674 -25.456  90.855  1.00 47.24           N  
ANISOU 1770  NE  ARG A1236     5424   7140   5386    155    217   1049       N  
ATOM   1771  CZ  ARG A1236      -5.596 -24.163  91.146  1.00 47.72           C  
ANISOU 1771  CZ  ARG A1236     5566   7194   5373    309    321    970       C  
ATOM   1772  NH1 ARG A1236      -6.612 -23.551  91.741  1.00 49.17           N  
ANISOU 1772  NH1 ARG A1236     5703   7517   5463    452    446   1078       N  
ATOM   1773  NH2 ARG A1236      -4.502 -23.480  90.841  1.00 46.88           N  
ANISOU 1773  NH2 ARG A1236     5594   6942   5275    322    298    795       N  
ATOM   1774  N   LYS A1237      -3.143 -29.241  94.261  1.00 47.29           N  
ANISOU 1774  N   LYS A1237     5600   7024   5343   -102    -34   1032       N  
ATOM   1775  CA  LYS A1237      -1.972 -30.114  94.223  1.00 48.11           C  
ANISOU 1775  CA  LYS A1237     5782   7007   5491   -180   -137    958       C  
ATOM   1776  C   LYS A1237      -2.143 -31.314  95.144  1.00 48.21           C  
ANISOU 1776  C   LYS A1237     5777   7063   5479   -248   -184   1065       C  
ATOM   1777  O   LYS A1237      -1.772 -32.437  94.782  1.00 47.83           O  
ANISOU 1777  O   LYS A1237     5760   6933   5481   -346   -285   1084       O  
ATOM   1778  CB  LYS A1237      -0.707 -29.345  94.606  1.00 48.26           C  
ANISOU 1778  CB  LYS A1237     5906   6954   5479   -114   -125    805       C  
ATOM   1779  CG  LYS A1237       0.554 -30.198  94.511  1.00 48.67           C  
ANISOU 1779  CG  LYS A1237     6016   6902   5573   -174   -223    747       C  
ATOM   1780  CD  LYS A1237       1.818 -29.395  94.738  1.00 48.56           C  
ANISOU 1780  CD  LYS A1237     6080   6836   5533   -130   -224    621       C  
ATOM   1781  CE  LYS A1237       2.098 -29.193  96.213  1.00 49.13           C  
ANISOU 1781  CE  LYS A1237     6201   6959   5507    -99   -201    621       C  
ATOM   1782  NZ  LYS A1237       3.393 -28.494  96.409  1.00 50.03           N  
ANISOU 1782  NZ  LYS A1237     6395   7022   5592    -92   -232    516       N  
ATOM   1783  N   LYS A1238      -2.725 -31.106  96.328  1.00 49.04           N  
ANISOU 1783  N   LYS A1238     5846   7292   5497   -191   -110   1143       N  
ATOM   1784  CA  LYS A1238      -2.911 -32.222  97.247  1.00 49.71           C  
ANISOU 1784  CA  LYS A1238     5909   7426   5553   -258   -153   1253       C  
ATOM   1785  C   LYS A1238      -3.919 -33.222  96.695  1.00 51.51           C  
ANISOU 1785  C   LYS A1238     6046   7699   5827   -388   -219   1418       C  
ATOM   1786  O   LYS A1238      -3.701 -34.437  96.771  1.00 54.80           O  
ANISOU 1786  O   LYS A1238     6496   8056   6268   -500   -321   1469       O  
ATOM   1787  CB  LYS A1238      -3.347 -31.699  98.615  1.00 52.51           C  
ANISOU 1787  CB  LYS A1238     6247   7912   5792   -155    -49   1304       C  
ATOM   1788  CG  LYS A1238      -3.629 -32.786  99.637  1.00 61.03           C  
ANISOU 1788  CG  LYS A1238     7291   9064   6833   -218    -82   1433       C  
ATOM   1789  CD  LYS A1238      -4.120 -32.185 100.940  1.00 67.67           C  
ANISOU 1789  CD  LYS A1238     8120  10044   7547    -95     37   1487       C  
ATOM   1790  CE  LYS A1238      -4.487 -33.258 101.954  1.00 71.72           C  
ANISOU 1790  CE  LYS A1238     8582  10648   8020   -160      9   1633       C  
ATOM   1791  NZ  LYS A1238      -4.984 -32.647 103.220  1.00 72.13           N  
ANISOU 1791  NZ  LYS A1238     8628  10842   7934    -21    136   1690       N  
ATOM   1792  N   SER A1239      -5.005 -32.730  96.093  1.00 52.37           N  
ANISOU 1792  N   SER A1239     6050   7906   5944   -381   -172   1510       N  
ATOM   1793  CA  SER A1239      -5.979 -33.632  95.491  1.00 56.07           C  
ANISOU 1793  CA  SER A1239     6430   8422   6452   -532   -254   1683       C  
ATOM   1794  C   SER A1239      -5.377 -34.396  94.316  1.00 59.63           C  
ANISOU 1794  C   SER A1239     6982   8687   6986   -654   -389   1613       C  
ATOM   1795  O   SER A1239      -5.639 -35.592  94.145  1.00 61.84           O  
ANISOU 1795  O   SER A1239     7288   8927   7282   -807   -505   1716       O  
ATOM   1796  CB  SER A1239      -7.210 -32.839  95.053  1.00 58.64           C  
ANISOU 1796  CB  SER A1239     6610   8906   6765   -489   -172   1801       C  
ATOM   1797  OG  SER A1239      -8.112 -33.655  94.330  1.00 64.73           O  
ANISOU 1797  OG  SER A1239     7296   9722   7577   -661   -271   1974       O  
ATOM   1798  N   LEU A1240      -4.526 -33.737  93.526  1.00 56.08           N  
ANISOU 1798  N   LEU A1240     6612   8116   6579   -586   -376   1439       N  
ATOM   1799  CA  LEU A1240      -3.892 -34.408  92.395  1.00 54.00           C  
ANISOU 1799  CA  LEU A1240     6459   7677   6381   -668   -487   1368       C  
ATOM   1800  C   LEU A1240      -2.944 -35.508  92.866  1.00 54.30           C  
ANISOU 1800  C   LEU A1240     6620   7598   6413   -704   -568   1331       C  
ATOM   1801  O   LEU A1240      -2.976 -36.641  92.359  1.00 55.30           O  
ANISOU 1801  O   LEU A1240     6833   7621   6556   -820   -682   1383       O  
ATOM   1802  CB  LEU A1240      -3.143 -33.379  91.549  1.00 51.78           C  
ANISOU 1802  CB  LEU A1240     6221   7316   6139   -569   -441   1200       C  
ATOM   1803  CG  LEU A1240      -2.057 -33.958  90.651  1.00 52.38           C  
ANISOU 1803  CG  LEU A1240     6430   7209   6262   -592   -525   1090       C  
ATOM   1804  CD1 LEU A1240      -2.710 -34.652  89.473  1.00 56.14           C  
ANISOU 1804  CD1 LEU A1240     6939   7619   6773   -717   -620   1163       C  
ATOM   1805  CD2 LEU A1240      -1.079 -32.882  90.202  1.00 49.14           C  
ANISOU 1805  CD2 LEU A1240     6049   6749   5874   -477   -466    927       C  
ATOM   1806  N   LEU A1241      -2.091 -35.189  93.841  1.00 52.24           N  
ANISOU 1806  N   LEU A1241     6383   7347   6118   -604   -514   1248       N  
ATOM   1807  CA  LEU A1241      -1.161 -36.189  94.345  1.00 58.26           C  
ANISOU 1807  CA  LEU A1241     7250   8016   6871   -621   -581   1223       C  
ATOM   1808  C   LEU A1241      -1.900 -37.347  95.003  1.00 63.59           C  
ANISOU 1808  C   LEU A1241     7917   8731   7514   -737   -647   1384       C  
ATOM   1809  O   LEU A1241      -1.477 -38.502  94.886  1.00 67.41           O  
ANISOU 1809  O   LEU A1241     8515   9095   8002   -802   -745   1402       O  
ATOM   1810  CB  LEU A1241      -0.182 -35.547  95.327  1.00 56.05           C  
ANISOU 1810  CB  LEU A1241     6980   7764   6552   -507   -516   1123       C  
ATOM   1811  CG  LEU A1241       0.819 -34.559  94.729  1.00 53.30           C  
ANISOU 1811  CG  LEU A1241     6664   7359   6231   -415   -480    969       C  
ATOM   1812  CD1 LEU A1241       1.726 -34.019  95.821  1.00 52.29           C  
ANISOU 1812  CD1 LEU A1241     6554   7267   6049   -341   -441    900       C  
ATOM   1813  CD2 LEU A1241       1.635 -35.211  93.610  1.00 50.08           C  
ANISOU 1813  CD2 LEU A1241     6345   6804   5879   -428   -554    913       C  
ATOM   1814  N   SER A1242      -3.018 -37.064  95.681  1.00 65.06           N  
ANISOU 1814  N   SER A1242     7975   9086   7661   -758   -594   1514       N  
ATOM   1815  CA  SER A1242      -3.817 -38.144  96.252  1.00 68.15           C  
ANISOU 1815  CA  SER A1242     8337   9535   8020   -889   -663   1694       C  
ATOM   1816  C   SER A1242      -4.451 -39.002  95.162  1.00 71.72           C  
ANISOU 1816  C   SER A1242     8834   9909   8509  -1058   -789   1792       C  
ATOM   1817  O   SER A1242      -4.569 -40.223  95.318  1.00 72.76           O  
ANISOU 1817  O   SER A1242     9049   9973   8624  -1188   -903   1888       O  
ATOM   1818  CB  SER A1242      -4.891 -37.569  97.174  1.00 68.59           C  
ANISOU 1818  CB  SER A1242     8226   9816   8018   -856   -563   1829       C  
ATOM   1819  OG  SER A1242      -5.833 -38.564  97.529  1.00 75.33           O  
ANISOU 1819  OG  SER A1242     9022  10752   8848  -1007   -637   2038       O  
ATOM   1820  N   LYS A1243      -4.850 -38.381  94.045  1.00 70.51           N  
ANISOU 1820  N   LYS A1243     8645   9751   8396  -1064   -780   1771       N  
ATOM   1821  CA  LYS A1243      -5.363 -39.148  92.915  1.00 76.54           C  
ANISOU 1821  CA  LYS A1243     9480  10419   9185  -1231   -912   1849       C  
ATOM   1822  C   LYS A1243      -4.296 -40.071  92.358  1.00 79.03           C  
ANISOU 1822  C   LYS A1243    10025  10490   9511  -1248  -1013   1738       C  
ATOM   1823  O   LYS A1243      -4.601 -41.187  91.925  1.00 82.07           O  
ANISOU 1823  O   LYS A1243    10538  10765   9880  -1404  -1152   1827       O  
ATOM   1824  CB  LYS A1243      -5.857 -38.211  91.810  1.00 78.32           C  
ANISOU 1824  CB  LYS A1243     9628  10681   9450  -1214   -874   1827       C  
ATOM   1825  CG  LYS A1243      -7.367 -38.113  91.661  1.00 82.71           C  
ANISOU 1825  CG  LYS A1243    10014  11419   9994  -1336   -889   2044       C  
ATOM   1826  CD  LYS A1243      -7.996 -37.335  92.805  1.00 86.12           C  
ANISOU 1826  CD  LYS A1243    10248  12091  10383  -1228   -747   2137       C  
ATOM   1827  CE  LYS A1243      -9.417 -36.909  92.466  1.00 89.03           C  
ANISOU 1827  CE  LYS A1243    10417  12666  10743  -1289   -723   2340       C  
ATOM   1828  NZ  LYS A1243      -9.454 -36.002  91.284  1.00 88.92           N  
ANISOU 1828  NZ  LYS A1243    10389  12620  10776  -1232   -688   2252       N  
ATOM   1829  N   PHE A1244      -3.041 -39.632  92.377  1.00 78.35           N  
ANISOU 1829  N   PHE A1244    10004  10323   9442  -1086   -948   1557       N  
ATOM   1830  CA  PHE A1244      -1.939 -40.503  91.992  1.00 79.03           C  
ANISOU 1830  CA  PHE A1244    10297  10205   9526  -1058  -1021   1466       C  
ATOM   1831  C   PHE A1244      -1.449 -41.372  93.143  1.00 80.99           C  
ANISOU 1831  C   PHE A1244    10607  10435   9732  -1052  -1047   1501       C  
ATOM   1832  O   PHE A1244      -0.525 -42.168  92.946  1.00 82.98           O  
ANISOU 1832  O   PHE A1244    11033  10526   9971  -1010  -1100   1442       O  
ATOM   1833  CB  PHE A1244      -0.785 -39.677  91.423  1.00 77.54           C  
ANISOU 1833  CB  PHE A1244    10133   9956   9372   -892   -944   1284       C  
ATOM   1834  CG  PHE A1244      -1.105 -39.030  90.111  1.00 77.32           C  
ANISOU 1834  CG  PHE A1244    10094   9900   9385   -900   -939   1239       C  
ATOM   1835  CD1 PHE A1244      -2.065 -39.575  89.274  1.00 78.72           C  
ANISOU 1835  CD1 PHE A1244    10322  10028   9560  -1054  -1037   1339       C  
ATOM   1836  CD2 PHE A1244      -0.455 -37.876  89.715  1.00 76.11           C  
ANISOU 1836  CD2 PHE A1244     9884   9769   9266   -769   -846   1107       C  
ATOM   1837  CE1 PHE A1244      -2.369 -38.983  88.064  1.00 76.75           C  
ANISOU 1837  CE1 PHE A1244    10063   9755   9345  -1066  -1036   1302       C  
ATOM   1838  CE2 PHE A1244      -0.752 -37.283  88.504  1.00 74.97           C  
ANISOU 1838  CE2 PHE A1244     9730   9598   9159   -777   -840   1068       C  
ATOM   1839  CZ  PHE A1244      -1.713 -37.836  87.680  1.00 74.71           C  
ANISOU 1839  CZ  PHE A1244     9743   9519   9125   -920   -932   1164       C  
ATOM   1840  N   GLY A1245      -2.038 -41.237  94.331  1.00 80.24           N  
ANISOU 1840  N   GLY A1245    10376  10503   9607  -1078  -1005   1599       N  
ATOM   1841  CA  GLY A1245      -1.643 -42.045  95.465  1.00 78.87           C  
ANISOU 1841  CA  GLY A1245    10252  10324   9391  -1079  -1031   1642       C  
ATOM   1842  C   GLY A1245      -0.412 -41.577  96.201  1.00 77.29           C  
ANISOU 1842  C   GLY A1245    10046  10134   9185   -913   -948   1514       C  
ATOM   1843  O   GLY A1245       0.194 -42.367  96.930  1.00 78.38           O  
ANISOU 1843  O   GLY A1245    10264  10225   9292   -898   -983   1527       O  
ATOM   1844  N   MET A1246      -0.010 -40.321  96.031  1.00 72.43           N  
ANISOU 1844  N   MET A1246     9347   9579   8592   -796   -848   1398       N  
ATOM   1845  CA  MET A1246       1.216 -39.818  96.629  1.00 68.86           C  
ANISOU 1845  CA  MET A1246     8898   9135   8131   -661   -788   1283       C  
ATOM   1846  C   MET A1246       0.936 -38.893  97.808  1.00 68.20           C  
ANISOU 1846  C   MET A1246     8691   9219   8003   -614   -694   1291       C  
ATOM   1847  O   MET A1246      -0.129 -38.277  97.910  1.00 68.28           O  
ANISOU 1847  O   MET A1246     8599   9345   8000   -636   -639   1351       O  
ATOM   1848  CB  MET A1246       2.064 -39.082  95.592  1.00 67.76           C  
ANISOU 1848  CB  MET A1246     8784   8925   8036   -569   -759   1145       C  
ATOM   1849  CG  MET A1246       2.604 -39.991  94.514  1.00 70.28           C  
ANISOU 1849  CG  MET A1246     9253   9072   8379   -569   -837   1122       C  
ATOM   1850  SD  MET A1246       3.713 -39.151  93.375  1.00 72.85           S  
ANISOU 1850  SD  MET A1246     9594   9338   8747   -443   -792    975       S  
ATOM   1851  CE  MET A1246       4.113 -40.504  92.287  1.00 75.11           C  
ANISOU 1851  CE  MET A1246    10091   9419   9029   -436   -883    986       C  
ATOM   1852  N   ASP A1247       1.913 -38.828  98.707  1.00 70.29           N  
ANISOU 1852  N   ASP A1247     8977   9497   8235   -543   -675   1238       N  
ATOM   1853  CA  ASP A1247       1.943 -37.852  99.782  1.00 73.67           C  
ANISOU 1853  CA  ASP A1247     9337  10050   8605   -480   -591   1211       C  
ATOM   1854  C   ASP A1247       2.330 -36.476  99.236  1.00 70.15           C  
ANISOU 1854  C   ASP A1247     8872   9609   8173   -402   -527   1088       C  
ATOM   1855  O   ASP A1247       2.939 -36.353  98.169  1.00 66.66           O  
ANISOU 1855  O   ASP A1247     8463   9077   7787   -383   -552   1012       O  
ATOM   1856  CB  ASP A1247       2.921 -38.303 100.867  1.00 82.10           C  
ANISOU 1856  CB  ASP A1247    10449  11118   9628   -449   -614   1202       C  
ATOM   1857  CG  ASP A1247       2.511 -37.841 102.246  1.00 91.64           C  
ANISOU 1857  CG  ASP A1247    11610  12459  10751   -430   -553   1243       C  
ATOM   1858  OD1 ASP A1247       1.556 -37.042 102.347  1.00 95.34           O  
ANISOU 1858  OD1 ASP A1247    12017  13020  11189   -413   -477   1266       O  
ATOM   1859  OD2 ASP A1247       3.143 -38.284 103.230  1.00 95.21           O  
ANISOU 1859  OD2 ASP A1247    12094  12924  11158   -422   -577   1257       O  
ATOM   1860  N   GLU A1248       1.947 -35.430  99.969  1.00 70.17           N  
ANISOU 1860  N   GLU A1248     8833   9716   8112   -351   -443   1073       N  
ATOM   1861  CA  GLU A1248       2.215 -34.064  99.528  1.00 68.84           C  
ANISOU 1861  CA  GLU A1248     8670   9547   7941   -283   -385    963       C  
ATOM   1862  C   GLU A1248       3.713 -33.806  99.394  1.00 62.93           C  
ANISOU 1862  C   GLU A1248     7978   8726   7205   -257   -426    855       C  
ATOM   1863  O   GLU A1248       4.516 -34.253 100.217  1.00 60.76           O  
ANISOU 1863  O   GLU A1248     7734   8456   6896   -260   -464    861       O  
ATOM   1864  CB  GLU A1248       1.616 -33.056 100.510  1.00 77.55           C  
ANISOU 1864  CB  GLU A1248     9764  10756   8945   -217   -290    968       C  
ATOM   1865  CG  GLU A1248       0.287 -33.461 101.115  1.00 89.02           C  
ANISOU 1865  CG  GLU A1248    11145  12325  10355   -227   -243   1112       C  
ATOM   1866  CD  GLU A1248      -0.365 -32.325 101.882  1.00 96.63           C  
ANISOU 1866  CD  GLU A1248    12111  13393  11210   -121   -125   1116       C  
ATOM   1867  OE1 GLU A1248      -0.535 -31.233 101.296  1.00 97.94           O  
ANISOU 1867  OE1 GLU A1248    12293  13546  11371    -54    -67   1048       O  
ATOM   1868  OE2 GLU A1248      -0.700 -32.522 103.071  1.00 99.64           O  
ANISOU 1868  OE2 GLU A1248    12493  13864  11503    -93    -88   1188       O  
ATOM   1869  N   GLY A1249       4.082 -33.060  98.355  1.00 58.13           N  
ANISOU 1869  N   GLY A1249     7375   8068   6643   -235   -419    771       N  
ATOM   1870  CA  GLY A1249       5.470 -32.686  98.153  1.00 53.37           C  
ANISOU 1870  CA  GLY A1249     6805   7424   6049   -216   -455    689       C  
ATOM   1871  C   GLY A1249       5.594 -31.734  96.985  1.00 52.07           C  
ANISOU 1871  C   GLY A1249     6634   7219   5930   -196   -434    610       C  
ATOM   1872  O   GLY A1249       4.613 -31.399  96.317  1.00 50.81           O  
ANISOU 1872  O   GLY A1249     6451   7058   5798   -193   -392    614       O  
ATOM   1873  N   VAL A1250       6.828 -31.291  96.745  1.00 49.59           N  
ANISOU 1873  N   VAL A1250     6335   6886   5622   -188   -467    551       N  
ATOM   1874  CA  VAL A1250       7.095 -30.395  95.622  1.00 47.95           C  
ANISOU 1874  CA  VAL A1250     6121   6641   5456   -175   -456    480       C  
ATOM   1875  C   VAL A1250       7.011 -31.196  94.328  1.00 46.44           C  
ANISOU 1875  C   VAL A1250     5908   6384   5354   -165   -474    496       C  
ATOM   1876  O   VAL A1250       7.751 -32.165  94.133  1.00 44.67           O  
ANISOU 1876  O   VAL A1250     5689   6129   5154   -150   -519    527       O  
ATOM   1877  CB  VAL A1250       8.462 -29.719  95.782  1.00 45.90           C  
ANISOU 1877  CB  VAL A1250     5873   6397   5170   -186   -497    439       C  
ATOM   1878  CG1 VAL A1250       8.644 -28.638  94.732  1.00 44.38           C  
ANISOU 1878  CG1 VAL A1250     5680   6175   5008   -185   -484    371       C  
ATOM   1879  CG2 VAL A1250       8.574 -29.146  97.195  1.00 46.39           C  
ANISOU 1879  CG2 VAL A1250     5992   6509   5126   -212   -501    435       C  
ATOM   1880  N   THR A1251       6.118 -30.789  93.431  1.00 46.08           N  
ANISOU 1880  N   THR A1251     5850   6313   5346   -166   -439    477       N  
ATOM   1881  CA  THR A1251       5.707 -31.630  92.314  1.00 46.75           C  
ANISOU 1881  CA  THR A1251     5938   6330   5497   -175   -461    505       C  
ATOM   1882  C   THR A1251       6.251 -31.083  90.998  1.00 43.43           C  
ANISOU 1882  C   THR A1251     5515   5859   5126   -147   -460    440       C  
ATOM   1883  O   THR A1251       5.971 -29.937  90.625  1.00 42.55           O  
ANISOU 1883  O   THR A1251     5384   5764   5019   -143   -420    388       O  
ATOM   1884  CB  THR A1251       4.185 -31.755  92.276  1.00 43.75           C  
ANISOU 1884  CB  THR A1251     5533   5972   5118   -215   -435    564       C  
ATOM   1885  OG1 THR A1251       3.745 -32.331  93.510  1.00 49.56           O  
ANISOU 1885  OG1 THR A1251     6263   6765   5802   -239   -436    639       O  
ATOM   1886  CG2 THR A1251       3.745 -32.650  91.129  1.00 43.71           C  
ANISOU 1886  CG2 THR A1251     5554   5886   5168   -253   -481    600       C  
ATOM   1887  N   PHE A1252       7.032 -31.908  90.309  1.00 42.90           N  
ANISOU 1887  N   PHE A1252     5478   5732   5090   -115   -499    447       N  
ATOM   1888  CA  PHE A1252       7.566 -31.621  88.989  1.00 43.50           C  
ANISOU 1888  CA  PHE A1252     5558   5759   5209    -76   -497    402       C  
ATOM   1889  C   PHE A1252       6.809 -32.446  87.963  1.00 43.98           C  
ANISOU 1889  C   PHE A1252     5681   5727   5303    -88   -518    424       C  
ATOM   1890  O   PHE A1252       6.453 -33.603  88.217  1.00 43.34           O  
ANISOU 1890  O   PHE A1252     5662   5598   5207   -111   -557    483       O  
ATOM   1891  CB  PHE A1252       9.062 -31.938  88.920  1.00 42.69           C  
ANISOU 1891  CB  PHE A1252     5452   5668   5101     -8   -517    409       C  
ATOM   1892  CG  PHE A1252       9.871 -31.218  89.956  1.00 42.89           C  
ANISOU 1892  CG  PHE A1252     5422   5788   5085    -22   -521    408       C  
ATOM   1893  CD1 PHE A1252       9.964 -31.716  91.251  1.00 43.41           C  
ANISOU 1893  CD1 PHE A1252     5493   5896   5105    -41   -541    453       C  
ATOM   1894  CD2 PHE A1252      10.525 -30.036  89.646  1.00 42.66           C  
ANISOU 1894  CD2 PHE A1252     5347   5805   5057    -32   -514    367       C  
ATOM   1895  CE1 PHE A1252      10.696 -31.053  92.215  1.00 44.74           C  
ANISOU 1895  CE1 PHE A1252     5627   6146   5224    -70   -558    455       C  
ATOM   1896  CE2 PHE A1252      11.262 -29.365  90.607  1.00 43.04           C  
ANISOU 1896  CE2 PHE A1252     5366   5931   5054    -72   -539    374       C  
ATOM   1897  CZ  PHE A1252      11.348 -29.873  91.894  1.00 46.68           C  
ANISOU 1897  CZ  PHE A1252     5839   6431   5465    -92   -562    417       C  
ATOM   1898  N   MET A1253       6.571 -31.848  86.806  1.00 42.00           N  
ANISOU 1898  N   MET A1253     5425   5445   5089    -84   -501    380       N  
ATOM   1899  CA  MET A1253       5.810 -32.484  85.745  1.00 43.27           C  
ANISOU 1899  CA  MET A1253     5653   5515   5273   -113   -529    399       C  
ATOM   1900  C   MET A1253       6.584 -32.378  84.440  1.00 41.82           C  
ANISOU 1900  C   MET A1253     5508   5269   5111    -43   -525    351       C  
ATOM   1901  O   MET A1253       7.216 -31.355  84.164  1.00 45.41           O  
ANISOU 1901  O   MET A1253     5897   5775   5583     -5   -487    300       O  
ATOM   1902  CB  MET A1253       4.429 -31.826  85.620  1.00 45.67           C  
ANISOU 1902  CB  MET A1253     5902   5857   5593   -189   -509    414       C  
ATOM   1903  CG  MET A1253       3.616 -32.220  84.401  1.00 52.76           C  
ANISOU 1903  CG  MET A1253     6852   6679   6516   -240   -546    437       C  
ATOM   1904  SD  MET A1253       2.278 -31.033  84.181  1.00 51.88           S  
ANISOU 1904  SD  MET A1253     6630   6655   6426   -291   -498    453       S  
ATOM   1905  CE  MET A1253       1.623 -31.505  82.583  1.00 49.45           C  
ANISOU 1905  CE  MET A1253     6392   6251   6147   -356   -558    476       C  
ATOM   1906  N   PHE A1254       6.548 -33.451  83.654  1.00 43.83           N  
ANISOU 1906  N   PHE A1254     5887   5411   5357    -25   -567    372       N  
ATOM   1907  CA  PHE A1254       7.050 -33.462  82.286  1.00 42.53           C  
ANISOU 1907  CA  PHE A1254     5788   5172   5200     46   -562    334       C  
ATOM   1908  C   PHE A1254       5.946 -33.979  81.382  1.00 42.44           C  
ANISOU 1908  C   PHE A1254     5884   5054   5188    -33   -613    351       C  
ATOM   1909  O   PHE A1254       5.243 -34.923  81.743  1.00 45.29           O  
ANISOU 1909  O   PHE A1254     6329   5358   5522   -110   -673    411       O  
ATOM   1910  CB  PHE A1254       8.299 -34.355  82.144  1.00 42.83           C  
ANISOU 1910  CB  PHE A1254     5915   5161   5197    179   -562    350       C  
ATOM   1911  CG  PHE A1254       8.664 -34.688  80.712  1.00 43.09           C  
ANISOU 1911  CG  PHE A1254     6067   5092   5214    269   -558    327       C  
ATOM   1912  CD1 PHE A1254       8.134 -35.808  80.082  1.00 45.33           C  
ANISOU 1912  CD1 PHE A1254     6552   5218   5454    258   -615    345       C  
ATOM   1913  CD2 PHE A1254       9.549 -33.891  80.006  1.00 42.75           C  
ANISOU 1913  CD2 PHE A1254     5947   5107   5187    360   -503    293       C  
ATOM   1914  CE1 PHE A1254       8.469 -36.115  78.773  1.00 47.47           C  
ANISOU 1914  CE1 PHE A1254     6962   5382   5691    351   -610    320       C  
ATOM   1915  CE2 PHE A1254       9.887 -34.194  78.695  1.00 48.89           C  
ANISOU 1915  CE2 PHE A1254     6838   5798   5940    458   -490    277       C  
ATOM   1916  CZ  PHE A1254       9.347 -35.308  78.080  1.00 49.02           C  
ANISOU 1916  CZ  PHE A1254     7071   5648   5906    461   -540    285       C  
ATOM   1917  N   ILE A1255       5.803 -33.378  80.203  1.00 42.04           N  
ANISOU 1917  N   ILE A1255     5834   4977   5162    -26   -598    308       N  
ATOM   1918  CA  ILE A1255       4.884 -33.887  79.192  1.00 42.41           C  
ANISOU 1918  CA  ILE A1255     6000   4915   5200   -102   -658    327       C  
ATOM   1919  C   ILE A1255       5.523 -33.709  77.821  1.00 43.04           C  
ANISOU 1919  C   ILE A1255     6155   4924   5274     -8   -637    270       C  
ATOM   1920  O   ILE A1255       5.949 -32.606  77.459  1.00 43.95           O  
ANISOU 1920  O   ILE A1255     6155   5116   5428     39   -576    221       O  
ATOM   1921  CB  ILE A1255       3.499 -33.210  79.250  1.00 42.68           C  
ANISOU 1921  CB  ILE A1255     5928   5018   5270   -237   -668    360       C  
ATOM   1922  CG1 ILE A1255       2.625 -33.736  78.105  1.00 43.18           C  
ANISOU 1922  CG1 ILE A1255     6113   4975   5319   -331   -745    393       C  
ATOM   1923  CG2 ILE A1255       3.624 -31.682  79.211  1.00 42.16           C  
ANISOU 1923  CG2 ILE A1255     5701   5066   5253   -201   -586    304       C  
ATOM   1924  CD1 ILE A1255       1.173 -33.354  78.204  1.00 45.84           C  
ANISOU 1924  CD1 ILE A1255     6348   5391   5680   -476   -772    470       C  
ATOM   1925  N   GLY A1256       5.597 -34.792  77.067  1.00 43.47           N  
ANISOU 1925  N   GLY A1256     6418   4828   5272     20   -691    281       N  
ATOM   1926  CA  GLY A1256       6.220 -34.759  75.759  1.00 43.89           C  
ANISOU 1926  CA  GLY A1256     6573   4804   5299    129   -667    234       C  
ATOM   1927  C   GLY A1256       6.588 -36.153  75.311  1.00 48.67           C  
ANISOU 1927  C   GLY A1256     7447   5236   5810    210   -714    252       C  
ATOM   1928  O   GLY A1256       6.535 -37.118  76.076  1.00 50.87           O  
ANISOU 1928  O   GLY A1256     7823   5458   6047    193   -760    298       O  
ATOM   1929  N   ARG A1257       6.971 -36.241  74.041  1.00 49.74           N  
ANISOU 1929  N   ARG A1257     7718   5278   5903    307   -700    215       N  
ATOM   1930  CA  ARG A1257       7.314 -37.525  73.446  1.00 54.04           C  
ANISOU 1930  CA  ARG A1257     8567   5631   6334    408   -738    224       C  
ATOM   1931  C   ARG A1257       8.581 -38.094  74.073  1.00 51.74           C  
ANISOU 1931  C   ARG A1257     8300   5363   5997    609   -673    246       C  
ATOM   1932  O   ARG A1257       9.507 -37.356  74.426  1.00 48.32           O  
ANISOU 1932  O   ARG A1257     7657   5093   5610    717   -581    244       O  
ATOM   1933  CB  ARG A1257       7.494 -37.380  71.934  1.00 60.04           C  
ANISOU 1933  CB  ARG A1257     9464   6300   7049    491   -722    179       C  
ATOM   1934  CG  ARG A1257       7.660 -38.710  71.210  1.00 69.39           C  
ANISOU 1934  CG  ARG A1257    11022   7251   8091    585   -774    184       C  
ATOM   1935  CD  ARG A1257       7.359 -38.583  69.734  1.00 77.94           C  
ANISOU 1935  CD  ARG A1257    12268   8220   9125    584   -797    142       C  
ATOM   1936  NE  ARG A1257       8.445 -37.950  68.993  1.00 85.18           N  
ANISOU 1936  NE  ARG A1257    13110   9216  10039    802   -671    106       N  
ATOM   1937  CZ  ARG A1257       9.279 -38.607  68.193  1.00 91.35           C  
ANISOU 1937  CZ  ARG A1257    14129   9881  10697   1029   -622     98       C  
ATOM   1938  NH1 ARG A1257       9.145 -39.916  68.026  1.00 94.88           N  
ANISOU 1938  NH1 ARG A1257    14937  10104  11010   1070   -693    110       N  
ATOM   1939  NH2 ARG A1257      10.243 -37.956  67.554  1.00 91.69           N  
ANISOU 1939  NH2 ARG A1257    14062  10032  10743   1221   -503     85       N  
ATOM   1940  N   PHE A1258       8.615 -39.419  74.208  1.00 52.83           N  
ANISOU 1940  N   PHE A1258     8700   5336   6036    653   -729    278       N  
ATOM   1941  CA  PHE A1258       9.786 -40.131  74.709  1.00 55.11           C  
ANISOU 1941  CA  PHE A1258     9053   5624   6261    867   -669    312       C  
ATOM   1942  C   PHE A1258      10.694 -40.444  73.524  1.00 60.98           C  
ANISOU 1942  C   PHE A1258     9981   6282   6908   1112   -600    296       C  
ATOM   1943  O   PHE A1258      10.380 -41.313  72.701  1.00 59.05           O  
ANISOU 1943  O   PHE A1258    10064   5819   6554   1140   -656    282       O  
ATOM   1944  CB  PHE A1258       9.382 -41.411  75.441  1.00 54.10           C  
ANISOU 1944  CB  PHE A1258     9139   5352   6064    809   -759    359       C  
ATOM   1945  CG  PHE A1258       8.671 -41.180  76.756  1.00 52.57           C  
ANISOU 1945  CG  PHE A1258     8750   5271   5954    609   -808    395       C  
ATOM   1946  CD1 PHE A1258       8.321 -39.904  77.174  1.00 50.13           C  
ANISOU 1946  CD1 PHE A1258     8130   5156   5762    494   -774    377       C  
ATOM   1947  CD2 PHE A1258       8.363 -42.254  77.580  1.00 52.47           C  
ANISOU 1947  CD2 PHE A1258     8884   5162   5890    549   -884    449       C  
ATOM   1948  CE1 PHE A1258       7.670 -39.707  78.381  1.00 50.03           C  
ANISOU 1948  CE1 PHE A1258     7959   5244   5808    336   -807    413       C  
ATOM   1949  CE2 PHE A1258       7.714 -42.063  78.783  1.00 51.16           C  
ANISOU 1949  CE2 PHE A1258     8541   5107   5792    378   -922    491       C  
ATOM   1950  CZ  PHE A1258       7.369 -40.787  79.185  1.00 49.61           C  
ANISOU 1950  CZ  PHE A1258     8036   5109   5706    279   -878    472       C  
ATOM   1951  N   ASP A1259      11.819 -39.736  73.436  1.00 65.26           N  
ANISOU 1951  N   ASP A1259    10320   6996   7479   1286   -481    306       N  
ATOM   1952  CA  ASP A1259      12.743 -39.885  72.322  1.00 67.02           C  
ANISOU 1952  CA  ASP A1259    10665   7186   7614   1538   -393    308       C  
ATOM   1953  C   ASP A1259      14.134 -39.469  72.779  1.00 67.97           C  
ANISOU 1953  C   ASP A1259    10545   7527   7753   1736   -275    376       C  
ATOM   1954  O   ASP A1259      14.318 -38.944  73.881  1.00 68.26           O  
ANISOU 1954  O   ASP A1259    10326   7734   7877   1648   -272    407       O  
ATOM   1955  CB  ASP A1259      12.289 -39.074  71.099  1.00 66.36           C  
ANISOU 1955  CB  ASP A1259    10569   7088   7558   1474   -393    247       C  
ATOM   1956  CG  ASP A1259      12.046 -37.599  71.413  1.00 67.97           C  
ANISOU 1956  CG  ASP A1259    10417   7499   7910   1311   -377    226       C  
ATOM   1957  OD1 ASP A1259      12.674 -37.047  72.340  1.00 67.09           O  
ANISOU 1957  OD1 ASP A1259    10052   7576   7864   1323   -330    264       O  
ATOM   1958  OD2 ASP A1259      11.213 -36.984  70.715  1.00 69.07           O  
ANISOU 1958  OD2 ASP A1259    10544   7606   8091   1168   -416    174       O  
ATOM   1959  N   ARG A1260      15.121 -39.726  71.926  1.00 67.13           N  
ANISOU 1959  N   ARG A1260    10530   7423   7553   2006   -177    412       N  
ATOM   1960  CA  ARG A1260      16.504 -39.367  72.206  1.00 67.41           C  
ANISOU 1960  CA  ARG A1260    10333   7688   7591   2209    -62    507       C  
ATOM   1961  C   ARG A1260      16.914 -38.193  71.330  1.00 64.63           C  
ANISOU 1961  C   ARG A1260     9780   7489   7289   2232      5    505       C  
ATOM   1962  O   ARG A1260      16.619 -38.175  70.132  1.00 67.92           O  
ANISOU 1962  O   ARG A1260    10359   7790   7657   2276     15    454       O  
ATOM   1963  CB  ARG A1260      17.436 -40.558  71.983  1.00 73.11           C  
ANISOU 1963  CB  ARG A1260    11282   8338   8159   2536     16    586       C  
ATOM   1964  CG  ARG A1260      17.196 -41.692  72.957  1.00 76.77           C  
ANISOU 1964  CG  ARG A1260    11925   8671   8573   2529    -44    605       C  
ATOM   1965  CD  ARG A1260      18.444 -42.518  73.179  1.00 83.33           C  
ANISOU 1965  CD  ARG A1260    12816   9556   9290   2861     59    722       C  
ATOM   1966  NE  ARG A1260      18.303 -43.384  74.348  1.00 89.23           N  
ANISOU 1966  NE  ARG A1260    13647  10237  10020   2825      2    753       N  
ATOM   1967  CZ  ARG A1260      17.764 -44.598  74.315  1.00 90.84           C  
ANISOU 1967  CZ  ARG A1260    14235  10167  10115   2852    -63    722       C  
ATOM   1968  NH1 ARG A1260      17.675 -45.317  75.428  1.00 89.55           N  
ANISOU 1968  NH1 ARG A1260    14118   9963   9943   2811   -115    759       N  
ATOM   1969  NH2 ARG A1260      17.312 -45.094  73.169  1.00 90.30           N  
ANISOU 1969  NH2 ARG A1260    14516   9856   9937   2910    -84    657       N  
ATOM   1970  N   GLY A1261      17.571 -37.208  71.936  1.00 62.00           N  
ANISOU 1970  N   GLY A1261     9103   7409   7046   2185     39    564       N  
ATOM   1971  CA  GLY A1261      18.079 -36.073  71.194  1.00 61.30           C  
ANISOU 1971  CA  GLY A1261     8806   7484   7001   2201     98    584       C  
ATOM   1972  C   GLY A1261      17.051 -35.037  70.802  1.00 58.55           C  
ANISOU 1972  C   GLY A1261     8393   7102   6752   1952     35    477       C  
ATOM   1973  O   GLY A1261      17.371 -34.144  70.009  1.00 58.01           O  
ANISOU 1973  O   GLY A1261     8198   7132   6709   1965     78    482       O  
ATOM   1974  N   GLN A1262      15.833 -35.113  71.336  1.00 59.38           N  
ANISOU 1974  N   GLN A1262     8571   7082   6909   1730    -64    393       N  
ATOM   1975  CA  GLN A1262      14.782 -34.186  70.933  1.00 59.11           C  
ANISOU 1975  CA  GLN A1262     8486   7015   6958   1514   -118    304       C  
ATOM   1976  C   GLN A1262      14.094 -33.538  72.131  1.00 55.93           C  
ANISOU 1976  C   GLN A1262     7914   6679   6656   1280   -182    278       C  
ATOM   1977  O   GLN A1262      14.395 -32.389  72.470  1.00 56.84           O  
ANISOU 1977  O   GLN A1262     7796   6957   6845   1200   -168    287       O  
ATOM   1978  CB  GLN A1262      13.762 -34.906  70.046  1.00 65.31           C  
ANISOU 1978  CB  GLN A1262     9567   7562   7685   1481   -173    235       C  
ATOM   1979  CG  GLN A1262      14.292 -35.226  68.654  1.00 73.91           C  
ANISOU 1979  CG  GLN A1262    10829   8578   8675   1690   -109    238       C  
ATOM   1980  CD  GLN A1262      13.551 -36.370  67.982  1.00 80.33           C  
ANISOU 1980  CD  GLN A1262    12018   9123   9379   1706   -171    193       C  
ATOM   1981  OE1 GLN A1262      12.459 -36.186  67.442  1.00 81.77           O  
ANISOU 1981  OE1 GLN A1262    12294   9192   9584   1531   -251    129       O  
ATOM   1982  NE2 GLN A1262      14.148 -37.559  68.006  1.00 83.04           N  
ANISOU 1982  NE2 GLN A1262    12592   9364   9597   1917   -141    235       N  
ATOM   1983  N   LYS A1263      13.153 -34.241  72.761  1.00 51.84           N  
ANISOU 1983  N   LYS A1263     7524   6038   6135   1167   -257    252       N  
ATOM   1984  CA  LYS A1263      12.385 -33.647  73.847  1.00 50.62           C  
ANISOU 1984  CA  LYS A1263     7225   5944   6064    959   -309    231       C  
ATOM   1985  C   LYS A1263      13.006 -33.853  75.222  1.00 51.12           C  
ANISOU 1985  C   LYS A1263     7177   6114   6130    974   -305    289       C  
ATOM   1986  O   LYS A1263      12.516 -33.263  76.192  1.00 46.46           O  
ANISOU 1986  O   LYS A1263     6460   5594   5599    822   -337    276       O  
ATOM   1987  CB  LYS A1263      10.948 -34.174  73.830  1.00 52.38           C  
ANISOU 1987  CB  LYS A1263     7606   6011   6287    803   -395    192       C  
ATOM   1988  CG  LYS A1263      10.113 -33.546  72.713  1.00 54.85           C  
ANISOU 1988  CG  LYS A1263     7945   6269   6628    713   -414    138       C  
ATOM   1989  CD  LYS A1263      10.596 -32.122  72.418  1.00 58.73           C  
ANISOU 1989  CD  LYS A1263     8218   6912   7186    717   -352    118       C  
ATOM   1990  CE  LYS A1263       9.804 -31.455  71.300  1.00 61.96           C  
ANISOU 1990  CE  LYS A1263     8644   7274   7624    637   -366     68       C  
ATOM   1991  NZ  LYS A1263      10.442 -30.182  70.836  1.00 61.20           N  
ANISOU 1991  NZ  LYS A1263     8374   7305   7573    669   -304     53       N  
ATOM   1992  N   GLY A1264      14.070 -34.649  75.328  1.00 51.84           N  
ANISOU 1992  N   GLY A1264     7318   6227   6154   1163   -263    358       N  
ATOM   1993  CA  GLY A1264      14.879 -34.673  76.532  1.00 49.13           C  
ANISOU 1993  CA  GLY A1264     6828   6024   5814   1191   -251    430       C  
ATOM   1994  C   GLY A1264      14.394 -35.519  77.687  1.00 48.75           C  
ANISOU 1994  C   GLY A1264     6857   5912   5752   1125   -306    441       C  
ATOM   1995  O   GLY A1264      14.898 -35.352  78.800  1.00 46.97           O  
ANISOU 1995  O   GLY A1264     6490   5814   5543   1102   -308    491       O  
ATOM   1996  N   VAL A1265      13.439 -36.429  77.474  1.00 50.51           N  
ANISOU 1996  N   VAL A1265     7304   5945   5940   1082   -359    407       N  
ATOM   1997  CA  VAL A1265      13.002 -37.264  78.590  1.00 52.65           C  
ANISOU 1997  CA  VAL A1265     7647   6163   6195   1014   -416    432       C  
ATOM   1998  C   VAL A1265      14.147 -38.136  79.098  1.00 53.11           C  
ANISOU 1998  C   VAL A1265     7742   6254   6185   1207   -378    515       C  
ATOM   1999  O   VAL A1265      14.183 -38.494  80.281  1.00 47.91           O  
ANISOU 1999  O   VAL A1265     7040   5635   5528   1164   -405    554       O  
ATOM   2000  CB  VAL A1265      11.773 -38.115  78.207  1.00 46.88           C  
ANISOU 2000  CB  VAL A1265     7159   5221   5430    913   -496    400       C  
ATOM   2001  CG1 VAL A1265      12.188 -39.346  77.431  1.00 51.46           C  
ANISOU 2001  CG1 VAL A1265     8027   5627   5897   1092   -493    419       C  
ATOM   2002  CG2 VAL A1265      11.001 -38.521  79.464  1.00 47.26           C  
ANISOU 2002  CG2 VAL A1265     7198   5262   5496    757   -565    424       C  
ATOM   2003  N   ASP A1266      15.097 -38.495  78.228  1.00 53.47           N  
ANISOU 2003  N   ASP A1266     7864   6290   6162   1433   -309    552       N  
ATOM   2004  CA  ASP A1266      16.257 -39.246  78.698  1.00 57.32           C  
ANISOU 2004  CA  ASP A1266     8358   6839   6580   1644   -258    652       C  
ATOM   2005  C   ASP A1266      17.105 -38.413  79.653  1.00 56.53           C  
ANISOU 2005  C   ASP A1266     7950   6992   6538   1615   -233    721       C  
ATOM   2006  O   ASP A1266      17.636 -38.937  80.644  1.00 60.26           O  
ANISOU 2006  O   ASP A1266     8382   7529   6985   1667   -235    797       O  
ATOM   2007  CB  ASP A1266      17.091 -39.720  77.509  1.00 61.98           C  
ANISOU 2007  CB  ASP A1266     9086   7387   7075   1917   -173    691       C  
ATOM   2008  CG  ASP A1266      17.362 -38.611  76.510  1.00 68.84           C  
ANISOU 2008  CG  ASP A1266     9809   8362   7986   1925   -121    670       C  
ATOM   2009  OD1 ASP A1266      16.510 -37.704  76.369  1.00 68.02           O  
ANISOU 2009  OD1 ASP A1266     9620   8257   7968   1709   -169    587       O  
ATOM   2010  OD2 ASP A1266      18.428 -38.648  75.860  1.00 72.39           O  
ANISOU 2010  OD2 ASP A1266    10227   8902   8377   2156    -29    746       O  
ATOM   2011  N   VAL A1267      17.210 -37.106  79.393  1.00 53.58           N  
ANISOU 2011  N   VAL A1267     7367   6755   6235   1516   -221    699       N  
ATOM   2012  CA  VAL A1267      17.938 -36.235  80.307  1.00 53.54           C  
ANISOU 2012  CA  VAL A1267     7094   6973   6275   1445   -223    763       C  
ATOM   2013  C   VAL A1267      17.233 -36.180  81.654  1.00 52.26           C  
ANISOU 2013  C   VAL A1267     6901   6805   6152   1254   -295    731       C  
ATOM   2014  O   VAL A1267      17.875 -36.243  82.712  1.00 54.50           O  
ANISOU 2014  O   VAL A1267     7070   7212   6426   1252   -307    808       O  
ATOM   2015  CB  VAL A1267      18.098 -34.831  79.695  1.00 52.33           C  
ANISOU 2015  CB  VAL A1267     6767   6936   6180   1358   -209    739       C  
ATOM   2016  CG1 VAL A1267      18.889 -33.930  80.634  1.00 50.16           C  
ANISOU 2016  CG1 VAL A1267     6244   6880   5935   1265   -230    814       C  
ATOM   2017  CG2 VAL A1267      18.768 -34.914  78.333  1.00 55.13           C  
ANISOU 2017  CG2 VAL A1267     7152   7302   6491   1555   -132    777       C  
ATOM   2018  N   LEU A1268      15.899 -36.096  81.640  1.00 50.52           N  
ANISOU 2018  N   LEU A1268     6779   6448   5966   1095   -344    631       N  
ATOM   2019  CA  LEU A1268      15.160 -36.048  82.897  1.00 49.51           C  
ANISOU 2019  CA  LEU A1268     6623   6323   5866    927   -401    611       C  
ATOM   2020  C   LEU A1268      15.283 -37.356  83.665  1.00 48.49           C  
ANISOU 2020  C   LEU A1268     6611   6131   5681    998   -422    668       C  
ATOM   2021  O   LEU A1268      15.363 -37.347  84.896  1.00 47.23           O  
ANISOU 2021  O   LEU A1268     6368   6050   5526    927   -450    702       O  
ATOM   2022  CB  LEU A1268      13.690 -35.719  82.637  1.00 49.22           C  
ANISOU 2022  CB  LEU A1268     6655   6174   5872    762   -440    518       C  
ATOM   2023  CG  LEU A1268      12.755 -35.866  83.845  1.00 49.16           C  
ANISOU 2023  CG  LEU A1268     6648   6154   5878    610   -491    510       C  
ATOM   2024  CD1 LEU A1268      13.171 -34.951  85.008  1.00 48.58           C  
ANISOU 2024  CD1 LEU A1268     6391   6244   5823    535   -491    526       C  
ATOM   2025  CD2 LEU A1268      11.319 -35.605  83.445  1.00 48.56           C  
ANISOU 2025  CD2 LEU A1268     6628   5989   5835    470   -521    450       C  
ATOM   2026  N   LEU A1269      15.306 -38.491  82.963  1.00 48.32           N  
ANISOU 2026  N   LEU A1269     6802   5959   5597   1140   -411    682       N  
ATOM   2027  CA  LEU A1269      15.421 -39.765  83.667  1.00 53.57           C  
ANISOU 2027  CA  LEU A1269     7608   6547   6200   1213   -434    738       C  
ATOM   2028  C   LEU A1269      16.807 -39.930  84.280  1.00 53.36           C  
ANISOU 2028  C   LEU A1269     7454   6681   6140   1372   -388    848       C  
ATOM   2029  O   LEU A1269      16.936 -40.417  85.411  1.00 54.99           O  
ANISOU 2029  O   LEU A1269     7641   6921   6331   1351   -416    899       O  
ATOM   2030  CB  LEU A1269      15.089 -40.920  82.721  1.00 58.77           C  
ANISOU 2030  CB  LEU A1269     8570   6979   6782   1325   -443    723       C  
ATOM   2031  CG  LEU A1269      13.648 -40.939  82.191  1.00 59.85           C  
ANISOU 2031  CG  LEU A1269     8849   6951   6939   1142   -514    641       C  
ATOM   2032  CD1 LEU A1269      13.470 -42.007  81.121  1.00 60.93           C  
ANISOU 2032  CD1 LEU A1269     9310   6859   6981   1253   -531    629       C  
ATOM   2033  CD2 LEU A1269      12.645 -41.138  83.318  1.00 57.62           C  
ANISOU 2033  CD2 LEU A1269     8552   6652   6687    936   -593    643       C  
ATOM   2034  N   LYS A1270      17.855 -39.493  83.569  1.00 54.60           N  
ANISOU 2034  N   LYS A1270     7505   6958   6285   1523   -318    899       N  
ATOM   2035  CA  LYS A1270      19.184 -39.494  84.173  1.00 56.12           C  
ANISOU 2035  CA  LYS A1270     7524   7349   6450   1650   -279   1030       C  
ATOM   2036  C   LYS A1270      19.240 -38.561  85.381  1.00 52.41           C  
ANISOU 2036  C   LYS A1270     6827   7048   6040   1449   -331   1042       C  
ATOM   2037  O   LYS A1270      19.874 -38.883  86.393  1.00 54.18           O  
ANISOU 2037  O   LYS A1270     6967   7379   6239   1475   -344   1135       O  
ATOM   2038  CB  LYS A1270      20.242 -39.086  83.144  1.00 61.34           C  
ANISOU 2038  CB  LYS A1270     8083   8135   7087   1830   -197   1101       C  
ATOM   2039  CG  LYS A1270      20.391 -40.022  81.951  1.00 71.22           C  
ANISOU 2039  CG  LYS A1270     9570   9236   8253   2079   -128   1106       C  
ATOM   2040  CD  LYS A1270      21.205 -39.364  80.840  1.00 74.55           C  
ANISOU 2040  CD  LYS A1270     9873   9788   8665   2216    -47   1157       C  
ATOM   2041  CE  LYS A1270      21.065 -40.089  79.509  1.00 75.54           C  
ANISOU 2041  CE  LYS A1270    10268   9727   8706   2424     14   1121       C  
ATOM   2042  NZ  LYS A1270      21.609 -39.260  78.392  1.00 75.53           N  
ANISOU 2042  NZ  LYS A1270    10143   9844   8711   2504     84   1146       N  
ATOM   2043  N   ALA A1271      18.562 -37.410  85.304  1.00 49.44           N  
ANISOU 2043  N   ALA A1271     6366   6687   5732   1251   -363    951       N  
ATOM   2044  CA  ALA A1271      18.546 -36.491  86.441  1.00 52.11           C  
ANISOU 2044  CA  ALA A1271     6536   7155   6106   1062   -416    951       C  
ATOM   2045  C   ALA A1271      17.801 -37.085  87.630  1.00 50.71           C  
ANISOU 2045  C   ALA A1271     6439   6906   5922    964   -466    928       C  
ATOM   2046  O   ALA A1271      18.193 -36.875  88.785  1.00 53.03           O  
ANISOU 2046  O   ALA A1271     6626   7317   6206    894   -501    980       O  
ATOM   2047  CB  ALA A1271      17.919 -35.155  86.039  1.00 47.51           C  
ANISOU 2047  CB  ALA A1271     5889   6579   5583    896   -431    853       C  
ATOM   2048  N   ILE A1272      16.726 -37.832  87.372  1.00 48.49           N  
ANISOU 2048  N   ILE A1272     6347   6439   5639    948   -479    862       N  
ATOM   2049  CA  ILE A1272      16.006 -38.474  88.466  1.00 52.18           C  
ANISOU 2049  CA  ILE A1272     6889   6844   6094    857   -527    859       C  
ATOM   2050  C   ILE A1272      16.874 -39.546  89.109  1.00 56.77           C  
ANISOU 2050  C   ILE A1272     7501   7453   6616    998   -524    965       C  
ATOM   2051  O   ILE A1272      16.898 -39.695  90.339  1.00 57.09           O  
ANISOU 2051  O   ILE A1272     7490   7554   6645    929   -559   1003       O  
ATOM   2052  CB  ILE A1272      14.670 -39.051  87.964  1.00 50.84           C  
ANISOU 2052  CB  ILE A1272     6909   6477   5930    792   -554    789       C  
ATOM   2053  CG1 ILE A1272      13.711 -37.918  87.590  1.00 52.03           C  
ANISOU 2053  CG1 ILE A1272     6998   6631   6141    636   -560    699       C  
ATOM   2054  CG2 ILE A1272      14.051 -39.968  89.021  1.00 49.17           C  
ANISOU 2054  CG2 ILE A1272     6790   6201   5692    724   -605    818       C  
ATOM   2055  CD1 ILE A1272      12.374 -38.395  87.040  1.00 51.22           C  
ANISOU 2055  CD1 ILE A1272     7051   6364   6045    552   -594    653       C  
ATOM   2056  N   GLU A1273      17.627 -40.286  88.291  1.00 58.15           N  
ANISOU 2056  N   GLU A1273     7763   7589   6743   1212   -476   1021       N  
ATOM   2057  CA  GLU A1273      18.532 -41.286  88.847  1.00 62.38           C  
ANISOU 2057  CA  GLU A1273     8326   8162   7214   1380   -460   1137       C  
ATOM   2058  C   GLU A1273      19.633 -40.634  89.674  1.00 59.78           C  
ANISOU 2058  C   GLU A1273     7745   8079   6889   1374   -457   1237       C  
ATOM   2059  O   GLU A1273      20.053 -41.180  90.700  1.00 59.56           O  
ANISOU 2059  O   GLU A1273     7688   8113   6829   1398   -478   1319       O  
ATOM   2060  CB  GLU A1273      19.134 -42.132  87.726  1.00 67.89           C  
ANISOU 2060  CB  GLU A1273     9181   8772   7844   1642   -393   1181       C  
ATOM   2061  CG  GLU A1273      18.158 -43.108  87.103  1.00 72.05           C  
ANISOU 2061  CG  GLU A1273    10017   9028   8331   1658   -417   1108       C  
ATOM   2062  CD  GLU A1273      18.850 -44.149  86.255  1.00 79.01           C  
ANISOU 2062  CD  GLU A1273    11107   9805   9111   1947   -354   1166       C  
ATOM   2063  OE1 GLU A1273      19.837 -43.798  85.574  1.00 81.67           O  
ANISOU 2063  OE1 GLU A1273    11339  10264   9426   2127   -272   1226       O  
ATOM   2064  OE2 GLU A1273      18.415 -45.320  86.279  1.00 81.36           O  
ANISOU 2064  OE2 GLU A1273    11679   9896   9339   1999   -386   1161       O  
ATOM   2065  N   ILE A1274      20.097 -39.453  89.259  1.00 58.65           N  
ANISOU 2065  N   ILE A1274     7422   8078   6783   1324   -443   1239       N  
ATOM   2066  CA  ILE A1274      21.105 -38.749  90.045  1.00 57.61           C  
ANISOU 2066  CA  ILE A1274     7057   8182   6650   1273   -466   1344       C  
ATOM   2067  C   ILE A1274      20.520 -38.284  91.372  1.00 57.92           C  
ANISOU 2067  C   ILE A1274     7056   8244   6709   1049   -543   1298       C  
ATOM   2068  O   ILE A1274      21.154 -38.414  92.427  1.00 65.53           O  
ANISOU 2068  O   ILE A1274     7925   9332   7642   1029   -578   1393       O  
ATOM   2069  CB  ILE A1274      21.682 -37.569  89.243  1.00 59.02           C  
ANISOU 2069  CB  ILE A1274     7073   8495   6858   1247   -448   1361       C  
ATOM   2070  CG1 ILE A1274      22.501 -38.067  88.054  1.00 59.61           C  
ANISOU 2070  CG1 ILE A1274     7156   8598   6896   1503   -360   1447       C  
ATOM   2071  CG2 ILE A1274      22.536 -36.679  90.134  1.00 58.80           C  
ANISOU 2071  CG2 ILE A1274     6821   8694   6827   1118   -505   1459       C  
ATOM   2072  CD1 ILE A1274      22.879 -36.971  87.092  1.00 52.90           C  
ANISOU 2072  CD1 ILE A1274     6174   7850   6077   1477   -337   1450       C  
ATOM   2073  N   LEU A1275      19.299 -37.745  91.347  1.00 53.86           N  
ANISOU 2073  N   LEU A1275     6615   7613   6236    886   -567   1161       N  
ATOM   2074  CA  LEU A1275      18.683 -37.241  92.571  1.00 54.24           C  
ANISOU 2074  CA  LEU A1275     6638   7682   6289    694   -625   1116       C  
ATOM   2075  C   LEU A1275      18.269 -38.349  93.528  1.00 56.31           C  
ANISOU 2075  C   LEU A1275     7002   7873   6519    704   -647   1140       C  
ATOM   2076  O   LEU A1275      18.157 -38.095  94.732  1.00 56.08           O  
ANISOU 2076  O   LEU A1275     6927   7908   6471    587   -691   1149       O  
ATOM   2077  CB  LEU A1275      17.462 -36.383  92.233  1.00 53.41           C  
ANISOU 2077  CB  LEU A1275     6582   7483   6228    550   -628    980       C  
ATOM   2078  CG  LEU A1275      17.765 -35.106  91.450  1.00 52.67           C  
ANISOU 2078  CG  LEU A1275     6391   7457   6165    502   -618    945       C  
ATOM   2079  CD1 LEU A1275      16.490 -34.517  90.874  1.00 46.82           C  
ANISOU 2079  CD1 LEU A1275     5728   6596   5466    413   -604    818       C  
ATOM   2080  CD2 LEU A1275      18.468 -34.117  92.362  1.00 51.73           C  
ANISOU 2080  CD2 LEU A1275     6140   7495   6019    380   -671    990       C  
ATOM   2081  N   SER A1276      18.051 -39.568  93.025  1.00 55.06           N  
ANISOU 2081  N   SER A1276     6998   7578   6345    840   -621   1152       N  
ATOM   2082  CA  SER A1276      17.442 -40.609  93.848  1.00 52.56           C  
ANISOU 2082  CA  SER A1276     6807   7163   5999    821   -652   1163       C  
ATOM   2083  C   SER A1276      18.308 -40.977  95.049  1.00 54.19           C  
ANISOU 2083  C   SER A1276     6929   7498   6163    852   -676   1273       C  
ATOM   2084  O   SER A1276      17.785 -41.456  96.062  1.00 52.75           O  
ANISOU 2084  O   SER A1276     6798   7283   5962    775   -713   1278       O  
ATOM   2085  CB  SER A1276      17.155 -41.848  92.997  1.00 54.47           C  
ANISOU 2085  CB  SER A1276     7263   7218   6216    961   -632   1163       C  
ATOM   2086  OG  SER A1276      18.353 -42.420  92.505  1.00 55.37           O  
ANISOU 2086  OG  SER A1276     7383   7371   6285   1187   -584   1257       O  
ATOM   2087  N   SER A1277      19.624 -40.782  94.958  1.00 56.42           N  
ANISOU 2087  N   SER A1277     7074   7938   6425    960   -656   1376       N  
ATOM   2088  CA  SER A1277      20.495 -41.057  96.096  1.00 55.79           C  
ANISOU 2088  CA  SER A1277     6891   8004   6302    978   -687   1498       C  
ATOM   2089  C   SER A1277      20.551 -39.916  97.107  1.00 55.62           C  
ANISOU 2089  C   SER A1277     6726   8122   6283    770   -749   1488       C  
ATOM   2090  O   SER A1277      21.096 -40.113  98.195  1.00 54.07           O  
ANISOU 2090  O   SER A1277     6462   8036   6047    744   -791   1577       O  
ATOM   2091  CB  SER A1277      21.913 -41.382  95.615  1.00 57.43           C  
ANISOU 2091  CB  SER A1277     6997   8348   6476   1188   -643   1646       C  
ATOM   2092  OG  SER A1277      22.457 -40.324  94.845  1.00 63.00           O  
ANISOU 2092  OG  SER A1277     7557   9172   7208   1170   -626   1656       O  
ATOM   2093  N   LYS A1278      20.023 -38.737  96.783  1.00 55.23           N  
ANISOU 2093  N   LYS A1278     6647   8067   6270    628   -759   1385       N  
ATOM   2094  CA  LYS A1278      20.051 -37.602  97.700  1.00 55.74           C  
ANISOU 2094  CA  LYS A1278     6623   8237   6317    436   -820   1367       C  
ATOM   2095  C   LYS A1278      18.864 -37.631  98.660  1.00 56.08           C  
ANISOU 2095  C   LYS A1278     6772   8189   6348    312   -841   1280       C  
ATOM   2096  O   LYS A1278      17.794 -38.154  98.342  1.00 56.81           O  
ANISOU 2096  O   LYS A1278     6985   8134   6466    328   -810   1207       O  
ATOM   2097  CB  LYS A1278      20.073 -36.286  96.919  1.00 55.78           C  
ANISOU 2097  CB  LYS A1278     6569   8273   6354    353   -819   1304       C  
ATOM   2098  CG  LYS A1278      21.243 -36.191  95.946  1.00 61.00           C  
ANISOU 2098  CG  LYS A1278     7107   9046   7024    470   -795   1405       C  
ATOM   2099  CD  LYS A1278      21.423 -34.789  95.404  1.00 65.24           C  
ANISOU 2099  CD  LYS A1278     7564   9644   7579    351   -818   1368       C  
ATOM   2100  CE  LYS A1278      22.807 -34.613  94.793  1.00 71.88           C  
ANISOU 2100  CE  LYS A1278     8234  10665   8411    432   -817   1520       C  
ATOM   2101  NZ  LYS A1278      23.026 -35.486  93.605  1.00 76.27           N  
ANISOU 2101  NZ  LYS A1278     8811  11178   8989    667   -723   1554       N  
ATOM   2102  N   LYS A1279      19.070 -37.073  99.858  1.00 58.22           N  
ANISOU 2102  N   LYS A1279     6997   8555   6569    184   -900   1301       N  
ATOM   2103  CA  LYS A1279      17.987 -37.029 100.841  1.00 57.42           C  
ANISOU 2103  CA  LYS A1279     6988   8388   6439     79   -911   1231       C  
ATOM   2104  C   LYS A1279      16.849 -36.119 100.392  1.00 57.07           C  
ANISOU 2104  C   LYS A1279     7007   8255   6420     -1   -880   1098       C  
ATOM   2105  O   LYS A1279      15.674 -36.400 100.678  1.00 57.86           O  
ANISOU 2105  O   LYS A1279     7194   8268   6522    -27   -854   1044       O  
ATOM   2106  CB  LYS A1279      18.523 -36.582 102.199  1.00 56.36           C  
ANISOU 2106  CB  LYS A1279     6812   8374   6229    -32   -981   1283       C  
ATOM   2107  CG  LYS A1279      18.957 -35.130 102.285  1.00 61.25           C  
ANISOU 2107  CG  LYS A1279     7387   9072   6813   -164  -1032   1258       C  
ATOM   2108  CD  LYS A1279      19.000 -34.673 103.741  1.00 70.74           C  
ANISOU 2108  CD  LYS A1279     8626  10331   7919   -298  -1101   1269       C  
ATOM   2109  CE  LYS A1279      19.341 -33.196 103.866  1.00 76.64           C  
ANISOU 2109  CE  LYS A1279     9384  11124   8611   -448  -1165   1235       C  
ATOM   2110  NZ  LYS A1279      19.212 -32.715 105.276  1.00 81.39           N  
ANISOU 2110  NZ  LYS A1279    10078  11745   9099   -577  -1229   1224       N  
ATOM   2111  N   GLU A1280      17.171 -35.061  99.639  1.00 54.55           N  
ANISOU 2111  N   GLU A1280     6641   7965   6121    -35   -880   1060       N  
ATOM   2112  CA  GLU A1280      16.143 -34.158  99.138  1.00 55.75           C  
ANISOU 2112  CA  GLU A1280     6851   8036   6295    -95   -845    941       C  
ATOM   2113  C   GLU A1280      15.159 -34.883  98.238  1.00 55.05           C  
ANISOU 2113  C   GLU A1280     6826   7821   6269    -18   -786    896       C  
ATOM   2114  O   GLU A1280      14.012 -34.442  98.106  1.00 56.68           O  
ANISOU 2114  O   GLU A1280     7088   7961   6487    -65   -754    817       O  
ATOM   2115  CB  GLU A1280      16.783 -32.994  98.378  1.00 58.56           C  
ANISOU 2115  CB  GLU A1280     7147   8441   6664   -135   -861    921       C  
ATOM   2116  CG  GLU A1280      17.641 -32.069  99.229  1.00 65.03           C  
ANISOU 2116  CG  GLU A1280     7928   9372   7408   -257   -941    962       C  
ATOM   2117  CD  GLU A1280      19.068 -32.563  99.378  1.00 72.20           C  
ANISOU 2117  CD  GLU A1280     8710  10419   8302   -225   -993   1108       C  
ATOM   2118  OE1 GLU A1280      19.940 -31.747  99.744  1.00 75.82           O  
ANISOU 2118  OE1 GLU A1280     9111  10986   8710   -336  -1072   1166       O  
ATOM   2119  OE2 GLU A1280      19.322 -33.761  99.124  1.00 72.88           O  
ANISOU 2119  OE2 GLU A1280     8763  10508   8422    -88   -958   1176       O  
ATOM   2120  N   PHE A1281      15.577 -36.009  97.654  1.00 52.98           N  
ANISOU 2120  N   PHE A1281     6568   7526   6036    100   -774    955       N  
ATOM   2121  CA  PHE A1281      14.705 -36.768  96.769  1.00 57.09           C  
ANISOU 2121  CA  PHE A1281     7180   7910   6601    158   -738    921       C  
ATOM   2122  C   PHE A1281      13.422 -37.169  97.477  1.00 58.91           C  
ANISOU 2122  C   PHE A1281     7487   8077   6818     86   -739    900       C  
ATOM   2123  O   PHE A1281      12.374 -37.298  96.831  1.00 55.87           O  
ANISOU 2123  O   PHE A1281     7163   7599   6467     66   -718    857       O  
ATOM   2124  CB  PHE A1281      15.450 -38.005  96.258  1.00 59.03           C  
ANISOU 2124  CB  PHE A1281     7461   8120   6848    308   -733    999       C  
ATOM   2125  CG  PHE A1281      14.689 -38.814  95.241  1.00 57.42           C  
ANISOU 2125  CG  PHE A1281     7389   7756   6673    366   -711    967       C  
ATOM   2126  CD1 PHE A1281      14.485 -38.330  93.958  1.00 54.51           C  
ANISOU 2126  CD1 PHE A1281     7033   7334   6345    388   -681    906       C  
ATOM   2127  CD2 PHE A1281      14.204 -40.074  95.564  1.00 56.41           C  
ANISOU 2127  CD2 PHE A1281     7385   7526   6523    389   -731   1005       C  
ATOM   2128  CE1 PHE A1281      13.795 -39.082  93.018  1.00 55.88           C  
ANISOU 2128  CE1 PHE A1281     7346   7353   6532    428   -675    882       C  
ATOM   2129  CE2 PHE A1281      13.514 -40.832  94.634  1.00 56.62           C  
ANISOU 2129  CE2 PHE A1281     7560   7392   6560    419   -732    985       C  
ATOM   2130  CZ  PHE A1281      13.310 -40.336  93.357  1.00 58.11           C  
ANISOU 2130  CZ  PHE A1281     7766   7527   6785    437   -706    922       C  
ATOM   2131  N   GLN A1282      13.475 -37.330  98.805  1.00 58.92           N  
ANISOU 2131  N   GLN A1282     7479   8141   6768     38   -765    941       N  
ATOM   2132  CA  GLN A1282      12.274 -37.724  99.537  1.00 58.84           C  
ANISOU 2132  CA  GLN A1282     7527   8093   6737    -26   -761    942       C  
ATOM   2133  C   GLN A1282      11.174 -36.674  99.430  1.00 54.13           C  
ANISOU 2133  C   GLN A1282     6927   7495   6144   -101   -723    867       C  
ATOM   2134  O   GLN A1282       9.989 -37.009  99.514  1.00 54.22           O  
ANISOU 2134  O   GLN A1282     6974   7466   6159   -138   -706    875       O  
ATOM   2135  CB  GLN A1282      12.604 -37.971 101.012  1.00 63.03           C  
ANISOU 2135  CB  GLN A1282     8044   8703   7200    -58   -792    999       C  
ATOM   2136  CG  GLN A1282      13.334 -39.269 101.308  1.00 70.70           C  
ANISOU 2136  CG  GLN A1282     9037   9664   8161     17   -825   1092       C  
ATOM   2137  CD  GLN A1282      13.573 -39.466 102.804  1.00 76.10           C  
ANISOU 2137  CD  GLN A1282     9705  10432   8776    -26   -858   1149       C  
ATOM   2138  OE1 GLN A1282      13.928 -38.527 103.519  1.00 74.05           O  
ANISOU 2138  OE1 GLN A1282     9397  10268   8471    -88   -872   1132       O  
ATOM   2139  NE2 GLN A1282      13.363 -40.686 103.282  1.00 80.23           N  
ANISOU 2139  NE2 GLN A1282    10287  10910   9285     -1   -876   1217       N  
ATOM   2140  N   GLU A1283      11.541 -35.407  99.270  1.00 47.47           N  
ANISOU 2140  N   GLU A1283     6044   6702   5293   -124   -712    808       N  
ATOM   2141  CA  GLU A1283      10.576 -34.316  99.257  1.00 51.52           C  
ANISOU 2141  CA  GLU A1283     6568   7215   5791   -173   -670    740       C  
ATOM   2142  C   GLU A1283      10.003 -34.022  97.872  1.00 53.04           C  
ANISOU 2142  C   GLU A1283     6760   7339   6053   -155   -635    690       C  
ATOM   2143  O   GLU A1283       9.130 -33.154  97.753  1.00 57.26           O  
ANISOU 2143  O   GLU A1283     7302   7874   6580   -180   -592    642       O  
ATOM   2144  CB  GLU A1283      11.223 -33.057  99.835  1.00 54.68           C  
ANISOU 2144  CB  GLU A1283     6965   7682   6129   -217   -685    699       C  
ATOM   2145  CG  GLU A1283      11.546 -33.181 101.319  1.00 63.90           C  
ANISOU 2145  CG  GLU A1283     8155   8915   7208   -254   -719    742       C  
ATOM   2146  CD  GLU A1283      12.355 -32.017 101.846  1.00 71.25           C  
ANISOU 2146  CD  GLU A1283     9108   9900   8066   -317   -762    713       C  
ATOM   2147  OE1 GLU A1283      13.489 -31.812 101.367  1.00 73.18           O  
ANISOU 2147  OE1 GLU A1283     9296  10178   8332   -329   -811    735       O  
ATOM   2148  OE2 GLU A1283      11.854 -31.307 102.742  1.00 77.72           O  
ANISOU 2148  OE2 GLU A1283    10007  10728   8794   -355   -749    679       O  
ATOM   2149  N   MET A1284      10.473 -34.700  96.832  1.00 49.96           N  
ANISOU 2149  N   MET A1284     6370   6891   5720   -101   -649    703       N  
ATOM   2150  CA  MET A1284      10.063 -34.421  95.464  1.00 48.32           C  
ANISOU 2150  CA  MET A1284     6169   6617   5572    -83   -624    656       C  
ATOM   2151  C   MET A1284       9.026 -35.431  94.983  1.00 50.20           C  
ANISOU 2151  C   MET A1284     6467   6767   5840    -92   -628    688       C  
ATOM   2152  O   MET A1284       8.970 -36.569  95.456  1.00 47.19           O  
ANISOU 2152  O   MET A1284     6134   6355   5441    -90   -660    752       O  
ATOM   2153  CB  MET A1284      11.275 -34.431  94.530  1.00 48.42           C  
ANISOU 2153  CB  MET A1284     6156   6624   5616    -11   -635    653       C  
ATOM   2154  CG  MET A1284      12.405 -33.513  94.987  1.00 50.70           C  
ANISOU 2154  CG  MET A1284     6375   7015   5872    -26   -654    653       C  
ATOM   2155  SD  MET A1284      13.929 -33.768  94.057  1.00 53.81           S  
ANISOU 2155  SD  MET A1284     6707   7447   6291     73   -665    704       S  
ATOM   2156  CE  MET A1284      14.991 -32.509  94.767  1.00 51.83           C  
ANISOU 2156  CE  MET A1284     6365   7335   5993    -10   -710    722       C  
ATOM   2157  N   ARG A1285       8.198 -34.994  94.039  1.00 45.05           N  
ANISOU 2157  N   ARG A1285     5818   6073   5226   -115   -604    650       N  
ATOM   2158  CA  ARG A1285       7.256 -35.857  93.342  1.00 48.34           C  
ANISOU 2158  CA  ARG A1285     6296   6401   5669   -145   -625    686       C  
ATOM   2159  C   ARG A1285       7.404 -35.586  91.856  1.00 48.38           C  
ANISOU 2159  C   ARG A1285     6324   6335   5723   -111   -618    634       C  
ATOM   2160  O   ARG A1285       7.623 -34.443  91.454  1.00 46.99           O  
ANISOU 2160  O   ARG A1285     6089   6200   5565    -97   -581    572       O  
ATOM   2161  CB  ARG A1285       5.808 -35.595  93.776  1.00 46.50           C  
ANISOU 2161  CB  ARG A1285     6029   6213   5426   -228   -604    721       C  
ATOM   2162  CG  ARG A1285       5.595 -35.506  95.277  1.00 47.34           C  
ANISOU 2162  CG  ARG A1285     6099   6414   5473   -250   -588    762       C  
ATOM   2163  CD  ARG A1285       5.699 -36.872  95.945  1.00 49.40           C  
ANISOU 2163  CD  ARG A1285     6413   6645   5710   -271   -642    845       C  
ATOM   2164  NE  ARG A1285       5.491 -36.775  97.386  1.00 48.02           N  
ANISOU 2164  NE  ARG A1285     6202   6568   5475   -290   -624    886       N  
ATOM   2165  CZ  ARG A1285       6.472 -36.696  98.280  1.00 51.03           C  
ANISOU 2165  CZ  ARG A1285     6582   6991   5815   -254   -630    873       C  
ATOM   2166  NH1 ARG A1285       7.739 -36.708  97.884  1.00 51.56           N  
ANISOU 2166  NH1 ARG A1285     6661   7029   5900   -196   -652    834       N  
ATOM   2167  NH2 ARG A1285       6.188 -36.608  99.573  1.00 51.37           N  
ANISOU 2167  NH2 ARG A1285     6607   7117   5794   -275   -614    911       N  
ATOM   2168  N   PHE A1286       7.293 -36.627  91.039  1.00 47.29           N  
ANISOU 2168  N   PHE A1286     6290   6084   5596    -98   -658    661       N  
ATOM   2169  CA  PHE A1286       7.458 -36.474  89.602  1.00 49.81           C  
ANISOU 2169  CA  PHE A1286     6652   6325   5948    -57   -654    615       C  
ATOM   2170  C   PHE A1286       6.290 -37.114  88.874  1.00 48.09           C  
ANISOU 2170  C   PHE A1286     6527   6007   5737   -139   -699    647       C  
ATOM   2171  O   PHE A1286       5.844 -38.209  89.233  1.00 49.53           O  
ANISOU 2171  O   PHE A1286     6802   6127   5890   -191   -756    716       O  
ATOM   2172  CB  PHE A1286       8.774 -37.093  89.124  1.00 52.31           C  
ANISOU 2172  CB  PHE A1286     7037   6590   6250     73   -658    614       C  
ATOM   2173  CG  PHE A1286       9.995 -36.436  89.698  1.00 50.35           C  
ANISOU 2173  CG  PHE A1286     6679   6458   5994    140   -625    606       C  
ATOM   2174  CD1 PHE A1286      10.617 -35.395  89.027  1.00 49.58           C  
ANISOU 2174  CD1 PHE A1286     6501   6414   5922    177   -590    557       C  
ATOM   2175  CD2 PHE A1286      10.517 -36.854  90.909  1.00 47.86           C  
ANISOU 2175  CD2 PHE A1286     6340   6204   5642    152   -640    657       C  
ATOM   2176  CE1 PHE A1286      11.742 -34.787  89.547  1.00 49.84           C  
ANISOU 2176  CE1 PHE A1286     6432   6563   5941    210   -579    570       C  
ATOM   2177  CE2 PHE A1286      11.642 -36.252  91.438  1.00 51.17           C  
ANISOU 2177  CE2 PHE A1286     6656   6739   6047    191   -626    666       C  
ATOM   2178  CZ  PHE A1286      12.254 -35.213  90.757  1.00 52.34           C  
ANISOU 2178  CZ  PHE A1286     6725   6944   6219    213   -600    627       C  
ATOM   2179  N   ILE A1287       5.799 -36.419  87.852  1.00 44.51           N  
ANISOU 2179  N   ILE A1287     6053   5540   5320   -162   -682    605       N  
ATOM   2180  CA  ILE A1287       4.740 -36.915  86.983  1.00 46.34           C  
ANISOU 2180  CA  ILE A1287     6368   5681   5557   -252   -735    640       C  
ATOM   2181  C   ILE A1287       5.263 -36.818  85.557  1.00 46.82           C  
ANISOU 2181  C   ILE A1287     6510   5648   5633   -180   -732    578       C  
ATOM   2182  O   ILE A1287       5.405 -35.713  85.020  1.00 45.26           O  
ANISOU 2182  O   ILE A1287     6221   5505   5472   -150   -679    517       O  
ATOM   2183  CB  ILE A1287       3.435 -36.124  87.143  1.00 46.34           C  
ANISOU 2183  CB  ILE A1287     6248   5777   5580   -357   -716    672       C  
ATOM   2184  CG1 ILE A1287       2.997 -36.101  88.606  1.00 44.92           C  
ANISOU 2184  CG1 ILE A1287     5982   5712   5375   -397   -698    735       C  
ATOM   2185  CG2 ILE A1287       2.341 -36.711  86.259  1.00 45.78           C  
ANISOU 2185  CG2 ILE A1287     6255   5629   5511   -473   -789    736       C  
ATOM   2186  CD1 ILE A1287       1.960 -35.044  88.904  1.00 47.68           C  
ANISOU 2186  CD1 ILE A1287     6193   6189   5733   -437   -640    758       C  
ATOM   2187  N   ILE A1288       5.552 -37.960  84.944  1.00 47.66           N  
ANISOU 2187  N   ILE A1288     6802   5606   5700   -146   -787    594       N  
ATOM   2188  CA  ILE A1288       6.119 -38.005  83.601  1.00 48.68           C  
ANISOU 2188  CA  ILE A1288     7039   5636   5822    -52   -779    541       C  
ATOM   2189  C   ILE A1288       5.045 -38.520  82.654  1.00 49.42           C  
ANISOU 2189  C   ILE A1288     7276   5603   5900   -168   -860    567       C  
ATOM   2190  O   ILE A1288       4.539 -39.636  82.824  1.00 50.81           O  
ANISOU 2190  O   ILE A1288     7607   5672   6026   -249   -947    633       O  
ATOM   2191  CB  ILE A1288       7.384 -38.873  83.561  1.00 49.83           C  
ANISOU 2191  CB  ILE A1288     7313   5705   5913    113   -769    542       C  
ATOM   2192  CG1 ILE A1288       8.385 -38.350  84.596  1.00 51.63           C  
ANISOU 2192  CG1 ILE A1288     7376   6084   6157    197   -706    542       C  
ATOM   2193  CG2 ILE A1288       8.010 -38.851  82.177  1.00 47.10           C  
ANISOU 2193  CG2 ILE A1288     7072   5274   5549    238   -743    494       C  
ATOM   2194  CD1 ILE A1288       8.982 -39.412  85.461  1.00 46.53           C  
ANISOU 2194  CD1 ILE A1288     6810   5411   5459    264   -726    599       C  
ATOM   2195  N   ILE A1289       4.655 -37.659  81.730  1.00 47.77           N  
ANISOU 2195  N   ILE A1289     7023   5402   5725   -187   -840    523       N  
ATOM   2196  CA  ILE A1289       3.557 -37.934  80.771  1.00 46.78           C  
ANISOU 2196  CA  ILE A1289     6991   5190   5591   -323   -918    555       C  
ATOM   2197  C   ILE A1289       4.133 -37.993  79.368  1.00 47.48           C  
ANISOU 2197  C   ILE A1289     7229   5156   5655   -229   -916    491       C  
ATOM   2198  O   ILE A1289       4.819 -37.076  78.985  1.00 48.23           O  
ANISOU 2198  O   ILE A1289     7220   5318   5787   -120   -831    421       O  
ATOM   2199  CB  ILE A1289       2.518 -36.817  80.889  1.00 46.21           C  
ANISOU 2199  CB  ILE A1289     6712   5263   5581   -436   -894    577       C  
ATOM   2200  CG1 ILE A1289       2.127 -36.598  82.343  1.00 46.64           C  
ANISOU 2200  CG1 ILE A1289     6621   5452   5646   -497   -877    643       C  
ATOM   2201  CG2 ILE A1289       1.323 -37.070  80.003  1.00 45.48           C  
ANISOU 2201  CG2 ILE A1289     6696   5104   5480   -586   -981    632       C  
ATOM   2202  CD1 ILE A1289       1.411 -35.330  82.582  1.00 45.05           C  
ANISOU 2202  CD1 ILE A1289     6205   5417   5495   -512   -800    638       C  
ATOM   2203  N   GLY A1290       3.824 -39.055  78.645  1.00 48.93           N  
ANISOU 2203  N   GLY A1290     7665   5158   5767   -276  -1011    519       N  
ATOM   2204  CA  GLY A1290       4.298 -39.207  77.267  1.00 50.80           C  
ANISOU 2204  CA  GLY A1290     8076   5263   5962   -194  -1015    463       C  
ATOM   2205  C   GLY A1290       4.386 -40.647  76.832  1.00 56.09           C  
ANISOU 2205  C   GLY A1290     9089   5707   6517   -161  -1100    485       C  
ATOM   2206  O   GLY A1290       4.048 -41.507  77.597  1.00 57.48           O  
ANISOU 2206  O   GLY A1290     9365   5825   6651   -224  -1167    547       O  
ATOM   2207  N   LYS A1291       4.809 -40.852  75.597  1.00 59.95           N  
ANISOU 2207  N   LYS A1291     9771   6062   6944    -54  -1095    432       N  
ATOM   2208  CA  LYS A1291       4.985 -42.180  74.973  1.00 66.22           C  
ANISOU 2208  CA  LYS A1291    10946   6611   7604     10  -1168    439       C  
ATOM   2209  C   LYS A1291       6.005 -42.058  73.842  1.00 65.80           C  
ANISOU 2209  C   LYS A1291    11013   6490   7499    234  -1085    364       C  
ATOM   2210  O   LYS A1291       6.328 -40.954  73.462  1.00 60.97           O  
ANISOU 2210  O   LYS A1291    10200   6006   6960    274  -1005    317       O  
ATOM   2211  CB  LYS A1291       3.651 -42.803  74.557  1.00 74.79           C  
ANISOU 2211  CB  LYS A1291    12241   7543   8633   -243  -1339    500       C  
ATOM   2212  CG  LYS A1291       2.672 -41.913  73.812  1.00 80.79           C  
ANISOU 2212  CG  LYS A1291    12852   8385   9461   -414  -1371    504       C  
ATOM   2213  CD  LYS A1291       1.369 -42.615  73.461  1.00 88.41           C  
ANISOU 2213  CD  LYS A1291    14029   9207  10358   -680  -1557    590       C  
ATOM   2214  CE  LYS A1291       0.231 -41.660  73.165  1.00 91.78           C  
ANISOU 2214  CE  LYS A1291    14196   9797  10877   -888  -1588    645       C  
ATOM   2215  NZ  LYS A1291      -1.048 -42.348  72.863  1.00 94.53           N  
ANISOU 2215  NZ  LYS A1291    14733  10027  11156  -1166  -1783    754       N  
ATOM   2216  N   GLY A1292       6.515 -43.175  73.349  1.00 68.72           N  
ANISOU 2216  N   GLY A1292    11722   6655   7732    388  -1102    360       N  
ATOM   2217  CA  GLY A1292       7.540 -43.082  72.305  1.00 66.58           C  
ANISOU 2217  CA  GLY A1292    11601   6311   7385    631  -1017    304       C  
ATOM   2218  C   GLY A1292       8.455 -44.276  72.337  1.00 69.71           C  
ANISOU 2218  C   GLY A1292    12304   6546   7637    882   -984    316       C  
ATOM   2219  O   GLY A1292       7.964 -45.377  72.363  1.00 72.73           O  
ANISOU 2219  O   GLY A1292    13053   6686   7894    831  -1098    336       O  
ATOM   2220  N   ASP A1293       9.752 -44.024  72.331  1.00 69.96           N  
ANISOU 2220  N   ASP A1293    12190   6713   7677   1150   -835    317       N  
ATOM   2221  CA  ASP A1293      10.776 -45.082  72.332  1.00 71.69           C  
ANISOU 2221  CA  ASP A1293    12677   6808   7753   1440   -776    343       C  
ATOM   2222  C   ASP A1293      10.475 -46.044  73.477  1.00 69.62           C  
ANISOU 2222  C   ASP A1293    12567   6438   7446   1365   -864    396       C  
ATOM   2223  O   ASP A1293      10.408 -45.613  74.608  1.00 70.31           O  
ANISOU 2223  O   ASP A1293    12374   6698   7643   1258   -862    431       O  
ATOM   2224  CB  ASP A1293      12.123 -44.408  72.547  1.00 76.13           C  
ANISOU 2224  CB  ASP A1293    12962   7606   8359   1706   -601    368       C  
ATOM   2225  CG  ASP A1293      13.287 -45.361  72.597  1.00 80.68           C  
ANISOU 2225  CG  ASP A1293    13782   8093   8781   2055   -512    415       C  
ATOM   2226  OD1 ASP A1293      13.114 -46.442  73.150  1.00 83.34           O  
ANISOU 2226  OD1 ASP A1293    14372   8267   9026   2085   -569    448       O  
ATOM   2227  OD2 ASP A1293      14.338 -44.999  72.078  1.00 81.89           O  
ANISOU 2227  OD2 ASP A1293    13864   8349   8901   2312   -377    430       O  
ATOM   2228  N   PRO A1294      10.354 -47.352  73.199  1.00 68.34           N  
ANISOU 2228  N   PRO A1294    12859   5990   7118   1417   -945    404       N  
ATOM   2229  CA  PRO A1294      10.027 -48.354  74.204  1.00 70.06           C  
ANISOU 2229  CA  PRO A1294    13239   6091   7288   1327  -1043    461       C  
ATOM   2230  C   PRO A1294      11.110 -48.450  75.278  1.00 69.49           C  
ANISOU 2230  C   PRO A1294    12982   6178   7245   1526   -933    513       C  
ATOM   2231  O   PRO A1294      10.781 -48.741  76.373  1.00 66.67           O  
ANISOU 2231  O   PRO A1294    12542   5855   6933   1379   -997    561       O  
ATOM   2232  CB  PRO A1294       9.873 -49.641  73.405  1.00 62.90           C  
ANISOU 2232  CB  PRO A1294    12902   4829   6168   1415  -1128    452       C  
ATOM   2233  CG  PRO A1294       9.578 -49.142  72.035  1.00 67.35           C  
ANISOU 2233  CG  PRO A1294    13575   5318   6696   1399  -1136    389       C  
ATOM   2234  CD  PRO A1294      10.473 -47.939  71.886  1.00 66.07           C  
ANISOU 2234  CD  PRO A1294    12980   5454   6670   1532   -969    362       C  
ATOM   2235  N   GLU A1295      12.371 -48.262  74.906  1.00 71.93           N  
ANISOU 2235  N   GLU A1295    13212   6595   7523   1855   -770    520       N  
ATOM   2236  CA  GLU A1295      13.382 -48.336  75.955  1.00 77.26           C  
ANISOU 2236  CA  GLU A1295    13681   7446   8226   2037   -669    590       C  
ATOM   2237  C   GLU A1295      13.185 -47.232  76.983  1.00 70.34           C  
ANISOU 2237  C   GLU A1295    12328   6858   7540   1836   -660    600       C  
ATOM   2238  O   GLU A1295      13.333 -47.464  78.187  1.00 68.50           O  
ANISOU 2238  O   GLU A1295    11971   6712   7344   1801   -670    653       O  
ATOM   2239  CB  GLU A1295      14.782 -48.244  75.352  1.00 86.96           C  
ANISOU 2239  CB  GLU A1295    14892   8767   9382   2423   -496    622       C  
ATOM   2240  CG  GLU A1295      15.059 -49.234  74.244  1.00 98.32           C  
ANISOU 2240  CG  GLU A1295    16812   9930  10615   2672   -477    609       C  
ATOM   2241  CD  GLU A1295      16.452 -49.073  73.671  1.00106.89           C  
ANISOU 2241  CD  GLU A1295    17836  11149  11629   3074   -287    663       C  
ATOM   2242  OE1 GLU A1295      17.353 -48.635  74.420  1.00109.11           O  
ANISOU 2242  OE1 GLU A1295    17768  11702  11986   3193   -185    744       O  
ATOM   2243  OE2 GLU A1295      16.644 -49.373  72.473  1.00110.59           O  
ANISOU 2243  OE2 GLU A1295    18601  11459  11959   3267   -243    634       O  
ATOM   2244  N   LEU A1296      12.839 -46.025  76.527  1.00 65.56           N  
ANISOU 2244  N   LEU A1296    11472   6393   7046   1705   -643    549       N  
ATOM   2245  CA  LEU A1296      12.598 -44.932  77.461  1.00 61.96           C  
ANISOU 2245  CA  LEU A1296    10604   6186   6752   1518   -638    551       C  
ATOM   2246  C   LEU A1296      11.325 -45.165  78.266  1.00 60.43           C  
ANISOU 2246  C   LEU A1296    10418   5936   6606   1216   -771    556       C  
ATOM   2247  O   LEU A1296      11.274 -44.842  79.459  1.00 58.06           O  
ANISOU 2247  O   LEU A1296     9880   5792   6387   1119   -771    588       O  
ATOM   2248  CB  LEU A1296      12.546 -43.604  76.707  1.00 59.11           C  
ANISOU 2248  CB  LEU A1296    10011   5966   6482   1470   -586    498       C  
ATOM   2249  CG  LEU A1296      13.844 -43.278  75.959  1.00 59.43           C  
ANISOU 2249  CG  LEU A1296     9994   6104   6482   1760   -449    515       C  
ATOM   2250  CD1 LEU A1296      13.724 -41.983  75.184  1.00 60.57           C  
ANISOU 2250  CD1 LEU A1296     9929   6372   6713   1691   -411    463       C  
ATOM   2251  CD2 LEU A1296      15.022 -43.212  76.916  1.00 59.14           C  
ANISOU 2251  CD2 LEU A1296     9738   6269   6462   1921   -362    600       C  
ATOM   2252  N   GLU A1297      10.299 -45.760  77.647  1.00 61.23           N  
ANISOU 2252  N   GLU A1297    10798   5819   6648   1062   -890    537       N  
ATOM   2253  CA  GLU A1297       9.101 -46.106  78.405  1.00 61.47           C  
ANISOU 2253  CA  GLU A1297    10843   5804   6708    777  -1023    572       C  
ATOM   2254  C   GLU A1297       9.416 -47.132  79.484  1.00 63.31           C  
ANISOU 2254  C   GLU A1297    11187   5984   6885    826  -1050    638       C  
ATOM   2255  O   GLU A1297       8.946 -47.012  80.622  1.00 61.08           O  
ANISOU 2255  O   GLU A1297    10720   5814   6674    665  -1087    680       O  
ATOM   2256  CB  GLU A1297       8.012 -46.642  77.476  1.00 65.35           C  
ANISOU 2256  CB  GLU A1297    11636   6068   7127    596  -1163    564       C  
ATOM   2257  CG  GLU A1297       7.465 -45.631  76.480  1.00 68.04           C  
ANISOU 2257  CG  GLU A1297    11856   6465   7531    495  -1159    511       C  
ATOM   2258  CD  GLU A1297       6.423 -46.236  75.551  1.00 74.45           C  
ANISOU 2258  CD  GLU A1297    12984   7048   8257    308  -1312    518       C  
ATOM   2259  OE1 GLU A1297       5.817 -47.264  75.922  1.00 78.01           O  
ANISOU 2259  OE1 GLU A1297    13670   7339   8632    162  -1446    579       O  
ATOM   2260  OE2 GLU A1297       6.216 -45.688  74.446  1.00 75.64           O  
ANISOU 2260  OE2 GLU A1297    13153   7177   8409    297  -1306    469       O  
ATOM   2261  N   GLY A1298      10.240 -48.131  79.156  1.00 64.84           N  
ANISOU 2261  N   GLY A1298    11682   6011   6944   1068  -1023    651       N  
ATOM   2262  CA  GLY A1298      10.599 -49.127  80.150  1.00 65.28           C  
ANISOU 2262  CA  GLY A1298    11856   6009   6939   1137  -1043    717       C  
ATOM   2263  C   GLY A1298      11.456 -48.545  81.257  1.00 65.99           C  
ANISOU 2263  C   GLY A1298    11586   6366   7120   1240   -934    751       C  
ATOM   2264  O   GLY A1298      11.301 -48.901  82.427  1.00 68.37           O  
ANISOU 2264  O   GLY A1298    11820   6714   7444   1154   -974    805       O  
ATOM   2265  N   TRP A1299      12.353 -47.622  80.905  1.00 65.16           N  
ANISOU 2265  N   TRP A1299    11246   6447   7066   1410   -805    729       N  
ATOM   2266  CA  TRP A1299      13.153 -46.943  81.918  1.00 65.26           C  
ANISOU 2266  CA  TRP A1299    10904   6726   7164   1471   -718    769       C  
ATOM   2267  C   TRP A1299      12.268 -46.130  82.858  1.00 63.62           C  
ANISOU 2267  C   TRP A1299    10420   6669   7084   1185   -772    758       C  
ATOM   2268  O   TRP A1299      12.433 -46.181  84.086  1.00 64.59           O  
ANISOU 2268  O   TRP A1299    10398   6906   7239   1146   -775    806       O  
ATOM   2269  CB  TRP A1299      14.183 -46.048  81.225  1.00 64.07           C  
ANISOU 2269  CB  TRP A1299    10564   6742   7040   1667   -590    759       C  
ATOM   2270  CG  TRP A1299      15.209 -45.443  82.124  1.00 63.38           C  
ANISOU 2270  CG  TRP A1299    10152   6920   7012   1757   -507    822       C  
ATOM   2271  CD1 TRP A1299      15.400 -45.699  83.453  1.00 61.00           C  
ANISOU 2271  CD1 TRP A1299     9737   6710   6730   1716   -526    882       C  
ATOM   2272  CD2 TRP A1299      16.198 -44.477  81.755  1.00 61.43           C  
ANISOU 2272  CD2 TRP A1299     9652   6884   6804   1888   -403    843       C  
ATOM   2273  NE1 TRP A1299      16.446 -44.947  83.932  1.00 60.54           N  
ANISOU 2273  NE1 TRP A1299     9380   6905   6719   1807   -447    938       N  
ATOM   2274  CE2 TRP A1299      16.953 -44.188  82.910  1.00 60.40           C  
ANISOU 2274  CE2 TRP A1299     9268   6968   6714   1907   -374    921       C  
ATOM   2275  CE3 TRP A1299      16.520 -43.828  80.559  1.00 63.17           C  
ANISOU 2275  CE3 TRP A1299     9838   7138   7025   1982   -338    812       C  
ATOM   2276  CZ2 TRP A1299      18.008 -43.278  82.903  1.00 60.15           C  
ANISOU 2276  CZ2 TRP A1299     8951   7182   6721   1999   -294    978       C  
ATOM   2277  CZ3 TRP A1299      17.565 -42.923  80.553  1.00 62.12           C  
ANISOU 2277  CZ3 TRP A1299     9415   7253   6935   2082   -250    868       C  
ATOM   2278  CH2 TRP A1299      18.297 -42.659  81.716  1.00 61.85           C  
ANISOU 2278  CH2 TRP A1299     9133   7428   6938   2082   -234    954       C  
ATOM   2279  N   ALA A1300      11.295 -45.405  82.302  1.00 59.54           N  
ANISOU 2279  N   ALA A1300     9842   6151   6631    991   -815    701       N  
ATOM   2280  CA  ALA A1300      10.392 -44.624  83.138  1.00 62.73           C  
ANISOU 2280  CA  ALA A1300    10001   6694   7140    745   -854    698       C  
ATOM   2281  C   ALA A1300       9.522 -45.522  84.013  1.00 61.84           C  
ANISOU 2281  C   ALA A1300    10005   6491   6999    576   -962    755       C  
ATOM   2282  O   ALA A1300       9.266 -45.199  85.177  1.00 62.28           O  
ANISOU 2282  O   ALA A1300     9862   6689   7112    468   -965    787       O  
ATOM   2283  CB  ALA A1300       9.525 -43.716  82.265  1.00 51.11           C  
ANISOU 2283  CB  ALA A1300     8456   5236   5729    599   -871    639       C  
ATOM   2284  N   ARG A1301       9.069 -46.661  83.481  1.00 63.93           N  
ANISOU 2284  N   ARG A1301    10607   6516   7168    547  -1055    775       N  
ATOM   2285  CA  ARG A1301       8.247 -47.565  84.282  1.00 66.34           C  
ANISOU 2285  CA  ARG A1301    11037   6729   7439    370  -1171    847       C  
ATOM   2286  C   ARG A1301       9.059 -48.221  85.392  1.00 66.11           C  
ANISOU 2286  C   ARG A1301    11011   6732   7376    500  -1141    900       C  
ATOM   2287  O   ARG A1301       8.546 -48.444  86.499  1.00 65.02           O  
ANISOU 2287  O   ARG A1301    10791   6653   7261    354  -1192    959       O  
ATOM   2288  CB  ARG A1301       7.600 -48.626  83.388  1.00 72.03           C  
ANISOU 2288  CB  ARG A1301    12151   7168   8049    290  -1297    861       C  
ATOM   2289  CG  ARG A1301       6.483 -48.101  82.490  1.00 75.67           C  
ANISOU 2289  CG  ARG A1301    12606   7603   8544     79  -1369    840       C  
ATOM   2290  CD  ARG A1301       5.287 -47.618  83.306  1.00 76.95           C  
ANISOU 2290  CD  ARG A1301    12521   7920   8795   -198  -1429    904       C  
ATOM   2291  NE  ARG A1301       4.212 -47.108  82.455  1.00 76.86           N  
ANISOU 2291  NE  ARG A1301    12483   7906   8815   -392  -1495    905       N  
ATOM   2292  CZ  ARG A1301       3.100 -46.534  82.908  1.00 76.48           C  
ANISOU 2292  CZ  ARG A1301    12206   8012   8842   -616  -1533    968       C  
ATOM   2293  NH1 ARG A1301       2.902 -46.388  84.211  1.00 73.16           N  
ANISOU 2293  NH1 ARG A1301    11574   7753   8469   -672  -1509   1027       N  
ATOM   2294  NH2 ARG A1301       2.183 -46.102  82.052  1.00 80.68           N  
ANISOU 2294  NH2 ARG A1301    12719   8543   9393   -772  -1590    981       N  
ATOM   2295  N   SER A1302      10.329 -48.540  85.121  1.00 66.67           N  
ANISOU 2295  N   SER A1302    11169   6776   7387    781  -1054    893       N  
ATOM   2296  CA  SER A1302      11.173 -49.087  86.178  1.00 68.94           C  
ANISOU 2296  CA  SER A1302    11428   7121   7645    920  -1016    956       C  
ATOM   2297  C   SER A1302      11.438 -48.047  87.255  1.00 65.54           C  
ANISOU 2297  C   SER A1302    10604   6973   7324    868   -954    964       C  
ATOM   2298  O   SER A1302      11.475 -48.375  88.446  1.00 68.10           O  
ANISOU 2298  O   SER A1302    10860   7363   7653    824   -974   1021       O  
ATOM   2299  CB  SER A1302      12.487 -49.613  85.598  1.00 73.50           C  
ANISOU 2299  CB  SER A1302    12166   7633   8127   1254   -925    967       C  
ATOM   2300  OG  SER A1302      13.375 -48.555  85.288  1.00 76.60           O  
ANISOU 2300  OG  SER A1302    12291   8234   8581   1398   -803    944       O  
ATOM   2301  N   LEU A1303      11.613 -46.782  86.863  1.00 62.38           N  
ANISOU 2301  N   LEU A1303     9960   6736   7007    865   -884    909       N  
ATOM   2302  CA  LEU A1303      11.726 -45.738  87.876  1.00 62.81           C  
ANISOU 2302  CA  LEU A1303     9681   7032   7151    782   -844    911       C  
ATOM   2303  C   LEU A1303      10.425 -45.583  88.656  1.00 61.29           C  
ANISOU 2303  C   LEU A1303     9419   6866   7005    521   -920    922       C  
ATOM   2304  O   LEU A1303      10.449 -45.323  89.864  1.00 60.70           O  
ANISOU 2304  O   LEU A1303     9176   6929   6957    461   -913    954       O  
ATOM   2305  CB  LEU A1303      12.137 -44.414  87.234  1.00 62.20           C  
ANISOU 2305  CB  LEU A1303     9392   7099   7140    820   -767    852       C  
ATOM   2306  CG  LEU A1303      13.566 -44.360  86.687  1.00 62.77           C  
ANISOU 2306  CG  LEU A1303     9441   7230   7178   1078   -676    872       C  
ATOM   2307  CD1 LEU A1303      13.956 -42.934  86.330  1.00 58.82           C  
ANISOU 2307  CD1 LEU A1303     8686   6910   6753   1068   -613    831       C  
ATOM   2308  CD2 LEU A1303      14.551 -44.954  87.686  1.00 64.94           C  
ANISOU 2308  CD2 LEU A1303     9678   7584   7411   1214   -651    961       C  
ATOM   2309  N   GLU A1304       9.280 -45.765  87.990  1.00 62.02           N  
ANISOU 2309  N   GLU A1304     9640   6831   7094    366   -994    907       N  
ATOM   2310  CA  GLU A1304       7.992 -45.630  88.665  1.00 62.69           C  
ANISOU 2310  CA  GLU A1304     9642   6962   7215    124  -1061    945       C  
ATOM   2311  C   GLU A1304       7.771 -46.745  89.679  1.00 66.31           C  
ANISOU 2311  C   GLU A1304    10215   7359   7620     65  -1133   1032       C  
ATOM   2312  O   GLU A1304       7.197 -46.515  90.751  1.00 66.17           O  
ANISOU 2312  O   GLU A1304    10042   7466   7634    -66  -1146   1078       O  
ATOM   2313  CB  GLU A1304       6.863 -45.610  87.633  1.00 62.30           C  
ANISOU 2313  CB  GLU A1304     9700   6804   7168    -30  -1133    935       C  
ATOM   2314  CG  GLU A1304       5.460 -45.480  88.219  1.00 63.14           C  
ANISOU 2314  CG  GLU A1304     9706   6978   7306   -278  -1202   1003       C  
ATOM   2315  CD  GLU A1304       4.375 -45.631  87.161  1.00 67.19           C  
ANISOU 2315  CD  GLU A1304    10343   7378   7807   -440  -1293   1022       C  
ATOM   2316  OE1 GLU A1304       4.615 -46.347  86.166  1.00 69.24           O  
ANISOU 2316  OE1 GLU A1304    10873   7436   8001   -388  -1345   1000       O  
ATOM   2317  OE2 GLU A1304       3.287 -45.035  87.316  1.00 67.38           O  
ANISOU 2317  OE2 GLU A1304    10203   7518   7879   -612  -1312   1066       O  
ATOM   2318  N   GLU A1305       8.221 -47.961  89.365  1.00 68.53           N  
ANISOU 2318  N   GLU A1305    10781   7447   7812    169  -1177   1059       N  
ATOM   2319  CA  GLU A1305       8.057 -49.052  90.321  1.00 72.25           C  
ANISOU 2319  CA  GLU A1305    11379   7846   8225    117  -1249   1145       C  
ATOM   2320  C   GLU A1305       9.110 -49.012  91.422  1.00 69.47           C  
ANISOU 2320  C   GLU A1305    10883   7633   7879    266  -1174   1167       C  
ATOM   2321  O   GLU A1305       8.823 -49.398  92.561  1.00 67.41           O  
ANISOU 2321  O   GLU A1305    10580   7421   7613    175  -1211   1234       O  
ATOM   2322  CB  GLU A1305       8.087 -50.407  89.608  1.00 82.45           C  
ANISOU 2322  CB  GLU A1305    13071   8854   9402    166  -1335   1170       C  
ATOM   2323  CG  GLU A1305       9.369 -50.717  88.855  1.00 90.32           C  
ANISOU 2323  CG  GLU A1305    14229   9755  10333    466  -1256   1127       C  
ATOM   2324  CD  GLU A1305       9.398 -52.135  88.310  1.00 96.94           C  
ANISOU 2324  CD  GLU A1305    15508  10293  11032    533  -1341   1157       C  
ATOM   2325  OE1 GLU A1305       8.943 -53.055  89.027  1.00 98.92           O  
ANISOU 2325  OE1 GLU A1305    15909  10444  11232    418  -1439   1231       O  
ATOM   2326  OE2 GLU A1305       9.871 -52.329  87.166  1.00 98.30           O  
ANISOU 2326  OE2 GLU A1305    15892  10322  11135    703  -1310   1109       O  
ATOM   2327  N   LYS A1306      10.325 -48.552  91.107  1.00 68.85           N  
ANISOU 2327  N   LYS A1306    10721   7630   7807    486  -1072   1126       N  
ATOM   2328  CA  LYS A1306      11.378 -48.462  92.114  1.00 67.97           C  
ANISOU 2328  CA  LYS A1306    10455   7672   7699    617  -1009   1164       C  
ATOM   2329  C   LYS A1306      11.094 -47.387  93.158  1.00 65.36           C  
ANISOU 2329  C   LYS A1306     9819   7568   7447    480   -985   1158       C  
ATOM   2330  O   LYS A1306      11.541 -47.510  94.303  1.00 67.59           O  
ANISOU 2330  O   LYS A1306    10005   7956   7721    499   -976   1209       O  
ATOM   2331  CB  LYS A1306      12.722 -48.195  91.432  1.00 71.85           C  
ANISOU 2331  CB  LYS A1306    10916   8211   8175    874   -912   1146       C  
ATOM   2332  CG  LYS A1306      13.928 -48.246  92.358  1.00 77.50           C  
ANISOU 2332  CG  LYS A1306    11491   9081   8876   1028   -856   1214       C  
ATOM   2333  CD  LYS A1306      14.173 -49.661  92.864  1.00 84.58           C  
ANISOU 2333  CD  LYS A1306    12615   9841   9682   1125   -894   1294       C  
ATOM   2334  CE  LYS A1306      15.432 -49.745  93.713  1.00 88.31           C  
ANISOU 2334  CE  LYS A1306    12943  10476  10135   1297   -835   1377       C  
ATOM   2335  NZ  LYS A1306      15.718 -51.145  94.134  1.00 92.00           N  
ANISOU 2335  NZ  LYS A1306    13649  10801  10507   1422   -864   1459       N  
ATOM   2336  N   HIS A1307      10.358 -46.335  92.800  1.00 63.80           N  
ANISOU 2336  N   HIS A1307     9482   7445   7315    349   -974   1099       N  
ATOM   2337  CA  HIS A1307      10.209 -45.166  93.660  1.00 59.97           C  
ANISOU 2337  CA  HIS A1307     8732   7167   6888    259   -934   1080       C  
ATOM   2338  C   HIS A1307       8.739 -44.803  93.808  1.00 59.98           C  
ANISOU 2338  C   HIS A1307     8685   7183   6920     49   -973   1081       C  
ATOM   2339  O   HIS A1307       8.024 -44.675  92.809  1.00 65.44           O  
ANISOU 2339  O   HIS A1307     9441   7793   7629    -16   -995   1052       O  
ATOM   2340  CB  HIS A1307      10.980 -43.965  93.095  1.00 57.32           C  
ANISOU 2340  CB  HIS A1307     8236   6947   6596    349   -857   1013       C  
ATOM   2341  CG  HIS A1307      12.442 -44.219  92.894  1.00 56.95           C  
ANISOU 2341  CG  HIS A1307     8194   6926   6519    558   -811   1038       C  
ATOM   2342  ND1 HIS A1307      13.309 -44.454  93.941  1.00 56.23           N  
ANISOU 2342  ND1 HIS A1307     8025   6940   6400    628   -801   1103       N  
ATOM   2343  CD2 HIS A1307      13.192 -44.267  91.767  1.00 56.01           C  
ANISOU 2343  CD2 HIS A1307     8137   6759   6385    721   -769   1022       C  
ATOM   2344  CE1 HIS A1307      14.529 -44.638  93.466  1.00 56.23           C  
ANISOU 2344  CE1 HIS A1307     8026   6967   6373    825   -755   1137       C  
ATOM   2345  NE2 HIS A1307      14.485 -44.530  92.150  1.00 57.89           N  
ANISOU 2345  NE2 HIS A1307     8321   7086   6588    892   -729   1089       N  
ATOM   2346  N   GLY A1308       8.306 -44.581  95.048  1.00 55.92           N  
ANISOU 2346  N   GLY A1308     8049   6790   6409    -48   -974   1121       N  
ATOM   2347  CA  GLY A1308       6.921 -44.227  95.292  1.00 57.52           C  
ANISOU 2347  CA  GLY A1308     8183   7041   6631   -224   -996   1148       C  
ATOM   2348  C   GLY A1308       6.567 -42.782  95.006  1.00 59.55           C  
ANISOU 2348  C   GLY A1308     8268   7419   6939   -251   -930   1079       C  
ATOM   2349  O   GLY A1308       5.381 -42.439  95.001  1.00 63.22           O  
ANISOU 2349  O   GLY A1308     8675   7927   7419   -375   -936   1108       O  
ATOM   2350  N   ASN A1309       7.563 -41.929  94.769  1.00 55.04           N  
ANISOU 2350  N   ASN A1309     7614   6908   6389   -139   -868   1003       N  
ATOM   2351  CA  ASN A1309       7.338 -40.525  94.455  1.00 55.13           C  
ANISOU 2351  CA  ASN A1309     7489   7016   6440   -156   -809    932       C  
ATOM   2352  C   ASN A1309       7.428 -40.233  92.960  1.00 56.74           C  
ANISOU 2352  C   ASN A1309     7740   7138   6681   -115   -800    871       C  
ATOM   2353  O   ASN A1309       7.541 -39.064  92.572  1.00 58.13           O  
ANISOU 2353  O   ASN A1309     7815   7383   6890   -100   -749    805       O  
ATOM   2354  CB  ASN A1309       8.325 -39.650  95.231  1.00 51.49           C  
ANISOU 2354  CB  ASN A1309     6909   6684   5970    -93   -761    896       C  
ATOM   2355  CG  ASN A1309       9.765 -39.938  94.864  1.00 52.10           C  
ANISOU 2355  CG  ASN A1309     7010   6742   6042     41   -758    889       C  
ATOM   2356  OD1 ASN A1309      10.080 -41.006  94.337  1.00 53.79           O  
ANISOU 2356  OD1 ASN A1309     7352   6844   6243    112   -786    921       O  
ATOM   2357  ND2 ASN A1309      10.649 -38.986  95.141  1.00 49.33           N  
ANISOU 2357  ND2 ASN A1309     6547   6504   5693     78   -727    858       N  
ATOM   2358  N   VAL A1310       7.390 -41.263  92.117  1.00 54.85           N  
ANISOU 2358  N   VAL A1310     7670   6744   6427    -96   -851    892       N  
ATOM   2359  CA  VAL A1310       7.454 -41.120  90.667  1.00 55.67           C  
ANISOU 2359  CA  VAL A1310     7850   6753   6551    -53   -848    839       C  
ATOM   2360  C   VAL A1310       6.231 -41.793  90.056  1.00 58.03           C  
ANISOU 2360  C   VAL A1310     8280   6929   6838   -184   -924    881       C  
ATOM   2361  O   VAL A1310       5.904 -42.934  90.405  1.00 62.32           O  
ANISOU 2361  O   VAL A1310     8963   7380   7337   -239   -998    954       O  
ATOM   2362  CB  VAL A1310       8.751 -41.722  90.096  1.00 55.58           C  
ANISOU 2362  CB  VAL A1310     7952   6659   6507    125   -834    826       C  
ATOM   2363  CG1 VAL A1310       8.694 -41.771  88.569  1.00 55.61           C  
ANISOU 2363  CG1 VAL A1310     8079   6538   6512    170   -838    781       C  
ATOM   2364  CG2 VAL A1310       9.957 -40.920  90.567  1.00 53.05           C  
ANISOU 2364  CG2 VAL A1310     7468   6487   6200    233   -767    804       C  
ATOM   2365  N   LYS A1311       5.565 -41.090  89.142  1.00 53.07           N  
ANISOU 2365  N   LYS A1311     7613   6303   6248   -243   -917    846       N  
ATOM   2366  CA  LYS A1311       4.381 -41.589  88.460  1.00 53.69           C  
ANISOU 2366  CA  LYS A1311     7797   6286   6318   -387   -998    897       C  
ATOM   2367  C   LYS A1311       4.548 -41.360  86.965  1.00 54.12           C  
ANISOU 2367  C   LYS A1311     7943   6238   6382   -339   -998    830       C  
ATOM   2368  O   LYS A1311       5.058 -40.319  86.541  1.00 49.45           O  
ANISOU 2368  O   LYS A1311     7236   5720   5832   -252   -919    752       O  
ATOM   2369  CB  LYS A1311       3.115 -40.884  88.973  1.00 54.84           C  
ANISOU 2369  CB  LYS A1311     7766   6576   6496   -533   -990    953       C  
ATOM   2370  CG  LYS A1311       1.890 -41.020  88.084  1.00 59.39           C  
ANISOU 2370  CG  LYS A1311     8386   7104   7077   -686  -1062   1011       C  
ATOM   2371  CD  LYS A1311       1.267 -42.399  88.198  1.00 62.54           C  
ANISOU 2371  CD  LYS A1311     8957   7385   7419   -827  -1191   1125       C  
ATOM   2372  CE  LYS A1311      -0.041 -42.478  87.417  1.00 63.49           C  
ANISOU 2372  CE  LYS A1311     9093   7489   7539  -1016  -1278   1213       C  
ATOM   2373  NZ  LYS A1311      -0.670 -43.831  87.487  1.00 64.07           N  
ANISOU 2373  NZ  LYS A1311     9356   7440   7548  -1188  -1428   1339       N  
ATOM   2374  N   VAL A1312       4.117 -42.336  86.169  1.00 56.94           N  
ANISOU 2374  N   VAL A1312     8524   6420   6692   -404  -1093    865       N  
ATOM   2375  CA  VAL A1312       4.241 -42.279  84.720  1.00 55.16           C  
ANISOU 2375  CA  VAL A1312     8431   6072   6456   -361  -1105    807       C  
ATOM   2376  C   VAL A1312       2.865 -42.492  84.107  1.00 57.11           C  
ANISOU 2376  C   VAL A1312     8744   6261   6695   -571  -1208    872       C  
ATOM   2377  O   VAL A1312       2.127 -43.392  84.523  1.00 59.35           O  
ANISOU 2377  O   VAL A1312     9129   6486   6937   -721  -1313    972       O  
ATOM   2378  CB  VAL A1312       5.244 -43.324  84.193  1.00 55.96           C  
ANISOU 2378  CB  VAL A1312     8800   5986   6476   -204  -1122    782       C  
ATOM   2379  CG1 VAL A1312       5.221 -43.378  82.669  1.00 50.46           C  
ANISOU 2379  CG1 VAL A1312     8282   5144   5748   -171  -1146    732       C  
ATOM   2380  CG2 VAL A1312       6.647 -43.015  84.699  1.00 51.82           C  
ANISOU 2380  CG2 VAL A1312     8173   5554   5962     11  -1014    739       C  
ATOM   2381  N   ILE A1313       2.526 -41.665  83.122  1.00 58.80           N  
ANISOU 2381  N   ILE A1313     8894   6498   6947   -590  -1187    827       N  
ATOM   2382  CA  ILE A1313       1.259 -41.737  82.403  1.00 59.31           C  
ANISOU 2382  CA  ILE A1313     8999   6527   7008   -787  -1283    895       C  
ATOM   2383  C   ILE A1313       1.588 -41.824  80.919  1.00 56.99           C  
ANISOU 2383  C   ILE A1313     8899   6074   6682   -728  -1306    823       C  
ATOM   2384  O   ILE A1313       2.095 -40.858  80.337  1.00 55.24           O  
ANISOU 2384  O   ILE A1313     8571   5912   6507   -608  -1211    732       O  
ATOM   2385  CB  ILE A1313       0.366 -40.522  82.686  1.00 58.84           C  
ANISOU 2385  CB  ILE A1313     8649   6682   7025   -871  -1227    928       C  
ATOM   2386  CG1 ILE A1313       0.050 -40.421  84.176  1.00 55.07           C  
ANISOU 2386  CG1 ILE A1313     7996   6364   6564   -907  -1193   1001       C  
ATOM   2387  CG2 ILE A1313      -0.910 -40.580  81.849  1.00 61.22           C  
ANISOU 2387  CG2 ILE A1313     8975   6965   7321  -1068  -1328   1017       C  
ATOM   2388  CD1 ILE A1313      -0.480 -39.060  84.573  1.00 55.33           C  
ANISOU 2388  CD1 ILE A1313     7754   6610   6659   -900  -1093   1003       C  
ATOM   2389  N   THR A1314       1.312 -42.977  80.307  1.00 60.72           N  
ANISOU 2389  N   THR A1314     9670   6336   7063   -812  -1435    864       N  
ATOM   2390  CA  THR A1314       1.546 -43.165  78.879  1.00 59.26           C  
ANISOU 2390  CA  THR A1314     9716   5977   6824   -763  -1468    802       C  
ATOM   2391  C   THR A1314       0.288 -43.023  78.029  1.00 60.08           C  
ANISOU 2391  C   THR A1314     9843   6058   6925   -990  -1580    866       C  
ATOM   2392  O   THR A1314       0.399 -42.900  76.806  1.00 61.16           O  
ANISOU 2392  O   THR A1314    10120   6087   7031   -956  -1594    808       O  
ATOM   2393  CB  THR A1314       2.178 -44.539  78.617  1.00 61.29           C  
ANISOU 2393  CB  THR A1314    10354   5980   6955   -679  -1538    794       C  
ATOM   2394  OG1 THR A1314       1.403 -45.555  79.265  1.00 65.84           O  
ANISOU 2394  OG1 THR A1314    11060   6478   7476   -877  -1678    910       O  
ATOM   2395  CG2 THR A1314       3.610 -44.575  79.142  1.00 59.99           C  
ANISOU 2395  CG2 THR A1314    10166   5840   6786   -402  -1407    724       C  
ATOM   2396  N   GLU A1315      -0.895 -43.041  78.634  1.00 62.12           N  
ANISOU 2396  N   GLU A1315     9964   6429   7211  -1216  -1658    996       N  
ATOM   2397  CA  GLU A1315      -2.131 -42.849  77.888  1.00 66.08           C  
ANISOU 2397  CA  GLU A1315    10442   6951   7714  -1441  -1764   1088       C  
ATOM   2398  C   GLU A1315      -2.301 -41.383  77.509  1.00 63.84           C  
ANISOU 2398  C   GLU A1315     9870   6855   7529  -1380  -1644   1038       C  
ATOM   2399  O   GLU A1315      -1.825 -40.479  78.203  1.00 61.76           O  
ANISOU 2399  O   GLU A1315     9367   6756   7342  -1234  -1498    978       O  
ATOM   2400  CB  GLU A1315      -3.332 -43.318  78.711  1.00 73.82           C  
ANISOU 2400  CB  GLU A1315    11333   8028   8689  -1694  -1877   1273       C  
ATOM   2401  CG  GLU A1315      -3.435 -42.659  80.083  1.00 80.15           C  
ANISOU 2401  CG  GLU A1315    11804   9079   9571  -1644  -1758   1311       C  
ATOM   2402  CD  GLU A1315      -4.519 -43.272  80.954  1.00 88.54           C  
ANISOU 2402  CD  GLU A1315    12796  10233  10612  -1873  -1866   1507       C  
ATOM   2403  OE1 GLU A1315      -5.299 -44.100  80.438  1.00 92.63           O  
ANISOU 2403  OE1 GLU A1315    13491  10643  11062  -2104  -2044   1629       O  
ATOM   2404  OE2 GLU A1315      -4.587 -42.929  82.157  1.00 90.74           O  
ANISOU 2404  OE2 GLU A1315    12851  10693  10933  -1830  -1778   1548       O  
ATOM   2405  N   MET A1316      -2.984 -41.150  76.391  1.00 67.35           N  
ANISOU 2405  N   MET A1316    10358   7266   7966  -1498  -1716   1064       N  
ATOM   2406  CA  MET A1316      -3.256 -39.780  75.984  1.00 70.76           C  
ANISOU 2406  CA  MET A1316    10529   7870   8486  -1454  -1614   1032       C  
ATOM   2407  C   MET A1316      -4.210 -39.125  76.975  1.00 67.29           C  
ANISOU 2407  C   MET A1316     9768   7686   8115  -1546  -1573   1154       C  
ATOM   2408  O   MET A1316      -5.123 -39.766  77.503  1.00 70.61           O  
ANISOU 2408  O   MET A1316    10173   8151   8506  -1739  -1679   1313       O  
ATOM   2409  CB  MET A1316      -3.844 -39.728  74.573  1.00 77.83           C  
ANISOU 2409  CB  MET A1316    11544   8677   9351  -1573  -1710   1050       C  
ATOM   2410  CG  MET A1316      -3.747 -38.339  73.954  1.00 82.14           C  
ANISOU 2410  CG  MET A1316    11883   9348   9978  -1462  -1585    969       C  
ATOM   2411  SD  MET A1316      -4.718 -38.102  72.457  1.00 88.33           S  
ANISOU 2411  SD  MET A1316    12725  10095  10742  -1636  -1697   1029       S  
ATOM   2412  CE  MET A1316      -6.386 -38.236  73.100  1.00 90.31           C  
ANISOU 2412  CE  MET A1316    12773  10535  11006  -1921  -1809   1277       C  
ATOM   2413  N   LEU A1317      -3.987 -37.843  77.235  1.00 59.73           N  
ANISOU 2413  N   LEU A1317     8561   6895   7237  -1403  -1418   1086       N  
ATOM   2414  CA  LEU A1317      -4.798 -37.089  78.175  1.00 56.65           C  
ANISOU 2414  CA  LEU A1317     7880   6746   6899  -1435  -1348   1186       C  
ATOM   2415  C   LEU A1317      -5.521 -35.971  77.440  1.00 55.09           C  
ANISOU 2415  C   LEU A1317     7509   6674   6749  -1452  -1304   1212       C  
ATOM   2416  O   LEU A1317      -5.040 -35.462  76.422  1.00 49.59           O  
ANISOU 2416  O   LEU A1317     6872   5901   6070  -1371  -1273   1099       O  
ATOM   2417  CB  LEU A1317      -3.941 -36.504  79.311  1.00 50.87           C  
ANISOU 2417  CB  LEU A1317     7022   6104   6201  -1244  -1200   1092       C  
ATOM   2418  CG  LEU A1317      -3.063 -37.455  80.130  1.00 50.92           C  
ANISOU 2418  CG  LEU A1317     7169   6011   6168  -1187  -1216   1056       C  
ATOM   2419  CD1 LEU A1317      -2.068 -36.653  80.964  1.00 52.02           C  
ANISOU 2419  CD1 LEU A1317     7188   6235   6344   -990  -1070    942       C  
ATOM   2420  CD2 LEU A1317      -3.891 -38.364  81.035  1.00 51.54           C  
ANISOU 2420  CD2 LEU A1317     7241   6134   6208  -1352  -1308   1219       C  
ATOM   2421  N   SER A1318      -6.686 -35.600  77.960  1.00 48.83           N  
ANISOU 2421  N   SER A1318     6497   6082   5972  -1549  -1296   1372       N  
ATOM   2422  CA  SER A1318      -7.398 -34.440  77.445  1.00 49.29           C  
ANISOU 2422  CA  SER A1318     6361   6292   6075  -1531  -1229   1411       C  
ATOM   2423  C   SER A1318      -6.641 -33.165  77.795  1.00 46.95           C  
ANISOU 2423  C   SER A1318     5949   6062   5829  -1296  -1048   1258       C  
ATOM   2424  O   SER A1318      -5.874 -33.115  78.764  1.00 46.34           O  
ANISOU 2424  O   SER A1318     5870   5986   5751  -1177   -972   1179       O  
ATOM   2425  CB  SER A1318      -8.811 -34.378  78.020  1.00 52.98           C  
ANISOU 2425  CB  SER A1318     6611   6983   6536  -1664  -1251   1644       C  
ATOM   2426  OG  SER A1318      -8.773 -34.172  79.422  1.00 57.61           O  
ANISOU 2426  OG  SER A1318     7063   7705   7123  -1568  -1147   1671       O  
ATOM   2427  N   ARG A1319      -6.849 -32.128  76.984  1.00 46.35           N  
ANISOU 2427  N   ARG A1319     5788   6035   5789  -1241   -990   1222       N  
ATOM   2428  CA  ARG A1319      -6.243 -30.843  77.303  1.00 49.15           C  
ANISOU 2428  CA  ARG A1319     6042   6452   6181  -1040   -830   1095       C  
ATOM   2429  C   ARG A1319      -6.809 -30.248  78.589  1.00 46.94           C  
ANISOU 2429  C   ARG A1319     5574   6366   5895   -974   -726   1179       C  
ATOM   2430  O   ARG A1319      -6.127 -29.451  79.237  1.00 46.47           O  
ANISOU 2430  O   ARG A1319     5487   6329   5842   -816   -611   1067       O  
ATOM   2431  CB  ARG A1319      -6.398 -29.867  76.129  1.00 51.89           C  
ANISOU 2431  CB  ARG A1319     6350   6804   6564  -1002   -796   1048       C  
ATOM   2432  CG  ARG A1319      -7.820 -29.479  75.769  1.00 57.52           C  
ANISOU 2432  CG  ARG A1319     6901   7673   7281  -1095   -812   1222       C  
ATOM   2433  CD  ARG A1319      -7.807 -28.436  74.652  1.00 61.65           C  
ANISOU 2433  CD  ARG A1319     7396   8189   7839  -1029   -764   1153       C  
ATOM   2434  NE  ARG A1319      -9.058 -27.686  74.561  1.00 64.58           N  
ANISOU 2434  NE  ARG A1319     7566   8752   8217  -1042   -722   1308       N  
ATOM   2435  CZ  ARG A1319      -9.165 -26.489  73.988  1.00 64.56           C  
ANISOU 2435  CZ  ARG A1319     7488   8798   8242   -935   -632   1264       C  
ATOM   2436  NH1 ARG A1319      -8.092 -25.904  73.463  1.00 60.16           N  
ANISOU 2436  NH1 ARG A1319     7035   8111   7712   -824   -584   1070       N  
ATOM   2437  NH2 ARG A1319     -10.341 -25.870  73.946  1.00 64.57           N  
ANISOU 2437  NH2 ARG A1319     7306   8987   8242   -932   -590   1426       N  
ATOM   2438  N   GLU A1320      -8.032 -30.626  78.983  1.00 47.02           N  
ANISOU 2438  N   GLU A1320     5464   6520   5882  -1093   -768   1382       N  
ATOM   2439  CA  GLU A1320      -8.574 -30.164  80.259  1.00 47.75           C  
ANISOU 2439  CA  GLU A1320     5389   6802   5950  -1013   -662   1475       C  
ATOM   2440  C   GLU A1320      -7.815 -30.765  81.437  1.00 50.37           C  
ANISOU 2440  C   GLU A1320     5796   7086   6256   -974   -652   1418       C  
ATOM   2441  O   GLU A1320      -7.497 -30.065  82.410  1.00 49.87           O  
ANISOU 2441  O   GLU A1320     5679   7093   6177   -825   -531   1361       O  
ATOM   2442  CB  GLU A1320     -10.063 -30.509  80.358  1.00 49.54           C  
ANISOU 2442  CB  GLU A1320     5452   7216   6153  -1155   -715   1737       C  
ATOM   2443  CG  GLU A1320     -10.972 -29.695  79.442  1.00 54.29           C  
ANISOU 2443  CG  GLU A1320     5919   7934   6774  -1161   -691   1832       C  
ATOM   2444  CD  GLU A1320     -10.953 -30.172  77.993  1.00 59.12           C  
ANISOU 2444  CD  GLU A1320     6651   8403   7408  -1318   -835   1814       C  
ATOM   2445  OE1 GLU A1320     -10.545 -31.326  77.740  1.00 60.63           O  
ANISOU 2445  OE1 GLU A1320     7023   8430   7584  -1459   -974   1789       O  
ATOM   2446  OE2 GLU A1320     -11.351 -29.387  77.104  1.00 61.11           O  
ANISOU 2446  OE2 GLU A1320     6834   8701   7684  -1292   -807   1826       O  
ATOM   2447  N   PHE A1321      -7.504 -32.058  81.368  1.00 47.28           N  
ANISOU 2447  N   PHE A1321     5547   6566   5851  -1105   -782   1431       N  
ATOM   2448  CA  PHE A1321      -6.720 -32.657  82.439  1.00 52.02           C  
ANISOU 2448  CA  PHE A1321     6225   7113   6426  -1062   -775   1374       C  
ATOM   2449  C   PHE A1321      -5.309 -32.081  82.476  1.00 45.70           C  
ANISOU 2449  C   PHE A1321     5514   6204   5646   -893   -696   1158       C  
ATOM   2450  O   PHE A1321      -4.743 -31.870  83.557  1.00 45.38           O  
ANISOU 2450  O   PHE A1321     5457   6197   5587   -794   -624   1105       O  
ATOM   2451  CB  PHE A1321      -6.690 -34.176  82.277  1.00 52.86           C  
ANISOU 2451  CB  PHE A1321     6492   7088   6506  -1232   -936   1437       C  
ATOM   2452  CG  PHE A1321      -5.992 -34.881  83.395  1.00 59.23           C  
ANISOU 2452  CG  PHE A1321     7371   7849   7283  -1198   -936   1406       C  
ATOM   2453  CD1 PHE A1321      -6.504 -34.837  84.683  1.00 64.13           C  
ANISOU 2453  CD1 PHE A1321     7854   8633   7878  -1189   -882   1514       C  
ATOM   2454  CD2 PHE A1321      -4.821 -35.582  83.167  1.00 60.32           C  
ANISOU 2454  CD2 PHE A1321     7715   7790   7414  -1160   -984   1277       C  
ATOM   2455  CE1 PHE A1321      -5.861 -35.480  85.726  1.00 63.07           C  
ANISOU 2455  CE1 PHE A1321     7786   8460   7716  -1159   -884   1487       C  
ATOM   2456  CE2 PHE A1321      -4.176 -36.234  84.208  1.00 63.08           C  
ANISOU 2456  CE2 PHE A1321     8126   8107   7736  -1122   -983   1258       C  
ATOM   2457  CZ  PHE A1321      -4.697 -36.181  85.487  1.00 61.81           C  
ANISOU 2457  CZ  PHE A1321     7827   8104   7554  -1130   -938   1360       C  
ATOM   2458  N   VAL A1322      -4.732 -31.797  81.308  1.00 44.96           N  
ANISOU 2458  N   VAL A1322     5508   5990   5583   -863   -710   1043       N  
ATOM   2459  CA  VAL A1322      -3.401 -31.202  81.274  1.00 43.77           C  
ANISOU 2459  CA  VAL A1322     5420   5761   5450   -714   -640    863       C  
ATOM   2460  C   VAL A1322      -3.428 -29.790  81.840  1.00 43.23           C  
ANISOU 2460  C   VAL A1322     5225   5815   5387   -588   -508    818       C  
ATOM   2461  O   VAL A1322      -2.502 -29.373  82.546  1.00 42.67           O  
ANISOU 2461  O   VAL A1322     5175   5735   5305   -486   -448    720       O  
ATOM   2462  CB  VAL A1322      -2.841 -31.237  79.840  1.00 48.84           C  
ANISOU 2462  CB  VAL A1322     6180   6262   6117   -711   -684    771       C  
ATOM   2463  CG1 VAL A1322      -1.554 -30.440  79.747  1.00 42.18           C  
ANISOU 2463  CG1 VAL A1322     5357   5378   5293   -562   -604    613       C  
ATOM   2464  CG2 VAL A1322      -2.597 -32.671  79.433  1.00 49.38           C  
ANISOU 2464  CG2 VAL A1322     6431   6178   6154   -802   -807    793       C  
ATOM   2465  N   ARG A1323      -4.495 -29.036  81.561  1.00 43.56           N  
ANISOU 2465  N   ARG A1323     5146   5970   5433   -591   -463    899       N  
ATOM   2466  CA  ARG A1323      -4.617 -27.711  82.156  1.00 43.32           C  
ANISOU 2466  CA  ARG A1323     5027   6045   5387   -456   -334    866       C  
ATOM   2467  C   ARG A1323      -4.749 -27.812  83.669  1.00 46.82           C  
ANISOU 2467  C   ARG A1323     5431   6584   5777   -411   -281    918       C  
ATOM   2468  O   ARG A1323      -4.197 -26.986  84.405  1.00 44.71           O  
ANISOU 2468  O   ARG A1323     5182   6329   5478   -293   -197    829       O  
ATOM   2469  CB  ARG A1323      -5.815 -26.965  81.564  1.00 43.80           C  
ANISOU 2469  CB  ARG A1323     4967   6220   5455   -452   -291    967       C  
ATOM   2470  CG  ARG A1323      -6.051 -25.597  82.204  1.00 46.53           C  
ANISOU 2470  CG  ARG A1323     5249   6668   5763   -290   -149    946       C  
ATOM   2471  CD  ARG A1323      -7.231 -24.857  81.592  1.00 46.64           C  
ANISOU 2471  CD  ARG A1323     5141   6802   5779   -261    -96   1057       C  
ATOM   2472  NE  ARG A1323      -8.494 -25.537  81.852  1.00 47.79           N  
ANISOU 2472  NE  ARG A1323     5149   7103   5904   -350   -125   1277       N  
ATOM   2473  CZ  ARG A1323      -9.652 -25.188  81.300  1.00 51.17           C  
ANISOU 2473  CZ  ARG A1323     5441   7667   6334   -361   -105   1430       C  
ATOM   2474  NH1 ARG A1323      -9.709 -24.163  80.457  1.00 46.22           N  
ANISOU 2474  NH1 ARG A1323     4807   7026   5728   -279    -52   1373       N  
ATOM   2475  NH2 ARG A1323     -10.752 -25.871  81.584  1.00 48.02           N  
ANISOU 2475  NH2 ARG A1323     4904   7427   5913   -461   -144   1653       N  
ATOM   2476  N   GLU A1324      -5.449 -28.843  84.152  1.00 48.22           N  
ANISOU 2476  N   GLU A1324     5565   6821   5933   -516   -340   1063       N  
ATOM   2477  CA  GLU A1324      -5.536 -29.052  85.594  1.00 46.66           C  
ANISOU 2477  CA  GLU A1324     5336   6712   5682   -478   -296   1116       C  
ATOM   2478  C   GLU A1324      -4.163 -29.358  86.183  1.00 44.66           C  
ANISOU 2478  C   GLU A1324     5206   6343   5422   -438   -311    977       C  
ATOM   2479  O   GLU A1324      -3.808 -28.847  87.251  1.00 44.65           O  
ANISOU 2479  O   GLU A1324     5206   6385   5373   -342   -237    934       O  
ATOM   2480  CB  GLU A1324      -6.516 -30.188  85.899  1.00 50.80           C  
ANISOU 2480  CB  GLU A1324     5793   7319   6189   -622   -375   1312       C  
ATOM   2481  CG  GLU A1324      -7.113 -30.137  87.293  1.00 65.47           C  
ANISOU 2481  CG  GLU A1324     7551   9342   7982   -570   -299   1428       C  
ATOM   2482  CD  GLU A1324      -8.083 -28.986  87.460  1.00 75.63           C  
ANISOU 2482  CD  GLU A1324     8697  10806   9234   -449   -168   1514       C  
ATOM   2483  OE1 GLU A1324      -8.656 -28.545  86.439  1.00 80.70           O  
ANISOU 2483  OE1 GLU A1324     9278  11477   9909   -466   -170   1555       O  
ATOM   2484  OE2 GLU A1324      -8.266 -28.521  88.605  1.00 77.81           O  
ANISOU 2484  OE2 GLU A1324     8933  11190   9440   -326    -61   1542       O  
ATOM   2485  N   LEU A1325      -3.361 -30.150  85.470  1.00 44.18           N  
ANISOU 2485  N   LEU A1325     5256   6134   5398   -501   -405    909       N  
ATOM   2486  CA  LEU A1325      -2.013 -30.460  85.937  1.00 43.63           C  
ANISOU 2486  CA  LEU A1325     5287   5969   5322   -452   -419    795       C  
ATOM   2487  C   LEU A1325      -1.139 -29.215  85.982  1.00 42.80           C  
ANISOU 2487  C   LEU A1325     5192   5854   5216   -333   -340    658       C  
ATOM   2488  O   LEU A1325      -0.426 -28.988  86.965  1.00 42.72           O  
ANISOU 2488  O   LEU A1325     5204   5857   5169   -276   -309    608       O  
ATOM   2489  CB  LEU A1325      -1.371 -31.509  85.030  1.00 52.62           C  
ANISOU 2489  CB  LEU A1325     6550   6956   6489   -513   -521    762       C  
ATOM   2490  CG  LEU A1325      -1.904 -32.936  85.109  1.00 54.67           C  
ANISOU 2490  CG  LEU A1325     6869   7174   6730   -642   -627    880       C  
ATOM   2491  CD1 LEU A1325      -1.404 -33.729  83.923  1.00 55.42           C  
ANISOU 2491  CD1 LEU A1325     7119   7098   6838   -681   -717    836       C  
ATOM   2492  CD2 LEU A1325      -1.450 -33.577  86.390  1.00 56.10           C  
ANISOU 2492  CD2 LEU A1325     7072   7368   6873   -627   -630    898       C  
ATOM   2493  N   TYR A1326      -1.194 -28.390  84.927  1.00 42.29           N  
ANISOU 2493  N   TYR A1326     5117   5766   5186   -307   -316    604       N  
ATOM   2494  CA  TYR A1326      -0.396 -27.170  84.881  1.00 41.63           C  
ANISOU 2494  CA  TYR A1326     5053   5666   5099   -214   -255    484       C  
ATOM   2495  C   TYR A1326      -0.759 -26.228  86.018  1.00 42.03           C  
ANISOU 2495  C   TYR A1326     5075   5810   5084   -138   -166    490       C  
ATOM   2496  O   TYR A1326       0.098 -25.482  86.507  1.00 41.78           O  
ANISOU 2496  O   TYR A1326     5098   5756   5019    -81   -139    399       O  
ATOM   2497  CB  TYR A1326      -0.611 -26.439  83.552  1.00 41.17           C  
ANISOU 2497  CB  TYR A1326     4982   5576   5084   -205   -243    446       C  
ATOM   2498  CG  TYR A1326       0.088 -26.987  82.329  1.00 42.07           C  
ANISOU 2498  CG  TYR A1326     5159   5579   5248   -240   -311    395       C  
ATOM   2499  CD1 TYR A1326       1.329 -27.610  82.409  1.00 42.44           C  
ANISOU 2499  CD1 TYR A1326     5278   5551   5295   -225   -352    339       C  
ATOM   2500  CD2 TYR A1326      -0.493 -26.850  81.081  1.00 40.55           C  
ANISOU 2500  CD2 TYR A1326     4954   5360   5092   -274   -329    411       C  
ATOM   2501  CE1 TYR A1326       1.962 -28.089  81.262  1.00 40.14           C  
ANISOU 2501  CE1 TYR A1326     5055   5164   5034   -226   -398    300       C  
ATOM   2502  CE2 TYR A1326       0.126 -27.317  79.944  1.00 42.93           C  
ANISOU 2502  CE2 TYR A1326     5332   5556   5424   -291   -384    363       C  
ATOM   2503  CZ  TYR A1326       1.349 -27.936  80.034  1.00 44.13           C  
ANISOU 2503  CZ  TYR A1326     5563   5634   5569   -258   -413    307       C  
ATOM   2504  OH  TYR A1326       1.938 -28.396  78.874  1.00 46.00           O  
ANISOU 2504  OH  TYR A1326     5886   5771   5822   -248   -454    269       O  
ATOM   2505  N   GLY A1327      -2.023 -26.228  86.428  1.00 42.81           N  
ANISOU 2505  N   GLY A1327     5096   6017   5153   -133   -123    607       N  
ATOM   2506  CA  GLY A1327      -2.514 -25.378  87.487  1.00 44.04           C  
ANISOU 2506  CA  GLY A1327     5236   6267   5228    -34    -24    631       C  
ATOM   2507  C   GLY A1327      -2.332 -25.917  88.879  1.00 46.60           C  
ANISOU 2507  C   GLY A1327     5580   6634   5491    -29    -21    663       C  
ATOM   2508  O   GLY A1327      -2.713 -25.249  89.844  1.00 48.67           O  
ANISOU 2508  O   GLY A1327     5852   6971   5669     65     65    683       O  
ATOM   2509  N   SER A1328      -1.762 -27.108  89.018  1.00 46.37           N  
ANISOU 2509  N   SER A1328     5570   6554   5492   -117   -109    672       N  
ATOM   2510  CA  SER A1328      -1.620 -27.755  90.315  1.00 47.88           C  
ANISOU 2510  CA  SER A1328     5774   6788   5630   -124   -115    716       C  
ATOM   2511  C   SER A1328      -0.181 -28.075  90.676  1.00 48.74           C  
ANISOU 2511  C   SER A1328     5973   6807   5741   -135   -171    616       C  
ATOM   2512  O   SER A1328       0.213 -27.895  91.831  1.00 47.00           O  
ANISOU 2512  O   SER A1328     5790   6615   5453    -98   -147    598       O  
ATOM   2513  CB  SER A1328      -2.454 -29.038  90.339  1.00 49.61           C  
ANISOU 2513  CB  SER A1328     5926   7054   5869   -226   -173    864       C  
ATOM   2514  OG  SER A1328      -3.771 -28.773  89.889  1.00 54.93           O  
ANISOU 2514  OG  SER A1328     6494   7831   6546   -234   -136    982       O  
ATOM   2515  N   VAL A1329       0.622 -28.528  89.711  1.00 50.22           N  
ANISOU 2515  N   VAL A1329     6194   6893   5995   -177   -241    560       N  
ATOM   2516  CA  VAL A1329       2.009 -28.874  89.991  1.00 47.08           C  
ANISOU 2516  CA  VAL A1329     5858   6432   5597   -175   -289    491       C  
ATOM   2517  C   VAL A1329       2.805 -27.612  90.301  1.00 42.60           C  
ANISOU 2517  C   VAL A1329     5329   5866   4992   -120   -252    394       C  
ATOM   2518  O   VAL A1329       2.388 -26.482  90.015  1.00 42.52           O  
ANISOU 2518  O   VAL A1329     5322   5869   4967    -80   -196    358       O  
ATOM   2519  CB  VAL A1329       2.638 -29.653  88.823  1.00 48.83           C  
ANISOU 2519  CB  VAL A1329     6112   6555   5885   -205   -358    469       C  
ATOM   2520  CG1 VAL A1329       1.778 -30.859  88.460  1.00 42.85           C  
ANISOU 2520  CG1 VAL A1329     5359   5773   5150   -279   -411    567       C  
ATOM   2521  CG2 VAL A1329       2.862 -28.730  87.623  1.00 41.75           C  
ANISOU 2521  CG2 VAL A1329     5213   5620   5030   -178   -338    394       C  
ATOM   2522  N   ASP A1330       3.936 -27.807  90.972  1.00 42.65           N  
ANISOU 2522  N   ASP A1330     5373   5861   4972   -123   -290    363       N  
ATOM   2523  CA  ASP A1330       4.793 -26.674  91.292  1.00 42.61           C  
ANISOU 2523  CA  ASP A1330     5416   5853   4922   -105   -283    285       C  
ATOM   2524  C   ASP A1330       5.647 -26.247  90.099  1.00 42.81           C  
ANISOU 2524  C   ASP A1330     5436   5826   5004   -111   -311    226       C  
ATOM   2525  O   ASP A1330       5.762 -25.048  89.818  1.00 41.89           O  
ANISOU 2525  O   ASP A1330     5351   5697   4867   -101   -290    167       O  
ATOM   2526  CB  ASP A1330       5.662 -27.022  92.499  1.00 43.08           C  
ANISOU 2526  CB  ASP A1330     5507   5939   4923   -122   -322    295       C  
ATOM   2527  CG  ASP A1330       4.832 -27.283  93.749  1.00 43.78           C  
ANISOU 2527  CG  ASP A1330     5608   6085   4940   -109   -286    351       C  
ATOM   2528  OD1 ASP A1330       4.023 -26.405  94.113  1.00 44.15           O  
ANISOU 2528  OD1 ASP A1330     5688   6160   4925    -66   -217    342       O  
ATOM   2529  OD2 ASP A1330       4.964 -28.370  94.351  1.00 44.05           O  
ANISOU 2529  OD2 ASP A1330     5625   6139   4974   -132   -320    410       O  
ATOM   2530  N   PHE A1331       6.222 -27.205  89.371  1.00 41.71           N  
ANISOU 2530  N   PHE A1331     5270   5653   4926   -117   -357    245       N  
ATOM   2531  CA  PHE A1331       7.151 -26.909  88.290  1.00 41.28           C  
ANISOU 2531  CA  PHE A1331     5204   5566   4916   -108   -379    205       C  
ATOM   2532  C   PHE A1331       6.889 -27.840  87.118  1.00 41.95           C  
ANISOU 2532  C   PHE A1331     5281   5592   5064    -91   -391    226       C  
ATOM   2533  O   PHE A1331       6.470 -28.988  87.294  1.00 41.27           O  
ANISOU 2533  O   PHE A1331     5214   5483   4982    -99   -412    280       O  
ATOM   2534  CB  PHE A1331       8.618 -27.061  88.712  1.00 41.57           C  
ANISOU 2534  CB  PHE A1331     5229   5634   4932   -110   -426    215       C  
ATOM   2535  CG  PHE A1331       9.007 -26.201  89.873  1.00 42.04           C  
ANISOU 2535  CG  PHE A1331     5317   5741   4914   -149   -439    199       C  
ATOM   2536  CD1 PHE A1331       9.514 -24.929  89.669  1.00 42.07           C  
ANISOU 2536  CD1 PHE A1331     5343   5747   4893   -182   -450    153       C  
ATOM   2537  CD2 PHE A1331       8.870 -26.668  91.173  1.00 42.56           C  
ANISOU 2537  CD2 PHE A1331     5407   5841   4924   -161   -447    234       C  
ATOM   2538  CE1 PHE A1331       9.871 -24.134  90.736  1.00 42.70           C  
ANISOU 2538  CE1 PHE A1331     5488   5850   4885   -233   -477    139       C  
ATOM   2539  CE2 PHE A1331       9.227 -25.880  92.245  1.00 44.69           C  
ANISOU 2539  CE2 PHE A1331     5731   6143   5109   -200   -466    218       C  
ATOM   2540  CZ  PHE A1331       9.727 -24.610  92.030  1.00 46.32           C  
ANISOU 2540  CZ  PHE A1331     5979   6338   5281   -240   -485    169       C  
ATOM   2541  N   VAL A1332       7.154 -27.328  85.919  1.00 40.55           N  
ANISOU 2541  N   VAL A1332     5096   5384   4929    -75   -384    186       N  
ATOM   2542  CA  VAL A1332       7.058 -28.086  84.679  1.00 40.37           C  
ANISOU 2542  CA  VAL A1332     5093   5292   4952    -53   -399    195       C  
ATOM   2543  C   VAL A1332       8.454 -28.151  84.077  1.00 43.98           C  
ANISOU 2543  C   VAL A1332     5541   5749   5418      3   -413    185       C  
ATOM   2544  O   VAL A1332       9.073 -27.110  83.824  1.00 43.81           O  
ANISOU 2544  O   VAL A1332     5479   5766   5399      1   -402    153       O  
ATOM   2545  CB  VAL A1332       6.056 -27.450  83.701  1.00 41.42           C  
ANISOU 2545  CB  VAL A1332     5220   5399   5120    -72   -372    170       C  
ATOM   2546  CG1 VAL A1332       6.206 -28.048  82.302  1.00 43.58           C  
ANISOU 2546  CG1 VAL A1332     5533   5595   5430    -49   -393    166       C  
ATOM   2547  CG2 VAL A1332       4.637 -27.641  84.215  1.00 41.81           C  
ANISOU 2547  CG2 VAL A1332     5260   5469   5157   -116   -359    219       C  
ATOM   2548  N   ILE A1333       8.954 -29.362  83.863  1.00 45.46           N  
ANISOU 2548  N   ILE A1333     5772   5899   5603     56   -436    225       N  
ATOM   2549  CA  ILE A1333      10.299 -29.558  83.336  1.00 41.01           C  
ANISOU 2549  CA  ILE A1333     5192   5356   5036    140   -436    243       C  
ATOM   2550  C   ILE A1333      10.220 -29.744  81.824  1.00 43.73           C  
ANISOU 2550  C   ILE A1333     5585   5624   5405    194   -422    222       C  
ATOM   2551  O   ILE A1333       9.491 -30.613  81.332  1.00 40.98           O  
ANISOU 2551  O   ILE A1333     5337   5178   5057    197   -439    226       O  
ATOM   2552  CB  ILE A1333      10.981 -30.759  84.012  1.00 41.74           C  
ANISOU 2552  CB  ILE A1333     5314   5453   5093    201   -457    307       C  
ATOM   2553  CG1 ILE A1333      11.080 -30.538  85.527  1.00 41.94           C  
ANISOU 2553  CG1 ILE A1333     5291   5557   5088    141   -474    328       C  
ATOM   2554  CG2 ILE A1333      12.359 -30.979  83.422  1.00 42.22           C  
ANISOU 2554  CG2 ILE A1333     5345   5556   5142    316   -443    347       C  
ATOM   2555  CD1 ILE A1333      11.611 -31.742  86.289  1.00 42.67           C  
ANISOU 2555  CD1 ILE A1333     5413   5655   5145    193   -497    396       C  
ATOM   2556  N   ILE A1334      10.989 -28.944  81.089  1.00 40.68           N  
ANISOU 2556  N   ILE A1334     5140   5285   5034    228   -401    207       N  
ATOM   2557  CA  ILE A1334      10.963 -28.930  79.627  1.00 40.52           C  
ANISOU 2557  CA  ILE A1334     5159   5205   5033    282   -381    183       C  
ATOM   2558  C   ILE A1334      12.399 -29.101  79.145  1.00 42.15           C  
ANISOU 2558  C   ILE A1334     5325   5472   5217    401   -359    232       C  
ATOM   2559  O   ILE A1334      13.059 -28.114  78.786  1.00 40.97           O  
ANISOU 2559  O   ILE A1334     5079   5407   5081    395   -344    235       O  
ATOM   2560  CB  ILE A1334      10.336 -27.634  79.082  1.00 42.46           C  
ANISOU 2560  CB  ILE A1334     5359   5457   5316    208   -366    125       C  
ATOM   2561  CG1 ILE A1334       9.011 -27.332  79.782  1.00 44.55           C  
ANISOU 2561  CG1 ILE A1334     5633   5704   5590    111   -374    102       C  
ATOM   2562  CG2 ILE A1334      10.099 -27.727  77.576  1.00 39.63           C  
ANISOU 2562  CG2 ILE A1334     5058   5025   4976    252   -352    101       C  
ATOM   2563  CD1 ILE A1334       8.428 -25.961  79.432  1.00 44.77           C  
ANISOU 2563  CD1 ILE A1334     5619   5748   5642     57   -350     53       C  
ATOM   2564  N   PRO A1335      12.934 -30.325  79.147  1.00 41.95           N  
ANISOU 2564  N   PRO A1335     5370   5416   5151    516   -355    284       N  
ATOM   2565  CA  PRO A1335      14.366 -30.509  78.875  1.00 43.26           C  
ANISOU 2565  CA  PRO A1335     5475   5677   5286    653   -322    360       C  
ATOM   2566  C   PRO A1335      14.690 -30.706  77.401  1.00 46.15           C  
ANISOU 2566  C   PRO A1335     5901   5998   5635    781   -277    361       C  
ATOM   2567  O   PRO A1335      15.520 -31.556  77.064  1.00 50.50           O  
ANISOU 2567  O   PRO A1335     6500   6555   6132    952   -241    427       O  
ATOM   2568  CB  PRO A1335      14.697 -31.765  79.689  1.00 43.49           C  
ANISOU 2568  CB  PRO A1335     5568   5689   5267    732   -332    421       C  
ATOM   2569  CG  PRO A1335      13.433 -32.573  79.610  1.00 46.91           C  
ANISOU 2569  CG  PRO A1335     6173   5953   5696    686   -363    367       C  
ATOM   2570  CD  PRO A1335      12.274 -31.593  79.506  1.00 42.24           C  
ANISOU 2570  CD  PRO A1335     5547   5341   5160    526   -382    292       C  
ATOM   2571  N   SER A1336      14.065 -29.923  76.522  1.00 42.96           N  
ANISOU 2571  N   SER A1336     5501   5553   5269    717   -273    295       N  
ATOM   2572  CA  SER A1336      14.181 -30.149  75.084  1.00 48.61           C  
ANISOU 2572  CA  SER A1336     6303   6202   5963    828   -236    284       C  
ATOM   2573  C   SER A1336      15.601 -29.918  74.579  1.00 50.80           C  
ANISOU 2573  C   SER A1336     6472   6616   6212    971   -179    368       C  
ATOM   2574  O   SER A1336      16.264 -28.948  74.955  1.00 49.17           O  
ANISOU 2574  O   SER A1336     6088   6561   6032    910   -182    411       O  
ATOM   2575  CB  SER A1336      13.234 -29.223  74.327  1.00 41.54           C  
ANISOU 2575  CB  SER A1336     5408   5257   5120    714   -247    204       C  
ATOM   2576  OG  SER A1336      11.908 -29.319  74.812  1.00 49.55           O  
ANISOU 2576  OG  SER A1336     6484   6183   6160    581   -294    151       O  
ATOM   2577  N   TYR A1337      16.069 -30.818  73.711  1.00 52.91           N  
ANISOU 2577  N   TYR A1337     6859   6831   6415   1162   -130    403       N  
ATOM   2578  CA  TYR A1337      17.257 -30.511  72.922  1.00 46.90           C  
ANISOU 2578  CA  TYR A1337     5996   6200   5622   1313    -61    487       C  
ATOM   2579  C   TYR A1337      16.962 -29.459  71.864  1.00 44.92           C  
ANISOU 2579  C   TYR A1337     5702   5954   5413   1246    -52    436       C  
ATOM   2580  O   TYR A1337      17.857 -28.702  71.473  1.00 48.47           O  
ANISOU 2580  O   TYR A1337     5991   6559   5867   1279    -18    507       O  
ATOM   2581  CB  TYR A1337      17.793 -31.775  72.252  1.00 46.37           C  
ANISOU 2581  CB  TYR A1337     6098   6065   5455   1568      3    539       C  
ATOM   2582  CG  TYR A1337      18.463 -32.770  73.174  1.00 47.44           C  
ANISOU 2582  CG  TYR A1337     6250   6241   5536   1691     16    628       C  
ATOM   2583  CD1 TYR A1337      17.722 -33.716  73.873  1.00 49.09           C  
ANISOU 2583  CD1 TYR A1337     6630   6294   5727   1651    -35    580       C  
ATOM   2584  CD2 TYR A1337      19.845 -32.790  73.309  1.00 53.29           C  
ANISOU 2584  CD2 TYR A1337     6830   7182   6235   1853     80    775       C  
ATOM   2585  CE1 TYR A1337      18.347 -34.645  74.708  1.00 50.66           C  
ANISOU 2585  CE1 TYR A1337     6852   6524   5871   1772    -22    664       C  
ATOM   2586  CE2 TYR A1337      20.475 -33.710  74.134  1.00 50.95           C  
ANISOU 2586  CE2 TYR A1337     6543   6930   5884   1981     96    868       C  
ATOM   2587  CZ  TYR A1337      19.725 -34.632  74.829  1.00 49.61           C  
ANISOU 2587  CZ  TYR A1337     6558   6591   5699   1943     47    806       C  
ATOM   2588  OH  TYR A1337      20.365 -35.540  75.643  1.00 54.41           O  
ANISOU 2588  OH  TYR A1337     7180   7241   6251   2074     63    901       O  
ATOM   2589  N   PHE A1338      15.713 -29.386  71.415  1.00 43.41           N  
ANISOU 2589  N   PHE A1338     5640   5603   5250   1143    -87    325       N  
ATOM   2590  CA  PHE A1338      15.326 -28.598  70.251  1.00 47.03           C  
ANISOU 2590  CA  PHE A1338     6100   6033   5735   1106    -76    273       C  
ATOM   2591  C   PHE A1338      13.893 -28.154  70.478  1.00 45.44           C  
ANISOU 2591  C   PHE A1338     5942   5728   5596    910   -139    173       C  
ATOM   2592  O   PHE A1338      13.005 -28.997  70.643  1.00 47.99           O  
ANISOU 2592  O   PHE A1338     6419   5913   5901    879   -178    135       O  
ATOM   2593  CB  PHE A1338      15.464 -29.430  68.962  1.00 47.73           C  
ANISOU 2593  CB  PHE A1338     6373   6017   5745   1289    -27    273       C  
ATOM   2594  CG  PHE A1338      14.845 -28.797  67.736  1.00 48.08           C  
ANISOU 2594  CG  PHE A1338     6464   5995   5809   1241    -26    206       C  
ATOM   2595  CD1 PHE A1338      13.678 -29.314  67.187  1.00 48.03           C  
ANISOU 2595  CD1 PHE A1338     6665   5798   5788   1185    -73    126       C  
ATOM   2596  CD2 PHE A1338      15.442 -27.707  67.115  1.00 50.02           C  
ANISOU 2596  CD2 PHE A1338     6550   6373   6085   1243     12    236       C  
ATOM   2597  CE1 PHE A1338      13.112 -28.751  66.051  1.00 52.03           C  
ANISOU 2597  CE1 PHE A1338     7212   6249   6308   1138    -77     73       C  
ATOM   2598  CE2 PHE A1338      14.878 -27.132  65.976  1.00 51.88           C  
ANISOU 2598  CE2 PHE A1338     6829   6546   6337   1203     14    177       C  
ATOM   2599  CZ  PHE A1338      13.711 -27.654  65.443  1.00 50.87           C  
ANISOU 2599  CZ  PHE A1338     6904   6230   6194   1154    -29     93       C  
ATOM   2600  N   GLU A1339      13.677 -26.843  70.530  1.00 42.26           N  
ANISOU 2600  N   GLU A1339     5403   5396   5256    779   -152    145       N  
ATOM   2601  CA  GLU A1339      12.361 -26.282  70.838  1.00 40.74           C  
ANISOU 2601  CA  GLU A1339     5225   5136   5118    613   -197     69       C  
ATOM   2602  C   GLU A1339      12.236 -24.939  70.142  1.00 45.19           C  
ANISOU 2602  C   GLU A1339     5702   5742   5725    545   -187     38       C  
ATOM   2603  O   GLU A1339      12.431 -23.880  70.750  1.00 43.69           O  
ANISOU 2603  O   GLU A1339     5396   5637   5566    454   -198     40       O  
ATOM   2604  CB  GLU A1339      12.163 -26.129  72.349  1.00 40.03           C  
ANISOU 2604  CB  GLU A1339     5069   5093   5046    514   -231     75       C  
ATOM   2605  CG  GLU A1339      10.709 -25.986  72.769  1.00 43.06           C  
ANISOU 2605  CG  GLU A1339     5499   5400   5462    388   -266     20       C  
ATOM   2606  CD  GLU A1339       9.906 -27.253  72.519  1.00 48.72           C  
ANISOU 2606  CD  GLU A1339     6372   5987   6151    402   -295     16       C  
ATOM   2607  OE1 GLU A1339       9.018 -27.238  71.637  1.00 50.68           O  
ANISOU 2607  OE1 GLU A1339     6693   6154   6410    362   -311    -14       O  
ATOM   2608  OE2 GLU A1339      10.177 -28.271  73.191  1.00 49.10           O  
ANISOU 2608  OE2 GLU A1339     6479   6015   6163    446   -309     51       O  
ATOM   2609  N   PRO A1340      11.921 -24.942  68.844  1.00 47.29           N  
ANISOU 2609  N   PRO A1340     6041   5940   5986    585   -170     10       N  
ATOM   2610  CA  PRO A1340      11.891 -23.669  68.102  1.00 45.82           C  
ANISOU 2610  CA  PRO A1340     5774   5797   5840    531   -157    -12       C  
ATOM   2611  C   PRO A1340      10.912 -22.638  68.657  1.00 42.20           C  
ANISOU 2611  C   PRO A1340     5268   5331   5435    379   -187    -63       C  
ATOM   2612  O   PRO A1340      11.197 -21.439  68.567  1.00 38.32           O  
ANISOU 2612  O   PRO A1340     4687   4904   4969    325   -183    -67       O  
ATOM   2613  CB  PRO A1340      11.528 -24.104  66.665  1.00 46.16           C  
ANISOU 2613  CB  PRO A1340     5941   5742   5857    602   -141    -38       C  
ATOM   2614  CG  PRO A1340      10.946 -25.481  66.802  1.00 47.83           C  
ANISOU 2614  CG  PRO A1340     6322   5827   6024    634   -170    -47       C  
ATOM   2615  CD  PRO A1340      11.642 -26.102  67.975  1.00 47.01           C  
ANISOU 2615  CD  PRO A1340     6185   5778   5897    681   -167      1       C  
ATOM   2616  N   PHE A1341       9.776 -23.049  69.227  1.00 42.89           N  
ANISOU 2616  N   PHE A1341     5417   5345   5532    315   -217    -92       N  
ATOM   2617  CA  PHE A1341       8.755 -22.066  69.573  1.00 45.33           C  
ANISOU 2617  CA  PHE A1341     5691   5653   5881    206   -227   -129       C  
ATOM   2618  C   PHE A1341       8.314 -22.087  71.037  1.00 52.89           C  
ANISOU 2618  C   PHE A1341     6627   6632   6836    146   -243   -125       C  
ATOM   2619  O   PHE A1341       8.022 -21.027  71.602  1.00 59.95           O  
ANISOU 2619  O   PHE A1341     7476   7560   7742     88   -237   -145       O  
ATOM   2620  CB  PHE A1341       7.566 -22.233  68.628  1.00 43.17           C  
ANISOU 2620  CB  PHE A1341     5488   5294   5622    178   -239   -152       C  
ATOM   2621  CG  PHE A1341       7.955 -22.123  67.184  1.00 45.75           C  
ANISOU 2621  CG  PHE A1341     5845   5595   5943    234   -223   -161       C  
ATOM   2622  CD1 PHE A1341       8.363 -20.902  66.663  1.00 41.86           C  
ANISOU 2622  CD1 PHE A1341     5273   5155   5475    226   -197   -175       C  
ATOM   2623  CD2 PHE A1341       7.956 -23.238  66.354  1.00 47.67           C  
ANISOU 2623  CD2 PHE A1341     6214   5754   6145    298   -235   -154       C  
ATOM   2624  CE1 PHE A1341       8.747 -20.791  65.333  1.00 41.99           C  
ANISOU 2624  CE1 PHE A1341     5312   5159   5482    283   -177   -177       C  
ATOM   2625  CE2 PHE A1341       8.330 -23.131  65.022  1.00 46.97           C  
ANISOU 2625  CE2 PHE A1341     6168   5641   6038    364   -214   -162       C  
ATOM   2626  CZ  PHE A1341       8.728 -21.906  64.513  1.00 46.23           C  
ANISOU 2626  CZ  PHE A1341     5971   5618   5976    358   -181   -172       C  
ATOM   2627  N   GLY A1342       8.262 -23.248  71.679  1.00 53.43           N  
ANISOU 2627  N   GLY A1342     6744   6676   6881    166   -262    -99       N  
ATOM   2628  CA  GLY A1342       8.035 -23.209  73.122  1.00 61.35           C  
ANISOU 2628  CA  GLY A1342     7717   7717   7875    118   -273    -88       C  
ATOM   2629  C   GLY A1342       6.655 -22.771  73.579  1.00 58.44           C  
ANISOU 2629  C   GLY A1342     7345   7338   7521     46   -272    -99       C  
ATOM   2630  O   GLY A1342       6.533 -22.058  74.583  1.00 53.06           O  
ANISOU 2630  O   GLY A1342     6630   6703   6829     15   -259   -107       O  
ATOM   2631  N   LEU A1343       5.610 -23.165  72.847  1.00 56.65           N  
ANISOU 2631  N   LEU A1343     7160   7057   7309     22   -284    -91       N  
ATOM   2632  CA  LEU A1343       4.240 -22.958  73.305  1.00 47.79           C  
ANISOU 2632  CA  LEU A1343     6015   5949   6193    -37   -282    -65       C  
ATOM   2633  C   LEU A1343       3.967 -23.688  74.623  1.00 43.58           C  
ANISOU 2633  C   LEU A1343     5484   5440   5633    -59   -297    -24       C  
ATOM   2634  O   LEU A1343       3.111 -23.260  75.410  1.00 42.35           O  
ANISOU 2634  O   LEU A1343     5286   5335   5471    -85   -274      1       O  
ATOM   2635  CB  LEU A1343       3.274 -23.427  72.204  1.00 48.10           C  
ANISOU 2635  CB  LEU A1343     6095   5934   6246    -77   -314    -38       C  
ATOM   2636  CG  LEU A1343       1.836 -23.853  72.524  1.00 48.00           C  
ANISOU 2636  CG  LEU A1343     6067   5938   6231   -154   -341     36       C  
ATOM   2637  CD1 LEU A1343       0.969 -22.651  72.886  1.00 50.01           C  
ANISOU 2637  CD1 LEU A1343     6228   6276   6499   -155   -286     52       C  
ATOM   2638  CD2 LEU A1343       1.221 -24.631  71.368  1.00 42.99           C  
ANISOU 2638  CD2 LEU A1343     5508   5232   5596   -213   -405     72       C  
ATOM   2639  N   VAL A1344       4.669 -24.795  74.877  1.00 39.35           N  
ANISOU 2639  N   VAL A1344     5001   4873   5077    -36   -328    -10       N  
ATOM   2640  CA  VAL A1344       4.448 -25.539  76.112  1.00 44.47           C  
ANISOU 2640  CA  VAL A1344     5655   5541   5699    -59   -346     33       C  
ATOM   2641  C   VAL A1344       4.880 -24.721  77.323  1.00 44.10           C  
ANISOU 2641  C   VAL A1344     5548   5571   5636    -48   -311     15       C  
ATOM   2642  O   VAL A1344       4.247 -24.790  78.390  1.00 40.53           O  
ANISOU 2642  O   VAL A1344     5077   5160   5162    -75   -304     47       O  
ATOM   2643  CB  VAL A1344       5.175 -26.897  76.046  1.00 49.18           C  
ANISOU 2643  CB  VAL A1344     6341   6075   6270    -23   -386     52       C  
ATOM   2644  CG1 VAL A1344       6.613 -26.703  75.605  1.00 51.33           C  
ANISOU 2644  CG1 VAL A1344     6610   6356   6537     69   -363     20       C  
ATOM   2645  CG2 VAL A1344       5.112 -27.614  77.398  1.00 53.74           C  
ANISOU 2645  CG2 VAL A1344     6921   6678   6819    -42   -404     95       C  
ATOM   2646  N   ALA A1345       5.928 -23.903  77.174  1.00 44.16           N  
ANISOU 2646  N   ALA A1345     5531   5603   5644    -16   -294    -28       N  
ATOM   2647  CA  ALA A1345       6.311 -23.011  78.262  1.00 43.28           C  
ANISOU 2647  CA  ALA A1345     5392   5549   5503    -27   -278    -45       C  
ATOM   2648  C   ALA A1345       5.219 -21.987  78.535  1.00 44.32           C  
ANISOU 2648  C   ALA A1345     5520   5695   5625    -44   -238    -60       C  
ATOM   2649  O   ALA A1345       4.922 -21.689  79.697  1.00 39.07           O  
ANISOU 2649  O   ALA A1345     4865   5064   4916    -48   -221    -53       O  
ATOM   2650  CB  ALA A1345       7.631 -22.307  77.939  1.00 38.22           C  
ANISOU 2650  CB  ALA A1345     4728   4933   4860    -16   -285    -69       C  
ATOM   2651  N   LEU A1346       4.599 -21.453  77.477  1.00 37.54           N  
ANISOU 2651  N   LEU A1346     4653   4813   4798    -42   -219    -74       N  
ATOM   2652  CA  LEU A1346       3.528 -20.481  77.662  1.00 39.48           C  
ANISOU 2652  CA  LEU A1346     4893   5079   5029    -32   -170    -73       C  
ATOM   2653  C   LEU A1346       2.322 -21.113  78.335  1.00 40.33           C  
ANISOU 2653  C   LEU A1346     4976   5227   5121    -37   -155     -3       C  
ATOM   2654  O   LEU A1346       1.667 -20.475  79.168  1.00 39.21           O  
ANISOU 2654  O   LEU A1346     4834   5129   4934     -5   -105     13       O  
ATOM   2655  CB  LEU A1346       3.117 -19.880  76.316  1.00 37.30           C  
ANISOU 2655  CB  LEU A1346     4604   4777   4793    -27   -156    -89       C  
ATOM   2656  CG  LEU A1346       4.132 -18.965  75.624  1.00 42.22           C  
ANISOU 2656  CG  LEU A1346     5243   5372   5425    -23   -161   -149       C  
ATOM   2657  CD1 LEU A1346       3.617 -18.508  74.252  1.00 41.73           C  
ANISOU 2657  CD1 LEU A1346     5167   5285   5405    -18   -148   -157       C  
ATOM   2658  CD2 LEU A1346       4.449 -17.770  76.510  1.00 37.31           C  
ANISOU 2658  CD2 LEU A1346     4669   4758   4749    -20   -142   -185       C  
ATOM   2659  N   GLU A1347       2.021 -22.367  77.989  1.00 38.11           N  
ANISOU 2659  N   GLU A1347     4684   4931   4866    -76   -199     49       N  
ATOM   2660  CA  GLU A1347       0.902 -23.056  78.622  1.00 38.66           C  
ANISOU 2660  CA  GLU A1347     4720   5049   4918   -105   -200    139       C  
ATOM   2661  C   GLU A1347       1.166 -23.264  80.104  1.00 43.43           C  
ANISOU 2661  C   GLU A1347     5334   5695   5474    -90   -187    149       C  
ATOM   2662  O   GLU A1347       0.278 -23.046  80.938  1.00 43.10           O  
ANISOU 2662  O   GLU A1347     5258   5725   5395    -72   -144    206       O  
ATOM   2663  CB  GLU A1347       0.657 -24.407  77.942  1.00 38.82           C  
ANISOU 2663  CB  GLU A1347     4764   5021   4964   -173   -274    191       C  
ATOM   2664  CG  GLU A1347       0.188 -24.337  76.502  1.00 38.67           C  
ANISOU 2664  CG  GLU A1347     4749   4963   4981   -204   -298    198       C  
ATOM   2665  CD  GLU A1347       0.195 -25.702  75.812  1.00 47.16           C  
ANISOU 2665  CD  GLU A1347     5906   5954   6059   -270   -386    232       C  
ATOM   2666  OE1 GLU A1347       0.696 -26.678  76.406  1.00 45.25           O  
ANISOU 2666  OE1 GLU A1347     5722   5676   5793   -277   -422    241       O  
ATOM   2667  OE2 GLU A1347      -0.302 -25.797  74.673  1.00 43.84           O  
ANISOU 2667  OE2 GLU A1347     5508   5494   5654   -315   -421    251       O  
ATOM   2668  N   ALA A1348       2.389 -23.673  80.455  1.00 43.31           N  
ANISOU 2668  N   ALA A1348     5360   5645   5452    -88   -221    106       N  
ATOM   2669  CA  ALA A1348       2.702 -23.875  81.867  1.00 42.69           C  
ANISOU 2669  CA  ALA A1348     5293   5605   5323    -80   -216    117       C  
ATOM   2670  C   ALA A1348       2.680 -22.555  82.628  1.00 39.41           C  
ANISOU 2670  C   ALA A1348     4898   5223   4853    -38   -160     77       C  
ATOM   2671  O   ALA A1348       2.098 -22.466  83.714  1.00 39.95           O  
ANISOU 2671  O   ALA A1348     4971   5343   4866    -16   -124    113       O  
ATOM   2672  CB  ALA A1348       4.060 -24.560  82.015  1.00 39.58           C  
ANISOU 2672  CB  ALA A1348     4929   5179   4931    -82   -266     92       C  
ATOM   2673  N   MET A1349       3.300 -21.512  82.064  1.00 39.10           N  
ANISOU 2673  N   MET A1349     4889   5151   4818    -25   -154      8       N  
ATOM   2674  CA  MET A1349       3.386 -20.232  82.762  1.00 42.94           C  
ANISOU 2674  CA  MET A1349     5441   5640   5235      6   -116    -36       C  
ATOM   2675  C   MET A1349       2.026 -19.569  82.918  1.00 41.65           C  
ANISOU 2675  C   MET A1349     5281   5508   5035     72    -37     -5       C  
ATOM   2676  O   MET A1349       1.775 -18.920  83.937  1.00 42.27           O  
ANISOU 2676  O   MET A1349     5431   5602   5028    123      8    -12       O  
ATOM   2677  CB  MET A1349       4.346 -19.293  82.028  1.00 41.85           C  
ANISOU 2677  CB  MET A1349     5340   5454   5108    -15   -141   -103       C  
ATOM   2678  CG  MET A1349       5.782 -19.781  82.003  1.00 42.97           C  
ANISOU 2678  CG  MET A1349     5466   5595   5266    -65   -210   -111       C  
ATOM   2679  SD  MET A1349       6.759 -19.006  80.702  1.00 40.14           S  
ANISOU 2679  SD  MET A1349     5095   5209   4948    -93   -240   -149       S  
ATOM   2680  CE  MET A1349       7.297 -17.521  81.550  1.00 39.33           C  
ANISOU 2680  CE  MET A1349     5103   5087   4753   -139   -262   -190       C  
ATOM   2681  N   CYS A1350       1.134 -19.727  81.935  1.00 39.69           N  
ANISOU 2681  N   CYS A1350     4963   5275   4841     79    -17     37       N  
ATOM   2682  CA  CYS A1350      -0.196 -19.141  82.058  1.00 44.39           C  
ANISOU 2682  CA  CYS A1350     5535   5929   5402    154     64     95       C  
ATOM   2683  C   CYS A1350      -0.974 -19.746  83.217  1.00 41.02           C  
ANISOU 2683  C   CYS A1350     5073   5590   4924    181     99    185       C  
ATOM   2684  O   CYS A1350      -1.787 -19.057  83.841  1.00 41.82           O  
ANISOU 2684  O   CYS A1350     5191   5747   4952    279    185    225       O  
ATOM   2685  CB  CYS A1350      -0.977 -19.322  80.755  1.00 46.41           C  
ANISOU 2685  CB  CYS A1350     5704   6201   5729    134     61    146       C  
ATOM   2686  SG  CYS A1350      -0.450 -18.218  79.428  1.00 51.20           S  
ANISOU 2686  SG  CYS A1350     6352   6727   6374    141     58     56       S  
ATOM   2687  N   LEU A1351      -0.739 -21.021  83.521  1.00 40.91           N  
ANISOU 2687  N   LEU A1351     5018   5588   4939    107     38    225       N  
ATOM   2688  CA  LEU A1351      -1.425 -21.699  84.612  1.00 46.10           C  
ANISOU 2688  CA  LEU A1351     5634   6330   5550    116     60    320       C  
ATOM   2689  C   LEU A1351      -0.705 -21.565  85.951  1.00 41.96           C  
ANISOU 2689  C   LEU A1351     5197   5797   4949    143     68    273       C  
ATOM   2690  O   LEU A1351      -1.134 -22.178  86.935  1.00 44.59           O  
ANISOU 2690  O   LEU A1351     5504   6199   5241    149     82    347       O  
ATOM   2691  CB  LEU A1351      -1.624 -23.178  84.274  1.00 41.56           C  
ANISOU 2691  CB  LEU A1351     4990   5764   5036     11    -19    398       C  
ATOM   2692  CG  LEU A1351      -2.900 -23.537  83.497  1.00 46.48           C  
ANISOU 2692  CG  LEU A1351     5511   6453   5695    -29    -22    519       C  
ATOM   2693  CD1 LEU A1351      -4.134 -23.051  84.242  1.00 45.72           C  
ANISOU 2693  CD1 LEU A1351     5338   6498   5536     51     72    634       C  
ATOM   2694  CD2 LEU A1351      -2.882 -22.990  82.086  1.00 41.36           C  
ANISOU 2694  CD2 LEU A1351     4862   5751   5103    -37    -34    473       C  
ATOM   2695  N   GLY A1352       0.383 -20.801  86.010  1.00 44.04           N  
ANISOU 2695  N   GLY A1352     5561   5983   5189    147     49    164       N  
ATOM   2696  CA  GLY A1352       1.109 -20.595  87.246  1.00 44.02           C  
ANISOU 2696  CA  GLY A1352     5654   5967   5103    154     40    122       C  
ATOM   2697  C   GLY A1352       2.173 -21.624  87.567  1.00 45.93           C  
ANISOU 2697  C   GLY A1352     5882   6193   5377     70    -46    115       C  
ATOM   2698  O   GLY A1352       2.835 -21.499  88.603  1.00 46.38           O  
ANISOU 2698  O   GLY A1352     6011   6246   5365     62    -66     89       O  
ATOM   2699  N   ALA A1353       2.350 -22.646  86.733  1.00 46.02           N  
ANISOU 2699  N   ALA A1353     5816   6192   5479     14    -99    142       N  
ATOM   2700  CA  ALA A1353       3.498 -23.530  86.885  1.00 46.26           C  
ANISOU 2700  CA  ALA A1353     5846   6197   5533    -38   -174    132       C  
ATOM   2701  C   ALA A1353       4.780 -22.806  86.482  1.00 45.81           C  
ANISOU 2701  C   ALA A1353     5828   6097   5480    -56   -211     57       C  
ATOM   2702  O   ALA A1353       4.820 -22.102  85.468  1.00 46.98           O  
ANISOU 2702  O   ALA A1353     5975   6212   5662    -51   -202     18       O  
ATOM   2703  CB  ALA A1353       3.308 -24.794  86.043  1.00 40.61           C  
ANISOU 2703  CB  ALA A1353     5076   5460   4894    -74   -216    182       C  
ATOM   2704  N   ILE A1354       5.743 -22.831  87.370  1.00 40.87           N  
ANISOU 2704  N   ILE A1354     5226   5482   4820    -86   -259     52       N  
ATOM   2705  CA  ILE A1354       7.012 -22.120  87.112  1.00 40.85           C  
ANISOU 2705  CA  ILE A1354     5244   5467   4810   -123   -307     12       C  
ATOM   2706  C   ILE A1354       7.797 -23.077  86.269  1.00 45.06           C  
ANISOU 2706  C   ILE A1354     5704   6001   5418   -126   -348     38       C  
ATOM   2707  O   ILE A1354       8.004 -24.167  86.708  1.00 40.61           O  
ANISOU 2707  O   ILE A1354     5114   5456   4861   -118   -372     85       O  
ATOM   2708  CB  ILE A1354       7.754 -21.930  88.431  1.00 41.55           C  
ANISOU 2708  CB  ILE A1354     5394   5582   4811   -164   -347     12       C  
ATOM   2709  CG1 ILE A1354       6.972 -21.036  89.388  1.00 42.14           C  
ANISOU 2709  CG1 ILE A1354     5577   5643   4790   -135   -296    -15       C  
ATOM   2710  CG2 ILE A1354       9.151 -21.430  88.164  1.00 41.73           C  
ANISOU 2710  CG2 ILE A1354     5423   5610   4823   -230   -415     -1       C  
ATOM   2711  CD1 ILE A1354       7.266 -21.307  90.809  1.00 42.96           C  
ANISOU 2711  CD1 ILE A1354     5760   5769   4793   -167   -330     -6       C  
ATOM   2712  N   PRO A1355       8.317 -22.818  84.904  1.00 40.05           N  
ANISOU 2712  N   PRO A1355     5045   5344   4830   -123   -350     13       N  
ATOM   2713  CA  PRO A1355       9.104 -23.676  84.008  1.00 41.02           C  
ANISOU 2713  CA  PRO A1355     5111   5467   5007    -96   -374     43       C  
ATOM   2714  C   PRO A1355      10.526 -23.930  84.502  1.00 42.92           C  
ANISOU 2714  C   PRO A1355     5315   5771   5222   -109   -423     87       C  
ATOM   2715  O   PRO A1355      11.198 -23.036  85.029  1.00 41.81           O  
ANISOU 2715  O   PRO A1355     5179   5669   5036   -168   -457     85       O  
ATOM   2716  CB  PRO A1355       9.099 -22.900  82.686  1.00 40.06           C  
ANISOU 2716  CB  PRO A1355     4978   5317   4926    -90   -358      6       C  
ATOM   2717  CG  PRO A1355       8.918 -21.475  83.093  1.00 43.58           C  
ANISOU 2717  CG  PRO A1355     5472   5760   5328   -135   -351    -38       C  
ATOM   2718  CD  PRO A1355       8.045 -21.493  84.318  1.00 39.89           C  
ANISOU 2718  CD  PRO A1355     5058   5293   4805   -133   -327    -40       C  
ATOM   2719  N   ILE A1356      10.997 -25.154  84.267  1.00 46.25           N  
ANISOU 2719  N   ILE A1356     5707   6200   5666    -51   -431    138       N  
ATOM   2720  CA  ILE A1356      12.410 -25.512  84.350  1.00 41.04           C  
ANISOU 2720  CA  ILE A1356     4986   5616   4993    -27   -464    203       C  
ATOM   2721  C   ILE A1356      12.771 -26.078  82.981  1.00 43.00           C  
ANISOU 2721  C   ILE A1356     5213   5842   5283     65   -439    221       C  
ATOM   2722  O   ILE A1356      12.361 -27.194  82.639  1.00 41.69           O  
ANISOU 2722  O   ILE A1356     5098   5612   5130    135   -423    230       O  
ATOM   2723  CB  ILE A1356      12.700 -26.526  85.467  1.00 43.80           C  
ANISOU 2723  CB  ILE A1356     5336   5997   5308    -10   -486    259       C  
ATOM   2724  CG1 ILE A1356      12.201 -26.010  86.825  1.00 41.74           C  
ANISOU 2724  CG1 ILE A1356     5116   5748   4996    -92   -504    237       C  
ATOM   2725  CG2 ILE A1356      14.195 -26.825  85.538  1.00 42.32           C  
ANISOU 2725  CG2 ILE A1356     5066   5910   5102     26   -516    347       C  
ATOM   2726  CD1 ILE A1356      12.526 -26.940  88.006  1.00 42.31           C  
ANISOU 2726  CD1 ILE A1356     5188   5860   5030    -85   -530    295       C  
ATOM   2727  N   ALA A1357      13.530 -25.319  82.194  1.00 40.98           N  
ANISOU 2727  N   ALA A1357     4898   5635   5038     64   -440    232       N  
ATOM   2728  CA  ALA A1357      13.648 -25.611  80.772  1.00 42.97           C  
ANISOU 2728  CA  ALA A1357     5148   5854   5323    152   -405    232       C  
ATOM   2729  C   ALA A1357      15.083 -25.476  80.287  1.00 45.19           C  
ANISOU 2729  C   ALA A1357     5328   6249   5594    204   -407    317       C  
ATOM   2730  O   ALA A1357      15.885 -24.720  80.846  1.00 41.94           O  
ANISOU 2730  O   ALA A1357     4836   5941   5159    126   -449    366       O  
ATOM   2731  CB  ALA A1357      12.755 -24.687  79.931  1.00 40.07           C  
ANISOU 2731  CB  ALA A1357     4812   5420   4991    107   -385    154       C  
ATOM   2732  N   SER A1358      15.391 -26.226  79.229  1.00 46.17           N  
ANISOU 2732  N   SER A1358     5465   6355   5724    337   -365    345       N  
ATOM   2733  CA  SER A1358      16.635 -26.023  78.504  1.00 43.88           C  
ANISOU 2733  CA  SER A1358     5070   6181   5423    410   -347    434       C  
ATOM   2734  C   SER A1358      16.628 -24.648  77.851  1.00 45.33           C  
ANISOU 2734  C   SER A1358     5202   6390   5632    315   -358    403       C  
ATOM   2735  O   SER A1358      15.608 -24.199  77.320  1.00 41.14           O  
ANISOU 2735  O   SER A1358     4745   5752   5133    273   -346    306       O  
ATOM   2736  CB  SER A1358      16.812 -27.105  77.437  1.00 42.75           C  
ANISOU 2736  CB  SER A1358     4990   5988   5264    596   -286    457       C  
ATOM   2737  OG  SER A1358      16.719 -28.400  77.999  1.00 47.84           O  
ANISOU 2737  OG  SER A1358     5720   6578   5877    684   -281    478       O  
ATOM   2738  N   ALA A1359      17.777 -23.974  77.881  1.00 43.91           N  
ANISOU 2738  N   ALA A1359     4891   6358   5434    275   -385    500       N  
ATOM   2739  CA  ALA A1359      17.898 -22.677  77.219  1.00 46.62           C  
ANISOU 2739  CA  ALA A1359     5190   6730   5795    179   -404    488       C  
ATOM   2740  C   ALA A1359      18.201 -22.923  75.740  1.00 46.50           C  
ANISOU 2740  C   ALA A1359     5147   6728   5793    314   -339    515       C  
ATOM   2741  O   ALA A1359      19.347 -22.876  75.285  1.00 45.75           O  
ANISOU 2741  O   ALA A1359     4927   6779   5676    372   -327    640       O  
ATOM   2742  CB  ALA A1359      18.965 -21.820  77.886  1.00 43.45           C  
ANISOU 2742  CB  ALA A1359     4672   6479   5359     46   -481    592       C  
ATOM   2743  N   VAL A1360      17.142 -23.205  74.982  1.00 44.91           N  
ANISOU 2743  N   VAL A1360     5065   6378   5620    366   -297    409       N  
ATOM   2744  CA  VAL A1360      17.219 -23.340  73.529  1.00 45.48           C  
ANISOU 2744  CA  VAL A1360     5150   6430   5699    480   -239    410       C  
ATOM   2745  C   VAL A1360      16.009 -22.648  72.918  1.00 45.85           C  
ANISOU 2745  C   VAL A1360     5285   6347   5789    400   -240    287       C  
ATOM   2746  O   VAL A1360      14.914 -22.668  73.492  1.00 46.35           O  
ANISOU 2746  O   VAL A1360     5434   6306   5871    329   -260    202       O  
ATOM   2747  CB  VAL A1360      17.283 -24.821  73.076  1.00 44.82           C  
ANISOU 2747  CB  VAL A1360     5157   6292   5581    676   -180    429       C  
ATOM   2748  CG1 VAL A1360      18.549 -25.505  73.587  1.00 43.51           C  
ANISOU 2748  CG1 VAL A1360     4896   6270   5365    790   -164    569       C  
ATOM   2749  CG2 VAL A1360      16.042 -25.587  73.526  1.00 41.61           C  
ANISOU 2749  CG2 VAL A1360     4907   5718   5184    655   -196    331       C  
ATOM   2750  N   GLY A1361      16.221 -21.998  71.774  1.00 45.47           N  
ANISOU 2750  N   GLY A1361     5202   6321   5754    414   -217    293       N  
ATOM   2751  CA  GLY A1361      15.112 -21.588  70.921  1.00 39.79           C  
ANISOU 2751  CA  GLY A1361     4571   5478   5070    384   -204    190       C  
ATOM   2752  C   GLY A1361      14.081 -20.717  71.622  1.00 43.27           C  
ANISOU 2752  C   GLY A1361     5052   5849   5541    236   -244    106       C  
ATOM   2753  O   GLY A1361      14.400 -19.743  72.323  1.00 46.56           O  
ANISOU 2753  O   GLY A1361     5419   6321   5952    124   -287    119       O  
ATOM   2754  N   GLY A1362      12.812 -21.087  71.434  1.00 39.82           N  
ANISOU 2754  N   GLY A1362     4717   5290   5124    238   -233     28       N  
ATOM   2755  CA  GLY A1362      11.730 -20.300  71.996  1.00 40.43           C  
ANISOU 2755  CA  GLY A1362     4831   5310   5221    133   -252    -39       C  
ATOM   2756  C   GLY A1362      11.689 -20.329  73.511  1.00 42.87           C  
ANISOU 2756  C   GLY A1362     5141   5642   5507     75   -281    -34       C  
ATOM   2757  O   GLY A1362      11.217 -19.374  74.135  1.00 45.57           O  
ANISOU 2757  O   GLY A1362     5502   5970   5842     -7   -296    -70       O  
ATOM   2758  N   LEU A1363      12.181 -21.410  74.126  1.00 40.13           N  
ANISOU 2758  N   LEU A1363     4787   5324   5137    127   -287     13       N  
ATOM   2759  CA  LEU A1363      12.256 -21.451  75.585  1.00 44.41           C  
ANISOU 2759  CA  LEU A1363     5326   5898   5651     72   -318     26       C  
ATOM   2760  C   LEU A1363      13.193 -20.369  76.102  1.00 48.01           C  
ANISOU 2760  C   LEU A1363     5721   6441   6079    -15   -359     60       C  
ATOM   2761  O   LEU A1363      12.852 -19.615  77.021  1.00 48.01           O  
ANISOU 2761  O   LEU A1363     5763   6426   6054   -105   -387     28       O  
ATOM   2762  CB  LEU A1363      12.727 -22.829  76.057  1.00 42.11           C  
ANISOU 2762  CB  LEU A1363     5035   5627   5337    151   -318     80       C  
ATOM   2763  CG  LEU A1363      11.919 -24.046  75.602  1.00 46.45           C  
ANISOU 2763  CG  LEU A1363     5677   6077   5895    224   -297     60       C  
ATOM   2764  CD1 LEU A1363      12.672 -25.349  75.903  1.00 39.66           C  
ANISOU 2764  CD1 LEU A1363     4834   5235   5000    325   -295    124       C  
ATOM   2765  CD2 LEU A1363      10.536 -24.046  76.251  1.00 43.86           C  
ANISOU 2765  CD2 LEU A1363     5406   5682   5578    151   -307     13       C  
ATOM   2766  N   ARG A1364      14.380 -20.269  75.497  1.00 48.22           N  
ANISOU 2766  N   ARG A1364     5659   6562   6102      8   -366    135       N  
ATOM   2767  CA  ARG A1364      15.322 -19.220  75.855  1.00 51.92           C  
ANISOU 2767  CA  ARG A1364     6064   7124   6542   -102   -424    191       C  
ATOM   2768  C   ARG A1364      14.735 -17.844  75.579  1.00 53.87           C  
ANISOU 2768  C   ARG A1364     6373   7302   6792   -201   -441    121       C  
ATOM   2769  O   ARG A1364      15.025 -16.891  76.308  1.00 54.22           O  
ANISOU 2769  O   ARG A1364     6447   7359   6794   -325   -504    128       O  
ATOM   2770  CB  ARG A1364      16.627 -19.424  75.078  1.00 58.10           C  
ANISOU 2770  CB  ARG A1364     6717   8039   7321    -44   -418    308       C  
ATOM   2771  CG  ARG A1364      17.858 -18.707  75.623  1.00 64.30           C  
ANISOU 2771  CG  ARG A1364     7398   8967   8065   -162   -495    423       C  
ATOM   2772  CD  ARG A1364      19.100 -19.050  74.785  1.00 70.37           C  
ANISOU 2772  CD  ARG A1364     8011   9897   8828    -73   -471    566       C  
ATOM   2773  NE  ARG A1364      20.330 -18.459  75.316  1.00 78.08           N  
ANISOU 2773  NE  ARG A1364     8860  11043   9762   -197   -554    713       N  
ATOM   2774  CZ  ARG A1364      21.305 -19.143  75.916  1.00 79.80           C  
ANISOU 2774  CZ  ARG A1364     8962  11411   9947   -158   -570    850       C  
ATOM   2775  NH1 ARG A1364      21.214 -20.457  76.060  1.00 81.24           N  
ANISOU 2775  NH1 ARG A1364     9156  11582  10131     17   -501    851       N  
ATOM   2776  NH2 ARG A1364      22.384 -18.514  76.364  1.00 77.81           N  
ANISOU 2776  NH2 ARG A1364     8586  11323   9653   -300   -661    998       N  
ATOM   2777  N   ASP A1365      13.893 -17.720  74.545  1.00 51.99           N  
ANISOU 2777  N   ASP A1365     6174   6983   6596   -150   -391     56       N  
ATOM   2778  CA  ASP A1365      13.271 -16.422  74.274  1.00 53.12           C  
ANISOU 2778  CA  ASP A1365     6386   7056   6740   -226   -400     -8       C  
ATOM   2779  C   ASP A1365      12.237 -16.042  75.336  1.00 52.41           C  
ANISOU 2779  C   ASP A1365     6409   6883   6620   -264   -401    -80       C  
ATOM   2780  O   ASP A1365      12.177 -14.883  75.764  1.00 52.68           O  
ANISOU 2780  O   ASP A1365     6522   6882   6611   -349   -435   -106       O  
ATOM   2781  CB  ASP A1365      12.620 -16.423  72.889  1.00 53.86           C  
ANISOU 2781  CB  ASP A1365     6485   7096   6885   -157   -346    -49       C  
ATOM   2782  CG  ASP A1365      13.634 -16.483  71.764  1.00 59.75           C  
ANISOU 2782  CG  ASP A1365     7136   7922   7645   -120   -339     19       C  
ATOM   2783  OD1 ASP A1365      14.762 -15.979  71.945  1.00 63.23           O  
ANISOU 2783  OD1 ASP A1365     7504   8463   8059   -188   -386     99       O  
ATOM   2784  OD2 ASP A1365      13.298 -17.031  70.692  1.00 63.48           O  
ANISOU 2784  OD2 ASP A1365     7609   8363   8147    -27   -290      4       O  
ATOM   2785  N   ILE A1366      11.412 -16.994  75.769  1.00 50.66           N  
ANISOU 2785  N   ILE A1366     6211   6628   6411   -197   -363   -104       N  
ATOM   2786  CA  ILE A1366      10.280 -16.665  76.633  1.00 51.43           C  
ANISOU 2786  CA  ILE A1366     6401   6660   6479   -205   -343   -159       C  
ATOM   2787  C   ILE A1366      10.715 -16.556  78.089  1.00 51.55           C  
ANISOU 2787  C   ILE A1366     6460   6701   6427   -263   -387   -143       C  
ATOM   2788  O   ILE A1366      10.451 -15.554  78.762  1.00 54.69           O  
ANISOU 2788  O   ILE A1366     6962   7056   6763   -313   -403   -178       O  
ATOM   2789  CB  ILE A1366       9.166 -17.716  76.460  1.00 50.50           C  
ANISOU 2789  CB  ILE A1366     6279   6510   6399   -127   -293   -170       C  
ATOM   2790  CG1 ILE A1366       8.531 -17.595  75.079  1.00 49.24           C  
ANISOU 2790  CG1 ILE A1366     6107   6310   6291    -91   -259   -191       C  
ATOM   2791  CG2 ILE A1366       8.112 -17.595  77.558  1.00 49.01           C  
ANISOU 2791  CG2 ILE A1366     6155   6294   6171   -124   -269   -191       C  
ATOM   2792  CD1 ILE A1366       7.651 -18.759  74.733  1.00 51.59           C  
ANISOU 2792  CD1 ILE A1366     6400   6581   6621    -42   -237   -179       C  
ATOM   2793  N   ILE A1367      11.370 -17.594  78.602  1.00 49.41           N  
ANISOU 2793  N   ILE A1367     6126   6492   6154   -249   -408    -90       N  
ATOM   2794  CA  ILE A1367      11.698 -17.642  80.018  1.00 51.65           C  
ANISOU 2794  CA  ILE A1367     6448   6802   6373   -301   -450    -71       C  
ATOM   2795  C   ILE A1367      12.814 -16.654  80.335  1.00 56.10           C  
ANISOU 2795  C   ILE A1367     7026   7408   6881   -420   -532    -35       C  
ATOM   2796  O   ILE A1367      13.751 -16.464  79.546  1.00 58.73           O  
ANISOU 2796  O   ILE A1367     7273   7805   7238   -450   -562     21       O  
ATOM   2797  CB  ILE A1367      12.066 -19.082  80.409  1.00 49.84           C  
ANISOU 2797  CB  ILE A1367     6147   6629   6161   -246   -448    -16       C  
ATOM   2798  CG1 ILE A1367      10.870 -19.996  80.117  1.00 39.18           C  
ANISOU 2798  CG1 ILE A1367     4812   5222   4853   -160   -387    -46       C  
ATOM   2799  CG2 ILE A1367      12.480 -19.154  81.867  1.00 40.51           C  
ANISOU 2799  CG2 ILE A1367     4995   5484   4911   -304   -496     12       C  
ATOM   2800  CD1 ILE A1367      11.215 -21.449  79.923  1.00 40.91           C  
ANISOU 2800  CD1 ILE A1367     4980   5463   5099    -89   -381      4       C  
ATOM   2801  N   THR A1368      12.711 -16.016  81.499  1.00 57.57           N  
ANISOU 2801  N   THR A1368     7330   7560   6984   -492   -572    -58       N  
ATOM   2802  CA  THR A1368      13.712 -15.091  82.006  1.00 58.07           C  
ANISOU 2802  CA  THR A1368     7444   7648   6971   -636   -674    -19       C  
ATOM   2803  C   THR A1368      14.114 -15.534  83.405  1.00 57.33           C  
ANISOU 2803  C   THR A1368     7378   7595   6810   -684   -726     17       C  
ATOM   2804  O   THR A1368      13.511 -16.436  83.991  1.00 57.42           O  
ANISOU 2804  O   THR A1368     7383   7603   6831   -599   -674      0       O  
ATOM   2805  CB  THR A1368      13.199 -13.641  82.040  1.00 60.38           C  
ANISOU 2805  CB  THR A1368     7920   7825   7196   -695   -690    -91       C  
ATOM   2806  OG1 THR A1368      12.233 -13.496  83.090  1.00 62.94           O  
ANISOU 2806  OG1 THR A1368     8399   8067   7448   -648   -652   -158       O  
ATOM   2807  CG2 THR A1368      12.558 -13.255  80.714  1.00 58.66           C  
ANISOU 2807  CG2 THR A1368     7684   7559   7047   -626   -624   -136       C  
ATOM   2808  N   ASN A1369      15.136 -14.872  83.949  1.00 59.15           N  
ANISOU 2808  N   ASN A1369     7643   7865   6965   -835   -839     77       N  
ATOM   2809  CA  ASN A1369      15.650 -15.241  85.266  1.00 59.21           C  
ANISOU 2809  CA  ASN A1369     7675   7922   6901   -902   -905    125       C  
ATOM   2810  C   ASN A1369      14.588 -15.082  86.350  1.00 59.88           C  
ANISOU 2810  C   ASN A1369     7947   7897   6909   -861   -868     32       C  
ATOM   2811  O   ASN A1369      14.634 -15.772  87.378  1.00 56.14           O  
ANISOU 2811  O   ASN A1369     7473   7458   6401   -852   -877     54       O  
ATOM   2812  CB  ASN A1369      16.880 -14.388  85.582  1.00 61.96           C  
ANISOU 2812  CB  ASN A1369     8046   8326   7169  -1102  -1052    214       C  
ATOM   2813  CG  ASN A1369      17.679 -14.910  86.757  1.00 62.53           C  
ANISOU 2813  CG  ASN A1369     8085   8493   7181  -1184  -1136    303       C  
ATOM   2814  OD1 ASN A1369      17.555 -16.069  87.153  1.00 63.36           O  
ANISOU 2814  OD1 ASN A1369     8097   8652   7324  -1078  -1081    320       O  
ATOM   2815  ND2 ASN A1369      18.520 -14.051  87.314  1.00 64.39           N  
ANISOU 2815  ND2 ASN A1369     8403   8747   7315  -1384  -1280    369       N  
ATOM   2816  N   GLU A1370      13.650 -14.178  86.107  1.00 60.33           N  
ANISOU 2816  N   GLU A1370     8162   7829   6933   -825   -820    -62       N  
ATOM   2817  CA  GLU A1370      12.597 -13.866  87.092  1.00 61.07           C  
ANISOU 2817  CA  GLU A1370     8436   7828   6942   -755   -764   -140       C  
ATOM   2818  C   GLU A1370      11.324 -14.663  86.808  1.00 53.40           C  
ANISOU 2818  C   GLU A1370     7391   6851   6046   -581   -628   -177       C  
ATOM   2819  O   GLU A1370      10.414 -14.557  87.581  1.00 50.41           O  
ANISOU 2819  O   GLU A1370     7131   6421   5603   -501   -564   -221       O  
ATOM   2820  CB  GLU A1370      12.356 -12.361  87.062  1.00 70.31           C  
ANISOU 2820  CB  GLU A1370     9848   8862   8003   -799   -787   -208       C  
ATOM   2821  CG  GLU A1370      13.612 -11.542  87.313  1.00 80.37           C  
ANISOU 2821  CG  GLU A1370    11235  10121   9181  -1006   -946   -165       C  
ATOM   2822  CD  GLU A1370      14.639 -11.476  86.185  1.00 89.24           C  
ANISOU 2822  CD  GLU A1370    12198  11321  10389  -1105  -1010    -93       C  
ATOM   2823  OE1 GLU A1370      14.243 -11.498  85.008  1.00 89.75           O  
ANISOU 2823  OE1 GLU A1370    12134  11401  10566  -1004   -924   -110       O  
ATOM   2824  OE2 GLU A1370      15.835 -11.399  86.486  1.00 92.85           O  
ANISOU 2824  OE2 GLU A1370    12651  11833  10795  -1289  -1150     -7       O  
ATOM   2825  N   THR A1371      11.283 -15.417  85.716  1.00 50.33           N  
ANISOU 2825  N   THR A1371     6821   6519   5785   -523   -585   -150       N  
ATOM   2826  CA  THR A1371      10.067 -16.177  85.351  1.00 46.38           C  
ANISOU 2826  CA  THR A1371     6259   6009   5352   -389   -477   -173       C  
ATOM   2827  C   THR A1371      10.346 -17.655  85.118  1.00 48.47           C  
ANISOU 2827  C   THR A1371     6359   6352   5705   -350   -469   -116       C  
ATOM   2828  O   THR A1371       9.540 -18.261  84.462  1.00 47.80           O  
ANISOU 2828  O   THR A1371     6207   6261   5694   -270   -406   -119       O  
ATOM   2829  CB  THR A1371       9.411 -15.607  84.100  1.00 47.22           C  
ANISOU 2829  CB  THR A1371     6361   6066   5513   -342   -425   -212       C  
ATOM   2830  OG1 THR A1371      10.353 -15.689  83.047  1.00 49.72           O  
ANISOU 2830  OG1 THR A1371     6566   6423   5901   -391   -468   -179       O  
ATOM   2831  CG2 THR A1371       8.995 -14.171  84.258  1.00 46.08           C  
ANISOU 2831  CG2 THR A1371     6406   5828   5273   -354   -421   -269       C  
ATOM   2832  N   GLY A1372      11.462 -18.184  85.597  1.00 47.39           N  
ANISOU 2832  N   GLY A1372     6168   6285   5554   -406   -535    -57       N  
ATOM   2833  CA  GLY A1372      11.723 -19.616  85.422  1.00 47.67           C  
ANISOU 2833  CA  GLY A1372     6075   6382   5656   -351   -524      0       C  
ATOM   2834  C   GLY A1372      13.154 -19.983  85.699  1.00 50.61           C  
ANISOU 2834  C   GLY A1372     6368   6848   6014   -412   -602     83       C  
ATOM   2835  O   GLY A1372      13.922 -19.116  86.032  1.00 55.50           O  
ANISOU 2835  O   GLY A1372     7021   7494   6574   -521   -677    105       O  
ATOM   2836  N   ILE A1373      13.468 -21.259  85.578  1.00 47.91           N  
ANISOU 2836  N   ILE A1373     5927   6559   5719   -341   -587    141       N  
ATOM   2837  CA  ILE A1373      14.835 -21.741  85.744  1.00 47.95           C  
ANISOU 2837  CA  ILE A1373     5827   6675   5715   -359   -643    244       C  
ATOM   2838  C   ILE A1373      15.285 -22.343  84.420  1.00 50.11           C  
ANISOU 2838  C   ILE A1373     5997   6982   6059   -263   -605    286       C  
ATOM   2839  O   ILE A1373      14.575 -23.173  83.839  1.00 47.87           O  
ANISOU 2839  O   ILE A1373     5728   6636   5823   -160   -543    254       O  
ATOM   2840  CB  ILE A1373      14.938 -22.769  86.884  1.00 43.10           C  
ANISOU 2840  CB  ILE A1373     5207   6097   5073   -335   -655    288       C  
ATOM   2841  CG1 ILE A1373      14.396 -22.172  88.192  1.00 43.44           C  
ANISOU 2841  CG1 ILE A1373     5371   6100   5034   -416   -682    240       C  
ATOM   2842  CG2 ILE A1373      16.378 -23.218  87.062  1.00 43.98           C  
ANISOU 2842  CG2 ILE A1373     5199   6342   5170   -345   -710    412       C  
ATOM   2843  CD1 ILE A1373      14.269 -23.182  89.330  1.00 43.71           C  
ANISOU 2843  CD1 ILE A1373     5412   6158   5040   -389   -683    272       C  
ATOM   2844  N   LEU A1374      16.453 -21.916  83.940  1.00 47.92           N  
ANISOU 2844  N   LEU A1374     5624   6805   5778   -299   -646    367       N  
ATOM   2845  CA  LEU A1374      16.966 -22.317  82.636  1.00 45.98           C  
ANISOU 2845  CA  LEU A1374     5284   6604   5582   -197   -604    416       C  
ATOM   2846  C   LEU A1374      18.292 -23.046  82.792  1.00 46.85           C  
ANISOU 2846  C   LEU A1374     5261   6865   5673   -143   -623    562       C  
ATOM   2847  O   LEU A1374      19.129 -22.669  83.620  1.00 44.91           O  
ANISOU 2847  O   LEU A1374     4959   6727   5380   -248   -700    648       O  
ATOM   2848  CB  LEU A1374      17.149 -21.105  81.716  1.00 42.91           C  
ANISOU 2848  CB  LEU A1374     4879   6219   5206   -267   -619    403       C  
ATOM   2849  CG  LEU A1374      15.873 -20.462  81.173  1.00 43.01           C  
ANISOU 2849  CG  LEU A1374     5003   6091   5248   -273   -577    273       C  
ATOM   2850  CD1 LEU A1374      16.202 -19.204  80.376  1.00 42.05           C  
ANISOU 2850  CD1 LEU A1374     4869   5980   5128   -355   -605    273       C  
ATOM   2851  CD2 LEU A1374      15.104 -21.453  80.317  1.00 42.51           C  
ANISOU 2851  CD2 LEU A1374     4955   5955   5240   -133   -496    231       C  
ATOM   2852  N   VAL A1375      18.491 -24.076  81.968  1.00 46.75           N  
ANISOU 2852  N   VAL A1375     5211   6863   5690     24   -555    600       N  
ATOM   2853  CA  VAL A1375      19.672 -24.926  82.052  1.00 49.68           C  
ANISOU 2853  CA  VAL A1375     5465   7375   6037    129   -548    746       C  
ATOM   2854  C   VAL A1375      20.201 -25.223  80.654  1.00 50.91           C  
ANISOU 2854  C   VAL A1375     5557   7578   6210    281   -480    804       C  
ATOM   2855  O   VAL A1375      19.501 -25.079  79.648  1.00 46.28           O  
ANISOU 2855  O   VAL A1375     5043   6882   5658    323   -433    713       O  
ATOM   2856  CB  VAL A1375      19.391 -26.251  82.793  1.00 51.36           C  
ANISOU 2856  CB  VAL A1375     5738   7540   6235    229   -525    746       C  
ATOM   2857  CG1 VAL A1375      19.174 -25.997  84.265  1.00 54.96           C  
ANISOU 2857  CG1 VAL A1375     6225   7998   6658     90   -594    730       C  
ATOM   2858  CG2 VAL A1375      18.184 -26.951  82.190  1.00 47.67           C  
ANISOU 2858  CG2 VAL A1375     5416   6895   5802    319   -463    630       C  
ATOM   2859  N   LYS A1376      21.470 -25.621  80.608  1.00 54.74           N  
ANISOU 2859  N   LYS A1376     5900   8238   6662    370   -473    969       N  
ATOM   2860  CA  LYS A1376      22.073 -26.076  79.365  1.00 56.46           C  
ANISOU 2860  CA  LYS A1376     6058   8518   6875    560   -390   1048       C  
ATOM   2861  C   LYS A1376      21.429 -27.382  78.918  1.00 52.32           C  
ANISOU 2861  C   LYS A1376     5690   7841   6349    758   -308    976       C  
ATOM   2862  O   LYS A1376      21.244 -28.307  79.714  1.00 52.40           O  
ANISOU 2862  O   LYS A1376     5769   7803   6339    808   -310    973       O  
ATOM   2863  CB  LYS A1376      23.577 -26.259  79.562  1.00 63.16           C  
ANISOU 2863  CB  LYS A1376     6706   9614   7677    626   -396   1268       C  
ATOM   2864  CG  LYS A1376      24.272 -27.153  78.550  1.00 70.84           C  
ANISOU 2864  CG  LYS A1376     7634  10664   8618    899   -286   1377       C  
ATOM   2865  CD  LYS A1376      25.706 -27.431  78.991  1.00 77.44           C  
ANISOU 2865  CD  LYS A1376     8259  11765   9401    973   -289   1617       C  
ATOM   2866  CE  LYS A1376      26.382 -28.450  78.087  1.00 82.28           C  
ANISOU 2866  CE  LYS A1376     8847  12452   9962   1295   -160   1735       C  
ATOM   2867  NZ  LYS A1376      26.451 -27.972  76.679  1.00 83.06           N  
ANISOU 2867  NZ  LYS A1376     8928  12563  10067   1369    -96   1734       N  
ATOM   2868  N   ALA A1377      21.109 -27.462  77.631  1.00 50.98           N  
ANISOU 2868  N   ALA A1377     5589   7590   6191    864   -244    925       N  
ATOM   2869  CA  ALA A1377      20.438 -28.639  77.095  1.00 48.44           C  
ANISOU 2869  CA  ALA A1377     5455   7096   5853   1028   -183    851       C  
ATOM   2870  C   ALA A1377      21.364 -29.848  77.119  1.00 50.54           C  
ANISOU 2870  C   ALA A1377     5718   7434   6051   1261   -123    980       C  
ATOM   2871  O   ALA A1377      22.577 -29.726  76.928  1.00 57.31           O  
ANISOU 2871  O   ALA A1377     6411   8491   6874   1358    -91   1138       O  
ATOM   2872  CB  ALA A1377      19.961 -28.371  75.669  1.00 47.67           C  
ANISOU 2872  CB  ALA A1377     5437   6904   5771   1078   -137    776       C  
ATOM   2873  N   GLY A1378      20.786 -31.018  77.375  1.00 50.03           N  
ANISOU 2873  N   GLY A1378     5836   7214   5959   1352   -110    926       N  
ATOM   2874  CA  GLY A1378      21.532 -32.257  77.313  1.00 53.90           C  
ANISOU 2874  CA  GLY A1378     6381   7727   6371   1601    -45   1032       C  
ATOM   2875  C   GLY A1378      22.404 -32.575  78.510  1.00 58.00           C  
ANISOU 2875  C   GLY A1378     6765   8407   6864   1619    -66   1166       C  
ATOM   2876  O   GLY A1378      23.229 -33.492  78.419  1.00 58.74           O  
ANISOU 2876  O   GLY A1378     6866   8566   6886   1852      0   1288       O  
ATOM   2877  N   ASP A1379      22.249 -31.869  79.629  1.00 58.34           N  
ANISOU 2877  N   ASP A1379     6700   8515   6953   1393   -153   1152       N  
ATOM   2878  CA  ASP A1379      23.109 -32.066  80.801  1.00 57.86           C  
ANISOU 2878  CA  ASP A1379     6498   8621   6864   1382   -187   1288       C  
ATOM   2879  C   ASP A1379      22.265 -32.517  81.984  1.00 53.44           C  
ANISOU 2879  C   ASP A1379     6053   7934   6317   1267   -247   1198       C  
ATOM   2880  O   ASP A1379      21.675 -31.678  82.686  1.00 53.46           O  
ANISOU 2880  O   ASP A1379     6033   7918   6362   1039   -322   1118       O  
ATOM   2881  CB  ASP A1379      23.862 -30.778  81.140  1.00 61.92           C  
ANISOU 2881  CB  ASP A1379     6776   9350   7399   1204   -251   1383       C  
ATOM   2882  CG  ASP A1379      24.958 -30.987  82.177  1.00 66.87           C  
ANISOU 2882  CG  ASP A1379     7233  10189   7985   1206   -288   1565       C  
ATOM   2883  OD1 ASP A1379      24.782 -31.799  83.106  1.00 68.17           O  
ANISOU 2883  OD1 ASP A1379     7469  10304   8130   1233   -303   1561       O  
ATOM   2884  OD2 ASP A1379      26.011 -30.329  82.061  1.00 71.51           O  
ANISOU 2884  OD2 ASP A1379     7607  11005   8557   1172   -308   1727       O  
ATOM   2885  N   PRO A1380      22.189 -33.823  82.252  1.00 50.45           N  
ANISOU 2885  N   PRO A1380     5810   7465   5894   1423   -216   1214       N  
ATOM   2886  CA  PRO A1380      21.385 -34.296  83.390  1.00 49.90           C  
ANISOU 2886  CA  PRO A1380     5843   7282   5833   1311   -274   1141       C  
ATOM   2887  C   PRO A1380      21.822 -33.725  84.735  1.00 62.89           C  
ANISOU 2887  C   PRO A1380     7327   9083   7484   1148   -348   1206       C  
ATOM   2888  O   PRO A1380      20.981 -33.556  85.630  1.00 49.18           O  
ANISOU 2888  O   PRO A1380     5649   7267   5771    984   -406   1116       O  
ATOM   2889  CB  PRO A1380      21.569 -35.821  83.340  1.00 50.99           C  
ANISOU 2889  CB  PRO A1380     6139   7330   5905   1541   -223   1191       C  
ATOM   2890  CG  PRO A1380      22.118 -36.117  81.975  1.00 52.71           C  
ANISOU 2890  CG  PRO A1380     6401   7546   6079   1771   -132   1238       C  
ATOM   2891  CD  PRO A1380      22.898 -34.918  81.571  1.00 51.96           C  
ANISOU 2891  CD  PRO A1380     6069   7661   6012   1718   -124   1313       C  
ATOM   2892  N   GLY A1381      23.117 -33.465  84.925  1.00 58.59           N  
ANISOU 2892  N   GLY A1381     6586   8765   6911   1193   -349   1373       N  
ATOM   2893  CA  GLY A1381      23.567 -32.950  86.207  1.00 57.76           C  
ANISOU 2893  CA  GLY A1381     6343   8804   6798   1023   -436   1444       C  
ATOM   2894  C   GLY A1381      23.097 -31.531  86.470  1.00 54.61           C  
ANISOU 2894  C   GLY A1381     5908   8404   6437    760   -514   1353       C  
ATOM   2895  O   GLY A1381      22.658 -31.208  87.580  1.00 55.07           O  
ANISOU 2895  O   GLY A1381     5996   8435   6492    592   -585   1301       O  
ATOM   2896  N   GLU A1382      23.156 -30.669  85.455  1.00 50.19           N  
ANISOU 2896  N   GLU A1382     5303   7863   5905    730   -499   1331       N  
ATOM   2897  CA  GLU A1382      22.626 -29.324  85.642  1.00 53.75           C  
ANISOU 2897  CA  GLU A1382     5758   8281   6383    494   -569   1234       C  
ATOM   2898  C   GLU A1382      21.114 -29.340  85.822  1.00 51.30           C  
ANISOU 2898  C   GLU A1382     5636   7749   6105    428   -564   1041       C  
ATOM   2899  O   GLU A1382      20.574 -28.517  86.569  1.00 53.79           O  
ANISOU 2899  O   GLU A1382     5990   8029   6420    248   -625    966       O  
ATOM   2900  CB  GLU A1382      23.020 -28.412  84.479  1.00 55.53           C  
ANISOU 2900  CB  GLU A1382     5896   8573   6629    479   -554   1259       C  
ATOM   2901  CG  GLU A1382      22.783 -26.941  84.807  1.00 64.50           C  
ANISOU 2901  CG  GLU A1382     7024   9711   7773    227   -645   1201       C  
ATOM   2902  CD  GLU A1382      23.175 -25.995  83.692  1.00 72.99           C  
ANISOU 2902  CD  GLU A1382     8016  10850   8867    193   -641   1231       C  
ATOM   2903  OE1 GLU A1382      23.850 -26.436  82.740  1.00 78.16           O  
ANISOU 2903  OE1 GLU A1382     8577  11599   9522    361   -572   1333       O  
ATOM   2904  OE2 GLU A1382      22.804 -24.804  83.772  1.00 75.38           O  
ANISOU 2904  OE2 GLU A1382     8360  11107   9176      5   -705   1157       O  
ATOM   2905  N   LEU A1383      20.412 -30.275  85.176  1.00 48.72           N  
ANISOU 2905  N   LEU A1383     5438   7276   5796    571   -494    971       N  
ATOM   2906  CA  LEU A1383      18.973 -30.377  85.403  1.00 48.72           C  
ANISOU 2906  CA  LEU A1383     5595   7093   5824    500   -496    822       C  
ATOM   2907  C   LEU A1383      18.675 -30.829  86.827  1.00 47.90           C  
ANISOU 2907  C   LEU A1383     5529   6978   5693    434   -539    824       C  
ATOM   2908  O   LEU A1383      17.733 -30.335  87.462  1.00 47.25           O  
ANISOU 2908  O   LEU A1383     5510   6827   5618    303   -567    732       O  
ATOM   2909  CB  LEU A1383      18.346 -31.332  84.386  1.00 49.49           C  
ANISOU 2909  CB  LEU A1383     5830   7040   5935    645   -434    769       C  
ATOM   2910  CG  LEU A1383      16.854 -31.636  84.555  1.00 50.67           C  
ANISOU 2910  CG  LEU A1383     6131   7014   6107    575   -442    650       C  
ATOM   2911  CD1 LEU A1383      16.027 -30.355  84.578  1.00 49.50           C  
ANISOU 2911  CD1 LEU A1383     5969   6844   5995    412   -463    554       C  
ATOM   2912  CD2 LEU A1383      16.367 -32.565  83.450  1.00 51.43           C  
ANISOU 2912  CD2 LEU A1383     6373   6964   6203    701   -400    617       C  
ATOM   2913  N   ALA A1384      19.487 -31.743  87.360  1.00 47.34           N  
ANISOU 2913  N   ALA A1384     5417   6986   5584    534   -540    936       N  
ATOM   2914  CA  ALA A1384      19.289 -32.175  88.737  1.00 49.61           C  
ANISOU 2914  CA  ALA A1384     5732   7275   5842    471   -583    949       C  
ATOM   2915  C   ALA A1384      19.576 -31.040  89.713  1.00 47.66           C  
ANISOU 2915  C   ALA A1384     5404   7133   5571    283   -659    960       C  
ATOM   2916  O   ALA A1384      18.848 -30.860  90.697  1.00 47.28           O  
ANISOU 2916  O   ALA A1384     5427   7033   5507    174   -692    896       O  
ATOM   2917  CB  ALA A1384      20.171 -33.387  89.033  1.00 48.75           C  
ANISOU 2917  CB  ALA A1384     5595   7233   5693    632   -566   1078       C  
ATOM   2918  N   ASN A1385      20.611 -30.245  89.437  1.00 48.30           N  
ANISOU 2918  N   ASN A1385     5349   7361   5641    240   -691   1048       N  
ATOM   2919  CA  ASN A1385      20.890 -29.087  90.280  1.00 53.71           C  
ANISOU 2919  CA  ASN A1385     5993   8125   6289     39   -782   1058       C  
ATOM   2920  C   ASN A1385      19.774 -28.049  90.190  1.00 52.02           C  
ANISOU 2920  C   ASN A1385     5897   7779   6089    -86   -788    902       C  
ATOM   2921  O   ASN A1385      19.425 -27.423  91.195  1.00 51.13           O  
ANISOU 2921  O   ASN A1385     5851   7645   5931   -224   -843    856       O  
ATOM   2922  CB  ASN A1385      22.249 -28.486  89.909  1.00 56.21           C  
ANISOU 2922  CB  ASN A1385     6137   8634   6587      3   -827   1208       C  
ATOM   2923  CG  ASN A1385      23.411 -29.238  90.559  1.00 58.40           C  
ANISOU 2923  CG  ASN A1385     6280   9087   6821     65   -854   1392       C  
ATOM   2924  OD1 ASN A1385      23.206 -30.038  91.466  1.00 57.01           O  
ANISOU 2924  OD1 ASN A1385     6156   8883   6624     98   -858   1394       O  
ATOM   2925  ND2 ASN A1385      24.631 -28.976  90.099  1.00 64.55           N  
ANISOU 2925  ND2 ASN A1385     6879  10061   7585     82   -874   1561       N  
ATOM   2926  N   ALA A1386      19.171 -27.880  89.007  1.00 46.63           N  
ANISOU 2926  N   ALA A1386     5253   7003   5460    -26   -726    821       N  
ATOM   2927  CA  ALA A1386      18.045 -26.959  88.879  1.00 47.66           C  
ANISOU 2927  CA  ALA A1386     5492   7013   5604   -118   -719    682       C  
ATOM   2928  C   ALA A1386      16.829 -27.457  89.646  1.00 47.19           C  
ANISOU 2928  C   ALA A1386     5552   6841   5538   -117   -694    598       C  
ATOM   2929  O   ALA A1386      16.073 -26.659  90.212  1.00 46.45           O  
ANISOU 2929  O   ALA A1386     5542   6693   5416   -212   -707    519       O  
ATOM   2930  CB  ALA A1386      17.694 -26.754  87.405  1.00 44.95           C  
ANISOU 2930  CB  ALA A1386     5153   6606   5320    -48   -659    629       C  
ATOM   2931  N   ILE A1387      16.630 -28.776  89.687  1.00 47.47           N  
ANISOU 2931  N   ILE A1387     5604   6843   5589     -4   -659    624       N  
ATOM   2932  CA  ILE A1387      15.532 -29.333  90.470  1.00 44.77           C  
ANISOU 2932  CA  ILE A1387     5359   6415   5238    -15   -645    572       C  
ATOM   2933  C   ILE A1387      15.781 -29.133  91.967  1.00 46.72           C  
ANISOU 2933  C   ILE A1387     5610   6726   5416   -104   -699    603       C  
ATOM   2934  O   ILE A1387      14.855 -28.822  92.730  1.00 45.15           O  
ANISOU 2934  O   ILE A1387     5490   6477   5186   -165   -695    542       O  
ATOM   2935  CB  ILE A1387      15.331 -30.815  90.100  1.00 44.83           C  
ANISOU 2935  CB  ILE A1387     5403   6360   5270    113   -610    603       C  
ATOM   2936  CG1 ILE A1387      14.800 -30.931  88.664  1.00 44.22           C  
ANISOU 2936  CG1 ILE A1387     5369   6188   5245    179   -563    552       C  
ATOM   2937  CG2 ILE A1387      14.398 -31.506  91.082  1.00 44.78           C  
ANISOU 2937  CG2 ILE A1387     5475   6296   5244     86   -613    588       C  
ATOM   2938  CD1 ILE A1387      14.832 -32.342  88.103  1.00 45.04           C  
ANISOU 2938  CD1 ILE A1387     5542   6217   5355    312   -539    589       C  
ATOM   2939  N   LEU A1388      17.035 -29.281  92.408  1.00 46.30           N  
ANISOU 2939  N   LEU A1388     5469   6794   5331   -111   -750    708       N  
ATOM   2940  CA  LEU A1388      17.353 -29.009  93.810  1.00 51.72           C  
ANISOU 2940  CA  LEU A1388     6165   7545   5943   -215   -816    742       C  
ATOM   2941  C   LEU A1388      17.169 -27.531  94.142  1.00 49.70           C  
ANISOU 2941  C   LEU A1388     5972   7277   5636   -361   -861    678       C  
ATOM   2942  O   LEU A1388      16.712 -27.184  95.237  1.00 49.37           O  
ANISOU 2942  O   LEU A1388     6025   7210   5525   -437   -886    640       O  
ATOM   2943  CB  LEU A1388      18.782 -29.456  94.122  1.00 52.62           C  
ANISOU 2943  CB  LEU A1388     6155   7808   6031   -198   -869    890       C  
ATOM   2944  CG  LEU A1388      19.025 -30.966  94.154  1.00 54.04           C  
ANISOU 2944  CG  LEU A1388     6305   7998   6229    -45   -831    966       C  
ATOM   2945  CD1 LEU A1388      20.511 -31.281  94.014  1.00 53.38           C  
ANISOU 2945  CD1 LEU A1388     6070   8081   6130     16   -858   1128       C  
ATOM   2946  CD2 LEU A1388      18.473 -31.556  95.446  1.00 52.52           C  
ANISOU 2946  CD2 LEU A1388     6188   7771   5995    -75   -847    954       C  
ATOM   2947  N   LYS A1389      17.493 -26.649  93.194  1.00 46.89           N  
ANISOU 2947  N   LYS A1389     5584   6930   5303   -395   -869    664       N  
ATOM   2948  CA  LYS A1389      17.260 -25.221  93.386  1.00 52.04           C  
ANISOU 2948  CA  LYS A1389     6330   7542   5902   -526   -911    596       C  
ATOM   2949  C   LYS A1389      15.769 -24.916  93.485  1.00 48.28           C  
ANISOU 2949  C   LYS A1389     5992   6932   5422   -499   -841    467       C  
ATOM   2950  O   LYS A1389      15.343 -24.100  94.313  1.00 47.36           O  
ANISOU 2950  O   LYS A1389     6003   6770   5222   -575   -864    412       O  
ATOM   2951  CB  LYS A1389      17.903 -24.442  92.233  1.00 53.95           C  
ANISOU 2951  CB  LYS A1389     6502   7820   6177   -559   -931    618       C  
ATOM   2952  CG  LYS A1389      17.503 -22.982  92.128  1.00 59.63           C  
ANISOU 2952  CG  LYS A1389     7343   8462   6853   -673   -960    532       C  
ATOM   2953  CD  LYS A1389      18.055 -22.172  93.291  1.00 68.67           C  
ANISOU 2953  CD  LYS A1389     8577   9635   7879   -841  -1075    562       C  
ATOM   2954  CE  LYS A1389      17.731 -20.689  93.140  1.00 74.02           C  
ANISOU 2954  CE  LYS A1389     9411  10216   8495   -951  -1112    479       C  
ATOM   2955  NZ  LYS A1389      18.289 -19.889  94.268  1.00 77.14           N  
ANISOU 2955  NZ  LYS A1389     9936  10617   8755  -1129  -1241    509       N  
ATOM   2956  N   ALA A1390      14.957 -25.582  92.658  1.00 46.54           N  
ANISOU 2956  N   ALA A1390     5753   6649   5281   -386   -757    428       N  
ATOM   2957  CA  ALA A1390      13.511 -25.412  92.751  1.00 46.59           C  
ANISOU 2957  CA  ALA A1390     5857   6559   5287   -355   -689    338       C  
ATOM   2958  C   ALA A1390      12.995 -25.888  94.101  1.00 51.18           C  
ANISOU 2958  C   ALA A1390     6500   7142   5805   -359   -685    346       C  
ATOM   2959  O   ALA A1390      12.095 -25.272  94.688  1.00 51.10           O  
ANISOU 2959  O   ALA A1390     6592   7087   5735   -371   -653    289       O  
ATOM   2960  CB  ALA A1390      12.821 -26.176  91.625  1.00 43.79           C  
ANISOU 2960  CB  ALA A1390     5462   6150   5024   -256   -621    322       C  
ATOM   2961  N   LEU A1391      13.577 -26.970  94.626  1.00 50.13           N  
ANISOU 2961  N   LEU A1391     6308   7066   5675   -338   -713    423       N  
ATOM   2962  CA  LEU A1391      13.183 -27.419  95.955  1.00 50.98           C  
ANISOU 2962  CA  LEU A1391     6468   7184   5717   -349   -717    440       C  
ATOM   2963  C   LEU A1391      13.572 -26.400  97.021  1.00 51.55           C  
ANISOU 2963  C   LEU A1391     6630   7281   5676   -452   -777    427       C  
ATOM   2964  O   LEU A1391      12.805 -26.163  97.961  1.00 52.31           O  
ANISOU 2964  O   LEU A1391     6831   7349   5696   -457   -753    392       O  
ATOM   2965  CB  LEU A1391      13.799 -28.783  96.262  1.00 52.01           C  
ANISOU 2965  CB  LEU A1391     6523   7366   5871   -303   -740    531       C  
ATOM   2966  CG  LEU A1391      13.569 -29.280  97.692  1.00 54.99           C  
ANISOU 2966  CG  LEU A1391     6946   7768   6178   -325   -756    561       C  
ATOM   2967  CD1 LEU A1391      12.079 -29.423  97.992  1.00 55.69           C  
ANISOU 2967  CD1 LEU A1391     7105   7796   6259   -296   -686    515       C  
ATOM   2968  CD2 LEU A1391      14.296 -30.590  97.939  1.00 54.70           C  
ANISOU 2968  CD2 LEU A1391     6838   7781   6163   -275   -783    658       C  
ATOM   2969  N   GLU A1392      14.743 -25.767  96.886  1.00 53.38           N  
ANISOU 2969  N   GLU A1392     6832   7565   5884   -537   -859    462       N  
ATOM   2970  CA  GLU A1392      15.114 -24.732  97.852  1.00 56.14           C  
ANISOU 2970  CA  GLU A1392     7302   7918   6110   -661   -937    451       C  
ATOM   2971  C   GLU A1392      14.138 -23.565  97.796  1.00 52.84           C  
ANISOU 2971  C   GLU A1392     7048   7393   5635   -665   -893    340       C  
ATOM   2972  O   GLU A1392      13.718 -23.043  98.835  1.00 50.64           O  
ANISOU 2972  O   GLU A1392     6928   7074   5239   -693   -899    301       O  
ATOM   2973  CB  GLU A1392      16.534 -24.218  97.598  1.00 63.83           C  
ANISOU 2973  CB  GLU A1392     8206   8976   7068   -777  -1048    529       C  
ATOM   2974  CG  GLU A1392      17.651 -25.244  97.679  1.00 75.68           C  
ANISOU 2974  CG  GLU A1392     9537  10611   8609   -765  -1094    665       C  
ATOM   2975  CD  GLU A1392      19.026 -24.602  97.534  1.00 86.20           C  
ANISOU 2975  CD  GLU A1392    10791  12055   9908   -898  -1211    770       C  
ATOM   2976  OE1 GLU A1392      19.476 -23.935  98.491  1.00 90.17           O  
ANISOU 2976  OE1 GLU A1392    11383  12580  10299  -1050  -1318    797       O  
ATOM   2977  OE2 GLU A1392      19.649 -24.745  96.457  1.00 88.63           O  
ANISOU 2977  OE2 GLU A1392    10952  12430  10292   -857  -1201    834       O  
ATOM   2978  N   LEU A1393      13.747 -23.160  96.584  1.00 48.79           N  
ANISOU 2978  N   LEU A1393     6509   6833   5197   -621   -841    292       N  
ATOM   2979  CA  LEU A1393      12.799 -22.059  96.431  1.00 50.07           C  
ANISOU 2979  CA  LEU A1393     6820   6896   5308   -601   -788    195       C  
ATOM   2980  C   LEU A1393      11.432 -22.408  97.008  1.00 53.97           C  
ANISOU 2980  C   LEU A1393     7375   7355   5775   -493   -685    160       C  
ATOM   2981  O   LEU A1393      10.749 -21.532  97.555  1.00 55.37           O  
ANISOU 2981  O   LEU A1393     7720   7472   5848   -472   -649    103       O  
ATOM   2982  CB  LEU A1393      12.659 -21.682  94.951  1.00 46.40           C  
ANISOU 2982  CB  LEU A1393     6290   6400   4941   -570   -752    164       C  
ATOM   2983  CG  LEU A1393      13.871 -21.072  94.244  1.00 51.10           C  
ANISOU 2983  CG  LEU A1393     6834   7028   5553   -674   -842    199       C  
ATOM   2984  CD1 LEU A1393      13.607 -20.921  92.758  1.00 55.87           C  
ANISOU 2984  CD1 LEU A1393     7359   7607   6264   -616   -787    171       C  
ATOM   2985  CD2 LEU A1393      14.216 -19.721  94.851  1.00 50.65           C  
ANISOU 2985  CD2 LEU A1393     6962   6920   5364   -802   -927    168       C  
ATOM   2986  N   SER A1394      11.029 -23.680  96.922  1.00 53.32           N  
ANISOU 2986  N   SER A1394     7170   7314   5775   -421   -637    206       N  
ATOM   2987  CA  SER A1394       9.706 -24.080  97.393  1.00 54.52           C  
ANISOU 2987  CA  SER A1394     7349   7457   5909   -332   -544    200       C  
ATOM   2988  C   SER A1394       9.530 -23.914  98.901  1.00 58.41           C  
ANISOU 2988  C   SER A1394     7966   7962   6264   -339   -547    204       C  
ATOM   2989  O   SER A1394       8.386 -23.873  99.367  1.00 59.00           O  
ANISOU 2989  O   SER A1394     8093   8033   6290   -257   -460    198       O  
ATOM   2990  CB  SER A1394       9.415 -25.529  96.990  1.00 52.61           C  
ANISOU 2990  CB  SER A1394     6965   7249   5775   -284   -519    261       C  
ATOM   2991  OG  SER A1394      10.287 -26.433  97.646  1.00 52.39           O  
ANISOU 2991  OG  SER A1394     6889   7273   5743   -319   -583    325       O  
ATOM   2992  N   ARG A1395      10.621 -23.848  99.678  1.00 62.94           N  
ANISOU 2992  N   ARG A1395     8582   8562   6771   -433   -646    228       N  
ATOM   2993  CA  ARG A1395      10.485 -23.632 101.121  1.00 66.55           C  
ANISOU 2993  CA  ARG A1395     9183   9021   7082   -447   -657    227       C  
ATOM   2994  C   ARG A1395       9.849 -22.282 101.428  1.00 70.18           C  
ANISOU 2994  C   ARG A1395     9859   9397   7410   -415   -614    147       C  
ATOM   2995  O   ARG A1395       9.192 -22.123 102.465  1.00 75.25           O  
ANISOU 2995  O   ARG A1395    10632  10030   7929   -355   -563    138       O  
ATOM   2996  CB  ARG A1395      11.849 -23.713 101.815  1.00 65.47           C  
ANISOU 2996  CB  ARG A1395     9056   8929   6892   -576   -789    275       C  
ATOM   2997  CG  ARG A1395      12.775 -24.802 101.314  1.00 67.84           C  
ANISOU 2997  CG  ARG A1395     9152   9312   7314   -603   -842    360       C  
ATOM   2998  CD  ARG A1395      12.513 -26.134 101.975  1.00 73.01           C  
ANISOU 2998  CD  ARG A1395     9728  10021   7994   -547   -814    423       C  
ATOM   2999  NE  ARG A1395      13.454 -27.148 101.508  1.00 75.73           N  
ANISOU 2999  NE  ARG A1395     9906  10432   8436   -551   -861    507       N  
ATOM   3000  CZ  ARG A1395      13.445 -28.417 101.901  1.00 76.79           C  
ANISOU 3000  CZ  ARG A1395     9964  10608   8606   -504   -851    574       C  
ATOM   3001  NH1 ARG A1395      12.542 -28.835 102.777  1.00 78.92           N  
ANISOU 3001  NH1 ARG A1395    10291  10868   8827   -467   -803    572       N  
ATOM   3002  NH2 ARG A1395      14.340 -29.268 101.417  1.00 75.36           N  
ANISOU 3002  NH2 ARG A1395     9654  10479   8500   -484   -887    652       N  
ATOM   3003  N   SER A1396      10.059 -21.298 100.562  1.00 66.36           N  
ANISOU 3003  N   SER A1396     9429   8849   6937   -446   -633     94       N  
ATOM   3004  CA  SER A1396       9.469 -19.975 100.688  1.00 63.95           C  
ANISOU 3004  CA  SER A1396     9347   8445   6506   -402   -590     16       C  
ATOM   3005  C   SER A1396       8.194 -19.886  99.858  1.00 60.66           C  
ANISOU 3005  C   SER A1396     8875   8016   6158   -254   -451     -6       C  
ATOM   3006  O   SER A1396       7.854 -20.791  99.093  1.00 63.45           O  
ANISOU 3006  O   SER A1396     9023   8428   6657   -217   -409     35       O  
ATOM   3007  CB  SER A1396      10.472 -18.899 100.264  1.00 63.67           C  
ANISOU 3007  CB  SER A1396     9421   8340   6430   -538   -706    -20       C  
ATOM   3008  OG  SER A1396      11.552 -18.851 101.179  1.00 68.91           O  
ANISOU 3008  OG  SER A1396    10165   9020   6999   -686   -842     14       O  
ATOM   3009  N   ASP A1397       7.468 -18.786 100.041  1.00 58.47           N  
ANISOU 3009  N   ASP A1397     8797   7659   5758   -166   -382    -65       N  
ATOM   3010  CA  ASP A1397       6.296 -18.530  99.217  1.00 61.61           C  
ANISOU 3010  CA  ASP A1397     9147   8053   6209    -26   -254    -75       C  
ATOM   3011  C   ASP A1397       6.713 -18.359  97.759  1.00 59.45           C  
ANISOU 3011  C   ASP A1397     8753   7758   6077    -88   -294    -94       C  
ATOM   3012  O   ASP A1397       7.701 -17.685  97.450  1.00 60.47           O  
ANISOU 3012  O   ASP A1397     8958   7827   6191   -205   -396   -132       O  
ATOM   3013  CB  ASP A1397       5.562 -17.285  99.723  1.00 68.15           C  
ANISOU 3013  CB  ASP A1397    10241   8795   6859     97   -173   -130       C  
ATOM   3014  CG  ASP A1397       4.176 -17.126  99.113  1.00 74.34           C  
ANISOU 3014  CG  ASP A1397    10959   9611   7676    276    -17   -108       C  
ATOM   3015  OD1 ASP A1397       3.817 -17.905  98.203  1.00 74.74           O  
ANISOU 3015  OD1 ASP A1397    10767   9740   7893    277      9    -57       O  
ATOM   3016  OD2 ASP A1397       3.443 -16.215  99.552  1.00 77.19           O  
ANISOU 3016  OD2 ASP A1397    11522   9921   7887    421     77   -133       O  
ATOM   3017  N   LEU A1398       5.965 -18.956  96.833  1.00 55.24           N  
ANISOU 3017  N   LEU A1398     8032   7279   5678    -18   -219    -58       N  
ATOM   3018  CA  LEU A1398       6.292 -18.891  95.382  1.00 52.22           C  
ANISOU 3018  CA  LEU A1398     7527   6882   5432    -59   -243    -72       C  
ATOM   3019  C   LEU A1398       5.253 -18.050  94.632  1.00 51.06           C  
ANISOU 3019  C   LEU A1398     7426   6692   5282     46   -148   -104       C  
ATOM   3020  O   LEU A1398       5.361 -17.934  93.424  1.00 49.74           O  
ANISOU 3020  O   LEU A1398     7155   6517   5228     27   -154   -112       O  
ATOM   3021  CB  LEU A1398       6.311 -20.316  94.831  1.00 49.18           C  
ANISOU 3021  CB  LEU A1398     6911   6575   5199    -76   -249     -6       C  
ATOM   3022  CG  LEU A1398       7.504 -21.185  95.211  1.00 50.90           C  
ANISOU 3022  CG  LEU A1398     7053   6835   5454   -177   -350     32       C  
ATOM   3023  CD1 LEU A1398       7.315 -22.605  94.736  1.00 50.90           C  
ANISOU 3023  CD1 LEU A1398     6870   6885   5586   -164   -342     93       C  
ATOM   3024  CD2 LEU A1398       8.793 -20.634  94.661  1.00 49.28           C  
ANISOU 3024  CD2 LEU A1398     6874   6599   5251   -288   -454      5       C  
ATOM   3025  N   SER A1399       4.361 -17.388  95.354  1.00 52.67           N  
ANISOU 3025  N   SER A1399     7786   6875   5353    171    -55   -116       N  
ATOM   3026  CA  SER A1399       3.263 -16.640  94.704  1.00 55.86           C  
ANISOU 3026  CA  SER A1399     8211   7263   5752    304     55   -121       C  
ATOM   3027  C   SER A1399       3.816 -15.582  93.757  1.00 54.58           C  
ANISOU 3027  C   SER A1399     8144   6994   5599    254      8   -196       C  
ATOM   3028  O   SER A1399       3.439 -15.591  92.614  1.00 56.26           O  
ANISOU 3028  O   SER A1399     8260   7214   5903    297     54   -191       O  
ATOM   3029  CB  SER A1399       2.403 -15.991  95.730  1.00 61.55           C  
ANISOU 3029  CB  SER A1399     9106   7980   6299    472    170   -111       C  
ATOM   3030  OG  SER A1399       1.507 -16.922  96.278  1.00 67.18           O  
ANISOU 3030  OG  SER A1399     9676   8823   7028    548    248    -13       O  
ATOM   3031  N   LYS A1400       4.807 -14.826  94.193  1.00 52.19           N  
ANISOU 3031  N   LYS A1400     8033   6596   5201    151    -93   -258       N  
ATOM   3032  CA  LYS A1400       5.367 -13.772  93.327  1.00 55.47           C  
ANISOU 3032  CA  LYS A1400     8545   6912   5620     83   -151   -317       C  
ATOM   3033  C   LYS A1400       5.978 -14.409  92.086  1.00 52.55           C  
ANISOU 3033  C   LYS A1400     7941   6592   5433    -25   -215   -295       C  
ATOM   3034  O   LYS A1400       5.684 -13.948  91.012  1.00 52.09           O  
ANISOU 3034  O   LYS A1400     7867   6495   5432    -22   -207   -321       O  
ATOM   3035  CB  LYS A1400       6.332 -12.892  94.115  1.00 61.14           C  
ANISOU 3035  CB  LYS A1400     9520   7522   6187    -39   -270   -367       C  
ATOM   3036  CG  LYS A1400       5.638 -11.960  95.097  1.00 72.29           C  
ANISOU 3036  CG  LYS A1400    11241   8841   7386     82   -207   -408       C  
ATOM   3037  CD  LYS A1400       6.552 -11.340  96.145  1.00 78.14           C  
ANISOU 3037  CD  LYS A1400    12270   9453   7964    -70   -351   -457       C  
ATOM   3038  CE  LYS A1400       5.903 -10.219  96.929  1.00 82.29           C  
ANISOU 3038  CE  LYS A1400    13159   9854   8255     72   -283   -508       C  
ATOM   3039  NZ  LYS A1400       6.893  -9.436  97.701  1.00 86.36           N  
ANISOU 3039  NZ  LYS A1400    14001  10219   8593    -96   -443   -557       N  
ATOM   3040  N   PHE A1401       6.673 -15.519  92.246  1.00 50.73           N  
ANISOU 3040  N   PHE A1401     7536   6450   5290   -103   -270   -245       N  
ATOM   3041  CA  PHE A1401       7.293 -16.166  91.077  1.00 49.59           C  
ANISOU 3041  CA  PHE A1401     7185   6354   5303   -175   -318   -217       C  
ATOM   3042  C   PHE A1401       6.198 -16.580  90.096  1.00 46.61           C  
ANISOU 3042  C   PHE A1401     6664   6009   5036    -73   -222   -198       C  
ATOM   3043  O   PHE A1401       6.274 -16.194  88.945  1.00 44.41           O  
ANISOU 3043  O   PHE A1401     6319   5713   4843    -91   -230   -212       O  
ATOM   3044  CB  PHE A1401       8.078 -17.366  91.577  1.00 53.27           C  
ANISOU 3044  CB  PHE A1401     7525   6901   5815   -250   -387   -160       C  
ATOM   3045  CG  PHE A1401       9.246 -17.712  90.715  1.00 55.50           C  
ANISOU 3045  CG  PHE A1401     7676   7219   6192   -350   -474   -131       C  
ATOM   3046  CD1 PHE A1401      10.332 -18.380  91.221  1.00 58.07           C  
ANISOU 3046  CD1 PHE A1401     7940   7524   6601   -348   -464   -148       C  
ATOM   3047  CD2 PHE A1401       9.255 -17.348  89.392  1.00 56.86           C  
ANISOU 3047  CD2 PHE A1401     7780   7457   6366   -434   -559    -75       C  
ATOM   3048  CE1 PHE A1401      11.402 -18.691  90.408  1.00 56.73           C  
ANISOU 3048  CE1 PHE A1401     7644   7401   6508   -421   -531   -109       C  
ATOM   3049  CE2 PHE A1401      10.329 -17.655  88.585  1.00 59.28           C  
ANISOU 3049  CE2 PHE A1401     7954   7819   6751   -501   -625    -27       C  
ATOM   3050  CZ  PHE A1401      11.402 -18.324  89.093  1.00 55.66           C  
ANISOU 3050  CZ  PHE A1401     7437   7342   6370   -490   -608    -44       C  
ATOM   3051  N   ARG A1402       5.118 -17.160  90.610  1.00 44.33           N  
ANISOU 3051  N   ARG A1402     6329   5774   4742     27   -135   -156       N  
ATOM   3052  CA  ARG A1402       4.016 -17.605  89.731  1.00 46.93           C  
ANISOU 3052  CA  ARG A1402     6526   6143   5162    105    -56   -118       C  
ATOM   3053  C   ARG A1402       3.405 -16.382  89.057  1.00 48.01           C  
ANISOU 3053  C   ARG A1402     6750   6227   5266    185     10   -155       C  
ATOM   3054  O   ARG A1402       3.183 -16.437  87.875  1.00 51.77           O  
ANISOU 3054  O   ARG A1402     7122   6713   5837    200     34   -142       O  
ATOM   3055  CB  ARG A1402       2.979 -18.434  90.487  1.00 44.02           C  
ANISOU 3055  CB  ARG A1402     6089   5860   4777    180     15    -40       C  
ATOM   3056  CG  ARG A1402       3.540 -19.655  91.185  1.00 43.97           C  
ANISOU 3056  CG  ARG A1402     6025   5899   4782    113    -45     -2       C  
ATOM   3057  CD  ARG A1402       2.428 -20.560  91.632  1.00 44.27           C  
ANISOU 3057  CD  ARG A1402     5975   6026   4819    173     20     91       C  
ATOM   3058  NE  ARG A1402       2.886 -21.551  92.570  1.00 44.40           N  
ANISOU 3058  NE  ARG A1402     5968   6078   4825    117    -33    125       N  
ATOM   3059  CZ  ARG A1402       3.551 -22.638  92.260  1.00 44.45           C  
ANISOU 3059  CZ  ARG A1402     5875   6090   4925     39   -106    151       C  
ATOM   3060  NH1 ARG A1402       3.776 -22.963  91.007  1.00 42.93           N  
ANISOU 3060  NH1 ARG A1402     5604   5868   4840      6   -135    143       N  
ATOM   3061  NH2 ARG A1402       4.012 -23.400  93.215  1.00 45.29           N  
ANISOU 3061  NH2 ARG A1402     5973   6226   5008      3   -147    186       N  
ATOM   3062  N   GLU A1403       3.259 -15.282  89.783  1.00 49.08           N  
ANISOU 3062  N   GLU A1403     7092   6297   5257    241     38   -199       N  
ATOM   3063  CA  GLU A1403       2.658 -14.057  89.221  1.00 50.08           C  
ANISOU 3063  CA  GLU A1403     7333   6358   5336    332    102   -235       C  
ATOM   3064  C   GLU A1403       3.554 -13.551  88.092  1.00 46.89           C  
ANISOU 3064  C   GLU A1403     6936   5881   4998    224     19   -290       C  
ATOM   3065  O   GLU A1403       3.027 -13.164  87.076  1.00 44.45           O  
ANISOU 3065  O   GLU A1403     6587   5558   4744    271     62   -294       O  
ATOM   3066  CB  GLU A1403       2.403 -13.055  90.345  1.00 57.95           C  
ANISOU 3066  CB  GLU A1403     8597   7279   6140    425    146   -274       C  
ATOM   3067  CG  GLU A1403       1.644 -11.825  89.908  1.00 67.12           C  
ANISOU 3067  CG  GLU A1403     9911   8364   7228    556    229   -305       C  
ATOM   3068  CD  GLU A1403       1.388 -10.767  90.974  1.00 80.19           C  
ANISOU 3068  CD  GLU A1403    11885   9917   8668    661    270   -350       C  
ATOM   3069  OE1 GLU A1403       2.203 -10.639  91.901  1.00 83.86           O  
ANISOU 3069  OE1 GLU A1403    12476  10347   9040    586    200   -375       O  
ATOM   3070  OE2 GLU A1403       0.366 -10.069  90.872  1.00 84.86           O  
ANISOU 3070  OE2 GLU A1403    12611  10459   9172    827    373   -356       O  
ATOM   3071  N   ASN A1404       4.864 -13.608  88.276  1.00 44.79           N  
ANISOU 3071  N   ASN A1404     6702   5585   4730     75   -102   -317       N  
ATOM   3072  CA  ASN A1404       5.790 -13.161  87.221  1.00 45.42           C  
ANISOU 3072  CA  ASN A1404     6751   5627   4880    -36   -184   -342       C  
ATOM   3073  C   ASN A1404       5.643 -14.079  86.013  1.00 46.95           C  
ANISOU 3073  C   ASN A1404     6710   5891   5236    -35   -168   -305       C  
ATOM   3074  O   ASN A1404       5.655 -13.570  84.920  1.00 45.47           O  
ANISOU 3074  O   ASN A1404     6494   5675   5107    -42   -167   -323       O  
ATOM   3075  CB  ASN A1404       7.240 -13.188  87.675  1.00 48.91           C  
ANISOU 3075  CB  ASN A1404     7227   6065   5291   -199   -318   -340       C  
ATOM   3076  CG  ASN A1404       7.580 -12.138  88.701  1.00 54.72           C  
ANISOU 3076  CG  ASN A1404     8234   6704   5854   -241   -368   -381       C  
ATOM   3077  OD1 ASN A1404       6.863 -11.170  88.875  1.00 58.48           O  
ANISOU 3077  OD1 ASN A1404     8905   7084   6231   -155   -312   -429       O  
ATOM   3078  ND2 ASN A1404       8.677 -12.346  89.391  1.00 55.55           N  
ANISOU 3078  ND2 ASN A1404     8366   6829   5910   -373   -478   -358       N  
ATOM   3079  N   CYS A1405       5.480 -15.379  86.236  1.00 42.44           N  
ANISOU 3079  N   CYS A1405     5989   5403   4732    -27   -159   -253       N  
ATOM   3080  CA  CYS A1405       5.384 -16.284  85.078  1.00 42.65           C  
ANISOU 3080  CA  CYS A1405     5834   5475   4894    -30   -154   -219       C  
ATOM   3081  C   CYS A1405       4.129 -15.942  84.297  1.00 41.76           C  
ANISOU 3081  C   CYS A1405     5691   5362   4816     62    -67   -210       C  
ATOM   3082  O   CYS A1405       4.233 -15.775  83.123  1.00 42.01           O  
ANISOU 3082  O   CYS A1405     5654   5380   4926     49    -73   -217       O  
ATOM   3083  CB  CYS A1405       5.335 -17.743  85.492  1.00 44.23           C  
ANISOU 3083  CB  CYS A1405     5922   5745   5138    -37   -165   -161       C  
ATOM   3084  SG  CYS A1405       6.873 -18.317  86.231  1.00 50.63           S  
ANISOU 3084  SG  CYS A1405     6721   6582   5934   -136   -267   -147       S  
ATOM   3085  N   LYS A1406       3.011 -15.787  84.984  1.00 41.80           N  
ANISOU 3085  N   LYS A1406     5739   5390   4752    163     16   -183       N  
ATOM   3086  CA  LYS A1406       1.744 -15.518  84.313  1.00 42.48           C  
ANISOU 3086  CA  LYS A1406     5775   5504   4863    258    103   -147       C  
ATOM   3087  C   LYS A1406       1.781 -14.181  83.580  1.00 44.46           C  
ANISOU 3087  C   LYS A1406     6127   5675   5089    287    120   -204       C  
ATOM   3088  O   LYS A1406       1.311 -14.073  82.438  1.00 43.70           O  
ANISOU 3088  O   LYS A1406     5948   5587   5067    304    142   -189       O  
ATOM   3089  CB  LYS A1406       0.613 -15.550  85.341  1.00 48.38           C  
ANISOU 3089  CB  LYS A1406     6544   6315   5523    375    197    -85       C  
ATOM   3090  CG  LYS A1406      -0.787 -15.441  84.771  1.00 56.74           C  
ANISOU 3090  CG  LYS A1406     7510   7446   6603    478    291     -4       C  
ATOM   3091  CD  LYS A1406      -1.812 -15.254  85.887  1.00 62.38           C  
ANISOU 3091  CD  LYS A1406     8262   8237   7204    620    398     68       C  
ATOM   3092  CE  LYS A1406      -1.556 -16.206  87.045  1.00 65.37           C  
ANISOU 3092  CE  LYS A1406     8623   8663   7553    579    370     98       C  
ATOM   3093  NZ  LYS A1406      -1.655 -17.634  86.645  1.00 66.98           N  
ANISOU 3093  NZ  LYS A1406     8640   8936   7873    472    310    171       N  
ATOM   3094  N   LYS A1407       2.383 -13.161  84.200  1.00 45.33           N  
ANISOU 3094  N   LYS A1407     6429   5702   5094    280     97   -268       N  
ATOM   3095  CA  LYS A1407       2.449 -11.848  83.570  1.00 46.44           C  
ANISOU 3095  CA  LYS A1407     6698   5750   5196    300    104   -322       C  
ATOM   3096  C   LYS A1407       3.336 -11.872  82.333  1.00 44.11           C  
ANISOU 3096  C   LYS A1407     6316   5435   5009    182     22   -345       C  
ATOM   3097  O   LYS A1407       3.001 -11.269  81.303  1.00 41.92           O  
ANISOU 3097  O   LYS A1407     6029   5128   4769    211     48   -356       O  
ATOM   3098  CB  LYS A1407       2.969 -10.823  84.577  1.00 52.05           C  
ANISOU 3098  CB  LYS A1407     7668   6357   5751    293     74   -381       C  
ATOM   3099  CG  LYS A1407       2.299  -9.470  84.490  1.00 61.41           C  
ANISOU 3099  CG  LYS A1407     9054   7450   6830    416    146   -414       C  
ATOM   3100  CD  LYS A1407       1.469  -9.190  85.735  1.00 67.86           C  
ANISOU 3100  CD  LYS A1407    10028   8262   7494    576    244   -400       C  
ATOM   3101  CE  LYS A1407       2.343  -9.085  86.975  1.00 71.26           C  
ANISOU 3101  CE  LYS A1407    10647   8627   7804    492    163   -443       C  
ATOM   3102  NZ  LYS A1407       1.547  -8.746  88.192  1.00 74.12           N  
ANISOU 3102  NZ  LYS A1407    11196   8972   7996    664    264   -435       N  
ATOM   3103  N   ARG A1408       4.464 -12.580  82.409  1.00 42.61           N  
ANISOU 3103  N   ARG A1408     6055   5270   4865     60    -70   -343       N  
ATOM   3104  CA  ARG A1408       5.336 -12.689  81.250  1.00 44.14           C  
ANISOU 3104  CA  ARG A1408     6151   5466   5153    -31   -135   -347       C  
ATOM   3105  C   ARG A1408       4.644 -13.438  80.120  1.00 47.89           C  
ANISOU 3105  C   ARG A1408     6463   5990   5743     14    -90   -314       C  
ATOM   3106  O   ARG A1408       4.732 -13.034  78.953  1.00 51.28           O  
ANISOU 3106  O   ARG A1408     6859   6397   6226      2    -95   -327       O  
ATOM   3107  CB  ARG A1408       6.635 -13.384  81.655  1.00 49.11           C  
ANISOU 3107  CB  ARG A1408     6725   6137   5797   -141   -228   -327       C  
ATOM   3108  CG  ARG A1408       7.524 -13.800  80.504  1.00 53.59           C  
ANISOU 3108  CG  ARG A1408     7158   6742   6462   -204   -277   -304       C  
ATOM   3109  CD  ARG A1408       8.182 -12.608  79.844  1.00 58.40           C  
ANISOU 3109  CD  ARG A1408     7833   7302   7053   -276   -326   -327       C  
ATOM   3110  NE  ARG A1408       9.077 -13.030  78.773  1.00 66.69           N  
ANISOU 3110  NE  ARG A1408     8743   8409   8188   -323   -365   -290       N  
ATOM   3111  CZ  ARG A1408       9.693 -12.197  77.941  1.00 73.30           C  
ANISOU 3111  CZ  ARG A1408     9586   9231   9033   -387   -405   -288       C  
ATOM   3112  NH1 ARG A1408       9.510 -10.888  78.056  1.00 78.36           N  
ANISOU 3112  NH1 ARG A1408    10384   9786   9603   -424   -422   -328       N  
ATOM   3113  NH2 ARG A1408      10.489 -12.672  76.993  1.00 71.37           N  
ANISOU 3113  NH2 ARG A1408     9203   9056   8859   -408   -427   -242       N  
ATOM   3114  N   ALA A1409       3.922 -14.517  80.446  1.00 45.18           N  
ANISOU 3114  N   ALA A1409     6028   5709   5430     59    -54   -265       N  
ATOM   3115  CA  ALA A1409       3.247 -15.267  79.391  1.00 45.06           C  
ANISOU 3115  CA  ALA A1409     5881   5730   5509     77    -31   -224       C  
ATOM   3116  C   ALA A1409       2.137 -14.443  78.751  1.00 47.02           C  
ANISOU 3116  C   ALA A1409     6141   5970   5756    154     39   -216       C  
ATOM   3117  O   ALA A1409       1.933 -14.508  77.533  1.00 46.41           O  
ANISOU 3117  O   ALA A1409     5993   5890   5750    143     35   -208       O  
ATOM   3118  CB  ALA A1409       2.691 -16.583  79.936  1.00 39.01           C  
ANISOU 3118  CB  ALA A1409     5033   5028   4763     86    -24   -160       C  
ATOM   3119  N   MET A1410       1.433 -13.633  79.544  1.00 46.22           N  
ANISOU 3119  N   MET A1410     6136   5862   5562    243    106   -214       N  
ATOM   3120  CA  MET A1410       0.380 -12.798  78.976  1.00 47.09           C  
ANISOU 3120  CA  MET A1410     6259   5973   5660    341    184   -194       C  
ATOM   3121  C   MET A1410       0.960 -11.698  78.095  1.00 45.97           C  
ANISOU 3121  C   MET A1410     6201   5744   5524    316    159   -261       C  
ATOM   3122  O   MET A1410       0.473 -11.460  76.984  1.00 46.23           O  
ANISOU 3122  O   MET A1410     6170   5781   5612    336    180   -244       O  
ATOM   3123  CB  MET A1410      -0.483 -12.197  80.087  1.00 52.76           C  
ANISOU 3123  CB  MET A1410     7078   6708   6259    475    277   -167       C  
ATOM   3124  CG  MET A1410      -1.349 -13.216  80.808  1.00 65.24           C  
ANISOU 3124  CG  MET A1410     8546   8404   7838    516    320    -70       C  
ATOM   3125  SD  MET A1410      -2.253 -12.512  82.204  1.00 74.25           S  
ANISOU 3125  SD  MET A1410     9814   9579   8819    698    442    -30       S  
ATOM   3126  CE  MET A1410      -3.018 -11.103  81.399  1.00 77.70           C  
ANISOU 3126  CE  MET A1410    10327   9981   9215    841    532    -28       C  
ATOM   3127  N   SER A1411       1.993 -11.000  78.574  1.00 46.88           N  
ANISOU 3127  N   SER A1411     6460   5779   5574    260    106   -327       N  
ATOM   3128  CA  SER A1411       2.539  -9.909  77.775  1.00 47.35           C  
ANISOU 3128  CA  SER A1411     6608   5755   5630    221     72   -378       C  
ATOM   3129  C   SER A1411       3.228 -10.423  76.516  1.00 45.62           C  
ANISOU 3129  C   SER A1411     6246   5559   5527    126     12   -375       C  
ATOM   3130  O   SER A1411       3.193  -9.750  75.478  1.00 45.05           O  
ANISOU 3130  O   SER A1411     6178   5452   5485    125     14   -390       O  
ATOM   3131  CB  SER A1411       3.497  -9.054  78.608  1.00 49.76           C  
ANISOU 3131  CB  SER A1411     7111   5970   5827    154      8   -433       C  
ATOM   3132  OG  SER A1411       4.706  -9.738  78.860  1.00 57.97           O  
ANISOU 3132  OG  SER A1411     8087   7042   6897     22    -87   -429       O  
ATOM   3133  N   PHE A1412       3.847 -11.608  76.577  1.00 43.75           N  
ANISOU 3133  N   PHE A1412     5894   5380   5348     60    -36   -352       N  
ATOM   3134  CA  PHE A1412       4.401 -12.202  75.362  1.00 41.45           C  
ANISOU 3134  CA  PHE A1412     5481   5114   5155      6    -76   -341       C  
ATOM   3135  C   PHE A1412       3.298 -12.546  74.368  1.00 45.96           C  
ANISOU 3135  C   PHE A1412     5964   5708   5790     63    -25   -311       C  
ATOM   3136  O   PHE A1412       3.471 -12.372  73.157  1.00 45.11           O  
ANISOU 3136  O   PHE A1412     5816   5588   5737     44    -38   -318       O  
ATOM   3137  CB  PHE A1412       5.222 -13.446  75.711  1.00 38.00           C  
ANISOU 3137  CB  PHE A1412     4962   4728   4747    -44   -125   -316       C  
ATOM   3138  CG  PHE A1412       5.835 -14.143  74.519  1.00 42.68           C  
ANISOU 3138  CG  PHE A1412     5453   5344   5419    -70   -155   -300       C  
ATOM   3139  CD1 PHE A1412       5.130 -15.113  73.817  1.00 39.75           C  
ANISOU 3139  CD1 PHE A1412     5010   4988   5106    -35   -134   -273       C  
ATOM   3140  CD2 PHE A1412       7.131 -13.848  74.117  1.00 47.65           C  
ANISOU 3140  CD2 PHE A1412     6067   5985   6054   -131   -208   -299       C  
ATOM   3141  CE1 PHE A1412       5.698 -15.763  72.725  1.00 40.59           C  
ANISOU 3141  CE1 PHE A1412     5059   5098   5264    -43   -158   -262       C  
ATOM   3142  CE2 PHE A1412       7.703 -14.494  73.025  1.00 47.04           C  
ANISOU 3142  CE2 PHE A1412     5903   5937   6034   -126   -220   -276       C  
ATOM   3143  CZ  PHE A1412       6.985 -15.453  72.330  1.00 42.49           C  
ANISOU 3143  CZ  PHE A1412     5284   5355   5506    -73   -192   -265       C  
ATOM   3144  N   SER A1413       2.145 -12.986  74.858  1.00 45.86           N  
ANISOU 3144  N   SER A1413     5920   5737   5766    128     28   -265       N  
ATOM   3145  CA  SER A1413       1.065 -13.370  73.961  1.00 43.79           C  
ANISOU 3145  CA  SER A1413     5564   5513   5560    158     59   -212       C  
ATOM   3146  C   SER A1413       0.388 -12.154  73.338  1.00 47.58           C  
ANISOU 3146  C   SER A1413     6082   5970   6025    223    113   -215       C  
ATOM   3147  O   SER A1413      -0.053 -12.208  72.187  1.00 45.80           O  
ANISOU 3147  O   SER A1413     5789   5757   5858    217    113   -191       O  
ATOM   3148  CB  SER A1413       0.043 -14.224  74.697  1.00 42.59           C  
ANISOU 3148  CB  SER A1413     5350   5436   5397    190     91   -133       C  
ATOM   3149  OG  SER A1413       0.637 -15.446  75.094  1.00 46.32           O  
ANISOU 3149  OG  SER A1413     5790   5920   5890    127     35   -126       O  
ATOM   3150  N   GLU A 238       0.395 -11.043  74.118  1.00 48.33           N  
ANISOU 3150  N   GLU A 238     6309   6022   6033    284    152   -250       N  
ATOM   3151  CA  GLU A 238      -0.168  -9.798  73.609  1.00 51.03           C  
ANISOU 3151  CA  GLU A 238     6723   6324   6343    362    206   -257       C  
ATOM   3152  C   GLU A 238       0.653  -9.277  72.428  1.00 45.53           C  
ANISOU 3152  C   GLU A 238     6038   5566   5696    287    151   -308       C  
ATOM   3153  O   GLU A 238       0.095  -8.857  71.417  1.00 47.98           O  
ANISOU 3153  O   GLU A 238     6313   5877   6041    319    177   -290       O  
ATOM   3154  CB  GLU A 238      -0.235  -8.743  74.717  1.00 58.45           C  
ANISOU 3154  CB  GLU A 238     7850   7203   7157    447    251   -290       C  
ATOM   3155  CG  GLU A 238      -1.261  -7.645  74.476  1.00 68.22           C  
ANISOU 3155  CG  GLU A 238     9162   8421   8337    592    344   -266       C  
ATOM   3156  CD  GLU A 238      -2.677  -8.099  74.779  1.00 75.97           C  
ANISOU 3156  CD  GLU A 238    10031   9525   9310    719    441   -157       C  
ATOM   3157  OE1 GLU A 238      -3.628  -7.506  74.222  1.00 78.31           O  
ANISOU 3157  OE1 GLU A 238    10303   9853   9597    830    515   -100       O  
ATOM   3158  OE2 GLU A 238      -2.838  -9.048  75.576  1.00 77.60           O  
ANISOU 3158  OE2 GLU A 238    10164   9805   9514    706    441   -114       O  
ATOM   3159  N   GLN A 239       1.981  -9.302  72.567  1.00 44.78           N  
ANISOU 3159  N   GLN A 239     5984   5431   5600    186     75   -358       N  
ATOM   3160  CA  GLN A 239       2.846  -8.867  71.475  1.00 46.64           C  
ANISOU 3160  CA  GLN A 239     6211   5630   5878    109     22   -386       C  
ATOM   3161  C   GLN A 239       2.684  -9.753  70.247  1.00 44.92           C  
ANISOU 3161  C   GLN A 239     5846   5464   5759     92     14   -356       C  
ATOM   3162  O   GLN A 239       2.691  -9.261  69.108  1.00 51.20           O  
ANISOU 3162  O   GLN A 239     6625   6239   6590     84     12   -362       O  
ATOM   3163  CB  GLN A 239       4.305  -8.862  71.934  1.00 48.03           C  
ANISOU 3163  CB  GLN A 239     6427   5790   6031      1    -61   -412       C  
ATOM   3164  CG  GLN A 239       4.580  -7.989  73.143  1.00 60.35           C  
ANISOU 3164  CG  GLN A 239     8166   7286   7481    -12    -79   -442       C  
ATOM   3165  CD  GLN A 239       5.983  -8.185  73.691  1.00 69.43           C  
ANISOU 3165  CD  GLN A 239     9324   8448   8607   -139   -173   -441       C  
ATOM   3166  OE1 GLN A 239       6.937  -8.364  72.935  1.00 75.54           O  
ANISOU 3166  OE1 GLN A 239    10009   9260   9435   -221   -229   -420       O  
ATOM   3167  NE2 GLN A 239       6.111  -8.171  75.012  1.00 70.87           N  
ANISOU 3167  NE2 GLN A 239     9609   8613   8706   -149   -190   -450       N  
ATOM   3168  N   VAL A 240       2.505 -11.061  70.460  1.00 43.96           N  
ANISOU 3168  N   VAL A 240     5633   5398   5672     85      6   -321       N  
ATOM   3169  CA  VAL A 240       2.379 -11.986  69.337  1.00 43.59           C  
ANISOU 3169  CA  VAL A 240     5488   5378   5698     63    -14   -294       C  
ATOM   3170  C   VAL A 240       1.107 -11.706  68.550  1.00 42.53           C  
ANISOU 3170  C   VAL A 240     5316   5257   5586    108     27   -256       C  
ATOM   3171  O   VAL A 240       1.131 -11.667  67.315  1.00 41.02           O  
ANISOU 3171  O   VAL A 240     5094   5054   5439     89     12   -256       O  
ATOM   3172  CB  VAL A 240       2.427 -13.448  69.823  1.00 43.15           C  
ANISOU 3172  CB  VAL A 240     5380   5359   5656     43    -39   -263       C  
ATOM   3173  CG1 VAL A 240       1.975 -14.405  68.705  1.00 35.70           C  
ANISOU 3173  CG1 VAL A 240     4378   4423   4765     26    -61   -228       C  
ATOM   3174  CG2 VAL A 240       3.830 -13.803  70.290  1.00 39.42           C  
ANISOU 3174  CG2 VAL A 240     4921   4885   5171      3    -84   -289       C  
ATOM   3175  N   SER A 241      -0.013 -11.476  69.244  1.00 42.55           N  
ANISOU 3175  N   SER A 241     5318   5294   5554    174     83   -211       N  
ATOM   3176  CA  SER A 241      -1.272 -11.217  68.546  1.00 47.15           C  
ANISOU 3176  CA  SER A 241     5843   5919   6155    221    124   -146       C  
ATOM   3177  C   SER A 241      -1.212  -9.916  67.754  1.00 46.60           C  
ANISOU 3177  C   SER A 241     5827   5797   6080    256    148   -180       C  
ATOM   3178  O   SER A 241      -1.691  -9.849  66.611  1.00 45.85           O  
ANISOU 3178  O   SER A 241     5677   5717   6029    249    145   -150       O  
ATOM   3179  CB  SER A 241      -2.431 -11.158  69.541  1.00 49.50           C  
ANISOU 3179  CB  SER A 241     6118   6288   6402    308    192    -69       C  
ATOM   3180  OG  SER A 241      -2.457 -12.304  70.363  1.00 60.02           O  
ANISOU 3180  OG  SER A 241     7408   7666   7733    270    168    -35       O  
ATOM   3181  N   ALA A 242      -0.622  -8.875  68.346  1.00 41.94           N  
ANISOU 3181  N   ALA A 242     5361   5142   5431    285    164   -241       N  
ATOM   3182  CA  ALA A 242      -0.539  -7.590  67.662  1.00 47.49           C  
ANISOU 3182  CA  ALA A 242     6144   5782   6119    313    180   -273       C  
ATOM   3183  C   ALA A 242       0.336  -7.685  66.416  1.00 44.97           C  
ANISOU 3183  C   ALA A 242     5785   5437   5864    220    117   -305       C  
ATOM   3184  O   ALA A 242      -0.037  -7.191  65.336  1.00 49.63           O  
ANISOU 3184  O   ALA A 242     6354   6019   6483    234    129   -292       O  
ATOM   3185  CB  ALA A 242      -0.003  -6.531  68.627  1.00 38.25           C  
ANISOU 3185  CB  ALA A 242     5151   4527   4856    338    188   -330       C  
ATOM   3186  N   ALA A 243       1.493  -8.346  66.539  1.00 43.73           N  
ANISOU 3186  N   ALA A 243     5612   5279   5725    135     56   -335       N  
ATOM   3187  CA  ALA A 243       2.340  -8.548  65.371  1.00 41.55           C  
ANISOU 3187  CA  ALA A 243     5289   4999   5501     70     10   -349       C  
ATOM   3188  C   ALA A 243       1.640  -9.401  64.323  1.00 44.66           C  
ANISOU 3188  C   ALA A 243     5588   5429   5951     76     11   -309       C  
ATOM   3189  O   ALA A 243       1.791  -9.158  63.121  1.00 48.04           O  
ANISOU 3189  O   ALA A 243     5997   5845   6410     60      0   -313       O  
ATOM   3190  CB  ALA A 243       3.665  -9.189  65.783  1.00 39.00           C  
ANISOU 3190  CB  ALA A 243     4951   4691   5175      4    -43   -364       C  
ATOM   3191  N   ARG A 244       0.844 -10.386  64.754  1.00 43.79           N  
ANISOU 3191  N   ARG A 244     5428   5363   5847     89     18   -265       N  
ATOM   3192  CA  ARG A 244       0.131 -11.218  63.787  1.00 42.70           C  
ANISOU 3192  CA  ARG A 244     5225   5251   5749     69     -2   -217       C  
ATOM   3193  C   ARG A 244      -0.879 -10.399  62.999  1.00 41.21           C  
ANISOU 3193  C   ARG A 244     5013   5074   5571    103     30   -179       C  
ATOM   3194  O   ARG A 244      -1.083 -10.638  61.803  1.00 37.71           O  
ANISOU 3194  O   ARG A 244     4541   4628   5159     71      3   -161       O  
ATOM   3195  CB  ARG A 244      -0.579 -12.375  64.490  1.00 40.31           C  
ANISOU 3195  CB  ARG A 244     4880   4993   5441     56    -14   -159       C  
ATOM   3196  CG  ARG A 244       0.318 -13.527  64.899  1.00 42.38           C  
ANISOU 3196  CG  ARG A 244     5161   5239   5701     17    -59   -183       C  
ATOM   3197  CD  ARG A 244      -0.218 -14.836  64.350  1.00 46.59           C  
ANISOU 3197  CD  ARG A 244     5679   5774   6248    -33   -111   -132       C  
ATOM   3198  NE  ARG A 244      -1.171 -15.452  65.257  1.00 50.46           N  
ANISOU 3198  NE  ARG A 244     6132   6316   6725    -49   -113    -59       N  
ATOM   3199  CZ  ARG A 244      -2.055 -16.385  64.918  1.00 45.25           C  
ANISOU 3199  CZ  ARG A 244     5451   5675   6068   -113   -164     20       C  
ATOM   3200  NH1 ARG A 244      -2.138 -16.816  63.669  1.00 37.73           N  
ANISOU 3200  NH1 ARG A 244     4530   4679   5125   -165   -218     27       N  
ATOM   3201  NH2 ARG A 244      -2.865 -16.885  65.843  1.00 45.80           N  
ANISOU 3201  NH2 ARG A 244     5473   5808   6121   -133   -165    100       N  
ATOM   3202  N   LYS A 245      -1.505  -9.416  63.648  1.00 41.37           N  
ANISOU 3202  N   LYS A 245     5058   5105   5556    177     91   -163       N  
ATOM   3203  CA  LYS A 245      -2.464  -8.574  62.934  1.00 49.48           C  
ANISOU 3203  CA  LYS A 245     6063   6151   6587    232    132   -116       C  
ATOM   3204  C   LYS A 245      -1.767  -7.692  61.904  1.00 49.03           C  
ANISOU 3204  C   LYS A 245     6056   6028   6545    215    118   -173       C  
ATOM   3205  O   LYS A 245      -2.228  -7.575  60.755  1.00 47.25           O  
ANISOU 3205  O   LYS A 245     5786   5816   6352    205    110   -141       O  
ATOM   3206  CB  LYS A 245      -3.253  -7.713  63.921  1.00 55.86           C  
ANISOU 3206  CB  LYS A 245     6907   6982   7334    349    214    -81       C  
ATOM   3207  CG  LYS A 245      -4.323  -8.471  64.680  1.00 65.36           C  
ANISOU 3207  CG  LYS A 245     8021   8289   8524    384    243     20       C  
ATOM   3208  CD  LYS A 245      -5.059  -7.557  65.650  1.00 76.01           C  
ANISOU 3208  CD  LYS A 245     9419   9667   9796    534    342     60       C  
ATOM   3209  CE  LYS A 245      -5.765  -6.417  64.925  1.00 82.76           C  
ANISOU 3209  CE  LYS A 245    10283  10525  10635    635    402    101       C  
ATOM   3210  NZ  LYS A 245      -6.576  -5.587  65.868  1.00 86.75           N  
ANISOU 3210  NZ  LYS A 245    10847  11065  11049    816    515    156       N  
ATOM   3211  N   VAL A 246      -0.644  -7.079  62.288  1.00 46.98           N  
ANISOU 3211  N   VAL A 246     5887   5704   6261    198    107   -247       N  
ATOM   3212  CA  VAL A 246       0.077  -6.248  61.321  1.00 44.92           C  
ANISOU 3212  CA  VAL A 246     5667   5390   6012    166     86   -287       C  
ATOM   3213  C   VAL A 246       0.580  -7.096  60.151  1.00 42.95           C  
ANISOU 3213  C   VAL A 246     5345   5159   5814    100     38   -286       C  
ATOM   3214  O   VAL A 246       0.505  -6.687  58.977  1.00 46.60           O  
ANISOU 3214  O   VAL A 246     5794   5610   6299     93     34   -281       O  
ATOM   3215  CB  VAL A 246       1.225  -5.494  62.020  1.00 46.29           C  
ANISOU 3215  CB  VAL A 246     5948   5502   6140    131     64   -344       C  
ATOM   3216  CG1 VAL A 246       2.054  -4.730  61.010  1.00 47.45           C  
ANISOU 3216  CG1 VAL A 246     6121   5609   6300     75     30   -367       C  
ATOM   3217  CG2 VAL A 246       0.668  -4.544  63.086  1.00 45.52           C  
ANISOU 3217  CG2 VAL A 246     5971   5357   5967    210    112   -351       C  
ATOM   3218  N   VAL A 247       1.058  -8.308  60.444  1.00 39.26           N  
ANISOU 3218  N   VAL A 247     4844   4715   5356     64      6   -289       N  
ATOM   3219  CA  VAL A 247       1.588  -9.161  59.388  1.00 38.75           C  
ANISOU 3219  CA  VAL A 247     4749   4656   5319     27    -32   -290       C  
ATOM   3220  C   VAL A 247       0.473  -9.644  58.475  1.00 40.97           C  
ANISOU 3220  C   VAL A 247     4994   4952   5621     23    -42   -243       C  
ATOM   3221  O   VAL A 247       0.654  -9.729  57.254  1.00 42.33           O  
ANISOU 3221  O   VAL A 247     5168   5110   5807      6    -62   -245       O  
ATOM   3222  CB  VAL A 247       2.391 -10.327  59.991  1.00 36.89           C  
ANISOU 3222  CB  VAL A 247     4510   4433   5074      9    -60   -300       C  
ATOM   3223  CG1 VAL A 247       2.684 -11.387  58.939  1.00 34.30           C  
ANISOU 3223  CG1 VAL A 247     4180   4099   4754      1    -90   -293       C  
ATOM   3224  CG2 VAL A 247       3.697  -9.799  60.563  1.00 36.69           C  
ANISOU 3224  CG2 VAL A 247     4504   4409   5028     -7    -66   -330       C  
ATOM   3225  N   LYS A 248      -0.707  -9.931  59.033  1.00 37.49           N  
ANISOU 3225  N   LYS A 248     4519   4548   5178     35    -30   -187       N  
ATOM   3226  CA  LYS A 248      -1.827 -10.315  58.183  1.00 40.11           C  
ANISOU 3226  CA  LYS A 248     4805   4909   5524      9    -53   -117       C  
ATOM   3227  C   LYS A 248      -2.207  -9.177  57.246  1.00 41.90           C  
ANISOU 3227  C   LYS A 248     5022   5134   5764     36    -28   -106       C  
ATOM   3228  O   LYS A 248      -2.514  -9.406  56.064  1.00 41.25           O  
ANISOU 3228  O   LYS A 248     4928   5050   5695     -2    -63    -80       O  
ATOM   3229  CB  LYS A 248      -3.026 -10.713  59.040  1.00 43.87           C  
ANISOU 3229  CB  LYS A 248     5222   5455   5990     15    -43    -30       C  
ATOM   3230  CG  LYS A 248      -4.308 -10.933  58.248  1.00 51.41           C  
ANISOU 3230  CG  LYS A 248     6108   6469   6956    -23    -71     76       C  
ATOM   3231  CD  LYS A 248      -5.503 -11.024  59.181  1.00 55.82           C  
ANISOU 3231  CD  LYS A 248     6580   7130   7499      3    -41    188       C  
ATOM   3232  CE  LYS A 248      -6.809 -11.098  58.409  1.00 58.02           C  
ANISOU 3232  CE  LYS A 248     6764   7496   7785    -39    -70    324       C  
ATOM   3233  NZ  LYS A 248      -7.967 -10.857  59.314  1.00 60.19           N  
ANISOU 3233  NZ  LYS A 248     6930   7900   8039     26    -12    453       N  
ATOM   3234  N   MET A 249      -2.139  -7.937  57.739  1.00 39.72           N  
ANISOU 3234  N   MET A 249     4771   4846   5474    101     29   -128       N  
ATOM   3235  CA  MET A 249      -2.456  -6.807  56.872  1.00 43.11           C  
ANISOU 3235  CA  MET A 249     5207   5262   5910    135     54   -118       C  
ATOM   3236  C   MET A 249      -1.468  -6.710  55.714  1.00 41.59           C  
ANISOU 3236  C   MET A 249     5043   5023   5736     85     18   -171       C  
ATOM   3237  O   MET A 249      -1.864  -6.552  54.548  1.00 37.99           O  
ANISOU 3237  O   MET A 249     4565   4573   5297     72      5   -143       O  
ATOM   3238  CB  MET A 249      -2.465  -5.509  57.678  1.00 44.75           C  
ANISOU 3238  CB  MET A 249     5483   5439   6081    218    116   -140       C  
ATOM   3239  CG  MET A 249      -2.896  -4.302  56.866  1.00 42.86           C  
ANISOU 3239  CG  MET A 249     5267   5178   5840    268    148   -122       C  
ATOM   3240  SD  MET A 249      -2.873  -2.779  57.823  1.00 44.19           S  
ANISOU 3240  SD  MET A 249     5577   5274   5939    375    215   -153       S  
ATOM   3241  CE  MET A 249      -1.109  -2.550  58.054  1.00 40.82           C  
ANISOU 3241  CE  MET A 249     5252   4758   5501    273    155   -256       C  
ATOM   3242  N   MET A 250      -0.172  -6.805  56.013  1.00 34.72           N  
ANISOU 3242  N   MET A 250     4214   4119   4857     60      3   -233       N  
ATOM   3243  CA  MET A 250       0.797  -6.696  54.923  1.00 34.45           C  
ANISOU 3243  CA  MET A 250     4192   4065   4833     28    -21   -263       C  
ATOM   3244  C   MET A 250       0.714  -7.879  53.963  1.00 40.28           C  
ANISOU 3244  C   MET A 250     4913   4813   5578      1    -58   -246       C  
ATOM   3245  O   MET A 250       0.979  -7.729  52.759  1.00 41.56           O  
ANISOU 3245  O   MET A 250     5083   4965   5744     -8    -69   -249       O  
ATOM   3246  CB  MET A 250       2.204  -6.540  55.482  1.00 34.39           C  
ANISOU 3246  CB  MET A 250     4211   4048   4809      6    -30   -304       C  
ATOM   3247  CG  MET A 250       2.358  -5.306  56.370  1.00 41.44           C  
ANISOU 3247  CG  MET A 250     5163   4906   5676     10    -13   -322       C  
ATOM   3248  SD  MET A 250       1.522  -3.822  55.726  1.00 45.55           S  
ANISOU 3248  SD  MET A 250     5731   5383   6194     47     18   -309       S  
ATOM   3249  CE  MET A 250       2.369  -3.588  54.156  1.00 48.68           C  
ANISOU 3249  CE  MET A 250     6100   5783   6613     -4    -11   -309       C  
ATOM   3250  N   ILE A 251       0.331  -9.055  54.456  1.00 37.68           N  
ANISOU 3250  N   ILE A 251     4580   4496   5242    -13    -82   -228       N  
ATOM   3251  CA  ILE A 251       0.162 -10.179  53.546  1.00 39.06           C  
ANISOU 3251  CA  ILE A 251     4783   4656   5404    -45   -130   -211       C  
ATOM   3252  C   ILE A 251      -1.009  -9.924  52.608  1.00 40.28           C  
ANISOU 3252  C   ILE A 251     4916   4821   5568    -74   -151   -156       C  
ATOM   3253  O   ILE A 251      -0.946 -10.247  51.413  1.00 38.78           O  
ANISOU 3253  O   ILE A 251     4767   4604   5363    -98   -185   -154       O  
ATOM   3254  CB  ILE A 251      -0.015 -11.489  54.336  1.00 41.88           C  
ANISOU 3254  CB  ILE A 251     5160   5009   5742    -67   -163   -196       C  
ATOM   3255  CG1 ILE A 251       1.293 -11.877  55.029  1.00 40.92           C  
ANISOU 3255  CG1 ILE A 251     5064   4880   5605    -33   -148   -245       C  
ATOM   3256  CG2 ILE A 251      -0.488 -12.601  53.422  1.00 34.93           C  
ANISOU 3256  CG2 ILE A 251     4344   4094   4834   -117   -229   -166       C  
ATOM   3257  CD1 ILE A 251       1.151 -13.034  55.998  1.00 39.18           C  
ANISOU 3257  CD1 ILE A 251     4863   4655   5366    -47   -172   -232       C  
ATOM   3258  N   VAL A 252      -2.088  -9.328  53.123  1.00 34.93           N  
ANISOU 3258  N   VAL A 252     4175   4189   4906    -64   -128   -100       N  
ATOM   3259  CA  VAL A 252      -3.207  -8.990  52.247  1.00 36.71           C  
ANISOU 3259  CA  VAL A 252     4358   4447   5141    -86   -144    -27       C  
ATOM   3260  C   VAL A 252      -2.767  -7.963  51.207  1.00 39.34           C  
ANISOU 3260  C   VAL A 252     4709   4753   5484    -61   -122    -60       C  
ATOM   3261  O   VAL A 252      -3.135  -8.052  50.027  1.00 42.11           O  
ANISOU 3261  O   VAL A 252     5066   5102   5833    -98   -159    -31       O  
ATOM   3262  CB  VAL A 252      -4.408  -8.491  53.074  1.00 41.10           C  
ANISOU 3262  CB  VAL A 252     4831   5082   5705    -49   -105     59       C  
ATOM   3263  CG1 VAL A 252      -5.514  -7.951  52.159  1.00 39.40           C  
ANISOU 3263  CG1 VAL A 252     4551   4920   5498    -54   -111    152       C  
ATOM   3264  CG2 VAL A 252      -4.948  -9.605  53.973  1.00 39.27           C  
ANISOU 3264  CG2 VAL A 252     4568   4893   5461    -91   -137    115       C  
ATOM   3265  N   VAL A 253      -1.904  -7.022  51.611  1.00 36.10           N  
ANISOU 3265  N   VAL A 253     4320   4317   5079    -11    -73   -120       N  
ATOM   3266  CA  VAL A 253      -1.396  -6.021  50.670  1.00 40.86           C  
ANISOU 3266  CA  VAL A 253     4943   4894   5689      1    -57   -147       C  
ATOM   3267  C   VAL A 253      -0.631  -6.695  49.531  1.00 39.66           C  
ANISOU 3267  C   VAL A 253     4825   4719   5523    -33    -95   -173       C  
ATOM   3268  O   VAL A 253      -0.872  -6.429  48.341  1.00 37.13           O  
ANISOU 3268  O   VAL A 253     4510   4394   5202    -46   -109   -155       O  
ATOM   3269  CB  VAL A 253      -0.507  -4.999  51.403  1.00 34.63           C  
ANISOU 3269  CB  VAL A 253     4188   4074   4894     31    -19   -197       C  
ATOM   3270  CG1 VAL A 253       0.350  -4.222  50.404  1.00 34.54           C  
ANISOU 3270  CG1 VAL A 253     4201   4038   4885     16    -22   -221       C  
ATOM   3271  CG2 VAL A 253      -1.353  -4.049  52.257  1.00 35.04           C  
ANISOU 3271  CG2 VAL A 253     4248   4127   4939     92     28   -171       C  
ATOM   3272  N   VAL A 254       0.296  -7.589  49.883  1.00 36.63           N  
ANISOU 3272  N   VAL A 254     4474   4324   5121    -35   -106   -210       N  
ATOM   3273  CA  VAL A 254       1.151  -8.192  48.867  1.00 37.22           C  
ANISOU 3273  CA  VAL A 254     4596   4379   5164    -31   -122   -231       C  
ATOM   3274  C   VAL A 254       0.355  -9.141  47.974  1.00 40.46           C  
ANISOU 3274  C   VAL A 254     5061   4764   5546    -66   -176   -202       C  
ATOM   3275  O   VAL A 254       0.586  -9.206  46.761  1.00 42.22           O  
ANISOU 3275  O   VAL A 254     5333   4967   5742    -62   -189   -206       O  
ATOM   3276  CB  VAL A 254       2.351  -8.892  49.525  1.00 40.21           C  
ANISOU 3276  CB  VAL A 254     4994   4763   5520      0   -111   -262       C  
ATOM   3277  CG1 VAL A 254       3.282  -9.438  48.457  1.00 41.22           C  
ANISOU 3277  CG1 VAL A 254     5173   4885   5603     40   -108   -271       C  
ATOM   3278  CG2 VAL A 254       3.095  -7.914  50.404  1.00 50.40           C  
ANISOU 3278  CG2 VAL A 254     6238   6082   6832      4    -79   -277       C  
ATOM   3279  N   CYS A 255      -0.593  -9.891  48.546  1.00 39.68           N  
ANISOU 3279  N   CYS A 255     4963   4668   5446   -109   -216   -166       N  
ATOM   3280  CA  CYS A 255      -1.406 -10.771  47.715  1.00 40.15           C  
ANISOU 3280  CA  CYS A 255     5087   4699   5469   -175   -291   -123       C  
ATOM   3281  C   CYS A 255      -2.274  -9.970  46.752  1.00 40.38           C  
ANISOU 3281  C   CYS A 255     5075   4754   5515   -208   -306    -72       C  
ATOM   3282  O   CYS A 255      -2.487 -10.387  45.606  1.00 36.99           O  
ANISOU 3282  O   CYS A 255     4721   4289   5044   -251   -360    -57       O  
ATOM   3283  CB  CYS A 255      -2.274 -11.679  48.587  1.00 45.35           C  
ANISOU 3283  CB  CYS A 255     5740   5368   6121   -237   -342    -71       C  
ATOM   3284  SG  CYS A 255      -1.363 -12.965  49.507  1.00 48.67           S  
ANISOU 3284  SG  CYS A 255     6249   5739   6504   -212   -349   -122       S  
ATOM   3285  N   THR A 256      -2.763  -8.806  47.189  1.00 39.30           N  
ANISOU 3285  N   THR A 256     4833   4672   5427   -181   -257    -43       N  
ATOM   3286  CA  THR A 256      -3.566  -7.974  46.301  1.00 42.38           C  
ANISOU 3286  CA  THR A 256     5176   5092   5832   -195   -262     13       C  
ATOM   3287  C   THR A 256      -2.728  -7.438  45.144  1.00 39.17           C  
ANISOU 3287  C   THR A 256     4819   4648   5415   -170   -246    -38       C  
ATOM   3288  O   THR A 256      -3.173  -7.454  43.989  1.00 39.83           O  
ANISOU 3288  O   THR A 256     4928   4726   5479   -210   -287     -4       O  
ATOM   3289  CB  THR A 256      -4.193  -6.838  47.111  1.00 41.22           C  
ANISOU 3289  CB  THR A 256     4932   5004   5727   -138   -198     53       C  
ATOM   3290  OG1 THR A 256      -5.101  -7.399  48.066  1.00 39.25           O  
ANISOU 3290  OG1 THR A 256     4624   4811   5478   -158   -212    124       O  
ATOM   3291  CG2 THR A 256      -4.937  -5.859  46.212  1.00 39.14           C  
ANISOU 3291  CG2 THR A 256     4621   4773   5477   -127   -189    114       C  
ATOM   3292  N   PHE A 257      -1.496  -7.009  45.434  1.00 35.45           N  
ANISOU 3292  N   PHE A 257     4362   4158   4950   -113   -192   -108       N  
ATOM   3293  CA  PHE A 257      -0.575  -6.596  44.375  1.00 35.86           C  
ANISOU 3293  CA  PHE A 257     4450   4190   4984    -89   -175   -141       C  
ATOM   3294  C   PHE A 257      -0.323  -7.735  43.388  1.00 39.21           C  
ANISOU 3294  C   PHE A 257     4977   4576   5345   -103   -220   -151       C  
ATOM   3295  O   PHE A 257      -0.362  -7.543  42.158  1.00 38.10           O  
ANISOU 3295  O   PHE A 257     4874   4423   5178   -109   -235   -142       O  
ATOM   3296  CB  PHE A 257       0.733  -6.133  45.021  1.00 34.67           C  
ANISOU 3296  CB  PHE A 257     4284   4047   4843    -45   -124   -189       C  
ATOM   3297  CG  PHE A 257       1.801  -5.713  44.049  1.00 38.49           C  
ANISOU 3297  CG  PHE A 257     4782   4538   5306    -21   -102   -202       C  
ATOM   3298  CD1 PHE A 257       2.691  -6.640  43.522  1.00 34.94           C  
ANISOU 3298  CD1 PHE A 257     4386   4087   4802     17   -100   -217       C  
ATOM   3299  CD2 PHE A 257       1.946  -4.379  43.700  1.00 38.12           C  
ANISOU 3299  CD2 PHE A 257     4698   4500   5284    -26    -80   -191       C  
ATOM   3300  CE1 PHE A 257       3.683  -6.251  42.653  1.00 40.94           C  
ANISOU 3300  CE1 PHE A 257     5143   4877   5537     54    -69   -210       C  
ATOM   3301  CE2 PHE A 257       2.941  -3.980  42.824  1.00 38.34           C  
ANISOU 3301  CE2 PHE A 257     4725   4549   5292    -13    -62   -187       C  
ATOM   3302  CZ  PHE A 257       3.810  -4.916  42.298  1.00 39.35           C  
ANISOU 3302  CZ  PHE A 257     4886   4698   5369     29    -54   -191       C  
ATOM   3303  N   ALA A 258      -0.092  -8.943  43.917  1.00 38.90           N  
ANISOU 3303  N   ALA A 258     5002   4509   5270   -102   -244   -169       N  
ATOM   3304  CA  ALA A 258       0.205 -10.085  43.056  1.00 38.48           C  
ANISOU 3304  CA  ALA A 258     5092   4394   5134    -96   -285   -184       C  
ATOM   3305  C   ALA A 258      -0.968 -10.408  42.140  1.00 39.46           C  
ANISOU 3305  C   ALA A 258     5279   4488   5226   -186   -370   -136       C  
ATOM   3306  O   ALA A 258      -0.785 -10.660  40.939  1.00 41.92           O  
ANISOU 3306  O   ALA A 258     5700   4754   5472   -180   -393   -144       O  
ATOM   3307  CB  ALA A 258       0.569 -11.299  43.915  1.00 38.28           C  
ANISOU 3307  CB  ALA A 258     5138   4334   5073    -78   -299   -207       C  
ATOM   3308  N   ILE A 259      -2.188 -10.356  42.680  1.00 38.89           N  
ANISOU 3308  N   ILE A 259     5133   4450   5193   -270   -416    -71       N  
ATOM   3309  CA  ILE A 259      -3.369 -10.654  41.875  1.00 38.12           C  
ANISOU 3309  CA  ILE A 259     5072   4346   5066   -379   -511      4       C  
ATOM   3310  C   ILE A 259      -3.582  -9.579  40.821  1.00 41.78           C  
ANISOU 3310  C   ILE A 259     5486   4840   5548   -372   -493     25       C  
ATOM   3311  O   ILE A 259      -3.874  -9.880  39.656  1.00 40.52           O  
ANISOU 3311  O   ILE A 259     5424   4643   5330   -426   -558     46       O  
ATOM   3312  CB  ILE A 259      -4.602 -10.796  42.787  1.00 43.69           C  
ANISOU 3312  CB  ILE A 259     5672   5118   5811   -461   -555     97       C  
ATOM   3313  CG1 ILE A 259      -4.525 -12.091  43.599  1.00 48.71           C  
ANISOU 3313  CG1 ILE A 259     6392   5707   6407   -501   -603     89       C  
ATOM   3314  CG2 ILE A 259      -5.889 -10.732  41.976  1.00 41.00           C  
ANISOU 3314  CG2 ILE A 259     5304   4818   5456   -577   -644    210       C  
ATOM   3315  CD1 ILE A 259      -5.451 -12.101  44.804  1.00 51.80           C  
ANISOU 3315  CD1 ILE A 259     6648   6185   6848   -546   -611    173       C  
ATOM   3316  N   CYS A 260      -3.440  -8.310  41.209  1.00 36.71           N  
ANISOU 3316  N   CYS A 260     4711   4258   4979   -308   -411     21       N  
ATOM   3317  CA  CYS A 260      -3.716  -7.224  40.281  1.00 42.31           C  
ANISOU 3317  CA  CYS A 260     5371   4996   5710   -301   -394     50       C  
ATOM   3318  C   CYS A 260      -2.741  -7.211  39.116  1.00 41.97           C  
ANISOU 3318  C   CYS A 260     5427   4903   5616   -264   -381     -7       C  
ATOM   3319  O   CYS A 260      -3.135  -6.888  37.990  1.00 40.62           O  
ANISOU 3319  O   CYS A 260     5277   4732   5423   -295   -412     25       O  
ATOM   3320  CB  CYS A 260      -3.684  -5.883  41.018  1.00 40.27           C  
ANISOU 3320  CB  CYS A 260     4990   4787   5524   -232   -309     51       C  
ATOM   3321  SG  CYS A 260      -5.086  -5.621  42.126  1.00 43.31           S  
ANISOU 3321  SG  CYS A 260     5250   5254   5954   -243   -307    149       S  
ATOM   3322  N   TRP A 261      -1.479  -7.579  39.347  1.00 41.65           N  
ANISOU 3322  N   TRP A 261     5444   4833   5549   -191   -333    -79       N  
ATOM   3323  CA  TRP A 261      -0.499  -7.488  38.275  1.00 37.81           C  
ANISOU 3323  CA  TRP A 261     5030   4326   5010   -132   -302   -115       C  
ATOM   3324  C   TRP A 261      -0.263  -8.791  37.513  1.00 42.43           C  
ANISOU 3324  C   TRP A 261     5802   4836   5485   -124   -349   -136       C  
ATOM   3325  O   TRP A 261       0.339  -8.740  36.435  1.00 43.82           O  
ANISOU 3325  O   TRP A 261     6055   4995   5599    -71   -327   -151       O  
ATOM   3326  CB  TRP A 261       0.831  -6.955  38.814  1.00 36.17           C  
ANISOU 3326  CB  TRP A 261     4760   4155   4829    -46   -214   -154       C  
ATOM   3327  CG  TRP A 261       0.742  -5.492  39.120  1.00 43.83           C  
ANISOU 3327  CG  TRP A 261     5605   5171   5877    -55   -176   -136       C  
ATOM   3328  CD1 TRP A 261       0.596  -4.916  40.351  1.00 43.97           C  
ANISOU 3328  CD1 TRP A 261     5540   5209   5956    -60   -153   -136       C  
ATOM   3329  CD2 TRP A 261       0.748  -4.418  38.170  1.00 39.14           C  
ANISOU 3329  CD2 TRP A 261     4981   4595   5297    -57   -161   -114       C  
ATOM   3330  NE1 TRP A 261       0.530  -3.547  40.225  1.00 43.88           N  
ANISOU 3330  NE1 TRP A 261     5470   5215   5988    -61   -125   -119       N  
ATOM   3331  CE2 TRP A 261       0.621  -3.217  38.897  1.00 40.54           C  
ANISOU 3331  CE2 TRP A 261     5070   4793   5541    -63   -131   -103       C  
ATOM   3332  CE3 TRP A 261       0.859  -4.355  36.775  1.00 39.59           C  
ANISOU 3332  CE3 TRP A 261     5091   4646   5306    -51   -170   -102       C  
ATOM   3333  CZ2 TRP A 261       0.598  -1.966  38.277  1.00 38.17           C  
ANISOU 3333  CZ2 TRP A 261     4737   4501   5264    -67   -113    -80       C  
ATOM   3334  CZ3 TRP A 261       0.838  -3.108  36.159  1.00 37.68           C  
ANISOU 3334  CZ3 TRP A 261     4794   4427   5095    -58   -150    -76       C  
ATOM   3335  CH2 TRP A 261       0.707  -1.933  36.911  1.00 36.75           C  
ANISOU 3335  CH2 TRP A 261     4592   4325   5048    -68   -124    -64       C  
ATOM   3336  N   LEU A 262      -0.716  -9.950  38.011  1.00 38.73           N  
ANISOU 3336  N   LEU A 262     5425   4314   4976   -172   -413   -134       N  
ATOM   3337  CA  LEU A 262      -0.486 -11.177  37.244  1.00 41.05           C  
ANISOU 3337  CA  LEU A 262     5944   4508   5143   -159   -464   -157       C  
ATOM   3338  C   LEU A 262      -1.105 -11.168  35.844  1.00 44.31           C  
ANISOU 3338  C   LEU A 262     6469   4879   5489   -224   -536   -128       C  
ATOM   3339  O   LEU A 262      -0.389 -11.496  34.877  1.00 43.52           O  
ANISOU 3339  O   LEU A 262     6521   4725   5288   -141   -513   -163       O  
ATOM   3340  CB  LEU A 262      -0.967 -12.388  38.053  1.00 39.77           C  
ANISOU 3340  CB  LEU A 262     5877   4286   4948   -223   -539   -151       C  
ATOM   3341  CG  LEU A 262      -0.762 -13.732  37.349  1.00 43.98           C  
ANISOU 3341  CG  LEU A 262     6693   4686   5331   -212   -603   -177       C  
ATOM   3342  CD1 LEU A 262       0.717 -13.950  37.061  1.00 40.29           C  
ANISOU 3342  CD1 LEU A 262     6312   4201   4796    -22   -495   -240       C  
ATOM   3343  CD2 LEU A 262      -1.333 -14.874  38.186  1.00 41.49           C  
ANISOU 3343  CD2 LEU A 262     6473   4305   4987   -302   -693   -160       C  
ATOM   3344  N   PRO A 263      -2.394 -10.858  35.649  1.00 43.50           N  
ANISOU 3344  N   PRO A 263     6305   4801   5421   -361   -621    -56       N  
ATOM   3345  CA  PRO A 263      -2.918 -10.848  34.271  1.00 42.87           C  
ANISOU 3345  CA  PRO A 263     6336   4684   5269   -428   -695    -24       C  
ATOM   3346  C   PRO A 263      -2.191  -9.882  33.349  1.00 44.29           C  
ANISOU 3346  C   PRO A 263     6478   4897   5452   -330   -610    -51       C  
ATOM   3347  O   PRO A 263      -2.011 -10.189  32.167  1.00 42.43           O  
ANISOU 3347  O   PRO A 263     6408   4600   5112   -318   -638    -63       O  
ATOM   3348  CB  PRO A 263      -4.391 -10.466  34.460  1.00 42.46           C  
ANISOU 3348  CB  PRO A 263     6149   4702   5283   -581   -782     83       C  
ATOM   3349  CG  PRO A 263      -4.711 -10.851  35.870  1.00 42.11           C  
ANISOU 3349  CG  PRO A 263     6015   4689   5296   -609   -786    104       C  
ATOM   3350  CD  PRO A 263      -3.455 -10.572  36.631  1.00 43.46           C  
ANISOU 3350  CD  PRO A 263     6135   4868   5509   -456   -656     13       C  
ATOM   3351  N   PHE A 264      -1.741  -8.738  33.868  1.00 45.02           N  
ANISOU 3351  N   PHE A 264     6373   5079   5651   -263   -510    -58       N  
ATOM   3352  CA  PHE A 264      -1.031  -7.746  33.061  1.00 41.23           C  
ANISOU 3352  CA  PHE A 264     5844   4640   5181   -185   -434    -70       C  
ATOM   3353  C   PHE A 264       0.279  -8.308  32.517  1.00 41.82           C  
ANISOU 3353  C   PHE A 264     6054   4680   5156    -56   -371   -124       C  
ATOM   3354  O   PHE A 264       0.557  -8.250  31.306  1.00 42.00           O  
ANISOU 3354  O   PHE A 264     6174   4683   5100    -18   -365   -124       O  
ATOM   3355  CB  PHE A 264      -0.784  -6.511  33.938  1.00 37.88           C  
ANISOU 3355  CB  PHE A 264     5211   4301   4881   -155   -355    -64       C  
ATOM   3356  CG  PHE A 264      -0.197  -5.325  33.219  1.00 38.65           C  
ANISOU 3356  CG  PHE A 264     5239   4445   5003   -107   -292    -58       C  
ATOM   3357  CD1 PHE A 264       1.178  -5.135  33.167  1.00 37.60           C  
ANISOU 3357  CD1 PHE A 264     5095   4341   4850    -10   -210    -87       C  
ATOM   3358  CD2 PHE A 264      -1.021  -4.368  32.654  1.00 39.34           C  
ANISOU 3358  CD2 PHE A 264     5257   4559   5133   -162   -315     -8       C  
ATOM   3359  CE1 PHE A 264       1.720  -4.028  32.530  1.00 41.60           C  
ANISOU 3359  CE1 PHE A 264     5531   4898   5378     15   -161    -66       C  
ATOM   3360  CE2 PHE A 264      -0.489  -3.258  32.021  1.00 42.07           C  
ANISOU 3360  CE2 PHE A 264     5545   4939   5499   -126   -262      1       C  
ATOM   3361  CZ  PHE A 264       0.884  -3.089  31.956  1.00 41.39           C  
ANISOU 3361  CZ  PHE A 264     5456   4879   5394    -45   -189    -29       C  
ATOM   3362  N   HIS A 265       1.095  -8.878  33.406  1.00 44.76           N  
ANISOU 3362  N   HIS A 265     6433   5051   5523     24   -320   -160       N  
ATOM   3363  CA  HIS A 265       2.354  -9.454  32.964  1.00 44.20           C  
ANISOU 3363  CA  HIS A 265     6477   4967   5349    173   -247   -190       C  
ATOM   3364  C   HIS A 265       2.142 -10.684  32.098  1.00 47.90           C  
ANISOU 3364  C   HIS A 265     7224   5314   5663    190   -309   -211       C  
ATOM   3365  O   HIS A 265       2.928 -10.916  31.176  1.00 51.28           O  
ANISOU 3365  O   HIS A 265     7776   5727   5981    315   -254   -222       O  
ATOM   3366  CB  HIS A 265       3.237  -9.764  34.168  1.00 43.45           C  
ANISOU 3366  CB  HIS A 265     6312   4912   5286    253   -182   -209       C  
ATOM   3367  CG  HIS A 265       3.680  -8.539  34.903  1.00 43.10           C  
ANISOU 3367  CG  HIS A 265     6034   4978   5364    244   -121   -188       C  
ATOM   3368  ND1 HIS A 265       4.331  -7.495  34.278  1.00 41.37           N  
ANISOU 3368  ND1 HIS A 265     5717   4838   5165    279    -62   -159       N  
ATOM   3369  CD2 HIS A 265       3.547  -8.178  36.201  1.00 40.45           C  
ANISOU 3369  CD2 HIS A 265     5564   4677   5127    196   -119   -189       C  
ATOM   3370  CE1 HIS A 265       4.590  -6.549  35.164  1.00 41.47           C  
ANISOU 3370  CE1 HIS A 265     5558   4919   5279    243    -35   -143       C  
ATOM   3371  NE2 HIS A 265       4.121  -6.937  36.338  1.00 39.97           N  
ANISOU 3371  NE2 HIS A 265     5350   4701   5136    198    -66   -165       N  
ATOM   3372  N   ILE A 266       1.086 -11.468  32.346  1.00 44.71           N  
ANISOU 3372  N   ILE A 266     6932   4820   5234     65   -426   -208       N  
ATOM   3373  CA  ILE A 266       0.813 -12.591  31.453  1.00 45.96           C  
ANISOU 3373  CA  ILE A 266     7394   4841   5229     53   -510   -223       C  
ATOM   3374  C   ILE A 266       0.442 -12.082  30.068  1.00 47.68           C  
ANISOU 3374  C   ILE A 266     7672   5048   5394     14   -544   -201       C  
ATOM   3375  O   ILE A 266       0.882 -12.631  29.051  1.00 46.70           O  
ANISOU 3375  O   ILE A 266     7783   4843   5119    102   -538   -226       O  
ATOM   3376  CB  ILE A 266      -0.292 -13.501  32.021  1.00 46.47           C  
ANISOU 3376  CB  ILE A 266     7562   4818   5279   -111   -651   -204       C  
ATOM   3377  CG1 ILE A 266       0.196 -14.268  33.251  1.00 48.46           C  
ANISOU 3377  CG1 ILE A 266     7824   5049   5540    -50   -619   -234       C  
ATOM   3378  CG2 ILE A 266      -0.768 -14.485  30.962  1.00 45.60           C  
ANISOU 3378  CG2 ILE A 266     7780   4553   4994   -175   -772   -205       C  
ATOM   3379  CD1 ILE A 266      -0.881 -15.135  33.871  1.00 50.26           C  
ANISOU 3379  CD1 ILE A 266     8136   5203   5758   -221   -759   -202       C  
ATOM   3380  N   PHE A 267      -0.343 -11.005  30.006  1.00 49.19           N  
ANISOU 3380  N   PHE A 267     7662   5324   5704   -102   -573   -151       N  
ATOM   3381  CA  PHE A 267      -0.750 -10.458  28.719  1.00 50.10           C  
ANISOU 3381  CA  PHE A 267     7816   5440   5780   -148   -609   -121       C  
ATOM   3382  C   PHE A 267       0.461 -10.002  27.923  1.00 47.54           C  
ANISOU 3382  C   PHE A 267     7505   5153   5404     25   -486   -148       C  
ATOM   3383  O   PHE A 267       0.520 -10.195  26.705  1.00 46.99           O  
ANISOU 3383  O   PHE A 267     7613   5029   5213     53   -505   -151       O  
ATOM   3384  CB  PHE A 267      -1.726  -9.297  28.942  1.00 48.83           C  
ANISOU 3384  CB  PHE A 267     7409   5381   5766   -273   -640    -53       C  
ATOM   3385  CG  PHE A 267      -2.183  -8.615  27.675  1.00 50.53           C  
ANISOU 3385  CG  PHE A 267     7631   5612   5956   -323   -675    -12       C  
ATOM   3386  CD1 PHE A 267      -1.450  -7.570  27.122  1.00 47.81           C  
ANISOU 3386  CD1 PHE A 267     7183   5337   5645   -224   -572    -19       C  
ATOM   3387  CD2 PHE A 267      -3.362  -8.998  27.057  1.00 53.61           C  
ANISOU 3387  CD2 PHE A 267     8123   5956   6290   -484   -821     48       C  
ATOM   3388  CE1 PHE A 267      -1.876  -6.939  25.967  1.00 51.24           C  
ANISOU 3388  CE1 PHE A 267     7624   5787   6058   -269   -605     21       C  
ATOM   3389  CE2 PHE A 267      -3.794  -8.370  25.899  1.00 52.82           C  
ANISOU 3389  CE2 PHE A 267     8026   5876   6166   -534   -858     92       C  
ATOM   3390  CZ  PHE A 267      -3.050  -7.340  25.352  1.00 52.11           C  
ANISOU 3390  CZ  PHE A 267     7838   5849   6111   -420   -745     74       C  
ATOM   3391  N   PHE A 268       1.455  -9.423  28.597  1.00 48.48           N  
ANISOU 3391  N   PHE A 268     7445   5371   5605    139   -362   -158       N  
ATOM   3392  CA  PHE A 268       2.620  -8.951  27.854  1.00 47.67           C  
ANISOU 3392  CA  PHE A 268     7325   5333   5455    292   -247   -156       C  
ATOM   3393  C   PHE A 268       3.728  -9.993  27.690  1.00 51.13           C  
ANISOU 3393  C   PHE A 268     7948   5733   5747    481   -170   -186       C  
ATOM   3394  O   PHE A 268       4.633  -9.783  26.877  1.00 43.88           O  
ANISOU 3394  O   PHE A 268     7054   4867   4751    624    -78   -169       O  
ATOM   3395  CB  PHE A 268       3.164  -7.672  28.496  1.00 46.59           C  
ANISOU 3395  CB  PHE A 268     6902   5335   5466    303   -163   -127       C  
ATOM   3396  CG  PHE A 268       2.336  -6.458  28.168  1.00 48.13           C  
ANISOU 3396  CG  PHE A 268     6956   5570   5761    181   -204    -89       C  
ATOM   3397  CD1 PHE A 268       2.426  -5.864  26.914  1.00 47.12           C  
ANISOU 3397  CD1 PHE A 268     6850   5463   5589    197   -190    -63       C  
ATOM   3398  CD2 PHE A 268       1.431  -5.944  29.085  1.00 44.86           C  
ANISOU 3398  CD2 PHE A 268     6401   5171   5473     63   -253    -74       C  
ATOM   3399  CE1 PHE A 268       1.651  -4.763  26.591  1.00 46.93           C  
ANISOU 3399  CE1 PHE A 268     6707   5472   5651     94   -227    -23       C  
ATOM   3400  CE2 PHE A 268       0.651  -4.841  28.765  1.00 45.81           C  
ANISOU 3400  CE2 PHE A 268     6407   5327   5673    -23   -281    -31       C  
ATOM   3401  CZ  PHE A 268       0.762  -4.251  27.514  1.00 45.64           C  
ANISOU 3401  CZ  PHE A 268     6407   5322   5611    -10   -271     -6       C  
ATOM   3402  N   LEU A 269       3.684 -11.109  28.418  1.00 51.80           N  
ANISOU 3402  N   LEU A 269     8165   5732   5783    498   -202   -220       N  
ATOM   3403  CA  LEU A 269       4.656 -12.176  28.213  1.00 57.23           C  
ANISOU 3403  CA  LEU A 269     9066   6366   6312    697   -130   -245       C  
ATOM   3404  C   LEU A 269       4.149 -13.281  27.299  1.00 62.40           C  
ANISOU 3404  C   LEU A 269    10093   6840   6777    697   -219   -280       C  
ATOM   3405  O   LEU A 269       4.961 -14.043  26.764  1.00 62.26           O  
ANISOU 3405  O   LEU A 269    10299   6766   6590    895   -147   -296       O  
ATOM   3406  CB  LEU A 269       5.074 -12.789  29.555  1.00 56.51           C  
ANISOU 3406  CB  LEU A 269     8927   6283   6262    743   -101   -260       C  
ATOM   3407  CG  LEU A 269       5.867 -11.875  30.494  1.00 56.04           C  
ANISOU 3407  CG  LEU A 269     8548   6396   6350    778     -4   -224       C  
ATOM   3408  CD1 LEU A 269       5.982 -12.506  31.867  1.00 53.96           C  
ANISOU 3408  CD1 LEU A 269     8250   6120   6134    776     -9   -242       C  
ATOM   3409  CD2 LEU A 269       7.246 -11.575  29.923  1.00 55.56           C  
ANISOU 3409  CD2 LEU A 269     8430   6456   6225    979    138   -176       C  
ATOM   3410  N   LEU A 270       2.839 -13.352  27.080  1.00 67.23           N  
ANISOU 3410  N   LEU A 270    10779   7363   7403    484   -372   -279       N  
ATOM   3411  CA  LEU A 270       2.265 -14.366  26.200  1.00 71.82           C  
ANISOU 3411  CA  LEU A 270    11731   7762   7797    438   -488   -302       C  
ATOM   3412  C   LEU A 270       2.864 -14.389  24.801  1.00 71.65           C  
ANISOU 3412  C   LEU A 270    11912   7705   7608    593   -427   -312       C  
ATOM   3413  O   LEU A 270       3.088 -15.492  24.282  1.00 75.79           O  
ANISOU 3413  O   LEU A 270    12800   8072   7926    694   -446   -349       O  
ATOM   3414  CB  LEU A 270       0.742 -14.193  26.131  1.00 74.83           C  
ANISOU 3414  CB  LEU A 270    12089   8102   8239    157   -668   -265       C  
ATOM   3415  CG  LEU A 270      -0.035 -15.090  27.097  1.00 76.06           C  
ANISOU 3415  CG  LEU A 270    12320   8171   8407      6   -794   -261       C  
ATOM   3416  CD1 LEU A 270      -1.518 -15.067  26.769  1.00 77.60           C  
ANISOU 3416  CD1 LEU A 270    12540   8330   8615   -267   -983   -197       C  
ATOM   3417  CD2 LEU A 270       0.506 -16.516  27.077  1.00 75.09           C  
ANISOU 3417  CD2 LEU A 270    12565   7874   8091    124   -803   -317       C  
ATOM   3418  N   PRO A 271       3.116 -13.262  24.128  1.00 70.46           N  
ANISOU 3418  N   PRO A 271    11574   7681   7517    620   -357   -278       N  
ATOM   3419  CA  PRO A 271       3.657 -13.360  22.761  1.00 72.80           C  
ANISOU 3419  CA  PRO A 271    12084   7942   7636    772   -299   -281       C  
ATOM   3420  C   PRO A 271       4.950 -14.154  22.671  1.00 74.31           C  
ANISOU 3420  C   PRO A 271    12455   8116   7666   1068   -154   -300       C  
ATOM   3421  O   PRO A 271       5.180 -14.827  21.661  1.00 79.34           O  
ANISOU 3421  O   PRO A 271    13425   8635   8084   1199   -144   -322       O  
ATOM   3422  CB  PRO A 271       3.864 -11.896  22.363  1.00 68.88           C  
ANISOU 3422  CB  PRO A 271    11275   7623   7271    758   -226   -229       C  
ATOM   3423  CG  PRO A 271       2.847 -11.164  23.136  1.00 67.93           C  
ANISOU 3423  CG  PRO A 271    10900   7555   7355    524   -322   -206       C  
ATOM   3424  CD  PRO A 271       2.781 -11.862  24.465  1.00 68.42           C  
ANISOU 3424  CD  PRO A 271    10944   7582   7471    499   -345   -232       C  
ATOM   3425  N   TYR A 272       5.807 -14.096  23.697  1.00 71.06           N  
ANISOU 3425  N   TYR A 272    11837   7820   7343   1187    -40   -284       N  
ATOM   3426  CA  TYR A 272       7.008 -14.924  23.696  1.00 73.49           C  
ANISOU 3426  CA  TYR A 272    12305   8124   7494   1479     99   -284       C  
ATOM   3427  C   TYR A 272       6.663 -16.409  23.733  1.00 79.25           C  
ANISOU 3427  C   TYR A 272    13455   8617   8039   1512     15   -348       C  
ATOM   3428  O   TYR A 272       7.362 -17.232  23.129  1.00 80.55           O  
ANISOU 3428  O   TYR A 272    13922   8699   7984   1758     97   -360       O  
ATOM   3429  CB  TYR A 272       7.894 -14.570  24.889  1.00 69.39           C  
ANISOU 3429  CB  TYR A 272    11464   7783   7119   1562    213   -240       C  
ATOM   3430  CG  TYR A 272       8.297 -13.117  24.987  1.00 66.86           C  
ANISOU 3430  CG  TYR A 272    10744   7684   6976   1513    283   -170       C  
ATOM   3431  CD1 TYR A 272       8.740 -12.409  23.873  1.00 66.49           C  
ANISOU 3431  CD1 TYR A 272    10652   7733   6879   1595    357   -119       C  
ATOM   3432  CD2 TYR A 272       8.235 -12.452  26.202  1.00 64.99           C  
ANISOU 3432  CD2 TYR A 272    10195   7553   6944   1381    269   -152       C  
ATOM   3433  CE1 TYR A 272       9.112 -11.077  23.982  1.00 66.40           C  
ANISOU 3433  CE1 TYR A 272    10290   7913   7024   1534    408    -49       C  
ATOM   3434  CE2 TYR A 272       8.603 -11.133  26.317  1.00 63.66           C  
ANISOU 3434  CE2 TYR A 272     9702   7564   6923   1326    319    -89       C  
ATOM   3435  CZ  TYR A 272       9.039 -10.449  25.215  1.00 63.44           C  
ANISOU 3435  CZ  TYR A 272     9633   7624   6847   1395    383    -36       C  
ATOM   3436  OH  TYR A 272       9.397  -9.131  25.368  1.00 60.87           O  
ANISOU 3436  OH  TYR A 272     8997   7465   6664   1320    419     33       O  
ATOM   3437  N   ILE A 273       5.594 -16.771  24.438  1.00 83.66           N  
ANISOU 3437  N   ILE A 273    14048   9066   8673   1272   -148   -381       N  
ATOM   3438  CA  ILE A 273       5.226 -18.175  24.615  1.00 89.76           C  
ANISOU 3438  CA  ILE A 273    15211   9610   9284   1265   -249   -433       C  
ATOM   3439  C   ILE A 273       4.368 -18.682  23.464  1.00 95.06           C  
ANISOU 3439  C   ILE A 273    16267  10077   9773   1147   -401   -462       C  
ATOM   3440  O   ILE A 273       4.552 -19.808  22.995  1.00 97.54           O  
ANISOU 3440  O   ILE A 273    17019  10192   9850   1271   -423   -504       O  
ATOM   3441  CB  ILE A 273       4.512 -18.352  25.971  1.00 90.05           C  
ANISOU 3441  CB  ILE A 273    15091   9639   9483   1054   -355   -437       C  
ATOM   3442  CG1 ILE A 273       5.507 -18.778  27.045  1.00 91.79           C  
ANISOU 3442  CG1 ILE A 273    15222   9924   9731   1246   -228   -438       C  
ATOM   3443  CG2 ILE A 273       3.368 -19.346  25.871  1.00 90.59           C  
ANISOU 3443  CG2 ILE A 273    15499   9478   9442    845   -565   -465       C  
ATOM   3444  CD1 ILE A 273       4.885 -18.893  28.411  1.00 93.09           C  
ANISOU 3444  CD1 ILE A 273    15215  10098  10056   1057   -316   -439       C  
ATOM   3445  N   ASN A 274       3.433 -17.859  22.993  1.00 97.07           N  
ANISOU 3445  N   ASN A 274    16380  10374  10127    912   -509   -435       N  
ATOM   3446  CA  ASN A 274       2.512 -18.253  21.928  1.00100.97           C  
ANISOU 3446  CA  ASN A 274    17206  10691  10465    753   -679   -445       C  
ATOM   3447  C   ASN A 274       2.051 -16.985  21.234  1.00103.66           C  
ANISOU 3447  C   ASN A 274    17289  11171  10924    627   -693   -398       C  
ATOM   3448  O   ASN A 274       1.030 -16.390  21.602  1.00103.52           O  
ANISOU 3448  O   ASN A 274    17038  11219  11075    367   -811   -354       O  
ATOM   3449  CB  ASN A 274       1.323 -19.046  22.471  1.00101.01           C  
ANISOU 3449  CB  ASN A 274    17374  10541  10463    473   -901   -444       C  
ATOM   3450  CG  ASN A 274       0.325 -19.427  21.390  1.00101.53           C  
ANISOU 3450  CG  ASN A 274    17773  10434  10367    267  -1103   -434       C  
ATOM   3451  OD1 ASN A 274       0.633 -19.397  20.198  1.00 99.95           O  
ANISOU 3451  OD1 ASN A 274    17799  10173  10003    379  -1072   -453       O  
ATOM   3452  ND2 ASN A 274      -0.882 -19.794  21.808  1.00102.76           N  
ANISOU 3452  ND2 ASN A 274    17960  10519  10563    -43  -1316   -391       N  
ATOM   3453  N   PRO A 275       2.785 -16.535  20.214  1.00106.53           N  
ANISOU 3453  N   PRO A 275    17687  11590  11198    816   -570   -396       N  
ATOM   3454  CA  PRO A 275       2.484 -15.231  19.607  1.00109.45           C  
ANISOU 3454  CA  PRO A 275    17779  12111  11696    720   -561   -347       C  
ATOM   3455  C   PRO A 275       1.187 -15.230  18.812  1.00115.84           C  
ANISOU 3455  C   PRO A 275    18746  12814  12454    455   -766   -328       C  
ATOM   3456  O   PRO A 275       1.203 -15.288  17.579  1.00117.16           O  
ANISOU 3456  O   PRO A 275    19155  12908  12455    498   -784   -334       O  
ATOM   3457  CB  PRO A 275       3.698 -14.980  18.703  1.00108.40           C  
ANISOU 3457  CB  PRO A 275    17701  12048  11438   1015   -374   -344       C  
ATOM   3458  CG  PRO A 275       4.202 -16.346  18.371  1.00108.51           C  
ANISOU 3458  CG  PRO A 275    18178  11869  11183   1217   -352   -398       C  
ATOM   3459  CD  PRO A 275       3.946 -17.191  19.586  1.00107.72           C  
ANISOU 3459  CD  PRO A 275    18128  11678  11123   1145   -422   -428       C  
ATOM   3460  N   ASP A 276       0.047 -15.160  19.522  1.00119.94           N  
ANISOU 3460  N   ASP A 276    19124  13336  13113    178   -923   -292       N  
ATOM   3461  CA  ASP A 276      -1.278 -15.049  18.901  1.00124.01           C  
ANISOU 3461  CA  ASP A 276    19708  13797  13613   -106  -1127   -238       C  
ATOM   3462  C   ASP A 276      -2.130 -14.112  19.764  1.00123.69           C  
ANISOU 3462  C   ASP A 276    19235  13927  13835   -306  -1173   -163       C  
ATOM   3463  O   ASP A 276      -2.997 -14.546  20.526  1.00130.73           O  
ANISOU 3463  O   ASP A 276    20099  14790  14783   -501  -1306   -124       O  
ATOM   3464  CB  ASP A 276      -1.940 -16.416  18.728  1.00127.54           C  
ANISOU 3464  CB  ASP A 276    20595  14007  13859   -251  -1325   -253       C  
ATOM   3465  CG  ASP A 276      -1.269 -17.255  17.662  1.00130.78           C  
ANISOU 3465  CG  ASP A 276    21487  14225  13977    -65  -1299   -322       C  
ATOM   3466  OD1 ASP A 276      -0.787 -18.361  17.983  1.00132.35           O  
ANISOU 3466  OD1 ASP A 276    21996  14266  14026     60  -1287   -380       O  
ATOM   3467  OD2 ASP A 276      -1.209 -16.796  16.504  1.00132.13           O  
ANISOU 3467  OD2 ASP A 276    21738  14404  14062    -28  -1285   -315       O  
ATOM   3468  N   LEU A 277      -1.876 -12.812  19.637  1.00118.14           N  
ANISOU 3468  N   LEU A 277    18200  13401  13285   -250  -1058   -134       N  
ATOM   3469  CA  LEU A 277      -2.675 -11.802  20.327  1.00111.61           C  
ANISOU 3469  CA  LEU A 277    16987  12730  12688   -408  -1087    -60       C  
ATOM   3470  C   LEU A 277      -3.625 -11.114  19.355  1.00111.77           C  
ANISOU 3470  C   LEU A 277    16960  12791  12717   -575  -1193     17       C  
ATOM   3471  O   LEU A 277      -3.438  -9.948  19.007  1.00111.21           O  
ANISOU 3471  O   LEU A 277    16661  12847  12748   -523  -1104     43       O  
ATOM   3472  CB  LEU A 277      -1.780 -10.763  21.012  1.00105.53           C  
ANISOU 3472  CB  LEU A 277    15878  12127  12092   -245   -895    -73       C  
ATOM   3473  CG  LEU A 277      -1.319 -11.053  22.445  1.00100.65           C  
ANISOU 3473  CG  LEU A 277    15130  11540  11572   -179   -824   -104       C  
ATOM   3474  CD1 LEU A 277      -0.570  -9.860  23.027  1.00 97.25           C  
ANISOU 3474  CD1 LEU A 277    14362  11276  11312    -67   -665    -99       C  
ATOM   3475  CD2 LEU A 277      -2.496 -11.430  23.332  1.00 98.52           C  
ANISOU 3475  CD2 LEU A 277    14801  11253  11379   -390   -966    -58       C  
ATOM   3476  N   LEU A 279      -4.769 -12.817  16.506  1.00121.21           N  
ANISOU 3476  N   LEU A 279    19045  13617  13393   -832  -1562     38       N  
ATOM   3477  CA  LEU A 279      -6.205 -13.023  16.651  1.00123.48           C  
ANISOU 3477  CA  LEU A 279    19304  13903  13710  -1149  -1787    148       C  
ATOM   3478  C   LEU A 279      -6.802 -12.039  17.648  1.00125.67           C  
ANISOU 3478  C   LEU A 279    19104  14391  14254  -1229  -1753    236       C  
ATOM   3479  O   LEU A 279      -6.429 -12.041  18.820  1.00124.76           O  
ANISOU 3479  O   LEU A 279    18814  14329  14261  -1143  -1656    204       O  
ATOM   3480  CB  LEU A 279      -6.493 -14.450  17.088  1.00123.05           C  
ANISOU 3480  CB  LEU A 279    19575  13666  13514  -1263  -1935    132       C  
ATOM   3481  N   LYS A 280      -7.736 -11.206  17.182  1.00130.40           N  
ANISOU 3481  N   LYS A 280    19505  15108  14933  -1385  -1833    350       N  
ATOM   3482  CA  LYS A 280      -8.409 -10.256  18.060  1.00134.01           C  
ANISOU 3482  CA  LYS A 280    19534  15762  15621  -1450  -1803    448       C  
ATOM   3483  C   LYS A 280      -9.086 -11.004  19.204  1.00138.93           C  
ANISOU 3483  C   LYS A 280    20116  16384  16288  -1597  -1906    505       C  
ATOM   3484  O   LYS A 280      -8.598 -10.981  20.337  1.00142.90           O  
ANISOU 3484  O   LYS A 280    20471  16924  16899  -1480  -1789    453       O  
ATOM   3485  CB  LYS A 280      -9.422  -9.414  17.275  1.00134.45           C  
ANISOU 3485  CB  LYS A 280    19435  15932  15719  -1604  -1897    583       C  
ATOM   3486  CG  LYS A 280      -9.845  -8.117  17.972  1.00133.04           C  
ANISOU 3486  CG  LYS A 280    18816  15962  15771  -1574  -1800    666       C  
ATOM   3487  CD  LYS A 280      -8.781  -7.030  17.843  1.00131.56           C  
ANISOU 3487  CD  LYS A 280    18486  15828  15671  -1334  -1587    576       C  
ATOM   3488  CE  LYS A 280      -9.195  -5.756  18.566  1.00129.95           C  
ANISOU 3488  CE  LYS A 280    17897  15802  15677  -1300  -1497    652       C  
ATOM   3489  NZ  LYS A 280      -8.101  -4.745  18.626  1.00128.08           N  
ANISOU 3489  NZ  LYS A 280    17534  15604  15526  -1087  -1300    565       N  
ATOM   3490  N   LYS A 281     -10.177 -11.709  18.913  1.00140.36           N  
ANISOU 3490  N   LYS A 281    20437  16519  16373  -1860  -2132    617       N  
ATOM   3491  CA  LYS A 281     -10.878 -12.509  19.915  1.00139.84           C  
ANISOU 3491  CA  LYS A 281    20354  16453  16328  -2029  -2255    693       C  
ATOM   3492  C   LYS A 281     -11.230 -11.668  21.141  1.00135.62           C  
ANISOU 3492  C   LYS A 281    19378  16125  16026  -1988  -2149    764       C  
ATOM   3493  O   LYS A 281     -10.940 -12.035  22.282  1.00135.53           O  
ANISOU 3493  O   LYS A 281    19305  16112  16080  -1927  -2087    722       O  
ATOM   3494  CB  LYS A 281     -10.054 -13.737  20.310  1.00140.56           C  
ANISOU 3494  CB  LYS A 281    20774  16344  16288  -1945  -2246    560       C  
ATOM   3495  N   PHE A 282     -11.855 -10.513  20.885  1.00130.43           N  
ANISOU 3495  N   PHE A 282    18427  15644  15488  -2010  -2123    873       N  
ATOM   3496  CA  PHE A 282     -12.227  -9.553  21.928  1.00123.26           C  
ANISOU 3496  CA  PHE A 282    17115  14931  14786  -1944  -2010    947       C  
ATOM   3497  C   PHE A 282     -11.007  -9.036  22.693  1.00113.40           C  
ANISOU 3497  C   PHE A 282    15770  13677  13640  -1675  -1780    790       C  
ATOM   3498  O   PHE A 282     -11.100  -8.737  23.886  1.00113.03           O  
ANISOU 3498  O   PHE A 282    15500  13723  13725  -1619  -1699    809       O  
ATOM   3499  CB  PHE A 282     -13.238 -10.162  22.911  1.00125.27           C  
ANISOU 3499  CB  PHE A 282    17257  15264  15078  -2124  -2132   1090       C  
ATOM   3500  CG  PHE A 282     -14.681  -9.998  22.504  1.00127.41           C  
ANISOU 3500  CG  PHE A 282    17385  15679  15347  -2362  -2305   1322       C  
ATOM   3501  CD1 PHE A 282     -15.490  -9.074  23.146  1.00126.72           C  
ANISOU 3501  CD1 PHE A 282    16915  15819  15415  -2344  -2247   1476       C  
ATOM   3502  CD2 PHE A 282     -15.233 -10.779  21.499  1.00129.63           C  
ANISOU 3502  CD2 PHE A 282    17920  15874  15460  -2601  -2529   1400       C  
ATOM   3503  CE1 PHE A 282     -16.818  -8.921  22.789  1.00127.90           C  
ANISOU 3503  CE1 PHE A 282    16906  16130  15561  -2548  -2398   1716       C  
ATOM   3504  CE2 PHE A 282     -16.562 -10.630  21.136  1.00130.54           C  
ANISOU 3504  CE2 PHE A 282    17884  16144  15573  -2836  -2699   1638       C  
ATOM   3505  CZ  PHE A 282     -17.355  -9.700  21.783  1.00129.79           C  
ANISOU 3505  CZ  PHE A 282    17375  16298  15642  -2805  -2629   1804       C  
ATOM   3506  N   ILE A 283      -9.852  -8.923  22.026  1.00104.74           N  
ANISOU 3506  N   ILE A 283    14838  12479  12479  -1511  -1676    647       N  
ATOM   3507  CA  ILE A 283      -8.630  -8.596  22.759  1.00 94.19           C  
ANISOU 3507  CA  ILE A 283    13432  11137  11219  -1280  -1480    513       C  
ATOM   3508  C   ILE A 283      -8.693  -7.198  23.365  1.00 85.87           C  
ANISOU 3508  C   ILE A 283    12032  10242  10352  -1184  -1346    549       C  
ATOM   3509  O   ILE A 283      -8.130  -6.965  24.442  1.00 83.77           O  
ANISOU 3509  O   ILE A 283    11641  10007  10183  -1066  -1227    491       O  
ATOM   3510  CB  ILE A 283      -7.380  -8.765  21.869  1.00 90.71           C  
ANISOU 3510  CB  ILE A 283    13225  10582  10659  -1120  -1394    381       C  
ATOM   3511  CG1 ILE A 283      -6.133  -8.972  22.729  1.00 89.39           C  
ANISOU 3511  CG1 ILE A 283    13057  10385  10522   -922  -1239    261       C  
ATOM   3512  CG2 ILE A 283      -7.180  -7.577  20.953  1.00 89.90           C  
ANISOU 3512  CG2 ILE A 283    13011  10553  10593  -1048  -1318    393       C  
ATOM   3513  CD1 ILE A 283      -6.133 -10.276  23.497  1.00 90.45           C  
ANISOU 3513  CD1 ILE A 283    13363  10415  10587   -965  -1306    230       C  
ATOM   3514  N   GLN A 284      -9.369  -6.247  22.710  1.00 80.26           N  
ANISOU 3514  N   GLN A 284    11179   9629   9688  -1230  -1366    645       N  
ATOM   3515  CA  GLN A 284      -9.420  -4.899  23.267  1.00 76.74           C  
ANISOU 3515  CA  GLN A 284    10444   9312   9402  -1124  -1237    677       C  
ATOM   3516  C   GLN A 284     -10.231  -4.867  24.554  1.00 73.06           C  
ANISOU 3516  C   GLN A 284     9776   8944   9039  -1165  -1244    766       C  
ATOM   3517  O   GLN A 284      -9.887  -4.139  25.492  1.00 68.29           O  
ANISOU 3517  O   GLN A 284     9007   8392   8547  -1036  -1114    733       O  
ATOM   3518  CB  GLN A 284      -9.998  -3.907  22.259  1.00 77.43           C  
ANISOU 3518  CB  GLN A 284    10438   9477   9507  -1154  -1257    768       C  
ATOM   3519  CG  GLN A 284      -9.837  -2.456  22.713  1.00 78.83           C  
ANISOU 3519  CG  GLN A 284    10376   9750   9826  -1013  -1111    777       C  
ATOM   3520  CD  GLN A 284     -10.696  -1.483  21.930  1.00 84.82           C  
ANISOU 3520  CD  GLN A 284    11008  10606  10616  -1052  -1140    903       C  
ATOM   3521  OE1 GLN A 284     -11.893  -1.704  21.737  1.00 88.42           O  
ANISOU 3521  OE1 GLN A 284    11402  11139  11056  -1191  -1261   1051       O  
ATOM   3522  NE2 GLN A 284     -10.086  -0.394  21.474  1.00 85.20           N  
ANISOU 3522  NE2 GLN A 284    11012  10657  10705   -933  -1034    859       N  
ATOM   3523  N   GLN A 285     -11.304  -5.656  24.622  1.00 74.14           N  
ANISOU 3523  N   GLN A 285     9930   9110   9131  -1348  -1400    888       N  
ATOM   3524  CA  GLN A 285     -12.047  -5.764  25.870  1.00 75.29           C  
ANISOU 3524  CA  GLN A 285     9890   9358   9360  -1384  -1406    983       C  
ATOM   3525  C   GLN A 285     -11.206  -6.452  26.935  1.00 69.76           C  
ANISOU 3525  C   GLN A 285     9266   8573   8667  -1305  -1340    856       C  
ATOM   3526  O   GLN A 285     -11.169  -6.012  28.094  1.00 70.46           O  
ANISOU 3526  O   GLN A 285     9181   8731   8860  -1210  -1238    854       O  
ATOM   3527  CB  GLN A 285     -13.356  -6.522  25.634  1.00 85.31           C  
ANISOU 3527  CB  GLN A 285    11162  10687  10564  -1623  -1604   1164       C  
ATOM   3528  CG  GLN A 285     -14.328  -5.842  24.667  1.00 95.31           C  
ANISOU 3528  CG  GLN A 285    12315  12070  11827  -1715  -1681   1326       C  
ATOM   3529  CD  GLN A 285     -13.957  -6.021  23.196  1.00104.11           C  
ANISOU 3529  CD  GLN A 285    13666  13069  12821  -1773  -1756   1267       C  
ATOM   3530  OE1 GLN A 285     -12.813  -6.334  22.860  1.00106.67           O  
ANISOU 3530  OE1 GLN A 285    14208  13239  13081  -1678  -1699   1090       O  
ATOM   3531  NE2 GLN A 285     -14.931  -5.821  22.314  1.00108.04           N  
ANISOU 3531  NE2 GLN A 285    14118  13652  13279  -1924  -1884   1428       N  
ATOM   3532  N   VAL A 286     -10.487  -7.509  26.545  1.00 62.88           N  
ANISOU 3532  N   VAL A 286     8667   7547   7676  -1329  -1391    748       N  
ATOM   3533  CA  VAL A 286      -9.595  -8.188  27.476  1.00 60.15           C  
ANISOU 3533  CA  VAL A 286     8409   7118   7328  -1238  -1323    627       C  
ATOM   3534  C   VAL A 286      -8.492  -7.245  27.933  1.00 56.28           C  
ANISOU 3534  C   VAL A 286     7806   6647   6932  -1024  -1131    515       C  
ATOM   3535  O   VAL A 286      -8.116  -7.229  29.112  1.00 57.67           O  
ANISOU 3535  O   VAL A 286     7890   6843   7180   -944  -1049    472       O  
ATOM   3536  CB  VAL A 286      -9.020  -9.462  26.826  1.00 60.20           C  
ANISOU 3536  CB  VAL A 286     8759   6948   7168  -1277  -1407    540       C  
ATOM   3537  CG1 VAL A 286      -7.959 -10.098  27.722  1.00 56.92           C  
ANISOU 3537  CG1 VAL A 286     8432   6450   6745  -1146  -1316    413       C  
ATOM   3538  CG2 VAL A 286     -10.135 -10.455  26.535  1.00 63.03           C  
ANISOU 3538  CG2 VAL A 286     9250   7273   7426  -1521  -1621    659       C  
ATOM   3539  N   TYR A 287      -7.985  -6.416  27.018  1.00 51.27           N  
ANISOU 3539  N   TYR A 287     7174   6013   6294   -942  -1066    478       N  
ATOM   3540  CA  TYR A 287      -6.922  -5.494  27.393  1.00 50.37           C  
ANISOU 3540  CA  TYR A 287     6959   5920   6260   -766   -902    389       C  
ATOM   3541  C   TYR A 287      -7.435  -4.405  28.325  1.00 46.57           C  
ANISOU 3541  C   TYR A 287     6225   5551   5918   -728   -832    451       C  
ATOM   3542  O   TYR A 287      -6.755  -4.042  29.289  1.00 42.37           O  
ANISOU 3542  O   TYR A 287     5618   5026   5453   -623   -728    387       O  
ATOM   3543  CB  TYR A 287      -6.285  -4.873  26.154  1.00 52.85           C  
ANISOU 3543  CB  TYR A 287     7337   6213   6530   -701   -857    352       C  
ATOM   3544  CG  TYR A 287      -5.211  -3.872  26.507  1.00 60.25           C  
ANISOU 3544  CG  TYR A 287     8163   7182   7546   -549   -706    285       C  
ATOM   3545  CD1 TYR A 287      -4.012  -4.288  27.076  1.00 63.89           C  
ANISOU 3545  CD1 TYR A 287     8679   7605   7992   -444   -624    190       C  
ATOM   3546  CD2 TYR A 287      -5.399  -2.512  26.290  1.00 61.92           C  
ANISOU 3546  CD2 TYR A 287     8220   7465   7840   -519   -652    329       C  
ATOM   3547  CE1 TYR A 287      -3.026  -3.377  27.410  1.00 66.21           C  
ANISOU 3547  CE1 TYR A 287     8866   7938   8351   -333   -504    150       C  
ATOM   3548  CE2 TYR A 287      -4.419  -1.595  26.621  1.00 64.15           C  
ANISOU 3548  CE2 TYR A 287     8422   7767   8184   -407   -534    278       C  
ATOM   3549  CZ  TYR A 287      -3.236  -2.032  27.179  1.00 67.48           C  
ANISOU 3549  CZ  TYR A 287     8890   8158   8590   -326   -466    193       C  
ATOM   3550  OH  TYR A 287      -2.263  -1.117  27.504  1.00 72.16           O  
ANISOU 3550  OH  TYR A 287     9398   8781   9238   -243   -367    163       O  
ATOM   3551  N   LEU A 288      -8.635  -3.878  28.066  1.00 45.46           N  
ANISOU 3551  N   LEU A 288     5961   5501   5812   -806   -889    582       N  
ATOM   3552  CA  LEU A 288      -9.185  -2.864  28.958  1.00 48.60           C  
ANISOU 3552  CA  LEU A 288     6140   6003   6323   -742   -814    650       C  
ATOM   3553  C   LEU A 288      -9.446  -3.438  30.344  1.00 48.00           C  
ANISOU 3553  C   LEU A 288     6002   5953   6283   -746   -808    662       C  
ATOM   3554  O   LEU A 288      -9.198  -2.770  31.353  1.00 43.73           O  
ANISOU 3554  O   LEU A 288     5356   5441   5819   -636   -703    635       O  
ATOM   3555  CB  LEU A 288     -10.467  -2.276  28.368  1.00 48.54           C  
ANISOU 3555  CB  LEU A 288     6009   6103   6331   -810   -874    811       C  
ATOM   3556  CG  LEU A 288     -10.298  -1.151  27.344  1.00 49.12           C  
ANISOU 3556  CG  LEU A 288     6062   6185   6415   -753   -830    815       C  
ATOM   3557  CD1 LEU A 288     -11.649  -0.741  26.784  1.00 52.66           C  
ANISOU 3557  CD1 LEU A 288     6388   6751   6869   -829   -904    994       C  
ATOM   3558  CD2 LEU A 288      -9.593   0.047  27.965  1.00 45.79           C  
ANISOU 3558  CD2 LEU A 288     5564   5759   6077   -590   -681    745       C  
ATOM   3559  N   ALA A 289      -9.871  -4.704  30.415  1.00 45.44           N  
ANISOU 3559  N   ALA A 289     5768   5605   5894   -876   -925    697       N  
ATOM   3560  CA  ALA A 289     -10.124  -5.326  31.712  1.00 49.69           C  
ANISOU 3560  CA  ALA A 289     6253   6168   6460   -891   -927    716       C  
ATOM   3561  C   ALA A 289      -8.826  -5.571  32.474  1.00 47.77           C  
ANISOU 3561  C   ALA A 289     6087   5835   6227   -777   -832    558       C  
ATOM   3562  O   ALA A 289      -8.726  -5.282  33.676  1.00 45.21           O  
ANISOU 3562  O   ALA A 289     5656   5549   5972   -701   -752    544       O  
ATOM   3563  CB  ALA A 289     -10.883  -6.639  31.517  1.00 52.53           C  
ANISOU 3563  CB  ALA A 289     6710   6513   6735  -1081  -1094    801       C  
ATOM   3564  N   ILE A 290      -7.821  -6.117  31.787  1.00 47.15           N  
ANISOU 3564  N   ILE A 290     6197   5644   6072   -758   -836    447       N  
ATOM   3565  CA  ILE A 290      -6.549  -6.406  32.435  1.00 45.96           C  
ANISOU 3565  CA  ILE A 290     6114   5427   5923   -647   -748    318       C  
ATOM   3566  C   ILE A 290      -5.871  -5.117  32.881  1.00 44.25           C  
ANISOU 3566  C   ILE A 290     5764   5253   5796   -515   -613    272       C  
ATOM   3567  O   ILE A 290      -5.332  -5.029  33.996  1.00 46.10           O  
ANISOU 3567  O   ILE A 290     5947   5492   6078   -445   -542    222       O  
ATOM   3568  CB  ILE A 290      -5.661  -7.228  31.483  1.00 48.55           C  
ANISOU 3568  CB  ILE A 290     6672   5643   6133   -631   -773    233       C  
ATOM   3569  CG1 ILE A 290      -6.135  -8.682  31.446  1.00 56.63           C  
ANISOU 3569  CG1 ILE A 290     7875   6586   7055   -750   -904    254       C  
ATOM   3570  CG2 ILE A 290      -4.215  -7.143  31.883  1.00 43.55           C  
ANISOU 3570  CG2 ILE A 290     6062   4978   5506   -482   -653    122       C  
ATOM   3571  CD1 ILE A 290      -5.362  -9.555  30.478  1.00 60.44           C  
ANISOU 3571  CD1 ILE A 290     8631   6938   7394   -720   -932    176       C  
ATOM   3572  N   MET A 291      -5.901  -4.084  32.033  1.00 42.73           N  
ANISOU 3572  N   MET A 291     5526   5088   5622   -488   -584    294       N  
ATOM   3573  CA  MET A 291      -5.320  -2.818  32.446  1.00 42.18           C  
ANISOU 3573  CA  MET A 291     5353   5045   5627   -384   -474    261       C  
ATOM   3574  C   MET A 291      -6.114  -2.181  33.575  1.00 38.32           C  
ANISOU 3574  C   MET A 291     4720   4621   5218   -360   -440    322       C  
ATOM   3575  O   MET A 291      -5.521  -1.543  34.450  1.00 43.82           O  
ANISOU 3575  O   MET A 291     5375   5312   5962   -279   -357    273       O  
ATOM   3576  CB  MET A 291      -5.211  -1.853  31.266  1.00 44.39           C  
ANISOU 3576  CB  MET A 291     5629   5335   5904   -366   -456    278       C  
ATOM   3577  CG  MET A 291      -4.510  -0.557  31.656  1.00 49.48           C  
ANISOU 3577  CG  MET A 291     6199   5987   6613   -275   -356    245       C  
ATOM   3578  SD  MET A 291      -4.001   0.467  30.270  1.00 59.24           S  
ANISOU 3578  SD  MET A 291     7455   7220   7833   -253   -331    248       S  
ATOM   3579  CE  MET A 291      -5.587   0.839  29.520  1.00 57.48           C  
ANISOU 3579  CE  MET A 291     7175   7049   7617   -314   -399    369       C  
ATOM   3580  N   TRP A 292      -7.440  -2.361  33.605  1.00 38.99           N  
ANISOU 3580  N   TRP A 292     4733   4774   5309   -427   -503    438       N  
ATOM   3581  CA  TRP A 292      -8.202  -1.819  34.723  1.00 43.74           C  
ANISOU 3581  CA  TRP A 292     5197   5450   5970   -377   -456    509       C  
ATOM   3582  C   TRP A 292      -7.788  -2.477  36.029  1.00 44.54           C  
ANISOU 3582  C   TRP A 292     5310   5531   6084   -355   -430    451       C  
ATOM   3583  O   TRP A 292      -7.599  -1.794  37.042  1.00 38.90           O  
ANISOU 3583  O   TRP A 292     4541   4824   5413   -262   -345    427       O  
ATOM   3584  CB  TRP A 292      -9.705  -1.997  34.504  1.00 40.92           C  
ANISOU 3584  CB  TRP A 292     4738   5201   5609   -454   -531    675       C  
ATOM   3585  CG  TRP A 292     -10.509  -1.316  35.579  1.00 45.02           C  
ANISOU 3585  CG  TRP A 292     5109   5817   6180   -364   -460    766       C  
ATOM   3586  CD1 TRP A 292     -11.044  -0.062  35.529  1.00 45.54           C  
ANISOU 3586  CD1 TRP A 292     5083   5942   6279   -259   -389    839       C  
ATOM   3587  CD2 TRP A 292     -10.837  -1.838  36.878  1.00 46.01           C  
ANISOU 3587  CD2 TRP A 292     5176   5986   6319   -351   -444    795       C  
ATOM   3588  NE1 TRP A 292     -11.695   0.224  36.704  1.00 45.47           N  
ANISOU 3588  NE1 TRP A 292     4970   6011   6294   -167   -324    914       N  
ATOM   3589  CE2 TRP A 292     -11.581  -0.849  37.550  1.00 46.24           C  
ANISOU 3589  CE2 TRP A 292     5079   6106   6383   -226   -356    889       C  
ATOM   3590  CE3 TRP A 292     -10.585  -3.051  37.530  1.00 45.87           C  
ANISOU 3590  CE3 TRP A 292     5210   5939   6281   -424   -493    756       C  
ATOM   3591  CZ2 TRP A 292     -12.074  -1.032  38.841  1.00 47.30           C  
ANISOU 3591  CZ2 TRP A 292     5131   6310   6529   -169   -312    946       C  
ATOM   3592  CZ3 TRP A 292     -11.070  -3.229  38.813  1.00 49.01           C  
ANISOU 3592  CZ3 TRP A 292     5517   6405   6700   -384   -457    811       C  
ATOM   3593  CH2 TRP A 292     -11.808  -2.225  39.455  1.00 48.01           C  
ANISOU 3593  CH2 TRP A 292     5259   6376   6605   -257   -365    906       C  
ATOM   3594  N   LEU A 293      -7.621  -3.801  36.023  1.00 38.75           N  
ANISOU 3594  N   LEU A 293     4665   4758   5300   -440   -505    425       N  
ATOM   3595  CA  LEU A 293      -7.206  -4.479  37.248  1.00 43.53           C  
ANISOU 3595  CA  LEU A 293     5285   5341   5913   -420   -483    372       C  
ATOM   3596  C   LEU A 293      -5.827  -3.998  37.696  1.00 42.24           C  
ANISOU 3596  C   LEU A 293     5159   5119   5771   -318   -388    247       C  
ATOM   3597  O   LEU A 293      -5.613  -3.654  38.880  1.00 44.74           O  
ANISOU 3597  O   LEU A 293     5424   5448   6128   -255   -325    222       O  
ATOM   3598  CB  LEU A 293      -7.207  -5.992  37.021  1.00 40.96           C  
ANISOU 3598  CB  LEU A 293     5083   4963   5516   -528   -586    364       C  
ATOM   3599  CG  LEU A 293      -6.833  -6.863  38.221  1.00 43.15           C  
ANISOU 3599  CG  LEU A 293     5389   5214   5793   -520   -578    318       C  
ATOM   3600  CD1 LEU A 293      -7.803  -6.634  39.379  1.00 38.72           C  
ANISOU 3600  CD1 LEU A 293     4674   4752   5286   -519   -561    413       C  
ATOM   3601  CD2 LEU A 293      -6.801  -8.327  37.811  1.00 39.15           C  
ANISOU 3601  CD2 LEU A 293     5049   4629   5197   -623   -688    308       C  
ATOM   3602  N   ALA A 294      -4.900  -3.894  36.740  1.00 38.00           N  
ANISOU 3602  N   ALA A 294     4708   4529   5201   -302   -379    181       N  
ATOM   3603  CA  ALA A 294      -3.551  -3.465  37.082  1.00 39.72           C  
ANISOU 3603  CA  ALA A 294     4945   4714   5432   -222   -301     90       C  
ATOM   3604  C   ALA A 294      -3.557  -2.057  37.668  1.00 40.64           C  
ANISOU 3604  C   ALA A 294     4975   4855   5610   -162   -230     98       C  
ATOM   3605  O   ALA A 294      -2.960  -1.813  38.722  1.00 42.12           O  
ANISOU 3605  O   ALA A 294     5150   5032   5822   -121   -182     54       O  
ATOM   3606  CB  ALA A 294      -2.649  -3.546  35.851  1.00 38.33           C  
ANISOU 3606  CB  ALA A 294     4858   4504   5202   -209   -300     48       C  
ATOM   3607  N   MET A 295      -4.254  -1.119  37.014  1.00 41.69           N  
ANISOU 3607  N   MET A 295     5066   5013   5762   -158   -228    158       N  
ATOM   3608  CA  MET A 295      -4.304   0.251  37.523  1.00 44.63           C  
ANISOU 3608  CA  MET A 295     5394   5386   6176    -89   -162    167       C  
ATOM   3609  C   MET A 295      -5.042   0.333  38.850  1.00 42.35           C  
ANISOU 3609  C   MET A 295     5053   5126   5912    -45   -133    201       C  
ATOM   3610  O   MET A 295      -4.707   1.174  39.690  1.00 36.70           O  
ANISOU 3610  O   MET A 295     4351   4380   5212     19    -75    171       O  
ATOM   3611  CB  MET A 295      -4.980   1.191  36.519  1.00 45.44           C  
ANISOU 3611  CB  MET A 295     5470   5509   6286    -80   -164    235       C  
ATOM   3612  CG  MET A 295      -4.341   1.251  35.143  1.00 56.89           C  
ANISOU 3612  CG  MET A 295     6971   6937   7707   -116   -188    212       C  
ATOM   3613  SD  MET A 295      -2.650   1.863  35.139  1.00 68.24           S  
ANISOU 3613  SD  MET A 295     8461   8326   9142    -92   -139    126       S  
ATOM   3614  CE  MET A 295      -2.860   3.518  35.781  1.00 70.05           C  
ANISOU 3614  CE  MET A 295     8679   8526   9411    -36    -86    146       C  
ATOM   3615  N   SER A 296      -6.051  -0.515  39.048  1.00 38.24           N  
ANISOU 3615  N   SER A 296     4480   4663   5386    -83   -176    273       N  
ATOM   3616  CA  SER A 296      -6.824  -0.489  40.279  1.00 41.08           C  
ANISOU 3616  CA  SER A 296     4773   5072   5762    -33   -143    326       C  
ATOM   3617  C   SER A 296      -5.987  -0.911  41.466  1.00 40.40           C  
ANISOU 3617  C   SER A 296     4730   4943   5677    -15   -116    239       C  
ATOM   3618  O   SER A 296      -6.348  -0.597  42.605  1.00 38.02           O  
ANISOU 3618  O   SER A 296     4400   4662   5384     53    -66    257       O  
ATOM   3619  CB  SER A 296      -8.041  -1.403  40.167  1.00 38.09           C  
ANISOU 3619  CB  SER A 296     4317   4784   5373   -103   -211    444       C  
ATOM   3620  OG  SER A 296      -7.671  -2.753  40.391  1.00 37.86           O  
ANISOU 3620  OG  SER A 296     4338   4728   5320   -190   -273    402       O  
ATOM   3621  N   SER A 297      -4.879  -1.614  41.219  1.00 40.50           N  
ANISOU 3621  N   SER A 297     4812   4903   5674    -64   -143    152       N  
ATOM   3622  CA  SER A 297      -3.979  -1.931  42.329  1.00 38.86           C  
ANISOU 3622  CA  SER A 297     4636   4661   5466    -44   -115     76       C  
ATOM   3623  C   SER A 297      -3.602  -0.692  43.147  1.00 42.91           C  
ANISOU 3623  C   SER A 297     5165   5144   5995     28    -49     46       C  
ATOM   3624  O   SER A 297      -3.270  -0.810  44.333  1.00 44.63           O  
ANISOU 3624  O   SER A 297     5398   5349   6212     51    -25     10       O  
ATOM   3625  CB  SER A 297      -2.698  -2.581  41.817  1.00 38.61           C  
ANISOU 3625  CB  SER A 297     4672   4589   5409    -76   -135      1       C  
ATOM   3626  OG  SER A 297      -1.855  -1.600  41.241  1.00 41.99           O  
ANISOU 3626  OG  SER A 297     5120   4993   5840    -57   -106    -30       O  
ATOM   3627  N   THR A 298      -3.641   0.499  42.540  1.00 40.40           N  
ANISOU 3627  N   THR A 298     4863   4805   5682     59    -25     59       N  
ATOM   3628  CA  THR A 298      -3.244   1.721  43.231  1.00 40.99           C  
ANISOU 3628  CA  THR A 298     4998   4824   5753    115     24     30       C  
ATOM   3629  C   THR A 298      -4.283   2.229  44.227  1.00 43.22           C  
ANISOU 3629  C   THR A 298     5276   5118   6027    211     76     79       C  
ATOM   3630  O   THR A 298      -3.977   3.162  44.975  1.00 37.15           O  
ANISOU 3630  O   THR A 298     4595   4283   5236    266    114     47       O  
ATOM   3631  CB  THR A 298      -2.950   2.844  42.227  1.00 43.42           C  
ANISOU 3631  CB  THR A 298     5345   5093   6059    114     28     34       C  
ATOM   3632  OG1 THR A 298      -4.162   3.222  41.564  1.00 36.96           O  
ANISOU 3632  OG1 THR A 298     4482   4313   5247    158     37    116       O  
ATOM   3633  CG2 THR A 298      -1.935   2.392  41.196  1.00 42.07           C  
ANISOU 3633  CG2 THR A 298     5173   4926   5886     37    -11      1       C  
ATOM   3634  N   MET A 299      -5.507   1.693  44.237  1.00 37.21           N  
ANISOU 3634  N   MET A 299     4424   4441   5272    236     76    166       N  
ATOM   3635  CA  MET A 299      -6.526   2.177  45.163  1.00 42.05           C  
ANISOU 3635  CA  MET A 299     5017   5092   5868    354    141    236       C  
ATOM   3636  C   MET A 299      -6.793   1.264  46.366  1.00 44.27           C  
ANISOU 3636  C   MET A 299     5256   5421   6143    360    148    247       C  
ATOM   3637  O   MET A 299      -7.534   1.669  47.271  1.00 38.64           O  
ANISOU 3637  O   MET A 299     4536   4742   5405    475    214    303       O  
ATOM   3638  CB  MET A 299      -7.846   2.420  44.409  1.00 43.72           C  
ANISOU 3638  CB  MET A 299     5129   5397   6084    398    149    369       C  
ATOM   3639  CG  MET A 299      -8.564   1.155  43.972  1.00 51.31           C  
ANISOU 3639  CG  MET A 299     5967   6467   7061    301     80    454       C  
ATOM   3640  SD  MET A 299     -10.053   1.461  42.992  1.00 53.21           S  
ANISOU 3640  SD  MET A 299     6078   6837   7304    323     69    634       S  
ATOM   3641  CE  MET A 299     -10.675  -0.207  42.791  1.00 53.96           C  
ANISOU 3641  CE  MET A 299     6067   7034   7400    161    -42    720       C  
ATOM   3642  N   TYR A 300      -6.216   0.061  46.422  1.00 37.40           N  
ANISOU 3642  N   TYR A 300     4369   4554   5286    256     89    200       N  
ATOM   3643  CA  TYR A 300      -6.655  -0.894  47.441  1.00 40.07           C  
ANISOU 3643  CA  TYR A 300     4655   4951   5620    251     87    233       C  
ATOM   3644  C   TYR A 300      -5.985  -0.698  48.798  1.00 37.85           C  
ANISOU 3644  C   TYR A 300     4450   4613   5318    302    130    156       C  
ATOM   3645  O   TYR A 300      -6.623  -0.953  49.827  1.00 37.91           O  
ANISOU 3645  O   TYR A 300     4421   4673   5309    359    166    204       O  
ATOM   3646  CB  TYR A 300      -6.428  -2.330  46.965  1.00 38.19           C  
ANISOU 3646  CB  TYR A 300     4389   4730   5392    123      0    224       C  
ATOM   3647  CG  TYR A 300      -7.268  -2.679  45.763  1.00 40.81           C  
ANISOU 3647  CG  TYR A 300     4658   5122   5728     56    -60    317       C  
ATOM   3648  CD1 TYR A 300      -8.655  -2.592  45.817  1.00 42.09           C  
ANISOU 3648  CD1 TYR A 300     4708   5397   5889     80    -55    463       C  
ATOM   3649  CD2 TYR A 300      -6.680  -3.072  44.571  1.00 39.43           C  
ANISOU 3649  CD2 TYR A 300     4534   4899   5548    -28   -122    271       C  
ATOM   3650  CE1 TYR A 300      -9.431  -2.896  44.719  1.00 41.41           C  
ANISOU 3650  CE1 TYR A 300     4561   5373   5801     -1   -124    563       C  
ATOM   3651  CE2 TYR A 300      -7.450  -3.378  43.463  1.00 39.89           C  
ANISOU 3651  CE2 TYR A 300     4556   5002   5599    -99   -187    355       C  
ATOM   3652  CZ  TYR A 300      -8.822  -3.286  43.542  1.00 41.24           C  
ANISOU 3652  CZ  TYR A 300     4613   5283   5771    -97   -195    502       C  
ATOM   3653  OH  TYR A 300      -9.586  -3.590  42.438  1.00 43.45           O  
ANISOU 3653  OH  TYR A 300     4855   5616   6039   -189   -275    600       O  
ATOM   3654  N   ASN A 301      -4.716  -0.281  48.835  1.00 36.75           N  
ANISOU 3654  N   ASN A 301     4409   4379   5174    274    123     51       N  
ATOM   3655  CA  ASN A 301      -3.994  -0.243  50.109  1.00 36.64           C  
ANISOU 3655  CA  ASN A 301     4470   4317   5137    289    142    -17       C  
ATOM   3656  C   ASN A 301      -4.653   0.646  51.160  1.00 43.69           C  
ANISOU 3656  C   ASN A 301     5422   5193   5984    417    217     10       C  
ATOM   3657  O   ASN A 301      -4.734   0.216  52.321  1.00 45.36           O  
ANISOU 3657  O   ASN A 301     5641   5420   6174    446    237      5       O  
ATOM   3658  CB  ASN A 301      -2.530   0.157  49.887  1.00 36.23           C  
ANISOU 3658  CB  ASN A 301     4501   4183   5081    222    111   -105       C  
ATOM   3659  CG  ASN A 301      -1.746  -0.892  49.118  1.00 51.35           C  
ANISOU 3659  CG  ASN A 301     6366   6123   7022    128     55   -131       C  
ATOM   3660  OD1 ASN A 301      -2.226  -2.007  48.896  1.00 45.56           O  
ANISOU 3660  OD1 ASN A 301     5567   5441   6301    103     30   -101       O  
ATOM   3661  ND2 ASN A 301      -0.529  -0.540  48.706  1.00 48.44           N  
ANISOU 3661  ND2 ASN A 301     6037   5717   6650     77     33   -177       N  
ATOM   3662  N   PRO A 302      -5.094   1.876  50.868  1.00 45.54           N  
ANISOU 3662  N   PRO A 302     5720   5390   6192    509    263     37       N  
ATOM   3663  CA  PRO A 302      -5.806   2.638  51.911  1.00 46.16           C  
ANISOU 3663  CA  PRO A 302     5878   5453   6207    664    347     71       C  
ATOM   3664  C   PRO A 302      -7.052   1.929  52.415  1.00 44.23           C  
ANISOU 3664  C   PRO A 302     5498   5345   5963    742    392    183       C  
ATOM   3665  O   PRO A 302      -7.372   2.020  53.605  1.00 40.23           O  
ANISOU 3665  O   PRO A 302     5036   4845   5403    844    452    196       O  
ATOM   3666  CB  PRO A 302      -6.151   3.962  51.215  1.00 45.52           C  
ANISOU 3666  CB  PRO A 302     5879   5316   6099    752    385     98       C  
ATOM   3667  CG  PRO A 302      -5.155   4.077  50.113  1.00 41.51           C  
ANISOU 3667  CG  PRO A 302     5385   4753   5633    614    310     37       C  
ATOM   3668  CD  PRO A 302      -4.939   2.672  49.635  1.00 39.64           C  
ANISOU 3668  CD  PRO A 302     4999   4604   5459    490    248     38       C  
ATOM   3669  N   ILE A 303      -7.753   1.193  51.543  1.00 41.23           N  
ANISOU 3669  N   ILE A 303     4956   5079   5631    685    357    273       N  
ATOM   3670  CA  ILE A 303      -8.925   0.445  51.991  1.00 42.93           C  
ANISOU 3670  CA  ILE A 303     5023   5442   5845    724    379    404       C  
ATOM   3671  C   ILE A 303      -8.508  -0.699  52.906  1.00 41.28           C  
ANISOU 3671  C   ILE A 303     4796   5246   5643    645    343    363       C  
ATOM   3672  O   ILE A 303      -9.145  -0.958  53.937  1.00 41.91           O  
ANISOU 3672  O   ILE A 303     4832   5400   5691    723    393    430       O  
ATOM   3673  CB  ILE A 303      -9.722  -0.061  50.776  1.00 42.48           C  
ANISOU 3673  CB  ILE A 303     4814   5495   5830    646    324    519       C  
ATOM   3674  CG1 ILE A 303     -10.124   1.111  49.880  1.00 44.96           C  
ANISOU 3674  CG1 ILE A 303     5145   5800   6137    732    362    563       C  
ATOM   3675  CG2 ILE A 303     -10.949  -0.841  51.236  1.00 41.29           C  
ANISOU 3675  CG2 ILE A 303     4498   5516   5674    659    330    683       C  
ATOM   3676  CD1 ILE A 303     -10.759   0.687  48.571  1.00 47.51           C  
ANISOU 3676  CD1 ILE A 303     5337   6215   6498    635    293    664       C  
ATOM   3677  N   ILE A 304      -7.415  -1.380  52.558  1.00 38.50           N  
ANISOU 3677  N   ILE A 304     4479   4824   5325    503    263    258       N  
ATOM   3678  CA  ILE A 304      -6.903  -2.463  53.390  1.00 38.01           C  
ANISOU 3678  CA  ILE A 304     4414   4762   5267    432    227    213       C  
ATOM   3679  C   ILE A 304      -6.476  -1.933  54.756  1.00 42.49           C  
ANISOU 3679  C   ILE A 304     5088   5271   5786    520    287    152       C  
ATOM   3680  O   ILE A 304      -6.755  -2.551  55.796  1.00 40.21           O  
ANISOU 3680  O   ILE A 304     4769   5031   5479    541    305    178       O  
ATOM   3681  CB  ILE A 304      -5.747  -3.172  52.657  1.00 37.02           C  
ANISOU 3681  CB  ILE A 304     4320   4571   5176    295    143    119       C  
ATOM   3682  CG1 ILE A 304      -6.261  -3.845  51.379  1.00 36.99           C  
ANISOU 3682  CG1 ILE A 304     4237   4617   5200    207     77    183       C  
ATOM   3683  CG2 ILE A 304      -5.045  -4.178  53.562  1.00 36.57           C  
ANISOU 3683  CG2 ILE A 304     4282   4498   5116    241    114     63       C  
ATOM   3684  CD1 ILE A 304      -5.157  -4.365  50.462  1.00 36.24           C  
ANISOU 3684  CD1 ILE A 304     4197   4453   5120    110     12     97       C  
ATOM   3685  N   TYR A 305      -5.838  -0.756  54.782  1.00 40.74           N  
ANISOU 3685  N   TYR A 305     5006   4941   5534    569    315     76       N  
ATOM   3686  CA  TYR A 305      -5.427  -0.180  56.060  1.00 41.51           C  
ANISOU 3686  CA  TYR A 305     5242   4963   5566    642    359     18       C  
ATOM   3687  C   TYR A 305      -6.636   0.204  56.897  1.00 44.66           C  
ANISOU 3687  C   TYR A 305     5638   5425   5905    816    457    110       C  
ATOM   3688  O   TYR A 305      -6.661  -0.031  58.113  1.00 43.95           O  
ANISOU 3688  O   TYR A 305     5589   5341   5769    867    491    102       O  
ATOM   3689  CB  TYR A 305      -4.545   1.052  55.853  1.00 40.37           C  
ANISOU 3689  CB  TYR A 305     5271   4680   5388    639    350    -67       C  
ATOM   3690  CG  TYR A 305      -3.308   0.847  55.015  1.00 38.98           C  
ANISOU 3690  CG  TYR A 305     5092   4458   5259    484    265   -137       C  
ATOM   3691  CD1 TYR A 305      -2.744  -0.412  54.844  1.00 38.42           C  
ANISOU 3691  CD1 TYR A 305     4919   4439   5239    373    207   -155       C  
ATOM   3692  CD2 TYR A 305      -2.695   1.931  54.401  1.00 41.26           C  
ANISOU 3692  CD2 TYR A 305     5490   4654   5533    458    245   -176       C  
ATOM   3693  CE1 TYR A 305      -1.600  -0.581  54.062  1.00 40.70           C  
ANISOU 3693  CE1 TYR A 305     5204   4701   5559    262    144   -204       C  
ATOM   3694  CE2 TYR A 305      -1.565   1.775  53.623  1.00 40.80           C  
ANISOU 3694  CE2 TYR A 305     5413   4577   5512    326    175   -219       C  
ATOM   3695  CZ  TYR A 305      -1.018   0.522  53.455  1.00 41.40           C  
ANISOU 3695  CZ  TYR A 305     5377   4719   5635    239    131   -230       C  
ATOM   3696  OH  TYR A 305       0.113   0.394  52.678  1.00 39.01           O  
ANISOU 3696  OH  TYR A 305     5054   4411   5356    137     76   -258       O  
ATOM   3697  N   CYS A 306      -7.653   0.788  56.261  1.00 44.24           N  
ANISOU 3697  N   CYS A 306     5532   5431   5846    919    510    209       N  
ATOM   3698  CA  CYS A 306      -8.857   1.155  56.996  1.00 47.29           C  
ANISOU 3698  CA  CYS A 306     5895   5906   6167   1112    619    325       C  
ATOM   3699  C   CYS A 306      -9.572  -0.073  57.557  1.00 47.83           C  
ANISOU 3699  C   CYS A 306     5783   6133   6256   1088    618    429       C  
ATOM   3700  O   CYS A 306     -10.164  -0.006  58.641  1.00 46.81           O  
ANISOU 3700  O   CYS A 306     5661   6063   6061   1227    702    491       O  
ATOM   3701  CB  CYS A 306      -9.788   1.959  56.087  1.00 46.72           C  
ANISOU 3701  CB  CYS A 306     5774   5888   6090   1224    672    432       C  
ATOM   3702  SG  CYS A 306     -11.292   2.553  56.882  1.00 51.16           S  
ANISOU 3702  SG  CYS A 306     6303   6579   6557   1508    828    605       S  
ATOM   3703  N   CYS A 307      -9.511  -1.206  56.851  1.00 48.54           N  
ANISOU 3703  N   CYS A 307     5730   6289   6425    914    521    452       N  
ATOM   3704  CA  CYS A 307     -10.229  -2.390  57.313  1.00 50.94           C  
ANISOU 3704  CA  CYS A 307     5872   6738   6744    866    502    564       C  
ATOM   3705  C   CYS A 307      -9.463  -3.156  58.387  1.00 45.88           C  
ANISOU 3705  C   CYS A 307     5288   6047   6095    804    475    474       C  
ATOM   3706  O   CYS A 307     -10.080  -3.739  59.285  1.00 46.54           O  
ANISOU 3706  O   CYS A 307     5293   6235   6154    841    505    562       O  
ATOM   3707  CB  CYS A 307     -10.538  -3.319  56.137  1.00 59.12           C  
ANISOU 3707  CB  CYS A 307     6768   7848   7849    697    396    633       C  
ATOM   3708  SG  CYS A 307     -11.856  -2.742  55.045  1.00 69.46           S  
ANISOU 3708  SG  CYS A 307     7936   9292   9163    757    420    814       S  
ATOM   3709  N   LEU A 308      -8.131  -3.185  58.316  1.00 46.19           N  
ANISOU 3709  N   LEU A 308     5451   5945   6152    711    418    316       N  
ATOM   3710  CA  LEU A 308      -7.352  -4.122  59.122  1.00 48.30           C  
ANISOU 3710  CA  LEU A 308     5744   6181   6426    622    371    243       C  
ATOM   3711  C   LEU A 308      -6.439  -3.457  60.149  1.00 49.82           C  
ANISOU 3711  C   LEU A 308     6108   6260   6563    676    404    128       C  
ATOM   3712  O   LEU A 308      -5.607  -4.144  60.753  1.00 51.87           O  
ANISOU 3712  O   LEU A 308     6397   6483   6828    595    358     58       O  
ATOM   3713  CB  LEU A 308      -6.529  -5.033  58.208  1.00 47.99           C  
ANISOU 3713  CB  LEU A 308     5682   6102   6451    450    264    181       C  
ATOM   3714  CG  LEU A 308      -7.359  -5.903  57.262  1.00 50.10           C  
ANISOU 3714  CG  LEU A 308     5814   6462   6758    362    204    289       C  
ATOM   3715  CD1 LEU A 308      -6.458  -6.750  56.374  1.00 47.45           C  
ANISOU 3715  CD1 LEU A 308     5508   6060   6462    220    107    212       C  
ATOM   3716  CD2 LEU A 308      -8.326  -6.781  58.066  1.00 49.55           C  
ANISOU 3716  CD2 LEU A 308     5634   6517   6675    358    206    413       C  
ATOM   3717  N   ASN A 309      -6.568  -2.151  60.374  1.00 46.18           N  
ANISOU 3717  N   ASN A 309     5773   5734   6038    808    476    111       N  
ATOM   3718  CA  ASN A 309      -5.695  -1.449  61.310  1.00 45.21           C  
ANISOU 3718  CA  ASN A 309     5849   5483   5844    838    488      4       C  
ATOM   3719  C   ASN A 309      -6.497  -0.378  62.030  1.00 48.13           C  
ANISOU 3719  C   ASN A 309     6341   5836   6111   1047    601     48       C  
ATOM   3720  O   ASN A 309      -7.054   0.520  61.387  1.00 46.70           O  
ANISOU 3720  O   ASN A 309     6191   5644   5910   1147    650     90       O  
ATOM   3721  CB  ASN A 309      -4.496  -0.829  60.589  1.00 45.83           C  
ANISOU 3721  CB  ASN A 309     6038   5435   5942    734    419   -101       C  
ATOM   3722  CG  ASN A 309      -3.466  -0.273  61.548  1.00 44.91           C  
ANISOU 3722  CG  ASN A 309     6116   5193   5754    709    396   -199       C  
ATOM   3723  OD1 ASN A 309      -3.600   0.848  62.045  1.00 42.39           O  
ANISOU 3723  OD1 ASN A 309     5984   4780   5343    813    443   -218       O  
ATOM   3724  ND2 ASN A 309      -2.427  -1.054  61.810  1.00 43.01           N  
ANISOU 3724  ND2 ASN A 309     5847   4948   5547    571    320   -253       N  
ATOM   3725  N   ASP A 310      -6.534  -0.468  63.366  1.00 42.19           N  
ANISOU 3725  N   ASP A 310     5670   5077   5282   1122    645     38       N  
ATOM   3726  CA  ASP A 310      -7.354   0.441  64.164  1.00 44.06           C  
ANISOU 3726  CA  ASP A 310     6037   5305   5398   1351    768     89       C  
ATOM   3727  C   ASP A 310      -6.898   1.886  64.021  1.00 44.46           C  
ANISOU 3727  C   ASP A 310     6351   5175   5366   1418    780      7       C  
ATOM   3728  O   ASP A 310      -7.728   2.804  63.973  1.00 47.41           O  
ANISOU 3728  O   ASP A 310     6811   5541   5663   1617    881     68       O  
ATOM   3729  CB  ASP A 310      -7.311   0.032  65.639  1.00 47.31           C  
ANISOU 3729  CB  ASP A 310     6512   5727   5735   1403    802     78       C  
ATOM   3730  CG  ASP A 310      -8.057  -1.264  65.916  1.00 54.29           C  
ANISOU 3730  CG  ASP A 310     7150   6804   6676   1383    814    194       C  
ATOM   3731  OD1 ASP A 310      -9.052  -1.547  65.219  1.00 57.13           O  
ANISOU 3731  OD1 ASP A 310     7316   7308   7084   1418    843    328       O  
ATOM   3732  OD2 ASP A 310      -7.653  -1.996  66.845  1.00 56.94           O  
ANISOU 3732  OD2 ASP A 310     7487   7147   7001   1324    787    162       O  
ATOM   3733  N   ARG A 311      -5.587   2.115  63.944  1.00 47.11           N  
ANISOU 3733  N   ARG A 311     6822   5368   5710   1254    677   -120       N  
ATOM   3734  CA  ARG A 311      -5.117   3.494  63.862  1.00 51.67           C  
ANISOU 3734  CA  ARG A 311     7673   5762   6198   1289    669   -191       C  
ATOM   3735  C   ARG A 311      -5.494   4.126  62.526  1.00 51.09           C  
ANISOU 3735  C   ARG A 311     7554   5687   6169   1315    680   -152       C  
ATOM   3736  O   ARG A 311      -5.951   5.276  62.483  1.00 51.15           O  
ANISOU 3736  O   ARG A 311     7746   5605   6085   1474    747   -139       O  
ATOM   3737  CB  ARG A 311      -3.608   3.551  64.104  1.00 57.23           C  
ANISOU 3737  CB  ARG A 311     8507   6338   6898   1081    542   -307       C  
ATOM   3738  CG  ARG A 311      -3.240   3.412  65.583  1.00 67.90           C  
ANISOU 3738  CG  ARG A 311    10012   7636   8152   1090    538   -354       C  
ATOM   3739  CD  ARG A 311      -1.829   3.907  65.872  1.00 77.95           C  
ANISOU 3739  CD  ARG A 311    11485   8754   9378    907    412   -451       C  
ATOM   3740  NE  ARG A 311      -1.566   4.024  67.306  1.00 87.15           N  
ANISOU 3740  NE  ARG A 311    12856   9840  10418    933    409   -493       N  
ATOM   3741  CZ  ARG A 311      -0.511   4.645  67.827  1.00 93.16           C  
ANISOU 3741  CZ  ARG A 311    13859  10449  11091    799    304   -564       C  
ATOM   3742  NH1 ARG A 311       0.387   5.212  67.032  1.00 95.31           N  
ANISOU 3742  NH1 ARG A 311    14181  10642  11389    629    197   -590       N  
ATOM   3743  NH2 ARG A 311      -0.353   4.707  69.144  1.00 94.96           N  
ANISOU 3743  NH2 ARG A 311    14277  10607  11196    827    301   -597       N  
ATOM   3744  N   PHE A 312      -5.351   3.379  61.428  1.00 49.65           N  
ANISOU 3744  N   PHE A 312     7142   5601   6120   1175    619   -129       N  
ATOM   3745  CA  PHE A 312      -5.746   3.916  60.131  1.00 46.79           C  
ANISOU 3745  CA  PHE A 312     6724   5250   5803   1195    626    -86       C  
ATOM   3746  C   PHE A 312      -7.256   4.102  60.028  1.00 47.70           C  
ANISOU 3746  C   PHE A 312     6746   5486   5893   1408    747     50       C  
ATOM   3747  O   PHE A 312      -7.715   5.060  59.395  1.00 49.22           O  
ANISOU 3747  O   PHE A 312     7007   5639   6054   1518    794     87       O  
ATOM   3748  CB  PHE A 312      -5.228   3.016  59.007  1.00 45.14           C  
ANISOU 3748  CB  PHE A 312     6310   5115   5727    999    532    -93       C  
ATOM   3749  CG  PHE A 312      -3.775   3.244  58.674  1.00 47.89           C  
ANISOU 3749  CG  PHE A 312     6753   5348   6094    819    427   -197       C  
ATOM   3750  CD1 PHE A 312      -3.382   4.377  57.969  1.00 47.99           C  
ANISOU 3750  CD1 PHE A 312     6902   5248   6083    801    402   -227       C  
ATOM   3751  CD2 PHE A 312      -2.804   2.336  59.067  1.00 47.62           C  
ANISOU 3751  CD2 PHE A 312     6665   5330   6097    672    352   -250       C  
ATOM   3752  CE1 PHE A 312      -2.043   4.597  57.668  1.00 47.65           C  
ANISOU 3752  CE1 PHE A 312     6928   5124   6054    626    302   -297       C  
ATOM   3753  CE2 PHE A 312      -1.469   2.546  58.763  1.00 48.60           C  
ANISOU 3753  CE2 PHE A 312     6851   5381   6235    514    260   -317       C  
ATOM   3754  CZ  PHE A 312      -1.088   3.678  58.064  1.00 50.20           C  
ANISOU 3754  CZ  PHE A 312     7176   5484   6414    485    232   -335       C  
ATOM   3755  N   ARG A 313      -8.044   3.222  60.651  1.00 46.40           N  
ANISOU 3755  N   ARG A 313     6420   5474   5734   1473    799    141       N  
ATOM   3756  CA  ARG A 313      -9.488   3.426  60.631  1.00 51.42           C  
ANISOU 3756  CA  ARG A 313     6950   6253   6335   1684    919    301       C  
ATOM   3757  C   ARG A 313      -9.873   4.670  61.419  1.00 55.82           C  
ANISOU 3757  C   ARG A 313     7760   6711   6738   1938   1039    304       C  
ATOM   3758  O   ARG A 313     -10.740   5.442  60.988  1.00 59.46           O  
ANISOU 3758  O   ARG A 313     8231   7207   7155   2124   1130    401       O  
ATOM   3759  CB  ARG A 313     -10.220   2.198  61.181  1.00 53.69           C  
ANISOU 3759  CB  ARG A 313     7006   6737   6655   1680    939    415       C  
ATOM   3760  CG  ARG A 313     -11.725   2.430  61.321  1.00 60.33           C  
ANISOU 3760  CG  ARG A 313     7725   7756   7444   1911   1071    612       C  
ATOM   3761  CD  ARG A 313     -12.508   1.177  61.678  1.00 67.12           C  
ANISOU 3761  CD  ARG A 313     8319   8838   8347   1870   1071    758       C  
ATOM   3762  NE  ARG A 313     -12.480   0.168  60.620  1.00 75.61           N  
ANISOU 3762  NE  ARG A 313     9181   9997   9551   1636    947    793       N  
ATOM   3763  CZ  ARG A 313     -13.345  -0.837  60.526  1.00 82.10           C  
ANISOU 3763  CZ  ARG A 313     9756  11021  10416   1574    924    958       C  
ATOM   3764  NH1 ARG A 313     -14.320  -0.962  61.416  1.00 86.21           N  
ANISOU 3764  NH1 ARG A 313    10178  11706  10871   1731   1024   1116       N  
ATOM   3765  NH2 ARG A 313     -13.243  -1.714  59.537  1.00 84.01           N  
ANISOU 3765  NH2 ARG A 313     9859  11303  10757   1352    798    973       N  
ATOM   3766  N   LEU A 314      -9.218   4.899  62.563  1.00 54.68           N  
ANISOU 3766  N   LEU A 314     7841   6433   6500   1955   1038    201       N  
ATOM   3767  CA  LEU A 314      -9.466   6.129  63.308  1.00 57.07           C  
ANISOU 3767  CA  LEU A 314     8452   6598   6632   2191   1140    184       C  
ATOM   3768  C   LEU A 314      -9.055   7.348  62.499  1.00 54.16           C  
ANISOU 3768  C   LEU A 314     8297   6051   6232   2190   1110    118       C  
ATOM   3769  O   LEU A 314      -9.727   8.386  62.537  1.00 55.18           O  
ANISOU 3769  O   LEU A 314     8598   6121   6246   2430   1218    168       O  
ATOM   3770  CB  LEU A 314      -8.715   6.103  64.639  1.00 60.71           C  
ANISOU 3770  CB  LEU A 314     9138   6932   6996   2164   1116     74       C  
ATOM   3771  CG  LEU A 314      -9.227   5.146  65.710  1.00 65.61           C  
ANISOU 3771  CG  LEU A 314     9624   7705   7600   2232   1177    142       C  
ATOM   3772  CD1 LEU A 314      -8.313   5.172  66.929  1.00 68.75           C  
ANISOU 3772  CD1 LEU A 314    10264   7953   7904   2171   1130     16       C  
ATOM   3773  CD2 LEU A 314     -10.654   5.513  66.088  1.00 67.41           C  
ANISOU 3773  CD2 LEU A 314     9823   8062   7727   2557   1358    302       C  
ATOM   3774  N   GLY A 315      -7.972   7.231  61.730  1.00 52.77           N  
ANISOU 3774  N   GLY A 315     8106   5793   6152   1931    968     20       N  
ATOM   3775  CA  GLY A 315      -7.556   8.354  60.909  1.00 53.89           C  
ANISOU 3775  CA  GLY A 315     8432   5775   6269   1907    929    -31       C  
ATOM   3776  C   GLY A 315      -8.540   8.651  59.796  1.00 55.54           C  
ANISOU 3776  C   GLY A 315     8487   6090   6525   2027    996     86       C  
ATOM   3777  O   GLY A 315      -8.826   9.814  59.505  1.00 58.89           O  
ANISOU 3777  O   GLY A 315     9111   6402   6864   2175   1049     96       O  
ATOM   3778  N   PHE A 316      -9.092   7.605  59.175  1.00 53.92           N  
ANISOU 3778  N   PHE A 316     7940   6101   6449   1965    992    182       N  
ATOM   3779  CA  PHE A 316     -10.103   7.816  58.144  1.00 53.25           C  
ANISOU 3779  CA  PHE A 316     7686   6141   6406   2069   1050    315       C  
ATOM   3780  C   PHE A 316     -11.388   8.390  58.726  1.00 58.45           C  
ANISOU 3780  C   PHE A 316     8384   6877   6946   2397   1218    452       C  
ATOM   3781  O   PHE A 316     -12.050   9.219  58.083  1.00 59.25           O  
ANISOU 3781  O   PHE A 316     8514   6986   7014   2557   1288    535       O  
ATOM   3782  CB  PHE A 316     -10.382   6.507  57.406  1.00 51.31           C  
ANISOU 3782  CB  PHE A 316     7088   6099   6307   1903    987    392       C  
ATOM   3783  CG  PHE A 316      -9.426   6.239  56.278  1.00 52.29           C  
ANISOU 3783  CG  PHE A 316     7159   6167   6540   1652    853    303       C  
ATOM   3784  CD1 PHE A 316      -9.639   6.795  55.029  1.00 54.22           C  
ANISOU 3784  CD1 PHE A 316     7368   6410   6823   1646    840    341       C  
ATOM   3785  CD2 PHE A 316      -8.311   5.441  56.469  1.00 52.35           C  
ANISOU 3785  CD2 PHE A 316     7155   6132   6606   1436    746    192       C  
ATOM   3786  CE1 PHE A 316      -8.759   6.555  53.988  1.00 55.81           C  
ANISOU 3786  CE1 PHE A 316     7524   6566   7114   1430    725    266       C  
ATOM   3787  CE2 PHE A 316      -7.425   5.200  55.433  1.00 53.42           C  
ANISOU 3787  CE2 PHE A 316     7242   6229   6828   1233    638    125       C  
ATOM   3788  CZ  PHE A 316      -7.650   5.757  54.194  1.00 53.29           C  
ANISOU 3788  CZ  PHE A 316     7193   6211   6845   1230    629    160       C  
ATOM   3789  N   LYS A 317     -11.739   7.990  59.949  1.00 60.26           N  
ANISOU 3789  N   LYS A 317     8624   7169   7105   2514   1292    486       N  
ATOM   3790  CA  LYS A 317     -12.887   8.603  60.604  1.00 66.36           C  
ANISOU 3790  CA  LYS A 317     9464   8010   7740   2858   1468    619       C  
ATOM   3791  C   LYS A 317     -12.640  10.082  60.861  1.00 64.50           C  
ANISOU 3791  C   LYS A 317     9636   7526   7345   3043   1525    536       C  
ATOM   3792  O   LYS A 317     -13.522  10.915  60.630  1.00 60.78           O  
ANISOU 3792  O   LYS A 317     9226   7079   6788   3310   1650    647       O  
ATOM   3793  CB  LYS A 317     -13.195   7.883  61.916  1.00 72.37           C  
ANISOU 3793  CB  LYS A 317    10177   8875   8446   2939   1531    661       C  
ATOM   3794  CG  LYS A 317     -13.983   6.596  61.761  1.00 77.43           C  
ANISOU 3794  CG  LYS A 317    10414   9808   9197   2869   1530    825       C  
ATOM   3795  CD  LYS A 317     -14.546   6.157  63.106  1.00 81.50           C  
ANISOU 3795  CD  LYS A 317    10904  10440   9621   3034   1635    909       C  
ATOM   3796  CE  LYS A 317     -15.391   4.902  62.977  1.00 83.70           C  
ANISOU 3796  CE  LYS A 317    10784  11017   9999   2956   1627   1097       C  
ATOM   3797  NZ  LYS A 317     -16.054   4.549  64.265  1.00 87.13           N  
ANISOU 3797  NZ  LYS A 317    11177  11591  10335   3142   1745   1210       N  
ATOM   3798  N   HIS A 318     -11.438  10.426  61.329  1.00 67.58           N  
ANISOU 3798  N   HIS A 318    10317   7674   7687   2899   1428    352       N  
ATOM   3799  CA  HIS A 318     -11.105  11.830  61.549  1.00 71.97           C  
ANISOU 3799  CA  HIS A 318    11301   7962   8081   3029   1451    265       C  
ATOM   3800  C   HIS A 318     -11.122  12.607  60.236  1.00 69.31           C  
ANISOU 3800  C   HIS A 318    10982   7564   7789   3008   1421    279       C  
ATOM   3801  O   HIS A 318     -11.549  13.767  60.196  1.00 71.04           O  
ANISOU 3801  O   HIS A 318    11461   7657   7873   3243   1510    304       O  
ATOM   3802  CB  HIS A 318      -9.734  11.923  62.226  1.00 79.99           C  
ANISOU 3802  CB  HIS A 318    12588   8752   9053   2809   1316     80       C  
ATOM   3803  CG  HIS A 318      -9.436  13.257  62.838  1.00 91.48           C  
ANISOU 3803  CG  HIS A 318    14538   9920  10301   2948   1335     -5       C  
ATOM   3804  ND1 HIS A 318     -10.306  14.325  62.770  1.00 96.71           N  
ANISOU 3804  ND1 HIS A 318    15412  10512  10820   3269   1474     67       N  
ATOM   3805  CD2 HIS A 318      -8.360  13.694  63.536  1.00 94.30           C  
ANISOU 3805  CD2 HIS A 318    15238  10036  10557   2804   1225   -148       C  
ATOM   3806  CE1 HIS A 318      -9.779  15.362  63.397  1.00 98.33           C  
ANISOU 3806  CE1 HIS A 318    16097  10426  10840   3320   1448    -40       C  
ATOM   3807  NE2 HIS A 318      -8.598  15.006  63.871  1.00 96.81           N  
ANISOU 3807  NE2 HIS A 318    15990  10125  10669   3028   1290   -169       N  
ATOM   3808  N   ALA A 319     -10.682  11.973  59.147  1.00 63.09           N  
ANISOU 3808  N   ALA A 319     9928   6863   7180   2741   1302    267       N  
ATOM   3809  CA  ALA A 319     -10.652  12.647  57.852  1.00 63.12           C  
ANISOU 3809  CA  ALA A 319     9930   6818   7233   2700   1265    280       C  
ATOM   3810  C   ALA A 319     -12.048  12.864  57.282  1.00 66.54           C  
ANISOU 3810  C   ALA A 319    10186   7432   7664   2954   1403    466       C  
ATOM   3811  O   ALA A 319     -12.274  13.844  56.562  1.00 66.99           O  
ANISOU 3811  O   ALA A 319    10369   7404   7682   3059   1431    492       O  
ATOM   3812  CB  ALA A 319      -9.794  11.854  56.866  1.00 56.07           C  
ANISOU 3812  CB  ALA A 319     8805   5978   6519   2359   1108    221       C  
ATOM   3813  N   PHE A 320     -12.993  11.971  57.580  1.00 68.73           N  
ANISOU 3813  N   PHE A 320    10168   7965   7980   3050   1483    610       N  
ATOM   3814  CA  PHE A 320     -14.331  12.069  57.011  1.00 75.62           C  
ANISOU 3814  CA  PHE A 320    10817   9054   8860   3263   1600    821       C  
ATOM   3815  C   PHE A 320     -15.399  12.372  58.057  1.00 86.09           C  
ANISOU 3815  C   PHE A 320    12200  10476  10033   3631   1792    960       C  
ATOM   3816  O   PHE A 320     -16.576  12.065  57.840  1.00 88.27           O  
ANISOU 3816  O   PHE A 320    12196  11015  10327   3788   1890   1175       O  
ATOM   3817  CB  PHE A 320     -14.669  10.794  56.239  1.00 72.49           C  
ANISOU 3817  CB  PHE A 320     9989   8914   8639   3054   1524    923       C  
ATOM   3818  CG  PHE A 320     -13.822  10.599  55.015  1.00 70.74           C  
ANISOU 3818  CG  PHE A 320     9704   8622   8551   2755   1365    822       C  
ATOM   3819  CD1 PHE A 320     -13.966  11.435  53.919  1.00 71.94           C  
ANISOU 3819  CD1 PHE A 320     9896   8725   8713   2790   1363    850       C  
ATOM   3820  CD2 PHE A 320     -12.869   9.599  54.966  1.00 67.34           C  
ANISOU 3820  CD2 PHE A 320     9184   8176   8228   2455   1226    705       C  
ATOM   3821  CE1 PHE A 320     -13.184  11.268  52.794  1.00 70.58           C  
ANISOU 3821  CE1 PHE A 320     9668   8494   8654   2527   1224    763       C  
ATOM   3822  CE2 PHE A 320     -12.083   9.427  53.845  1.00 66.49           C  
ANISOU 3822  CE2 PHE A 320     9024   8012   8227   2208   1094    622       C  
ATOM   3823  CZ  PHE A 320     -12.242  10.261  52.757  1.00 68.23           C  
ANISOU 3823  CZ  PHE A 320     9279   8189   8455   2241   1094    651       C  
ATOM   3824  N   ARG A 321     -15.004  12.934  59.197  1.00 94.43           N  
ANISOU 3824  N   ARG A 321    13610  11335  10933   3765   1842    853       N  
ATOM   3825  CA  ARG A 321     -15.941  13.370  60.238  1.00104.80           C  
ANISOU 3825  CA  ARG A 321    15050  12703  12067   4154   2039    971       C  
ATOM   3826  C   ARG A 321     -17.188  14.128  59.752  1.00114.55           C  
ANISOU 3826  C   ARG A 321    16230  14068  13226   4500   2206   1178       C  
ATOM   3827  O   ARG A 321     -18.259  13.989  60.347  1.00116.80           O  
ANISOU 3827  O   ARG A 321    16386  14563  13428   4788   2372   1367       O  
ATOM   3828  CB  ARG A 321     -15.197  14.227  61.278  1.00107.08           C  
ANISOU 3828  CB  ARG A 321    15845  12672  12169   4247   2050    794       C  
ATOM   3829  CG  ARG A 321     -14.420  15.435  60.746  1.00108.68           C  
ANISOU 3829  CG  ARG A 321    16432  12556  12307   4194   1972    648       C  
ATOM   3830  CD  ARG A 321     -13.440  15.939  61.814  1.00110.15           C  
ANISOU 3830  CD  ARG A 321    17078  12435  12340   4149   1913    457       C  
ATOM   3831  NE  ARG A 321     -12.967  17.306  61.591  1.00113.12           N  
ANISOU 3831  NE  ARG A 321    17912  12491  12578   4202   1881    356       N  
ATOM   3832  CZ  ARG A 321     -11.776  17.623  61.091  1.00113.03           C  
ANISOU 3832  CZ  ARG A 321    18060  12267  12617   3884   1693    204       C  
ATOM   3833  NH1 ARG A 321     -11.441  18.898  60.933  1.00115.01           N  
ANISOU 3833  NH1 ARG A 321    18744  12229  12725   3944   1666    132       N  
ATOM   3834  NH2 ARG A 321     -10.917  16.673  60.747  1.00110.17           N  
ANISOU 3834  NH2 ARG A 321    17434  11986  12441   3511   1532    134       N  
HETATM 3835  N   YCM A 322     -17.061  14.910  58.683  1.00121.69           N  
ANISOU 3835  N   YCM A 322    17218  14863  14154   4479   2168   1157       N  
HETATM 3836  CA  YCM A 322     -18.220  15.704  58.151  1.00132.41           C  
ANISOU 3836  CA  YCM A 322    18535  16337  15437   4817   2326   1359       C  
HETATM 3837  CB  YCM A 322     -17.791  16.533  56.944  1.00137.20           C  
ANISOU 3837  CB  YCM A 322    19272  16772  16086   4717   2241   1286       C  
HETATM 3838  SG  YCM A 322     -17.237  15.469  55.655  1.00138.41           S  
ANISOU 3838  SG  YCM A 322    19031  17052  16506   4248   2029   1250       S  
HETATM 3839  CD  YCM A 322     -15.996  16.555  55.044  1.00140.19           C  
ANISOU 3839  CD  YCM A 322    19655  16902  16708   4087   1903   1025       C  
HETATM 3840  CE  YCM A 322     -14.686  16.203  55.708  1.00140.66           C  
ANISOU 3840  CE  YCM A 322    19900  16766  16779   3816   1766    806       C  
HETATM 3841  OZ1 YCM A 322     -14.676  15.680  56.813  1.00141.49           O  
ANISOU 3841  OZ1 YCM A 322    20022  16903  16835   3856   1802    787       O  
HETATM 3842  NZ2 YCM A 322     -13.577  16.494  55.033  1.00139.77           N  
ANISOU 3842  NZ2 YCM A 322    19915  16462  16729   3541   1609    654       N  
HETATM 3843  C   YCM A 322     -19.377  14.824  57.762  1.00135.98           C  
ANISOU 3843  C   YCM A 322    18485  17189  15993   4860   2386   1621       C  
HETATM 3844  O   YCM A 322     -20.531  15.154  58.041  1.00139.28           O  
ANISOU 3844  O   YCM A 322    18825  17792  16303   5218   2571   1840       O  
ATOM   3845  N   CYS A 323     -19.077  13.702  57.113  1.00135.50           N  
ANISOU 3845  N   CYS A 323    18087  17266  16130   4496   2227   1611       N  
ATOM   3846  CA  CYS A 323     -20.102  12.763  56.660  1.00136.44           C  
ANISOU 3846  CA  CYS A 323    17728  17756  16356   4460   2239   1858       C  
ATOM   3847  C   CYS A 323     -20.978  12.271  57.811  1.00139.12           C  
ANISOU 3847  C   CYS A 323    17925  18326  16608   4687   2383   2037       C  
ATOM   3848  O   CYS A 323     -20.492  12.069  58.925  1.00139.61           O  
ANISOU 3848  O   CYS A 323    18167  18276  16601   4700   2399   1916       O  
ATOM   3849  CB  CYS A 323     -19.454  11.572  55.950  1.00132.89           C  
ANISOU 3849  CB  CYS A 323    17027  17357  16108   4013   2028   1776       C  
ATOM   3850  SG  CYS A 323     -18.954  11.900  54.247  1.00130.46           S  
ANISOU 3850  SG  CYS A 323    16691  16951  15929   3772   1882   1701       S  
ATOM   3851  N   PRO A 324     -22.275  12.076  57.542  1.00140.57           N  
ANISOU 3851  N   PRO A 324    17773  18844  16791   4862   2486   2339       N  
ATOM   3852  CA  PRO A 324     -23.219  11.678  58.603  1.00142.14           C  
ANISOU 3852  CA  PRO A 324    17810  19302  16895   5110   2642   2555       C  
ATOM   3853  C   PRO A 324     -23.117  10.200  58.972  1.00140.80           C  
ANISOU 3853  C   PRO A 324    17348  19304  16846   4808   2523   2578       C  
ATOM   3854  O   PRO A 324     -24.097   9.451  58.937  1.00142.24           O  
ANISOU 3854  O   PRO A 324    17145  19831  17069   4806   2547   2847       O  
ATOM   3855  CB  PRO A 324     -24.576  12.037  57.982  1.00143.82           C  
ANISOU 3855  CB  PRO A 324    17772  19809  17064   5284   2738   2867       C  
ATOM   3856  CG  PRO A 324     -24.364  11.888  56.518  1.00142.34           C  
ANISOU 3856  CG  PRO A 324    17397  19633  17054   5068   2601   2866       C  
ATOM   3857  CD  PRO A 324     -22.955  12.338  56.261  1.00140.77           C  
ANISOU 3857  CD  PRO A 324    17572  19028  16885   4867   2475   2514       C  
ATOM   3858  N   PHE A 325     -21.908   9.770  59.336  1.00137.61           N  
ANISOU 3858  N   PHE A 325    17132  18658  16495   4542   2389   2303       N  
ATOM   3859  CA  PHE A 325     -21.699   8.444  59.907  1.00135.01           C  
ANISOU 3859  CA  PHE A 325    16607  18441  16249   4297   2294   2294       C  
ATOM   3860  C   PHE A 325     -20.852   8.561  61.167  1.00133.41           C  
ANISOU 3860  C   PHE A 325    16735  18005  15949   4343   2320   2079       C  
ATOM   3861  O   PHE A 325     -21.275   8.162  62.257  1.00134.57           O  
ANISOU 3861  O   PHE A 325    16832  18282  16018   4484   2416   2172       O  
ATOM   3862  CB  PHE A 325     -21.012   7.500  58.913  1.00132.45           C  
ANISOU 3862  CB  PHE A 325    16115  18090  16121   3847   2062   2187       C  
ATOM   3863  CG  PHE A 325     -21.368   7.749  57.475  1.00132.96           C  
ANISOU 3863  CG  PHE A 325    16022  18227  16271   3765   2001   2280       C  
ATOM   3864  CD1 PHE A 325     -22.638   7.466  56.997  1.00134.76           C  
ANISOU 3864  CD1 PHE A 325    15898  18787  16518   3834   2043   2591       C  
ATOM   3865  CD2 PHE A 325     -20.419   8.236  56.591  1.00131.37           C  
ANISOU 3865  CD2 PHE A 325    16014  17772  16129   3601   1893   2068       C  
ATOM   3866  CE1 PHE A 325     -22.961   7.687  55.668  1.00134.44           C  
ANISOU 3866  CE1 PHE A 325    15716  18813  16552   3747   1978   2679       C  
ATOM   3867  CE2 PHE A 325     -20.735   8.456  55.261  1.00131.11           C  
ANISOU 3867  CE2 PHE A 325    15842  17804  16171   3523   1835   2151       C  
ATOM   3868  CZ  PHE A 325     -22.007   8.183  54.800  1.00132.47           C  
ANISOU 3868  CZ  PHE A 325    15677  18297  16359   3596   1876   2452       C  
ATOM   3869  N   ILE A 326     -19.644   9.106  61.012  1.00130.14           N  
ANISOU 3869  N   ILE A 326    16656  17254  15536   4214   2227   1801       N  
ATOM   3870  CA  ILE A 326     -18.698   9.213  62.114  1.00127.31           C  
ANISOU 3870  CA  ILE A 326    16626  16654  15094   4199   2214   1583       C  
ATOM   3871  C   ILE A 326     -19.175  10.261  63.113  1.00131.42           C  
ANISOU 3871  C   ILE A 326    17451  17098  15384   4625   2419   1623       C  
ATOM   3872  O   ILE A 326     -19.749  11.293  62.736  1.00134.22           O  
ANISOU 3872  O   ILE A 326    17924  17433  15642   4901   2538   1710       O  
ATOM   3873  CB  ILE A 326     -17.296   9.551  61.574  1.00121.60           C  
ANISOU 3873  CB  ILE A 326    16156  15615  14433   3928   2047   1308       C  
ATOM   3874  CG1 ILE A 326     -16.855   8.529  60.516  1.00116.20           C  
ANISOU 3874  CG1 ILE A 326    15178  15011  13960   3541   1861   1279       C  
ATOM   3875  CG2 ILE A 326     -16.280   9.607  62.707  1.00121.00           C  
ANISOU 3875  CG2 ILE A 326    16399  15304  14272   3874   2011   1099       C  
ATOM   3876  CD1 ILE A 326     -17.145   8.928  59.070  1.00113.69           C  
ANISOU 3876  CD1 ILE A 326    14741  14732  13723   3495   1823   1346       C  
ATOM   3877  N   SER A 327     -18.933  10.007  64.396  1.00131.45           N  
ANISOU 3877  N   SER A 327    17603  17051  15290   4692   2463   1559       N  
ATOM   3878  CA  SER A 327     -19.272  10.968  65.442  1.00133.91           C  
ANISOU 3878  CA  SER A 327    18265  17255  15362   5094   2652   1571       C  
ATOM   3879  C   SER A 327     -18.020  11.416  66.189  1.00133.07           C  
ANISOU 3879  C   SER A 327    18619  16781  15159   4997   2570   1287       C  
ATOM   3880  O   SER A 327     -18.039  11.589  67.407  1.00134.65           O  
ANISOU 3880  O   SER A 327    19057  16912  15194   5193   2667   1258       O  
ATOM   3881  CB  SER A 327     -20.284  10.371  66.424  1.00136.41           C  
ANISOU 3881  CB  SER A 327    18367  17864  15600   5328   2811   1791       C  
ATOM   3882  OG  SER A 327     -19.653   9.493  67.340  1.00136.40           O  
ANISOU 3882  OG  SER A 327    18370  17831  15625   5132   2730   1677       O  
TER    3883      SER A 327                                                      
HETATM 3884  C10 GAW A1501       6.114  -4.569  25.768  1.00 53.63           C  
ANISOU 3884  C10 GAW A1501     7470   6580   6327    550    121     42       C  
HETATM 3885  C13 GAW A1501       4.922  -2.813  27.801  1.00 49.88           C  
ANISOU 3885  C13 GAW A1501     6675   6118   6160    282     32     39       C  
HETATM 3886  C15 GAW A1501       2.872  -2.050  29.121  1.00 38.50           C  
ANISOU 3886  C15 GAW A1501     5133   4598   4898     82    -84     17       C  
HETATM 3887  C20 GAW A1501       3.266   1.423  29.029  1.00 40.79           C  
ANISOU 3887  C20 GAW A1501     5161   4980   5357    -12    -40    113       C  
HETATM 3888  C21 GAW A1501       3.702   0.285  31.294  1.00 44.27           C  
ANISOU 3888  C21 GAW A1501     5577   5410   5833     10    -28     50       C  
HETATM 3889  C22 GAW A1501       4.376  -0.513  32.224  1.00 42.85           C  
ANISOU 3889  C22 GAW A1501     5392   5247   5641     48     -6     25       C  
HETATM 3890  C24 GAW A1501       2.556  -0.474  33.829  1.00 44.12           C  
ANISOU 3890  C24 GAW A1501     5539   5320   5903    -30    -69    -15       C  
HETATM 3891  C26 GAW A1501       2.413   0.691  31.691  1.00 43.58           C  
ANISOU 3891  C26 GAW A1501     5482   5270   5806    -44    -71     44       C  
HETATM 3892  C01 GAW A1501       8.414  -2.890  29.501  1.00 54.07           C  
ANISOU 3892  C01 GAW A1501     6937   6923   6685    480    227    147       C  
HETATM 3893  C02 GAW A1501       7.375  -3.642  30.285  1.00 52.55           C  
ANISOU 3893  C02 GAW A1501     6837   6607   6521    432    163     62       C  
HETATM 3894  C03 GAW A1501       7.631  -3.897  31.654  1.00 52.28           C  
ANISOU 3894  C03 GAW A1501     6738   6586   6542    417    162     47       C  
HETATM 3895  C04 GAW A1501       6.728  -4.585  32.460  1.00 54.13           C  
ANISOU 3895  C04 GAW A1501     7041   6723   6804    372    107    -18       C  
HETATM 3896  C05 GAW A1501       5.541  -5.034  31.896  1.00 52.45           C  
ANISOU 3896  C05 GAW A1501     6958   6406   6563    329     42    -58       C  
HETATM 3897  C06 GAW A1501       5.285  -4.782  30.538  1.00 50.05           C  
ANISOU 3897  C06 GAW A1501     6725   6089   6205    334     34    -43       C  
HETATM 3898  C07 GAW A1501       6.161  -4.090  29.686  1.00 51.27           C  
ANISOU 3898  C07 GAW A1501     6820   6331   6329    391     96     11       C  
HETATM 3899  C08 GAW A1501       5.823  -3.859  28.218  1.00 50.13           C  
ANISOU 3899  C08 GAW A1501     6762   6166   6118    398     85     25       C  
HETATM 3900  C09 GAW A1501       6.376  -4.700  27.190  1.00 53.05           C  
ANISOU 3900  C09 GAW A1501     7288   6530   6338    533    130     29       C  
HETATM 3901  C12 GAW A1501       4.726  -2.750  26.381  1.00 44.35           C  
ANISOU 3901  C12 GAW A1501     6068   5403   5378    302     25     56       C  
HETATM 3902  C16 GAW A1501       4.896  -0.544  29.035  1.00 45.27           C  
ANISOU 3902  C16 GAW A1501     5811   5603   5786    137     29     86       C  
HETATM 3903  C18 GAW A1501       4.331   0.703  29.911  1.00 45.22           C  
ANISOU 3903  C18 GAW A1501     5704   5579   5899     38      0     94       C  
HETATM 3904  C19 GAW A1501       5.530   1.615  30.185  1.00 47.09           C  
ANISOU 3904  C19 GAW A1501     5841   5892   6159     25     38    145       C  
HETATM 3905  C23 GAW A1501       3.835  -0.884  33.456  1.00 43.96           C  
ANISOU 3905  C23 GAW A1501     5527   5349   5826     24    -29    -10       C  
HETATM 3906  C25 GAW A1501       1.850   0.326  32.926  1.00 47.81           C  
ANISOU 3906  C25 GAW A1501     6005   5777   6383    -59    -87     17       C  
HETATM 3907  C27 GAW A1501       0.395   0.808  33.332  1.00 54.35           C  
ANISOU 3907  C27 GAW A1501     6808   6575   7267    -95   -121     38       C  
HETATM 3908  C31 GAW A1501       4.664  -1.783  34.458  1.00 47.17           C  
ANISOU 3908  C31 GAW A1501     5929   5780   6215     69     -3    -33       C  
HETATM 3909  C36 GAW A1501       7.138  -6.876  24.955  1.00 63.93           C  
ANISOU 3909  C36 GAW A1501     9159   7807   7327    854    208      8       C  
HETATM 3910  C37 GAW A1501       6.051  -7.929  24.689  1.00 67.02           C  
ANISOU 3910  C37 GAW A1501     9820   8015   7629    796     98    -65       C  
HETATM 3911  C39 GAW A1501       6.208  -6.760  22.474  1.00 65.82           C  
ANISOU 3911  C39 GAW A1501     9683   7935   7390    831    139      1       C  
HETATM 3912  C40 GAW A1501       6.268  -5.416  23.251  1.00 61.32           C  
ANISOU 3912  C40 GAW A1501     8792   7486   7019    717    149     46       C  
HETATM 3913  C41 GAW A1501       4.111  -7.505  23.365  1.00 67.61           C  
ANISOU 3913  C41 GAW A1501    10035   7958   7694    556    -84    -79       C  
HETATM 3914  F28 GAW A1501       0.389   2.103  33.597  1.00 54.60           F  
ANISOU 3914  F28 GAW A1501     6800   6601   7345   -100   -100     57       F  
HETATM 3915  F29 GAW A1501      -0.057   0.210  34.386  1.00 54.11           F  
ANISOU 3915  F29 GAW A1501     6770   6533   7256    -97   -132     21       F  
HETATM 3916  F30 GAW A1501      -0.496   0.602  32.392  1.00 58.51           F  
ANISOU 3916  F30 GAW A1501     7362   7097   7771   -118   -162     69       F  
HETATM 3917  F32 GAW A1501       4.041  -2.887  34.728  1.00 48.33           F  
ANISOU 3917  F32 GAW A1501     6150   5875   6337     82    -31    -69       F  
HETATM 3918  F33 GAW A1501       5.845  -2.150  33.984  1.00 49.54           F  
ANISOU 3918  F33 GAW A1501     6226   6145   6451    142     44     -6       F  
HETATM 3919  F34 GAW A1501       4.941  -1.182  35.570  1.00 50.16           F  
ANISOU 3919  F34 GAW A1501     6236   6171   6651     32      1    -31       F  
HETATM 3920  N11 GAW A1501       5.265  -3.553  25.438  1.00 48.68           N  
ANISOU 3920  N11 GAW A1501     6767   5945   5785    419     63     55       N  
HETATM 3921  N14 GAW A1501       4.241  -1.803  28.666  1.00 38.91           N  
ANISOU 3921  N14 GAW A1501     5153   4725   4904    167     -6     43       N  
HETATM 3922  N35 GAW A1501       6.712  -5.452  24.709  1.00 59.48           N  
ANISOU 3922  N35 GAW A1501     8406   7305   6889    713    177     44       N  
HETATM 3923  N38 GAW A1501       5.561  -7.859  23.278  1.00 68.37           N  
ANISOU 3923  N38 GAW A1501    10156   8126   7697    780     57    -64       N  
HETATM 3924  O17 GAW A1501       6.030  -0.381  28.625  1.00 44.68           O  
ANISOU 3924  O17 GAW A1501     5696   5611   5668    196     87    131       O  
HETATM 3925  C1  CIT A1502       5.474  17.297  19.865  1.00 61.36           C  
ANISOU 3925  C1  CIT A1502     7718   7568   8029   -695   -210    965       C  
HETATM 3926  O1  CIT A1502       6.001  16.601  18.958  1.00 63.74           O  
ANISOU 3926  O1  CIT A1502     7928   8004   8285   -664   -171    999       O  
HETATM 3927  O2  CIT A1502       4.392  16.955  20.417  1.00 49.52           O  
ANISOU 3927  O2  CIT A1502     6267   5985   6563   -614   -201    880       O  
HETATM 3928  C2  CIT A1502       6.172  18.574  20.289  1.00 60.09           C  
ANISOU 3928  C2  CIT A1502     7619   7345   7867   -835   -274   1039       C  
HETATM 3929  C3  CIT A1502       5.640  18.979  21.647  1.00 64.21           C  
ANISOU 3929  C3  CIT A1502     8265   7708   8422   -838   -306    970       C  
HETATM 3930  O7  CIT A1502       4.222  18.797  21.670  1.00 63.10           O  
ANISOU 3930  O7  CIT A1502     8176   7487   8311   -707   -275    895       O  
HETATM 3931  C4  CIT A1502       6.374  18.078  22.635  1.00 64.00           C  
ANISOU 3931  C4  CIT A1502     8170   7752   8397   -854   -297    940       C  
HETATM 3932  C5  CIT A1502       6.068  18.325  24.083  1.00 64.10           C  
ANISOU 3932  C5  CIT A1502     8296   7629   8430   -865   -327    874       C  
HETATM 3933  O3  CIT A1502       5.161  19.116  24.398  1.00 68.08           O  
ANISOU 3933  O3  CIT A1502     8943   7978   8944   -829   -342    841       O  
HETATM 3934  O4  CIT A1502       6.752  17.702  24.919  1.00 66.71           O  
ANISOU 3934  O4  CIT A1502     8575   8014   8759   -897   -329    861       O  
HETATM 3935  C6  CIT A1502       5.923  20.441  21.898  1.00 66.13           C  
ANISOU 3935  C6  CIT A1502     8649   7827   8651   -961   -382   1032       C  
HETATM 3936  O5  CIT A1502       6.946  20.943  21.388  1.00 66.27           O  
ANISOU 3936  O5  CIT A1502     8628   7915   8638  -1092   -424   1138       O  
HETATM 3937  O6  CIT A1502       5.131  21.091  22.618  1.00 67.34           O  
ANISOU 3937  O6  CIT A1502     8960   7811   8815   -925   -401    982       O  
HETATM 3938  C1  OLA A1503      -3.155 -20.544  55.811  1.00 58.60           C  
ANISOU 3938  C1  OLA A1503     7809   6867   7590   -566   -695    100       C  
HETATM 3939  O1  OLA A1503      -2.903 -20.849  54.622  1.00 64.38           O  
ANISOU 3939  O1  OLA A1503     8689   7504   8270   -572   -739     69       O  
HETATM 3940  O2  OLA A1503      -3.601 -21.363  56.661  1.00 45.52           O  
ANISOU 3940  O2  OLA A1503     6164   5214   5917   -639   -748    159       O  
HETATM 3941  C2  OLA A1503      -2.909 -19.107  56.203  1.00 61.48           C  
ANISOU 3941  C2  OLA A1503     7993   7337   8030   -466   -577     66       C  
HETATM 3942  C3  OLA A1503      -1.829 -18.518  55.294  1.00 64.34           C  
ANISOU 3942  C3  OLA A1503     8403   7654   8391   -363   -520    -30       C  
HETATM 3943  C4  OLA A1503      -2.377 -17.836  54.041  1.00 68.77           C  
ANISOU 3943  C4  OLA A1503     8949   8223   8958   -398   -537     -7       C  
HETATM 3944  C5  OLA A1503      -1.281 -17.042  53.333  1.00 70.77           C  
ANISOU 3944  C5  OLA A1503     9210   8461   9221   -288   -462    -92       C  
HETATM 3945  C6  OLA A1503      -1.841 -16.184  52.201  1.00 74.21           C  
ANISOU 3945  C6  OLA A1503     9608   8917   9673   -316   -467    -69       C  
HETATM 3946  C7  OLA A1503      -1.901 -16.939  50.877  1.00 74.38           C  
ANISOU 3946  C7  OLA A1503     9797   8844   9622   -361   -545    -68       C  
HETATM 3947  C8  OLA A1503      -0.508 -17.131  50.286  1.00 74.01           C  
ANISOU 3947  C8  OLA A1503     9861   8730   9527   -240   -495   -155       C  
HETATM 3948  C9  OLA A1503      -0.596 -18.015  49.064  1.00 74.58           C  
ANISOU 3948  C9  OLA A1503    10144   8689   9503   -270   -572   -156       C  
HETATM 3949  C1  OLA A1504       1.863 -18.420  56.542  1.00 73.79           C  
ANISOU 3949  C1  OLA A1504     9615   8842   9578    -60   -339   -214       C  
HETATM 3950  O1  OLA A1504       2.018 -19.589  56.963  1.00 69.08           O  
ANISOU 3950  O1  OLA A1504     9117   8193   8937    -57   -374   -208       O  
HETATM 3951  O2  OLA A1504       1.792 -17.423  57.290  1.00 77.09           O  
ANISOU 3951  O2  OLA A1504     9904   9338  10050    -60   -293   -216       O  
HETATM 3952  C2  OLA A1504       1.747 -18.189  55.056  1.00 74.76           C  
ANISOU 3952  C2  OLA A1504     9801   8924   9679    -61   -354   -221       C  
HETATM 3953  C3  OLA A1504       2.298 -16.811  54.714  1.00 72.17           C  
ANISOU 3953  C3  OLA A1504     9363   8662   9396    -11   -284   -248       C  
HETATM 3954  C4  OLA A1504       2.329 -16.629  53.204  1.00 70.31           C  
ANISOU 3954  C4  OLA A1504     9194   8388   9132      1   -292   -256       C  
HETATM 3955  C5  OLA A1504       2.883 -15.269  52.801  1.00 69.21           C  
ANISOU 3955  C5  OLA A1504     8951   8311   9034     40   -230   -275       C  
HETATM 3956  C6  OLA A1504       3.366 -15.336  51.358  1.00 70.46           C  
ANISOU 3956  C6  OLA A1504     9192   8435   9145     90   -224   -287       C  
HETATM 3957  C7  OLA A1504       3.060 -14.058  50.593  1.00 70.81           C  
ANISOU 3957  C7  OLA A1504     9159   8515   9231     64   -206   -282       C  
HETATM 3958  C8  OLA A1504       2.572 -14.420  49.194  1.00 71.36           C  
ANISOU 3958  C8  OLA A1504     9340   8522   9252     46   -248   -275       C  
HETATM 3959  C9  OLA A1504       2.765 -13.253  48.255  1.00 71.08           C  
ANISOU 3959  C9  OLA A1504     9244   8524   9240     60   -213   -276       C  
HETATM 3960  C10 OLA A1504       3.214 -13.453  47.017  1.00 71.84           C  
ANISOU 3960  C10 OLA A1504     9430   8589   9277    111   -207   -284       C  
HETATM 3961  C11 OLA A1504       3.539 -14.844  46.526  1.00 72.11           C  
ANISOU 3961  C11 OLA A1504     9651   8538   9208    169   -231   -296       C  
HETATM 3962  C12 OLA A1504       3.058 -15.004  45.092  1.00 74.92           C  
ANISOU 3962  C12 OLA A1504    10138   8827   9502    149   -274   -293       C  
HETATM 3963  C1  OLA A1505      15.700  12.289  26.312  1.00 95.83           C  
ANISOU 3963  C1  OLA A1505    11115  13090  12204   -992   -154   1503       C  
HETATM 3964  O1  OLA A1505      16.328  12.867  25.396  1.00 97.44           O  
ANISOU 3964  O1  OLA A1505    11231  13422  12371  -1051   -158   1652       O  
HETATM 3965  O2  OLA A1505      14.779  11.475  26.095  1.00 95.46           O  
ANISOU 3965  O2  OLA A1505    11147  12953  12170   -821    -84   1351       O  
HETATM 3966  C2  OLA A1505      16.062  12.584  27.747  1.00 94.45           C  
ANISOU 3966  C2  OLA A1505    10960  12871  12057  -1145   -248   1515       C  
HETATM 3967  C3  OLA A1505      15.559  11.445  28.628  1.00 93.49           C  
ANISOU 3967  C3  OLA A1505    10878  12685  11960  -1006   -197   1366       C  
HETATM 3968  C4  OLA A1505      14.214  11.764  29.272  1.00 91.87           C  
ANISOU 3968  C4  OLA A1505    10874  12218  11813  -1011   -238   1180       C  
HETATM 3969  C5  OLA A1505      13.725  10.597  30.127  1.00 89.97           C  
ANISOU 3969  C5  OLA A1505    10660  11931  11595   -881   -188   1049       C  
HETATM 3970  C6  OLA A1505      12.652  11.047  31.114  1.00 87.61           C  
ANISOU 3970  C6  OLA A1505    10534  11408  11346   -922   -244    910       C  
HETATM 3971  C7  OLA A1505      11.613  11.919  30.421  1.00 85.76           C  
ANISOU 3971  C7  OLA A1505    10425  11026  11133   -922   -259    855       C  
HETATM 3972  C8  OLA A1505      10.725  12.633  31.432  1.00 83.26           C  
ANISOU 3972  C8  OLA A1505    10285  10501  10847   -970   -316    759       C  
HETATM 3973  C9  OLA A1505       9.640  11.696  31.906  1.00 80.53           C  
ANISOU 3973  C9  OLA A1505     9979  10084  10535   -819   -257    621       C  
HETATM 3974  C10 OLA A1505       9.424  11.526  33.206  1.00 80.95           C  
ANISOU 3974  C10 OLA A1505    10097  10061  10602   -827   -278    557       C  
HETATM 3975  C11 OLA A1505      10.255  12.263  34.231  1.00 82.28           C  
ANISOU 3975  C11 OLA A1505    10319  10198  10746   -988   -366    611       C  
HETATM 3976  C12 OLA A1505       9.428  12.532  35.485  1.00 82.96           C  
ANISOU 3976  C12 OLA A1505    10570  10111  10841   -971   -388    509       C  
HETATM 3977  C13 OLA A1505      10.185  12.091  36.735  1.00 83.85           C  
ANISOU 3977  C13 OLA A1505    10661  10261  10938  -1039   -425    517       C  
HETATM 3978  C14 OLA A1505       9.876  12.992  37.924  1.00 86.05           C  
ANISOU 3978  C14 OLA A1505    11150  10357  11187  -1115   -496    473       C  
HETATM 3979  C15 OLA A1505       8.390  12.970  38.259  1.00 86.88           C  
ANISOU 3979  C15 OLA A1505    11379  10318  11314   -956   -435    351       C  
HETATM 3980  C2  OLA A1506     -11.554  14.589  53.177  1.00 78.80           C  
ANISOU 3980  C2  OLA A1506    11686   8842   9410   2692   1224    474       C  
HETATM 3981  C3  OLA A1506     -10.154  14.661  52.581  1.00 76.50           C  
ANISOU 3981  C3  OLA A1506    11482   8395   9188   2376   1055    324       C  
HETATM 3982  C4  OLA A1506     -10.206  14.508  51.068  1.00 75.67           C  
ANISOU 3982  C4  OLA A1506    11149   8389   9211   2243    996    374       C  
HETATM 3983  C5  OLA A1506      -8.825  14.656  50.443  1.00 72.19           C  
ANISOU 3983  C5  OLA A1506    10794   7807   8826   1954    843    245       C  
HETATM 3984  C6  OLA A1506      -8.958  14.890  48.945  1.00 68.09           C  
ANISOU 3984  C6  OLA A1506    10139   7341   8390   1888    807    298       C  
HETATM 3985  C7  OLA A1506      -7.599  14.929  48.257  1.00 63.60           C  
ANISOU 3985  C7  OLA A1506     9609   6673   7883   1601    662    193       C  
HETATM 3986  C8  OLA A1506      -7.738  15.415  46.820  1.00 63.35           C  
ANISOU 3986  C8  OLA A1506     9508   6659   7904   1566    638    244       C  
HETATM 3987  C8  OLA A1507      15.123  -5.422  50.269  1.00 84.31           C  
ANISOU 3987  C8  OLA A1507     9865  11241  10927   -107    -60    320       C  
HETATM 3988  C9  OLA A1507      14.808  -4.133  50.990  1.00 83.60           C  
ANISOU 3988  C9  OLA A1507     9830  11071  10864   -290   -148    293       C  
HETATM 3989  C10 OLA A1507      15.179  -2.971  50.463  1.00 83.39           C  
ANISOU 3989  C10 OLA A1507     9780  11071  10833   -403   -192    357       C  
HETATM 3990  C11 OLA A1507      15.909  -2.936  49.143  1.00 82.38           C  
ANISOU 3990  C11 OLA A1507     9542  11075  10682   -350   -148    463       C  
HETATM 3991  C12 OLA A1507      15.726  -1.571  48.492  1.00 79.93           C  
ANISOU 3991  C12 OLA A1507     9270  10717  10384   -474   -197    477       C  
HETATM 3992  C13 OLA A1507      16.802  -1.310  47.443  1.00 79.81           C  
ANISOU 3992  C13 OLA A1507     9110  10878  10335   -476   -180    633       C  
HETATM 3993  C14 OLA A1507      16.410  -1.855  46.072  1.00 79.71           C  
ANISOU 3993  C14 OLA A1507     9103  10866  10317   -307    -83    600       C  
HETATM 3994  C15 OLA A1507      17.057  -3.207  45.786  1.00 79.72           C  
ANISOU 3994  C15 OLA A1507     9018  11000  10271   -114     10    659       C  
HETATM 3995  C16 OLA A1507      16.951  -3.569  44.308  1.00 77.77           C  
ANISOU 3995  C16 OLA A1507     8781  10777   9990     38     96    664       C  
HETATM 3996  C17 OLA A1507      17.470  -4.978  44.048  1.00 76.99           C  
ANISOU 3996  C17 OLA A1507     8657  10771   9826    260    196    702       C  
HETATM 3997  C18 OLA A1507      17.680  -5.218  42.568  1.00 76.77           C  
ANISOU 3997  C18 OLA A1507     8630  10804   9736    411    283    748       C  
HETATM 3998  C2  OLA A1508      18.157 -15.797  58.866  1.00 71.69           C  
ANISOU 3998  C2  OLA A1508     8202   9933   9102    658     89    476       C  
HETATM 3999  C3  OLA A1508      19.436 -15.640  58.058  1.00 76.66           C  
ANISOU 3999  C3  OLA A1508     8682  10764   9682    757    144    642       C  
HETATM 4000  C4  OLA A1508      19.143 -15.753  56.567  1.00 79.74           C  
ANISOU 4000  C4  OLA A1508     9154  11100  10045    883    214    608       C  
HETATM 4001  C5  OLA A1508      18.462 -17.075  56.229  1.00 80.12           C  
ANISOU 4001  C5  OLA A1508     9406  10988  10048   1056    267    510       C  
HETATM 4002  C6  OLA A1508      18.119 -17.145  54.744  1.00 80.33           C  
ANISOU 4002  C6  OLA A1508     9541  10944  10035   1162    322    470       C  
HETATM 4003  C7  OLA A1508      17.742 -18.568  54.346  1.00 80.34           C  
ANISOU 4003  C7  OLA A1508     9762  10806   9956   1356    374    410       C  
HETATM 4004  C8  OLA A1508      16.787 -18.571  53.160  1.00 79.80           C  
ANISOU 4004  C8  OLA A1508     9871  10578   9873   1364    373    304       C  
HETATM 4005  C9  OLA A1508      17.532 -18.228  51.894  1.00 81.52           C  
ANISOU 4005  C9  OLA A1508    10038  10906  10031   1491    451    391       C  
HETATM 4006  C10 OLA A1508      17.110 -18.712  50.729  1.00 83.08           C  
ANISOU 4006  C10 OLA A1508    10427  10986  10155   1608    488    336       C  
HETATM 4007  C11 OLA A1508      15.886 -19.596  50.676  1.00 82.39           C  
ANISOU 4007  C11 OLA A1508    10606  10653  10045   1589    436    196       C  
HETATM 4008  C13 OLA A1509       0.052  15.112  52.180  1.00 65.11           C  
ANISOU 4008  C13 OLA A1509    10675   6205   7859    396     -8   -312       C  
HETATM 4009  C14 OLA A1509      -0.389  15.459  53.597  1.00 70.48           C  
ANISOU 4009  C14 OLA A1509    11629   6751   8399    545     40   -353       C  
HETATM 4010  C15 OLA A1509       0.727  16.161  54.362  1.00 71.24           C  
ANISOU 4010  C15 OLA A1509    12036   6657   8375    353    -99   -399       C  
HETATM 4011  C16 OLA A1509       0.265  16.574  55.753  1.00 72.39           C  
ANISOU 4011  C16 OLA A1509    12501   6645   8358    514    -51   -445       C  
HETATM 4012  C17 OLA A1509       1.377  17.307  56.495  1.00 74.02           C  
ANISOU 4012  C17 OLA A1509    13049   6647   8430    298   -212   -485       C  
HETATM 4013  C18 OLA A1509       0.811  18.154  57.614  1.00 76.45           C  
ANISOU 4013  C18 OLA A1509    13794   6722   8531    488   -165   -531       C  
HETATM 4014  C6  OLA A1510      -9.687  -8.542  42.273  1.00 73.70           C  
ANISOU 4014  C6  OLA A1510     8930   9346   9727   -657   -650    628       C  
HETATM 4015  C7  OLA A1510      -9.734  -7.073  42.671  1.00 72.60           C  
ANISOU 4015  C7  OLA A1510     8665   9270   9648   -504   -519    629       C  
HETATM 4016  C8  OLA A1510      -9.057  -6.843  44.015  1.00 74.35           C  
ANISOU 4016  C8  OLA A1510     8881   9470   9900   -390   -419    541       C  
HETATM 4017  C9  OLA A1510      -9.536  -7.876  45.007  1.00 78.89           C  
ANISOU 4017  C9  OLA A1510     9423  10089  10462   -453   -463    603       C  
HETATM 4018  C10 OLA A1510      -9.209  -7.787  46.295  1.00 81.17           C  
ANISOU 4018  C10 OLA A1510     9688  10384  10770   -368   -387    560       C  
HETATM 4019  C11 OLA A1510      -8.370  -6.637  46.801  1.00 80.84           C  
ANISOU 4019  C11 OLA A1510     9663  10296  10756   -219   -267    451       C  
HETATM 4020  C12 OLA A1510      -8.664  -6.367  48.274  1.00 80.54           C  
ANISOU 4020  C12 OLA A1510     9560  10316  10728   -127   -189    478       C  
HETATM 4021  C13 OLA A1510      -9.973  -5.613  48.469  1.00 81.28           C  
ANISOU 4021  C13 OLA A1510     9518  10542  10825    -53   -139    632       C  
HETATM 4022  C14 OLA A1510     -10.067  -5.033  49.879  1.00 80.78           C  
ANISOU 4022  C14 OLA A1510     9430  10509  10754     90    -31    632       C  
HETATM 4023  C15 OLA A1510      -9.880  -6.100  50.955  1.00 77.66           C  
ANISOU 4023  C15 OLA A1510     9038  10119  10349     42    -54    617       C  
HETATM 4024  C16 OLA A1510     -10.136  -5.525  52.346  1.00 74.78           C  
ANISOU 4024  C16 OLA A1510     8648   9800   9965    189     54    638       C  
HETATM 4025  C17 OLA A1510      -9.565  -6.422  53.440  1.00 71.99           C  
ANISOU 4025  C17 OLA A1510     8336   9413   9603    153     39    574       C  
HETATM 4026  C18 OLA A1510     -10.303  -7.740  53.522  1.00 71.45           C  
ANISOU 4026  C18 OLA A1510     8179   9436   9532     23    -49    693       C  
HETATM 4027  C3  OLA A1511      16.244 -13.017  27.601  1.00 87.51           C  
ANISOU 4027  C3  OLA A1511    12252  11475   9521   2678   1144    467       C  
HETATM 4028  C4  OLA A1511      17.318 -12.806  28.663  1.00 87.11           C  
ANISOU 4028  C4  OLA A1511    11892  11657   9551   2722   1213    601       C  
HETATM 4029  C5  OLA A1511      16.702 -12.634  30.047  1.00 85.97           C  
ANISOU 4029  C5  OLA A1511    11636  11439   9589   2471   1087    522       C  
HETATM 4030  C6  OLA A1511      17.762 -12.261  31.079  1.00 86.67           C  
ANISOU 4030  C6  OLA A1511    11402  11766   9763   2474   1136    663       C  
HETATM 4031  C7  OLA A1511      17.373 -12.734  32.477  1.00 86.52           C  
ANISOU 4031  C7  OLA A1511    11384  11652   9838   2363   1056    585       C  
HETATM 4032  C8  OLA A1511      17.000 -11.578  33.402  1.00 84.90           C  
ANISOU 4032  C8  OLA A1511    10928  11488   9841   2055    943    574       C  
HETATM 4033  C9  OLA A1511      16.611 -12.137  34.752  1.00 84.14           C  
ANISOU 4033  C9  OLA A1511    10856  11295   9817   1971    874    497       C  
HETATM 4034  C10 OLA A1511      16.950 -11.534  35.893  1.00 83.65           C  
ANISOU 4034  C10 OLA A1511    10557  11345   9882   1826    834    549       C  
HETATM 4035  C11 OLA A1511      17.734 -10.241  35.914  1.00 82.81           C  
ANISOU 4035  C11 OLA A1511    10155  11459   9852   1715    839    692       C  
HETATM 4036  C12 OLA A1511      17.358  -9.433  37.151  1.00 79.44           C  
ANISOU 4036  C12 OLA A1511     9584  11013   9585   1450    724    656       C  
HETATM 4037  C10 OLC A1512      -6.383 -13.392  49.487  1.00 76.75           C  
ANISOU 4037  C10 OLC A1512     9575   9506  10081   -556   -566    285       C  
HETATM 4038  C9  OLC A1512      -5.445 -13.684  50.381  1.00 76.63           C  
ANISOU 4038  C9  OLC A1512     9600   9448  10068   -486   -517    196       C  
HETATM 4039  C11 OLC A1512      -6.949 -11.992  49.448  1.00 75.91           C  
ANISOU 4039  C11 OLC A1512     9318   9497  10025   -488   -489    333       C  
HETATM 4040  C8  OLC A1512      -4.981 -12.600  51.321  1.00 76.54           C  
ANISOU 4040  C8  OLC A1512     9490   9484  10107   -364   -399    147       C  
HETATM 4041  C24 OLC A1512       0.385 -14.445  60.911  1.00 67.75           C  
ANISOU 4041  C24 OLC A1512     8411   8365   8966    -58   -156   -178       C  
HETATM 4042  C12 OLC A1512      -6.410 -11.262  48.225  1.00 73.27           C  
ANISOU 4042  C12 OLC A1512     9034   9113   9693   -450   -469    269       C  
HETATM 4043  C7  OLC A1512      -4.098 -13.186  52.413  1.00 75.95           C  
ANISOU 4043  C7  OLC A1512     9459   9373  10025   -323   -373     78       C  
HETATM 4044  C13 OLC A1512      -7.046  -9.884  48.106  1.00 71.19           C  
ANISOU 4044  C13 OLC A1512     8641   8935   9472   -384   -401    325       C  
HETATM 4045  C6  OLC A1512      -4.906 -13.920  53.468  1.00 76.98           C  
ANISOU 4045  C6  OLC A1512     9542   9557  10150   -378   -406    160       C  
HETATM 4046  C5  OLC A1512      -4.110 -13.889  54.764  1.00 79.49           C  
ANISOU 4046  C5  OLC A1512     9852   9871  10479   -301   -341     94       C  
HETATM 4047  C4  OLC A1512      -4.616 -14.912  55.768  1.00 83.06           C  
ANISOU 4047  C4  OLC A1512    10294  10350  10913   -358   -383    156       C  
HETATM 4048  C3  OLC A1512      -3.626 -15.016  56.919  1.00 85.55           C  
ANISOU 4048  C3  OLC A1512    10629  10644  11230   -286   -330     76       C  
HETATM 4049  C2  OLC A1512      -2.202 -15.094  56.378  1.00 87.26           C  
ANISOU 4049  C2  OLC A1512    10945  10775  11435   -235   -317    -34       C  
HETATM 4050  C21 OLC A1512      -1.615 -13.901  59.560  1.00 76.17           C  
ANISOU 4050  C21 OLC A1512     9417   9469  10055   -105   -173    -78       C  
HETATM 4051  C1  OLC A1512      -1.228 -15.238  57.518  1.00 86.02           C  
ANISOU 4051  C1  OLC A1512    10794  10614  11276   -176   -275    -91       C  
HETATM 4052  C22 OLC A1512      -1.045 -14.859  60.586  1.00 70.87           C  
ANISOU 4052  C22 OLC A1512     8777   8784   9364   -109   -189    -96       C  
HETATM 4053  O19 OLC A1512      -0.716 -16.317  57.766  1.00 89.90           O  
ANISOU 4053  O19 OLC A1512    11361  11060  11737   -184   -309   -108       O  
HETATM 4054  O25 OLC A1512       1.062 -15.530  61.557  1.00 64.79           O  
ANISOU 4054  O25 OLC A1512     8075   7973   8570    -59   -180   -191       O  
HETATM 4055  O23 OLC A1512      -1.894 -14.808  61.734  1.00 69.79           O  
ANISOU 4055  O23 OLC A1512     8581   8713   9224   -106   -165    -38       O  
HETATM 4056  O20 OLC A1512      -0.908 -14.089  58.345  1.00 82.41           O  
ANISOU 4056  O20 OLC A1512    10268  10200  10843   -114   -201   -122       O  
HETATM 4057  C10 OLC A1513      15.038 -15.457  50.513  1.00 82.46           C  
ANISOU 4057  C10 OLC A1513    10175  10811  10344   1029    298    172       C  
HETATM 4058  C9  OLC A1513      15.840 -14.892  51.415  1.00 83.85           C  
ANISOU 4058  C9  OLC A1513    10170  11132  10559    960    284    255       C  
HETATM 4059  C11 OLC A1513      14.691 -14.765  49.219  1.00 80.50           C  
ANISOU 4059  C11 OLC A1513     9954  10538  10095   1010    306    153       C  
HETATM 4060  C8  OLC A1513      16.432 -13.518  51.210  1.00 83.59           C  
ANISOU 4060  C8  OLC A1513     9958  11235  10568    843    267    338       C  
HETATM 4061  C24 OLC A1513      21.363 -14.376  61.061  1.00114.31           C  
ANISOU 4061  C24 OLC A1513    13095  15870  14467    373    -57    908       C  
HETATM 4062  C16 OLC A1513      15.898 -15.557  44.017  1.00 84.07           C  
ANISOU 4062  C16 OLC A1513    10717  11039  10189   1598    573    274       C  
HETATM 4063  C12 OLC A1513      14.353 -15.823  48.176  1.00 80.78           C  
ANISOU 4063  C12 OLC A1513    10205  10457  10031   1170    346    109       C  
HETATM 4064  C7  OLC A1513      16.489 -12.808  52.559  1.00 83.58           C  
ANISOU 4064  C7  OLC A1513     9856  11267  10635    661    189    345       C  
HETATM 4065  C15 OLC A1513      16.351 -14.585  45.101  1.00 83.02           C  
ANISOU 4065  C15 OLC A1513    10319  11053  10172   1434    534    340       C  
HETATM 4066  C13 OLC A1513      14.605 -15.304  46.764  1.00 82.16           C  
ANISOU 4066  C13 OLC A1513    10380  10674  10163   1232    393    144       C  
HETATM 4067  C6  OLC A1513      17.455 -13.516  53.503  1.00 85.54           C  
ANISOU 4067  C6  OLC A1513    10018  11636  10848    729    205    441       C  
HETATM 4068  C14 OLC A1513      16.097 -15.139  46.499  1.00 83.28           C  
ANISOU 4068  C14 OLC A1513    10363  11030  10250   1373    484    295       C  
HETATM 4069  C5  OLC A1513      17.143 -13.212  54.964  1.00 86.05           C  
ANISOU 4069  C5  OLC A1513    10066  11662  10967    568    124    399       C  
HETATM 4070  C4  OLC A1513      17.746 -11.890  55.423  1.00 88.92           C  
ANISOU 4070  C4  OLC A1513    10290  12133  11361    382     54    481       C  
HETATM 4071  C3  OLC A1513      18.841 -12.116  56.459  1.00 94.03           C  
ANISOU 4071  C3  OLC A1513    10806  12939  11984    361     30    608       C  
HETATM 4072  C2  OLC A1513      18.837 -10.994  57.489  1.00 99.27           C  
ANISOU 4072  C2  OLC A1513    11440  13596  12682    124    -80    609       C  
HETATM 4073  C21 OLC A1513      21.595 -12.148  59.949  1.00112.78           C  
ANISOU 4073  C21 OLC A1513    12812  15737  14302    116   -139    971       C  
HETATM 4074  C1  OLC A1513      20.105 -11.022  58.312  1.00106.22           C  
ANISOU 4074  C1  OLC A1513    12161  14669  13528     71   -121    775       C  
HETATM 4075  C22 OLC A1513      22.224 -13.524  60.138  1.00115.40           C  
ANISOU 4075  C22 OLC A1513    13081  16177  14587    333    -57   1056       C  
HETATM 4076  O19 OLC A1513      20.816 -10.033  58.382  1.00108.83           O  
ANISOU 4076  O19 OLC A1513    12388  15112  13851    -87   -192    889       O  
HETATM 4077  O25 OLC A1513      22.108 -15.528  61.472  1.00115.75           O  
ANISOU 4077  O25 OLC A1513    13210  16169  14600    540     -2   1011       O  
HETATM 4078  O23 OLC A1513      22.347 -14.171  58.866  1.00117.54           O  
ANISOU 4078  O23 OLC A1513    13360  16476  14822    563     62   1078       O  
HETATM 4079  O20 OLC A1513      20.501 -12.220  59.036  1.00109.86           O  
ANISOU 4079  O20 OLC A1513    12593  15189  13960    196    -84    815       O  
HETATM 4080  C10 OLC A1514     -11.454   8.568  32.454  1.00 68.61           C  
ANISOU 4080  C10 OLC A1514     8080   8734   9255    397      1    983       C  
HETATM 4081  C9  OLC A1514     -11.138   9.507  31.569  1.00 70.12           C  
ANISOU 4081  C9  OLC A1514     8336   8865   9443    414      9    971       C  
HETATM 4082  C8  OLC A1514     -11.572   9.358  30.131  1.00 73.27           C  
ANISOU 4082  C8  OLC A1514     8669   9334   9837    326    -64   1051       C  
HETATM 4083  C24 OLC A1514     -12.690   6.232  19.927  1.00 88.61           C  
ANISOU 4083  C24 OLC A1514    10736  11480  11453   -604   -792   1336       C  
HETATM 4084  C7  OLC A1514     -12.056  10.698  29.593  1.00 77.56           C  
ANISOU 4084  C7  OLC A1514     9222   9872  10374    443    -14   1135       C  
HETATM 4085  C6  OLC A1514     -13.015  10.464  28.434  1.00 83.92           C  
ANISOU 4085  C6  OLC A1514     9904  10807  11172    383    -81   1281       C  
HETATM 4086  C5  OLC A1514     -12.643  11.280  27.200  1.00 87.72           C  
ANISOU 4086  C5  OLC A1514    10450  11233  11647    364    -96   1269       C  
HETATM 4087  C4  OLC A1514     -13.069  10.531  25.942  1.00 91.40           C  
ANISOU 4087  C4  OLC A1514    10840  11792  12097    214   -206   1343       C  
HETATM 4088  C3  OLC A1514     -12.455   9.133  25.927  1.00 92.73           C  
ANISOU 4088  C3  OLC A1514    11042  11942  12250     55   -286   1245       C  
HETATM 4089  C2  OLC A1514     -13.071   8.244  24.853  1.00 94.32           C  
ANISOU 4089  C2  OLC A1514    11191  12232  12414    -99   -409   1334       C  
HETATM 4090  C21 OLC A1514     -12.758   8.488  20.987  1.00 93.63           C  
ANISOU 4090  C21 OLC A1514    11230  12127  12218   -325   -585   1371       C  
HETATM 4091  C1  OLC A1514     -12.491   8.573  23.495  1.00 97.10           C  
ANISOU 4091  C1  OLC A1514    11627  12528  12737   -158   -444   1289       C  
HETATM 4092  C22 OLC A1514     -13.432   7.564  19.980  1.00 90.89           C  
ANISOU 4092  C22 OLC A1514    10882  11849  11803   -490   -727   1461       C  
HETATM 4093  O19 OLC A1514     -11.488   9.262  23.390  1.00 97.19           O  
ANISOU 4093  O19 OLC A1514    11732  12437  12759   -107   -384   1181       O  
HETATM 4094  O25 OLC A1514     -13.169   5.448  18.828  1.00 88.39           O  
ANISOU 4094  O25 OLC A1514    10769  11477  11337   -764   -932   1401       O  
HETATM 4095  O23 OLC A1514     -14.780   7.331  20.402  1.00 90.73           O  
ANISOU 4095  O23 OLC A1514    10707  11972  11796   -516   -776   1641       O  
HETATM 4096  O20 OLC A1514     -13.142   8.064  22.295  1.00 98.39           O  
ANISOU 4096  O20 OLC A1514    11763  12766  12853   -286   -558   1389       O  
HETATM 4097  C10 OLC A1515      14.858 -22.527  52.353  1.00 79.77           C  
ANISOU 4097  C10 OLC A1515    10712   9982   9613   1677    360     71       C  
HETATM 4098  C9  OLC A1515      13.980 -22.442  53.352  1.00 78.30           C  
ANISOU 4098  C9  OLC A1515    10504   9730   9518   1483    269      8       C  
HETATM 4099  C8  OLC A1515      14.415 -22.680  54.780  1.00 76.54           C  
ANISOU 4099  C8  OLC A1515    10163   9585   9334   1464    261     49       C  
HETATM 4100  C24 OLC A1515      18.228 -16.763  64.900  1.00105.54           C  
ANISOU 4100  C24 OLC A1515    12454  14228  13419    338   -130    463       C  
HETATM 4101  C7  OLC A1515      13.891 -21.548  55.656  1.00 75.44           C  
ANISOU 4101  C7  OLC A1515     9831   9503   9329   1229    195     21       C  
HETATM 4102  C6  OLC A1515      14.592 -21.503  57.010  1.00 76.15           C  
ANISOU 4102  C6  OLC A1515     9762   9716   9454   1209    194     83       C  
HETATM 4103  C5  OLC A1515      14.226 -20.214  57.733  1.00 77.51           C  
ANISOU 4103  C5  OLC A1515     9764   9948   9736    996    138     63       C  
HETATM 4104  C4  OLC A1515      14.936 -20.074  59.073  1.00 79.34           C  
ANISOU 4104  C4  OLC A1515     9849  10301   9995    954    125    125       C  
HETATM 4105  C3  OLC A1515      14.715 -18.671  59.626  1.00 83.67           C  
ANISOU 4105  C3  OLC A1515    10260  10903  10626    758     72    112       C  
HETATM 4106  C2  OLC A1515      15.089 -18.565  61.102  1.00 91.80           C  
ANISOU 4106  C2  OLC A1515    11197  12004  11678    677     33    146       C  
HETATM 4107  C21 OLC A1515      18.541 -17.937  62.717  1.00104.28           C  
ANISOU 4107  C21 OLC A1515    12336  14079  13206    664     19    503       C  
HETATM 4108  C1  OLC A1515      16.573 -18.322  61.255  1.00 98.19           C  
ANISOU 4108  C1  OLC A1515    11842  13009  12459    722     55    286       C  
HETATM 4109  C22 OLC A1515      18.990 -16.763  63.581  1.00106.59           C  
ANISOU 4109  C22 OLC A1515    12505  14469  13525    456    -67    559       C  
HETATM 4110  O19 OLC A1515      17.330 -18.468  60.309  1.00101.23           O  
ANISOU 4110  O19 OLC A1515    12186  13479  12798    851    115    364       O  
HETATM 4111  O25 OLC A1515      18.512 -15.551  65.608  1.00105.22           O  
ANISOU 4111  O25 OLC A1515    12353  14238  13388    136   -217    494       O  
HETATM 4112  O23 OLC A1515      20.396 -16.865  63.841  1.00108.81           O  
ANISOU 4112  O23 OLC A1515    12610  14967  13763    491    -65    742       O  
HETATM 4113  O20 OLC A1515      17.127 -17.900  62.532  1.00100.60           O  
ANISOU 4113  O20 OLC A1515    12030  13414  12780    610      3    344       O  
HETATM 4114  C8  OLC A1516      10.106  11.461  41.981  1.00 75.91           C  
ANISOU 4114  C8  OLC A1516     9973   8999   9870  -1114   -533    324       C  
HETATM 4115  C24 OLC A1516       9.711  10.233  54.148  1.00105.35           C  
ANISOU 4115  C24 OLC A1516    14748  12092  13190  -1195   -762   -107       C  
HETATM 4116  C7  OLC A1516       9.701  10.932  43.352  1.00 77.25           C  
ANISOU 4116  C7  OLC A1516    10212   9105  10032  -1057   -519    239       C  
HETATM 4117  C6  OLC A1516      10.651  11.407  44.447  1.00 80.80           C  
ANISOU 4117  C6  OLC A1516    10757   9524  10419  -1235   -631    287       C  
HETATM 4118  C5  OLC A1516      10.271  10.784  45.787  1.00 81.11           C  
ANISOU 4118  C5  OLC A1516    10854   9514  10449  -1168   -610    203       C  
HETATM 4119  C4  OLC A1516      11.044  11.389  46.954  1.00 83.67           C  
ANISOU 4119  C4  OLC A1516    11328   9768  10695  -1347   -731    238       C  
HETATM 4120  C3  OLC A1516      10.456  10.930  48.286  1.00 87.06           C  
ANISOU 4120  C3  OLC A1516    11860  10115  11105  -1258   -702    139       C  
HETATM 4121  C2  OLC A1516       8.933  10.829  48.219  1.00 90.53           C  
ANISOU 4121  C2  OLC A1516    12374  10454  11571  -1036   -587     29       C  
HETATM 4122  C21 OLC A1516       9.582  10.121  51.663  1.00103.52           C  
ANISOU 4122  C21 OLC A1516    14218  12019  13095  -1133   -681    -39       C  
HETATM 4123  C1  OLC A1516       8.337  10.727  49.605  1.00 95.87           C  
ANISOU 4123  C1  OLC A1516    13207  11020  12199   -962   -570    -52       C  
HETATM 4124  C22 OLC A1516       8.825   9.875  52.959  1.00104.73           C  
ANISOU 4124  C22 OLC A1516    14514  12073  13205  -1019   -639   -130       C  
HETATM 4125  O19 OLC A1516       7.480  11.514  49.971  1.00 96.79           O  
ANISOU 4125  O19 OLC A1516    13545  10970  12260   -878   -549   -106       O  
HETATM 4126  O25 OLC A1516       8.976  11.038  55.078  1.00106.05           O  
ANISOU 4126  O25 OLC A1516    15156  11967  13172  -1130   -763   -183       O  
HETATM 4127  O23 OLC A1516       7.665  10.712  52.967  1.00107.07           O  
ANISOU 4127  O23 OLC A1516    15026  12200  13456   -881   -583   -193       O  
HETATM 4128  O20 OLC A1516       8.792   9.715  50.545  1.00100.09           O  
ANISOU 4128  O20 OLC A1516    13642  11645  12743   -978   -573    -60       O  
HETATM 4129  C1  PEG A1517      -3.121   3.890   9.262  1.00 82.32           C  
ANISOU 4129  C1  PEG A1517    11502  10175   9601   -384   -622    640       C  
HETATM 4130  O1  PEG A1517      -3.902   5.055   8.981  1.00 82.47           O  
ANISOU 4130  O1  PEG A1517    11366  10248   9721   -459   -658    728       O  
HETATM 4131  C2  PEG A1517      -1.636   4.221   9.150  1.00 79.61           C  
ANISOU 4131  C2  PEG A1517    11132   9880   9237   -233   -473    611       C  
HETATM 4132  O2  PEG A1517      -1.218   4.980  10.284  1.00 72.61           O  
ANISOU 4132  O2  PEG A1517    10036   9044   8508   -208   -399    614       O  
HETATM 4133  C3  PEG A1517      -1.255   4.168  11.451  1.00 74.58           C  
ANISOU 4133  C3  PEG A1517    10294   9253   8789   -205   -407    556       C  
HETATM 4134  C4  PEG A1517      -0.670   4.928  12.635  1.00 72.08           C  
ANISOU 4134  C4  PEG A1517     9783   8985   8618   -172   -326    554       C  
HETATM 4135  O4  PEG A1517      -1.363   4.512  13.811  1.00 67.82           O  
ANISOU 4135  O4  PEG A1517     9204   8407   8158   -225   -374    527       O  
HETATM 4136  C1  PEG A1518       9.853  19.123  25.028  1.00 90.88           C  
ANISOU 4136  C1  PEG A1518    11565  11230  11736  -1316   -493   1150       C  
HETATM 4137  O1  PEG A1518       9.574  19.351  26.414  1.00 90.43           O  
ANISOU 4137  O1  PEG A1518    11653  11021  11686  -1346   -540   1075       O  
HETATM 4138  C2  PEG A1518      10.354  17.695  24.844  1.00 89.86           C  
ANISOU 4138  C2  PEG A1518    11236  11300  11606  -1218   -410   1149       C  
HETATM 4139  O2  PEG A1518      10.804  17.192  26.101  1.00 89.96           O  
ANISOU 4139  O2  PEG A1518    11234  11323  11623  -1250   -429   1124       O  
HETATM 4140  C3  PEG A1518      11.218  15.831  26.021  1.00 88.69           C  
ANISOU 4140  C3  PEG A1518    10912  11329  11457  -1139   -347   1116       C  
HETATM 4141  C4  PEG A1518      11.429  15.289  27.430  1.00 90.44           C  
ANISOU 4141  C4  PEG A1518    11142  11529  11691  -1151   -364   1063       C  
HETATM 4142  O4  PEG A1518      12.821  15.318  27.764  1.00 92.57           O  
ANISOU 4142  O4  PEG A1518    11293  11952  11927  -1282   -407   1204       O  
HETATM 4143  C1  PEG A1519      -5.259  14.035  29.251  1.00 84.69           C  
ANISOU 4143  C1  PEG A1519    10825  10112  11242    220      0    579       C  
HETATM 4144  O1  PEG A1519      -6.426  13.911  28.429  1.00 84.25           O  
ANISOU 4144  O1  PEG A1519    10674  10144  11193    268     -1    672       O  
HETATM 4145  C2  PEG A1519      -4.496  15.307  28.895  1.00 87.05           C  
ANISOU 4145  C2  PEG A1519    11253  10303  11519    189     -9    573       C  
HETATM 4146  O2  PEG A1519      -3.093  15.113  29.077  1.00 87.90           O  
ANISOU 4146  O2  PEG A1519    11393  10384  11620     67    -42    506       O  
HETATM 4147  C3  PEG A1519      -2.399  16.357  29.183  1.00 88.13           C  
ANISOU 4147  C3  PEG A1519    11569  10295  11621     29    -60    506       C  
HETATM 4148  C4  PEG A1519      -1.003  16.226  28.585  1.00 85.50           C  
ANISOU 4148  C4  PEG A1519    11207   9996  11283   -122   -107    495       C  
HETATM 4149  O4  PEG A1519      -1.096  16.289  27.156  1.00 83.13           O  
ANISOU 4149  O4  PEG A1519    10840   9760  10985   -144   -117    546       O  
HETATM 4150  C1  PEG A1520      19.288  -0.788  33.795  1.00 96.01           C  
ANISOU 4150  C1  PEG A1520    10770  13757  11951    476    488   1289       C  
HETATM 4151  O1  PEG A1520      19.178   0.052  34.951  1.00 96.43           O  
ANISOU 4151  O1  PEG A1520    10785  13756  12098    233    363   1277       O  
HETATM 4152  C2  PEG A1520      19.267   0.067  32.534  1.00 94.45           C  
ANISOU 4152  C2  PEG A1520    10554  13596  11735    440    495   1347       C  
HETATM 4153  O2  PEG A1520      20.089   1.215  32.741  1.00 95.21           O  
ANISOU 4153  O2  PEG A1520    10469  13846  11862    240    423   1521       O  
HETATM 4154  C3  PEG A1520      20.387   1.908  31.529  1.00 95.64           C  
ANISOU 4154  C3  PEG A1520    10461  14000  11879    230    448   1630       C  
HETATM 4155  C4  PEG A1520      21.101   3.218  31.849  1.00 95.72           C  
ANISOU 4155  C4  PEG A1520    10311  14129  11927    -33    337   1802       C  
HETATM 4156  O4  PEG A1520      20.253   4.050  32.649  1.00 93.70           O  
ANISOU 4156  O4  PEG A1520    10183  13650  11768   -256    203   1665       O  
HETATM 4157  C1  PEG A1521     -11.678  -7.438  35.407  1.00 82.46           C  
ANISOU 4157  C1  PEG A1521    10198  10469  10665  -1033  -1009    900       C  
HETATM 4158  O1  PEG A1521     -12.033  -6.554  36.475  1.00 81.04           O  
ANISOU 4158  O1  PEG A1521     9816  10405  10573   -909   -892    951       O  
HETATM 4159  C2  PEG A1521     -10.412  -8.199  35.780  1.00 81.23           C  
ANISOU 4159  C2  PEG A1521    10224  10165  10476   -984   -979    724       C  
HETATM 4160  O2  PEG A1521     -10.102  -9.145  34.758  1.00 81.63           O  
ANISOU 4160  O2  PEG A1521    10504  10093  10418  -1087  -1090    679       O  
HETATM 4161  C3  PEG A1521      -8.832  -9.759  34.969  1.00 81.69           C  
ANISOU 4161  C3  PEG A1521    10685   9967  10385  -1002  -1042    520       C  
HETATM 4162  C4  PEG A1521      -8.654 -10.924  34.001  1.00 83.06           C  
ANISOU 4162  C4  PEG A1521    11136  10002  10420  -1105  -1167    489       C  
HETATM 4163  O4  PEG A1521      -8.669 -10.435  32.656  1.00 85.77           O  
ANISOU 4163  O4  PEG A1521    11540  10329  10720  -1115  -1189    492       O  
HETATM 4164  C1  PEG A1522      20.669 -24.514  88.808  1.00 83.09           C  
ANISOU 4164  C1  PEG A1522     9754  11808  10007   -415   -912    896       C  
HETATM 4165  O1  PEG A1522      19.812 -23.398  88.547  1.00 79.01           O  
ANISOU 4165  O1  PEG A1522     9364  11166   9490   -508   -915    765       O  
HETATM 4166  C2  PEG A1522      21.761 -24.598  87.747  1.00 88.10           C  
ANISOU 4166  C2  PEG A1522    10217  12588  10670   -345   -898   1031       C  
HETATM 4167  O2  PEG A1522      22.694 -25.602  88.139  1.00 92.72           O  
ANISOU 4167  O2  PEG A1522    10676  13318  11236   -250   -898   1183       O  
HETATM 4168  C3  PEG A1522      24.032 -25.277  87.766  1.00 95.06           C  
ANISOU 4168  C3  PEG A1522    10784  13824  11512   -278   -943   1369       C  
HETATM 4169  C4  PEG A1522      24.985 -25.908  88.775  1.00 96.75           C  
ANISOU 4169  C4  PEG A1522    10882  14205  11674   -280   -997   1537       C  
HETATM 4170  O4  PEG A1522      24.568 -25.558  90.102  1.00 96.41           O  
ANISOU 4170  O4  PEG A1522    10956  14095  11580   -452  -1086   1471       O  
HETATM 4171  C1  PEG A1523       3.503  14.315  15.307  1.00 78.93           C  
ANISOU 4171  C1  PEG A1523     9885  10024  10079   -385    -98    919       C  
HETATM 4172  O1  PEG A1523       3.752  15.198  16.404  1.00 79.06           O  
ANISOU 4172  O1  PEG A1523     9898   9977  10163   -449   -120    928       O  
HETATM 4173  C2  PEG A1523       4.663  14.410  14.329  1.00 79.14           C  
ANISOU 4173  C2  PEG A1523     9868  10170  10032   -391    -61   1000       C  
HETATM 4174  O2  PEG A1523       5.815  13.857  14.955  1.00 78.52           O  
ANISOU 4174  O2  PEG A1523     9728  10175   9931   -379    -21   1010       O  
HETATM 4175  C3  PEG A1523       7.000  14.529  14.534  1.00 82.28           C  
ANISOU 4175  C3  PEG A1523    10128  10759  10377   -433     -3   1127       C  
HETATM 4176  C4  PEG A1523       8.229  13.742  14.972  1.00 84.91           C  
ANISOU 4176  C4  PEG A1523    10376  11222  10663   -392     53   1161       C  
HETATM 4177  O4  PEG A1523       8.412  12.613  14.108  1.00 87.05           O  
ANISOU 4177  O4  PEG A1523    10666  11577  10830   -255    124   1148       O  
HETATM 4178  C1  PEG A1524       2.608  14.995  35.539  1.00 90.35           C  
ANISOU 4178  C1  PEG A1524    12103  10413  11815   -380   -207    241       C  
HETATM 4179  O1  PEG A1524       4.003  15.198  35.286  1.00 90.57           O  
ANISOU 4179  O1  PEG A1524    12106  10480  11825   -550   -277    286       O  
HETATM 4180  C2  PEG A1524       1.861  14.807  34.222  1.00 88.76           C  
ANISOU 4180  C2  PEG A1524    11794  10282  11648   -307   -167    272       C  
HETATM 4181  O2  PEG A1524       2.126  15.907  33.355  1.00 90.44           O  
ANISOU 4181  O2  PEG A1524    12081  10442  11839   -366   -202    326       O  
HETATM 4182  C3  PEG A1524       1.151  16.002  32.318  1.00 92.11           C  
ANISOU 4182  C3  PEG A1524    12244  10682  12073   -272   -162    355       C  
HETATM 4183  C4  PEG A1524       1.496  17.157  31.383  1.00 93.22           C  
ANISOU 4183  C4  PEG A1524    12463  10767  12189   -341   -201    415       C  
HETATM 4184  O4  PEG A1524       2.636  16.804  30.593  1.00 92.96           O  
ANISOU 4184  O4  PEG A1524    12313  10847  12163   -470   -236    452       O  
HETATM 4185  C1  PEG A1525       7.558 -10.343  69.508  1.00 96.40           C  
ANISOU 4185  C1  PEG A1525    12257  12055  12317   -191   -209   -347       C  
HETATM 4186  O1  PEG A1525       6.666 -10.625  68.424  1.00 92.93           O  
ANISOU 4186  O1  PEG A1525    11772  11604  11932   -127   -162   -352       O  
HETATM 4187  C2  PEG A1525       8.027 -11.654  70.127  1.00 97.61           C  
ANISOU 4187  C2  PEG A1525    12340  12269  12479   -182   -222   -317       C  
HETATM 4188  O2  PEG A1525       8.491 -12.504  69.079  1.00 98.50           O  
ANISOU 4188  O2  PEG A1525    12357  12426  12642   -153   -219   -287       O  
HETATM 4189  C3  PEG A1525       9.116 -13.687  69.572  1.00 98.36           C  
ANISOU 4189  C3  PEG A1525    12288  12463  12622   -134   -232   -251       C  
HETATM 4190  C4  PEG A1525       9.506 -14.575  68.397  1.00 97.05           C  
ANISOU 4190  C4  PEG A1525    12060  12325  12491    -73   -216   -223       C  
HETATM 4191  O4  PEG A1525      10.128 -15.764  68.893  1.00 98.12           O  
ANISOU 4191  O4  PEG A1525    12162  12505  12613    -33   -223   -183       O  
HETATM 4192  C1  PEG A1526     -17.697  -4.419  27.625  1.00100.82           C  
ANISOU 4192  C1  PEG A1526    12072  13418  12816  -1678  -1594   1928       C  
HETATM 4193  O1  PEG A1526     -18.620  -5.471  27.929  1.00101.78           O  
ANISOU 4193  O1  PEG A1526    12159  13627  12887  -1900  -1762   2104       O  
HETATM 4194  C2  PEG A1526     -17.981  -3.214  28.515  1.00100.53           C  
ANISOU 4194  C2  PEG A1526    11781  13521  12893  -1452  -1411   1987       C  
HETATM 4195  O2  PEG A1526     -17.824  -3.575  29.887  1.00 99.42           O  
ANISOU 4195  O2  PEG A1526    11592  13389  12794  -1383  -1340   1951       O  
HETATM 4196  C3  PEG A1526     -17.663  -2.427  30.718  1.00 97.70           C  
ANISOU 4196  C3  PEG A1526    11235  13221  12664  -1132  -1144   1921       C  
HETATM 4197  C4  PEG A1526     -17.591  -2.863  32.176  1.00 96.70           C  
ANISOU 4197  C4  PEG A1526    11058  13114  12569  -1074  -1082   1900       C  
HETATM 4198  O4  PEG A1526     -17.137  -1.772  32.982  1.00 95.74           O  
ANISOU 4198  O4  PEG A1526    10881  12979  12516   -822   -888   1812       O  
HETATM 4199  C1  PEG A1527     -14.473  14.251  44.263  1.00 97.30           C  
ANISOU 4199  C1  PEG A1527    12640  11994  12336   2319   1025   1113       C  
HETATM 4200  O1  PEG A1527     -15.569  13.343  44.113  1.00 96.95           O  
ANISOU 4200  O1  PEG A1527    12276  12224  12338   2337   1043   1295       O  
HETATM 4201  C2  PEG A1527     -14.516  14.835  45.669  1.00 99.45           C  
ANISOU 4201  C2  PEG A1527    13152  12151  12484   2543   1135   1076       C  
HETATM 4202  O2  PEG A1527     -14.240  13.799  46.610  1.00 99.89           O  
ANISOU 4202  O2  PEG A1527    13132  12261  12563   2449   1112   1024       O  
HETATM 4203  C3  PEG A1527     -14.881  14.045  47.859  1.00101.12           C  
ANISOU 4203  C3  PEG A1527    13377  12437  12608   2710   1246   1086       C  
HETATM 4204  C4  PEG A1527     -14.383  13.044  48.893  1.00100.76           C  
ANISOU 4204  C4  PEG A1527    13299  12405  12581   2590   1209   1000       C  
HETATM 4205  O4  PEG A1527     -13.077  13.436  49.327  1.00101.01           O  
ANISOU 4205  O4  PEG A1527    13617  12181  12579   2469   1140    794       O  
HETATM 4206  C1  PEG A1528      -8.019 -16.064  65.951  1.00 90.54           C  
ANISOU 4206  C1  PEG A1528    10720  11917  11764   -145    -96    624       C  
HETATM 4207  O1  PEG A1528      -8.165 -14.989  66.892  1.00 91.47           O  
ANISOU 4207  O1  PEG A1528    10813  12092  11849     17     30    617       O  
HETATM 4208  C2  PEG A1528      -7.314 -15.552  64.698  1.00 87.76           C  
ANISOU 4208  C2  PEG A1528    10448  11455  11443   -148   -116    511       C  
HETATM 4209  O2  PEG A1528      -5.956 -15.245  65.012  1.00 84.11           O  
ANISOU 4209  O2  PEG A1528    10096  10881  10981    -91    -86    349       O  
HETATM 4210  C3  PEG A1528      -5.615 -13.900  64.675  1.00 80.22           C  
ANISOU 4210  C3  PEG A1528     9630  10358  10492      7    -16    276       C  
HETATM 4211  C4  PEG A1528      -4.351 -13.498  65.428  1.00 79.27           C  
ANISOU 4211  C4  PEG A1528     9606  10158  10357     62     18    145       C  
HETATM 4212  O4  PEG A1528      -4.494 -12.172  65.954  1.00 80.29           O  
ANISOU 4212  O4  PEG A1528     9757  10297  10451    180    108    126       O  
HETATM 4213  C1  PEG A1529      -4.304 -12.950  27.644  1.00 80.62           C  
ANISOU 4213  C1  PEG A1529    12221   9021   9388   -723  -1150     29       C  
HETATM 4214  O1  PEG A1529      -5.167 -12.729  26.521  1.00 82.34           O  
ANISOU 4214  O1  PEG A1529    12507   9230   9549   -868  -1269     98       O  
HETATM 4215  C2  PEG A1529      -5.119 -12.980  28.932  1.00 78.84           C  
ANISOU 4215  C2  PEG A1529    11795   8874   9287   -845  -1199     96       C  
HETATM 4216  O2  PEG A1529      -4.265 -13.319  30.023  1.00 78.29           O  
ANISOU 4216  O2  PEG A1529    11693   8797   9255   -713  -1096     25       O  
HETATM 4217  C3  PEG A1529      -4.965 -13.356  31.266  1.00 75.83           C  
ANISOU 4217  C3  PEG A1529    11199   8558   9053   -810  -1130     85       C  
HETATM 4218  C4  PEG A1529      -4.157 -14.170  32.270  1.00 75.31           C  
ANISOU 4218  C4  PEG A1529    11210   8434   8971   -707  -1072     11       C  
HETATM 4219  O4  PEG A1529      -4.841 -14.212  33.527  1.00 75.97           O  
ANISOU 4219  O4  PEG A1529    11115   8592   9159   -800  -1102     71       O  
HETATM 4220  C1  PEG A1530     -13.126   8.144  48.269  1.00 83.46           C  
ANISOU 4220  C1  PEG A1530    10374  10574  10761   1697    818    899       C  
HETATM 4221  O1  PEG A1530     -13.769   8.230  46.992  1.00 83.08           O  
ANISOU 4221  O1  PEG A1530    10175  10633  10758   1668    790   1017       O  
HETATM 4222  C2  PEG A1530     -12.210   6.925  48.315  1.00 81.73           C  
ANISOU 4222  C2  PEG A1530    10101  10338  10614   1447    701    786       C  
HETATM 4223  O2  PEG A1530     -11.959   6.574  49.674  1.00 82.06           O  
ANISOU 4223  O2  PEG A1530    10210  10353  10616   1488    736    732       O  
HETATM 4224  C3  PEG A1530     -11.085   5.454  49.797  1.00 80.21           C  
ANISOU 4224  C3  PEG A1530     9936  10099  10440   1276    636    630       C  
HETATM 4225  C4  PEG A1530     -11.404   4.724  51.096  1.00 81.20           C  
ANISOU 4225  C4  PEG A1530    10013  10300  10539   1323    675    662       C  
HETATM 4226  O4  PEG A1530     -10.251   4.707  51.943  1.00 82.79           O  
ANISOU 4226  O4  PEG A1530    10385  10353  10718   1268    652    501       O  
HETATM 4227  C1  PEG A1531       4.599 -18.316  49.331  1.00 91.46           C  
ANISOU 4227  C1  PEG A1531    12338  10872  11539    295   -256   -314       C  
HETATM 4228  O1  PEG A1531       4.178 -19.500  50.017  1.00 91.48           O  
ANISOU 4228  O1  PEG A1531    12463  10794  11502    258   -317   -310       O  
HETATM 4229  C2  PEG A1531       5.747 -18.657  48.386  1.00 92.51           C  
ANISOU 4229  C2  PEG A1531    12579  10992  11579    461   -192   -321       C  
HETATM 4230  O2  PEG A1531       6.765 -17.666  48.509  1.00 91.45           O  
ANISOU 4230  O2  PEG A1531    12260  10992  11494    532   -104   -304       O  
HETATM 4231  C3  PEG A1531       8.051 -18.272  48.586  1.00 91.31           C  
ANISOU 4231  C3  PEG A1531    12276  11011  11407    701    -32   -282       C  
HETATM 4232  C4  PEG A1531       8.342 -18.540  50.058  1.00 91.51           C  
ANISOU 4232  C4  PEG A1531    12211  11084  11476    689    -30   -270       C  
HETATM 4233  O4  PEG A1531       9.592 -19.219  50.212  1.00 93.10           O  
ANISOU 4233  O4  PEG A1531    12438  11332  11604    863     40   -233       O  
HETATM 4234  C1  PEG A1532      -3.971 -41.074  99.244  1.00100.03           C  
ANISOU 4234  C1  PEG A1532    12443  13637  11928  -1090   -814   2001       C  
HETATM 4235  O1  PEG A1532      -3.763 -42.010  98.180  1.00 99.84           O  
ANISOU 4235  O1  PEG A1532    12568  13423  11944  -1204   -949   1995       O  
HETATM 4236  C2  PEG A1532      -2.638 -40.457  99.652  1.00 99.13           C  
ANISOU 4236  C2  PEG A1532    12391  13462  11811   -922   -743   1808       C  
HETATM 4237  O2  PEG A1532      -1.739 -41.490 100.050  1.00100.01           O  
ANISOU 4237  O2  PEG A1532    12635  13450  11914   -939   -822   1784       O  
HETATM 4238  C3  PEG A1532      -0.562 -40.967 100.665  1.00 99.51           C  
ANISOU 4238  C3  PEG A1532    12599  13375  11834   -801   -762   1647       C  
HETATM 4239  C4  PEG A1532       0.202 -42.093 101.354  1.00100.87           C  
ANISOU 4239  C4  PEG A1532    12877  13467  11983   -816   -833   1667       C  
HETATM 4240  O4  PEG A1532       0.684 -43.027 100.380  1.00100.79           O  
ANISOU 4240  O4  PEG A1532    13016  13270  12010   -853   -934   1646       O  
HETATM 4241  C1  PEG A1533      17.992  -4.336  32.169  1.00 93.26           C  
ANISOU 4241  C1  PEG A1533    10942  13133  11359   1137    736    991       C  
HETATM 4242  O1  PEG A1533      18.262  -4.074  33.551  1.00 92.26           O  
ANISOU 4242  O1  PEG A1533    10690  13042  11321    993    668   1016       O  
HETATM 4243  C2  PEG A1533      18.973  -3.557  31.300  1.00 94.16           C  
ANISOU 4243  C2  PEG A1533    10878  13469  11429   1151    787   1182       C  
HETATM 4244  O2  PEG A1533      18.718  -3.810  29.918  1.00 94.25           O  
ANISOU 4244  O2  PEG A1533    11022  13446  11342   1301    858   1158       O  
HETATM 4245  C3  PEG A1533      19.527  -2.981  29.083  1.00 94.98           C  
ANISOU 4245  C3  PEG A1533    10946  13740  11401   1294    899   1334       C  
HETATM 4246  C4  PEG A1533      19.454  -3.468  27.641  1.00 96.63           C  
ANISOU 4246  C4  PEG A1533    11301  13941  11472   1512   1003   1328       C  
HETATM 4247  O4  PEG A1533      20.071  -4.756  27.541  1.00 98.10           O  
ANISOU 4247  O4  PEG A1533    11564  14195  11515   1808   1132   1370       O  
HETATM 4248  C1  PEG A1534      10.173 -15.360  31.967  1.00 98.02           C  
ANISOU 4248  C1  PEG A1534    14171  11797  11276   1623    383   -162       C  
HETATM 4249  O1  PEG A1534      11.244 -15.634  31.055  1.00 99.96           O  
ANISOU 4249  O1  PEG A1534    14511  12109  11361   1889    517   -104       O  
HETATM 4250  C2  PEG A1534      10.735 -15.090  33.358  1.00 96.79           C  
ANISOU 4250  C2  PEG A1534    13748  11776  11253   1603    419   -122       C  
HETATM 4251  O2  PEG A1534       9.760 -15.458  34.331  1.00 96.34           O  
ANISOU 4251  O2  PEG A1534    13725  11602  11278   1426    302   -189       O  
HETATM 4252  C3  PEG A1534      10.324 -15.603  35.634  1.00 94.02           C  
ANISOU 4252  C3  PEG A1534    13273  11392  11057   1449    336   -163       C  
HETATM 4253  C4  PEG A1534       9.499 -16.614  36.423  1.00 93.40           C  
ANISOU 4253  C4  PEG A1534    13367  11151  10971   1364    238   -231       C  
HETATM 4254  O4  PEG A1534       9.912 -16.617  37.795  1.00 93.08           O  
ANISOU 4254  O4  PEG A1534    13145  11195  11025   1350    258   -209       O  
HETATM 4255  C1  PEG A1535     -14.198   4.986  58.017  1.00 98.47           C  
ANISOU 4255  C1  PEG A1535    12385  12759  12272   2290   1235    964       C  
HETATM 4256  O1  PEG A1535     -15.427   4.357  58.397  1.00101.50           O  
ANISOU 4256  O1  PEG A1535    12519  13402  12645   2394   1308   1182       O  
HETATM 4257  C2  PEG A1535     -14.494   6.179  57.117  1.00 97.50           C  
ANISOU 4257  C2  PEG A1535    12349  12576  12118   2421   1283    995       C  
HETATM 4258  O2  PEG A1535     -15.088   5.728  55.902  1.00 96.66           O  
ANISOU 4258  O2  PEG A1535    11980  12633  12112   2312   1226   1123       O  
HETATM 4259  C3  PEG A1535     -15.427   6.817  55.045  1.00 98.09           C  
ANISOU 4259  C3  PEG A1535    12225  12776  12267   2439   1273   1168       C  
HETATM 4260  C4  PEG A1535     -15.804   6.288  53.665  1.00 97.75           C  
ANISOU 4260  C4  PEG A1535    11932  12870  12337   2264   1177   1267       C  
HETATM 4261  O4  PEG A1535     -16.019   7.383  52.767  1.00 97.56           O  
ANISOU 4261  O4  PEG A1535    11984  12792  12294   2373   1214   1294       O  
HETATM 4262  C1  PEG A1536      24.094  -7.897  59.387  1.00122.15           C  
ANISOU 4262  C1  PEG A1536    13624  17343  15446   -596   -464   1448       C  
HETATM 4263  O1  PEG A1536      24.811  -6.768  59.901  1.00123.54           O  
ANISOU 4263  O1  PEG A1536    13737  17610  15593   -881   -620   1588       O  
HETATM 4264  C2  PEG A1536      25.094  -8.976  58.991  1.00123.53           C  
ANISOU 4264  C2  PEG A1536    13592  17762  15582   -375   -358   1627       C  
HETATM 4265  O2  PEG A1536      24.414 -10.130  58.500  1.00122.74           O  
ANISOU 4265  O2  PEG A1536    13592  17552  15492    -99   -216   1490       O  
HETATM 4266  C3  PEG A1536      25.302 -10.978  57.774  1.00124.16           C  
ANISOU 4266  C3  PEG A1536    13615  17942  15619    140    -97   1654       C  
HETATM 4267  C4  PEG A1536      25.071 -12.419  58.204  1.00123.57           C  
ANISOU 4267  C4  PEG A1536    13616  17809  15525    373     -5   1583       C  
HETATM 4268  O4  PEG A1536      25.224 -12.490  59.626  1.00123.79           O  
ANISOU 4268  O4  PEG A1536    13628  17845  15562    239    -96   1596       O  
HETATM 4269  C1  PEG A1537      -1.546   1.720  17.121  1.00 82.51           C  
ANISOU 4269  C1  PEG A1537    11143  10149  10059   -221   -413    367       C  
HETATM 4270  O1  PEG A1537      -2.716   2.111  16.389  1.00 82.13           O  
ANISOU 4270  O1  PEG A1537    11091  10101  10014   -324   -506    433       O  
HETATM 4271  C2  PEG A1537      -1.481   2.425  18.476  1.00 82.09           C  
ANISOU 4271  C2  PEG A1537    10905  10131  10157   -219   -367    368       C  
HETATM 4272  O2  PEG A1537      -2.303   1.742  19.423  1.00 82.53           O  
ANISOU 4272  O2  PEG A1537    10958  10152  10247   -277   -429    357       O  
HETATM 4273  C3  PEG A1537      -2.100   2.196  20.763  1.00 81.81           C  
ANISOU 4273  C3  PEG A1537    10731  10083  10271   -254   -377    342       C  
HETATM 4274  C4  PEG A1537      -2.856   1.297  21.738  1.00 81.39           C  
ANISOU 4274  C4  PEG A1537    10690  10000  10236   -304   -436    330       C  
HETATM 4275  O4  PEG A1537      -2.209   1.325  23.016  1.00 80.71           O  
ANISOU 4275  O4  PEG A1537    10531   9920  10216   -251   -369    285       O  
HETATM 4276  C1  PEG A1538       9.788 -11.620  94.922  1.00119.35           C  
ANISOU 4276  C1  PEG A1538    17043  14836  13469   -592   -713   -345       C  
HETATM 4277  O1  PEG A1538       9.943 -11.132  96.261  1.00121.66           O  
ANISOU 4277  O1  PEG A1538    17664  15011  13552   -663   -794   -381       O  
HETATM 4278  C2  PEG A1538      10.941 -12.529  94.498  1.00117.58           C  
ANISOU 4278  C2  PEG A1538    16564  14745  13365   -738   -817   -259       C  
HETATM 4279  O2  PEG A1538      10.644 -13.102  93.231  1.00115.86           O  
ANISOU 4279  O2  PEG A1538    16199  14553  13270   -800   -850   -240       O  
HETATM 4280  C3  PEG A1538      11.790 -13.660  92.609  1.00112.68           C  
ANISOU 4280  C3  PEG A1538    15494  14292  13026   -807   -851   -164       C  
HETATM 4281  C4  PEG A1538      11.434 -14.135  91.216  1.00108.23           C  
ANISOU 4281  C4  PEG A1538    14788  13745  12591   -802   -832   -160       C  
HETATM 4282  O4  PEG A1538      12.414 -15.084  90.832  1.00105.84           O  
ANISOU 4282  O4  PEG A1538    14228  13549  12437   -723   -773   -112       O  
HETATM 4283  C10 OLC A1539      10.630 -22.473  56.974  1.00 75.49           C  
ANISOU 4283  C10 OLC A1539    10101   9160   9421    875    -16   -165       C  
HETATM 4284  C9  OLC A1539      10.047 -21.716  57.898  1.00 74.48           C  
ANISOU 4284  C9  OLC A1539     9837   9075   9386    720    -54   -182       C  
HETATM 4285  C8  OLC A1539       9.633 -22.317  59.221  1.00 74.14           C  
ANISOU 4285  C8  OLC A1539     9803   9006   9361    657    -97   -186       C  
HETATM 4286  C24 OLC A1539      15.160 -15.621  68.478  1.00 98.57           C  
ANISOU 4286  C24 OLC A1539    11882  12977  12595    -46   -293    137       C  
HETATM 4287  C7  OLC A1539       9.924 -21.335  60.349  1.00 74.61           C  
ANISOU 4287  C7  OLC A1539     9666   9188   9495    578    -90   -171       C  
HETATM 4288  C6  OLC A1539      11.412 -21.025  60.446  1.00 77.82           C  
ANISOU 4288  C6  OLC A1539     9953   9731   9885    677    -33   -107       C  
HETATM 4289  C5  OLC A1539      11.722 -20.137  61.648  1.00 79.65           C  
ANISOU 4289  C5  OLC A1539    10024  10067  10173    577    -48    -87       C  
HETATM 4290  C4  OLC A1539      11.931 -20.966  62.908  1.00 82.51           C  
ANISOU 4290  C4  OLC A1539    10394  10438  10519    591    -63    -67       C  
HETATM 4291  C3  OLC A1539      12.777 -20.203  63.920  1.00 85.77           C  
ANISOU 4291  C3  OLC A1539    10651  10984  10954    535    -69    -17       C  
HETATM 4292  C2  OLC A1539      11.991 -19.082  64.591  1.00 89.51           C  
ANISOU 4292  C2  OLC A1539    11083  11443  11484    376   -111    -67       C  
HETATM 4293  C21 OLC A1539      13.369 -17.013  67.431  1.00 98.39           C  
ANISOU 4293  C21 OLC A1539    12004  12769  12613    123   -205      8       C  
HETATM 4294  C1  OLC A1539      12.983 -18.162  65.263  1.00 94.44           C  
ANISOU 4294  C1  OLC A1539    11581  12190  12110    312   -127    -11       C  
HETATM 4295  C22 OLC A1539      14.385 -15.901  67.197  1.00 98.91           C  
ANISOU 4295  C22 OLC A1539    11976  12937  12669     47   -234     76       C  
HETATM 4296  O19 OLC A1539      14.167 -18.242  64.980  1.00 98.62           O  
ANISOU 4296  O19 OLC A1539    12030  12830  12613    375   -108     74       O  
HETATM 4297  O25 OLC A1539      14.865 -14.295  68.930  1.00 97.50           O  
ANISOU 4297  O25 OLC A1539    11796  12797  12453   -193   -348     99       O  
HETATM 4298  O23 OLC A1539      15.305 -16.331  66.189  1.00100.80           O  
ANISOU 4298  O23 OLC A1539    12138  13268  12894    152   -194    159       O  
HETATM 4299  O20 OLC A1539      12.568 -17.187  66.262  1.00 95.92           O  
ANISOU 4299  O20 OLC A1539    11753  12371  12321    177   -170    -44       O  
HETATM 4300  C24 OLC A1540      -7.690  17.005  57.831  1.00 99.99           C  
ANISOU 4300  C24 OLC A1540    16069  10428  11496   2504    993   -119       C  
HETATM 4301  C3  OLC A1540      -4.383  16.753  52.277  1.00 84.77           C  
ANISOU 4301  C3  OLC A1540    13440   8617  10153   1362    451   -172       C  
HETATM 4302  C2  OLC A1540      -4.704  15.878  53.485  1.00 85.61           C  
ANISOU 4302  C2  OLC A1540    13476   8811  10241   1449    513   -184       C  
HETATM 4303  C21 OLC A1540      -7.966  16.074  55.514  1.00 95.89           C  
ANISOU 4303  C21 OLC A1540    14901  10236  11296   2301    946     -6       C  
HETATM 4304  C1  OLC A1540      -6.190  15.905  53.760  1.00 88.65           C  
ANISOU 4304  C1  OLC A1540    13817   9286  10580   1779    687    -95       C  
HETATM 4305  C22 OLC A1540      -8.144  15.805  57.008  1.00 98.44           C  
ANISOU 4305  C22 OLC A1540    15359  10537  11505   2432   1012    -30       C  
HETATM 4306  O19 OLC A1540      -6.977  16.219  52.884  1.00 89.80           O  
ANISOU 4306  O19 OLC A1540    13865   9499  10755   1907    754    -11       O  
HETATM 4307  O25 OLC A1540      -8.216  16.882  59.158  1.00100.71           O  
ANISOU 4307  O25 OLC A1540    16298  10515  11454   2727   1104   -110       O  
HETATM 4308  O23 OLC A1540      -9.521  15.547  57.299  1.00101.06           O  
ANISOU 4308  O23 OLC A1540    15539  11050  11810   2738   1187    104       O  
HETATM 4309  O20 OLC A1540      -6.695  15.584  55.085  1.00 92.40           O  
ANISOU 4309  O20 OLC A1540    14363   9779  10965   1952    778    -92       O  
HETATM 4310  C1  PEG A1541      -3.535 -15.304  47.233  1.00 91.84           C  
ANISOU 4310  C1  PEG A1541    12010  11069  11817   -495   -636     24       C  
HETATM 4311  O1  PEG A1541      -4.306 -14.099  47.188  1.00 93.64           O  
ANISOU 4311  O1  PEG A1541    12062  11402  12115   -507   -602     83       O  
HETATM 4312  C2  PEG A1541      -3.116 -15.678  45.818  1.00 90.04           C  
ANISOU 4312  C2  PEG A1541    11962  10742  11507   -490   -676    -16       C  
HETATM 4313  O2  PEG A1541      -1.975 -14.917  45.423  1.00 87.89           O  
ANISOU 4313  O2  PEG A1541    11668  10477  11251   -353   -572    -95       O  
HETATM 4314  C3  PEG A1541      -1.724 -15.071  44.026  1.00 88.21           C  
ANISOU 4314  C3  PEG A1541    11852  10447  11216   -341   -598   -116       C  
HETATM 4315  C4  PEG A1541      -0.255 -14.807  43.715  1.00 86.08           C  
ANISOU 4315  C4  PEG A1541    11611  10170  10926   -181   -495   -194       C  
HETATM 4316  O4  PEG A1541      -0.016 -15.021  42.318  1.00 84.32           O  
ANISOU 4316  O4  PEG A1541    11545   9879  10614   -153   -515   -211       O  
HETATM 4317  C1  PEG A1542     -24.229   6.146  25.369  1.00106.24           C  
ANISOU 4317  C1  PEG A1542    11040  15501  13826   -381   -856   3399       C  
HETATM 4318  O1  PEG A1542     -24.818   6.575  24.137  1.00107.28           O  
ANISOU 4318  O1  PEG A1542    11095  15735  13933   -446   -934   3558       O  
HETATM 4319  C2  PEG A1542     -25.322   5.641  26.304  1.00108.74           C  
ANISOU 4319  C2  PEG A1542    11112  16070  14136   -383   -864   3658       C  
HETATM 4320  O2  PEG A1542     -24.732   4.955  27.407  1.00108.07           O  
ANISOU 4320  O2  PEG A1542    11117  15879  14067   -387   -831   3500       O  
HETATM 4321  C3  PEG A1542     -24.094   5.873  28.291  1.00107.33           C  
ANISOU 4321  C3  PEG A1542    11109  15661  14010    -90   -619   3333       C  
HETATM 4322  C4  PEG A1542     -24.724   5.795  29.676  1.00108.72           C  
ANISOU 4322  C4  PEG A1542    11123  15995  14191     65   -513   3472       C  
HETATM 4323  O4  PEG A1542     -24.583   4.475  30.210  1.00108.59           O  
ANISOU 4323  O4  PEG A1542    11123  15970  14168   -147   -626   3437       O  
HETATM 4324  O   HOH A1601      17.957 -11.586  86.638  1.00 94.67           O  
ANISOU 4324  O   HOH A1601    12590  12338  11043  -1542  -1352    245       O  
HETATM 4325  O   HOH A1602       3.227  20.653  23.500  1.00 45.80           O  
ANISOU 4325  O   HOH A1602     6315   4958   6129   -698   -333    850       O  
HETATM 4326  O   HOH A1603      19.379 -37.758  74.113  1.00 74.71           O  
ANISOU 4326  O   HOH A1603    10414   9331   8642   2359     95    787       O  
HETATM 4327  O   HOH A1604      -0.746   2.835  48.770  1.00 57.09           O  
ANISOU 4327  O   HOH A1604     7353   6652   7688    159     84   -173       O  
HETATM 4328  O   HOH A1605     -10.914 -21.257  73.810  1.00 85.34           O  
ANISOU 4328  O   HOH A1605     9674  11869  10883   -345   -130   1326       O  
HETATM 4329  O   HOH A1606       4.873  23.336  22.382  1.00 58.52           O  
ANISOU 4329  O   HOH A1606     8127   6453   7656  -1021   -493   1060       O  
HETATM 4330  O   HOH A1607       4.220  14.937  19.356  1.00 46.53           O  
ANISOU 4330  O   HOH A1607     5782   5765   6133   -486   -132    833       O  
HETATM 4331  O   HOH A1608       5.728 -45.036  91.705  1.00 59.02           O  
ANISOU 4331  O   HOH A1608     8769   6833   6823   -310  -1119   1101       O  
HETATM 4332  O   HOH A1609      -4.790   6.852   7.858  1.00 49.71           O  
ANISOU 4332  O   HOH A1609     7056   6179   5651   -531   -695    870       O  
HETATM 4333  O   HOH A1610      -2.346   6.016  15.292  1.00 57.78           O  
ANISOU 4333  O   HOH A1610     7669   7159   7125   -295   -383    582       O  
HETATM 4334  O   HOH A1611      19.588 -21.836  86.803  1.00 68.92           O  
ANISOU 4334  O   HOH A1611     8102   9825   8259   -567   -900    692       O  
HETATM 4335  O   HOH A1612       8.258  17.076  18.391  1.00 66.23           O  
ANISOU 4335  O   HOH A1612     8102   8532   8531   -808   -176   1194       O  
HETATM 4336  O   HOH A1613       0.860 -24.906  95.789  1.00 58.38           O  
ANISOU 4336  O   HOH A1613     7536   8140   6504    156     43    458       O  
HETATM 4337  O   HOH A1614      15.320 -36.737  74.128  1.00 51.38           O  
ANISOU 4337  O   HOH A1614     7640   5992   5891   1601   -180    439       O  
HETATM 4338  O   HOH A1615      -5.900   9.026  22.245  1.00 41.06           O  
ANISOU 4338  O   HOH A1615     5020   5014   5568   -204   -302    693       O  
HETATM 4339  O   HOH A1616       0.433  -1.238  42.219  1.00 61.05           O  
ANISOU 4339  O   HOH A1616     7568   7380   8247    -44    -62   -120       O  
HETATM 4340  O   HOH A1617       4.408 -43.746  93.048  1.00 72.86           O  
ANISOU 4340  O   HOH A1617    10181   8870   8631   -489  -1069   1152       O  
HETATM 4341  O   HOH A1618      -4.766  -7.303  60.561  1.00 48.93           O  
ANISOU 4341  O   HOH A1618     5864   6171   6557    311    184     47       O  
HETATM 4342  O   HOH A1619       3.900   4.097  23.685  1.00 54.24           O  
ANISOU 4342  O   HOH A1619     6884   6808   6917    -14     -5    308       O  
HETATM 4343  O   HOH A1620       4.122 -25.295  96.454  1.00 60.12           O  
ANISOU 4343  O   HOH A1620     7884   8230   6727    -14   -171    315       O  
HETATM 4344  O   HOH A1621      -5.500 -25.741  73.421  1.00 48.55           O  
ANISOU 4344  O   HOH A1621     5807   6378   6260   -649   -530    722       O  
HETATM 4345  O   HOH A1622      21.270 -24.400  76.164  1.00 58.27           O  
ANISOU 4345  O   HOH A1622     6336   8621   7182    568   -305    900       O  
HETATM 4346  O   HOH A1623      16.024  -6.597  64.492  1.00 52.55           O  
ANISOU 4346  O   HOH A1623     6186   7045   6735   -790   -573    208       O  
HETATM 4347  O   HOH A1624       1.604 -25.875  93.277  1.00 44.39           O  
ANISOU 4347  O   HOH A1624     5634   6258   4972     15    -85    424       O  
HETATM 4348  O   HOH A1625      -4.102 -17.721  83.692  1.00 59.66           O  
ANISOU 4348  O   HOH A1625     7377   8160   7131    495    373    376       O  
HETATM 4349  O   HOH A1626      -9.016 -28.043  83.132  1.00 47.33           O  
ANISOU 4349  O   HOH A1626     5062   7109   5811   -608   -294   1510       O  
HETATM 4350  O   HOH A1627      -1.430  -4.043  47.374  1.00 43.45           O  
ANISOU 4350  O   HOH A1627     5283   5192   6033     -6    -59   -122       O  
HETATM 4351  O   HOH A1628       5.380  -5.593  53.272  1.00 36.29           O  
ANISOU 4351  O   HOH A1628     4418   4332   5038    -67    -65   -296       O  
HETATM 4352  O   HOH A1629      19.914 -30.062  81.177  1.00 55.98           O  
ANISOU 4352  O   HOH A1629     6471   8021   6776    838   -326    860       O  
HETATM 4353  O   HOH A1630       5.288  18.558  17.320  1.00 58.81           O  
ANISOU 4353  O   HOH A1630     7398   7292   7657   -727   -221   1105       O  
HETATM 4354  O   HOH A1631      -1.521 -20.365  91.538  1.00 62.46           O  
ANISOU 4354  O   HOH A1631     8090   8568   7074    457    305    339       O  
HETATM 4355  O   HOH A1632       8.795 -25.849  69.375  1.00 40.04           O  
ANISOU 4355  O   HOH A1632     5326   4789   5099    365   -276    -71       O  
HETATM 4356  O   HOH A1633       5.501  -8.239  31.654  1.00 53.13           O  
ANISOU 4356  O   HOH A1633     7469   6313   6404    497     14   -140       O  
HETATM 4357  O   HOH A1634      10.712 -31.200  76.304  1.00 42.83           O  
ANISOU 4357  O   HOH A1634     5817   5190   5268    509   -374    175       O  
HETATM 4358  O   HOH A1635       7.406  -1.261  26.444  1.00 55.55           O  
ANISOU 4358  O   HOH A1635     7194   7088   6824    409    194    196       O  
HETATM 4359  O   HOH A1636      -7.702   4.239  48.099  1.00 40.04           O  
ANISOU 4359  O   HOH A1636     4938   4780   5494    738    359    289       O  
HETATM 4360  O   HOH A1637      -9.074   9.586  14.268  1.00 53.09           O  
ANISOU 4360  O   HOH A1637     6616   6759   6795   -513   -666   1135       O  
HETATM 4361  O   HOH A1638      -2.626  11.160  13.983  1.00 48.83           O  
ANISOU 4361  O   HOH A1638     6253   6089   6211   -315   -313    816       O  
HETATM 4362  O   HOH A1639      12.181 -37.174  75.019  1.00 46.83           O  
ANISOU 4362  O   HOH A1639     7264   5137   5393   1094   -406    313       O  
HETATM 4363  O   HOH A1640      -3.197   0.722  46.800  1.00 47.09           O  
ANISOU 4363  O   HOH A1640     5798   5594   6501    182     75    -26       O  
HETATM 4364  O   HOH A1641       3.427  -2.271  46.112  1.00 57.38           O  
ANISOU 4364  O   HOH A1641     7101   6941   7761    -59    -41   -214       O  
HETATM 4365  O   HOH A1642       4.232   1.367  62.517  1.00 58.26           O  
ANISOU 4365  O   HOH A1642     8301   6505   7327   -104   -118   -480       O  
HETATM 4366  O   HOH A1643       1.169   2.693  25.383  1.00 56.41           O  
ANISOU 4366  O   HOH A1643     7236   6924   7272    -88   -132    209       O  
HETATM 4367  O   HOH A1644      18.145 -31.562  77.957  1.00 47.07           O  
ANISOU 4367  O   HOH A1644     5787   6457   5641   1133   -193    658       O  
HETATM 4368  O   HOH A1645      15.586 -18.243  88.164  1.00 69.70           O  
ANISOU 4368  O   HOH A1645     8914   9381   8189   -773   -877    203       O  
HETATM 4369  O   HOH A1646       1.600   3.925  30.501  1.00 55.43           O  
ANISOU 4369  O   HOH A1646     6913   6754   7394   -120    -80    141       O  
HETATM 4370  O   HOH A1647       0.756   2.701  51.231  1.00 42.91           O  
ANISOU 4370  O   HOH A1647     5695   4786   5825     93     51   -258       O  
HETATM 4371  O   HOH A1648       7.205 -30.715  79.753  1.00 40.95           O  
ANISOU 4371  O   HOH A1648     5445   5022   5091     80   -469    194       O  
HETATM 4372  O   HOH A1649      15.658 -25.158  69.546  1.00 47.80           O  
ANISOU 4372  O   HOH A1649     5826   6370   5965    844    -85    260       O  
HETATM 4373  O   HOH A1650      -2.854  -4.042  61.239  1.00 45.89           O  
ANISOU 4373  O   HOH A1650     5840   5533   6064    432    256   -166       O  
HETATM 4374  O   HOH A1651      -8.291   7.053   7.122  1.00 63.17           O  
ANISOU 4374  O   HOH A1651     8662   7952   7389   -841  -1012   1126       O  
HETATM 4375  O   HOH A1652      -3.272  10.183  32.432  1.00 56.14           O  
ANISOU 4375  O   HOH A1652     7103   6576   7649     66    -24    330       O  
HETATM 4376  O   HOH A1653      18.611 -22.560  70.345  1.00 59.69           O  
ANISOU 4376  O   HOH A1653     6814   8382   7485    678   -127    531       O  
HETATM 4377  O   HOH A1654      -4.067  -7.226  35.306  1.00 39.29           O  
ANISOU 4377  O   HOH A1654     5277   4516   5136   -417   -550     96       O  
HETATM 4378  O   HOH A1655      -4.797   9.909  35.348  1.00 53.36           O  
ANISOU 4378  O   HOH A1655     6771   6204   7300    256     60    331       O  
HETATM 4379  O   HOH A1656       1.863  14.172  20.362  1.00 42.13           O  
ANISOU 4379  O   HOH A1656     5290   5076   5643   -369   -142    709       O  
HETATM 4380  O   HOH A1657      17.580 -30.057  80.172  1.00 45.01           O  
ANISOU 4380  O   HOH A1657     5350   6304   5449    761   -313    611       O  
HETATM 4381  O   HOH A1658       6.626  11.155  12.125  1.00 46.34           O  
ANISOU 4381  O   HOH A1658     5752   6324   5532    -84    130   1017       O  
HETATM 4382  O   HOH A1659       7.823 -16.084  95.002  1.00 59.31           O  
ANISOU 4382  O   HOH A1659     8813   7556   6167   -236   -405   -218       O  
HETATM 4383  O   HOH A1660      20.107   2.886  60.875  1.00 75.42           O  
ANISOU 4383  O   HOH A1660     9400   9923   9333  -2190  -1343    841       O  
HETATM 4384  O   HOH A1661       4.255  -5.501  38.911  1.00 36.63           O  
ANISOU 4384  O   HOH A1661     4674   4351   4892    110    -45   -162       O  
HETATM 4385  O   HOH A1662      22.592 -41.538  92.160  1.00 69.66           O  
ANISOU 4385  O   HOH A1662     8647   9795   8027   1599   -464   1642       O  
HETATM 4386  O   HOH A1663       0.531 -16.411  92.708  1.00 64.04           O  
ANISOU 4386  O   HOH A1663     8991   8417   6922    572    302     -8       O  
HETATM 4387  O   HOH A1664      -0.645  -2.159  45.021  1.00 62.70           O  
ANISOU 4387  O   HOH A1664     7752   7595   8475    -12    -49   -127       O  
HETATM 4388  O   HOH A1665      -2.435   2.782  26.822  1.00 58.56           O  
ANISOU 4388  O   HOH A1665     7425   7142   7684   -209   -267    270       O  
HETATM 4389  O   HOH A1666       3.884  19.582  18.703  1.00 48.17           O  
ANISOU 4389  O   HOH A1666     6233   5691   6379   -703   -266   1027       O  
HETATM 4390  O   HOH A1667      -2.309 -22.195  97.392  1.00 49.73           O  
ANISOU 4390  O   HOH A1667     6598   7248   5048    619    438    582       O  
HETATM 4391  O   HOH A1668      -1.085 -44.497  81.587  1.00 64.72           O  
ANISOU 4391  O   HOH A1668    10226   6854   7509  -1328  -1714   1184       O  
HETATM 4392  O   HOH A1669       5.835 -37.571  67.223  1.00 64.73           O  
ANISOU 4392  O   HOH A1669    10703   6437   7453    363   -894     81       O  
HETATM 4393  O   HOH A1670       0.010  11.657  67.297  1.00 72.29           O  
ANISOU 4393  O   HOH A1670    12972   6730   7766    928    155   -728       O  
HETATM 4394  O   HOH A1671       1.353  -2.805  47.166  1.00 67.23           O  
ANISOU 4394  O   HOH A1671     8353   8161   9030    -21    -36   -211       O  
HETATM 4395  O   HOH A1672      -4.139 -18.409  69.231  1.00 57.13           O  
ANISOU 4395  O   HOH A1672     6806   7415   7485   -151   -147    281       O  
HETATM 4396  O   HOH A1673       6.591 -26.070  68.971  1.00 57.98           O  
ANISOU 4396  O   HOH A1673     7692   6944   7392    200   -348    -87       O  
HETATM 4397  O   HOH A1674      -0.998 -18.862  93.676  1.00 65.80           O  
ANISOU 4397  O   HOH A1674     8867   8918   7217    607    378    236       O  
CONECT  635 1230                                                                
CONECT 1230  635                                                                
CONECT 1628 1634                                                                
CONECT 1634 1628 1635                                                           
CONECT 1635 1634 1636 1642                                                      
CONECT 1636 1635 1637                                                           
CONECT 1637 1636 1638                                                           
CONECT 1638 1637 1639                                                           
CONECT 1639 1638 1640 1641                                                      
CONECT 1640 1639                                                                
CONECT 1641 1639                                                                
CONECT 1642 1635 1643 1644                                                      
CONECT 1643 1642                                                                
CONECT 1644 1642                                                                
CONECT 3826 3835                                                                
CONECT 3835 3826 3836                                                           
CONECT 3836 3835 3837 3843                                                      
CONECT 3837 3836 3838                                                           
CONECT 3838 3837 3839                                                           
CONECT 3839 3838 3840                                                           
CONECT 3840 3839 3841 3842                                                      
CONECT 3841 3840                                                                
CONECT 3842 3840                                                                
CONECT 3843 3836 3844 3845                                                      
CONECT 3844 3843                                                                
CONECT 3845 3843                                                                
CONECT 3884 3900 3920 3922                                                      
CONECT 3885 3899 3901 3921                                                      
CONECT 3886 3921                                                                
CONECT 3887 3903                                                                
CONECT 3888 3889 3891 3903                                                      
CONECT 3889 3888 3905                                                           
CONECT 3890 3905 3906                                                           
CONECT 3891 3888 3906                                                           
CONECT 3892 3893                                                                
CONECT 3893 3892 3894 3898                                                      
CONECT 3894 3893 3895                                                           
CONECT 3895 3894 3896                                                           
CONECT 3896 3895 3897                                                           
CONECT 3897 3896 3898                                                           
CONECT 3898 3893 3897 3899                                                      
CONECT 3899 3885 3898 3900                                                      
CONECT 3900 3884 3899                                                           
CONECT 3901 3885 3920                                                           
CONECT 3902 3903 3921 3924                                                      
CONECT 3903 3887 3888 3902 3904                                                 
CONECT 3904 3903                                                                
CONECT 3905 3889 3890 3908                                                      
CONECT 3906 3890 3891 3907                                                      
CONECT 3907 3906 3914 3915 3916                                                 
CONECT 3908 3905 3917 3918 3919                                                 
CONECT 3909 3910 3922                                                           
CONECT 3910 3909 3923                                                           
CONECT 3911 3912 3923                                                           
CONECT 3912 3911 3922                                                           
CONECT 3913 3923                                                                
CONECT 3914 3907                                                                
CONECT 3915 3907                                                                
CONECT 3916 3907                                                                
CONECT 3917 3908                                                                
CONECT 3918 3908                                                                
CONECT 3919 3908                                                                
CONECT 3920 3884 3901                                                           
CONECT 3921 3885 3886 3902                                                      
CONECT 3922 3884 3909 3912                                                      
CONECT 3923 3910 3911 3913                                                      
CONECT 3924 3902                                                                
CONECT 3925 3926 3927 3928                                                      
CONECT 3926 3925                                                                
CONECT 3927 3925                                                                
CONECT 3928 3925 3929                                                           
CONECT 3929 3928 3930 3931 3935                                                 
CONECT 3930 3929                                                                
CONECT 3931 3929 3932                                                           
CONECT 3932 3931 3933 3934                                                      
CONECT 3933 3932                                                                
CONECT 3934 3932                                                                
CONECT 3935 3929 3936 3937                                                      
CONECT 3936 3935                                                                
CONECT 3937 3935                                                                
CONECT 3938 3939 3940 3941                                                      
CONECT 3939 3938                                                                
CONECT 3940 3938                                                                
CONECT 3941 3938 3942                                                           
CONECT 3942 3941 3943                                                           
CONECT 3943 3942 3944                                                           
CONECT 3944 3943 3945                                                           
CONECT 3945 3944 3946                                                           
CONECT 3946 3945 3947                                                           
CONECT 3947 3946 3948                                                           
CONECT 3948 3947                                                                
CONECT 3949 3950 3951 3952                                                      
CONECT 3950 3949                                                                
CONECT 3951 3949                                                                
CONECT 3952 3949 3953                                                           
CONECT 3953 3952 3954                                                           
CONECT 3954 3953 3955                                                           
CONECT 3955 3954 3956                                                           
CONECT 3956 3955 3957                                                           
CONECT 3957 3956 3958                                                           
CONECT 3958 3957 3959                                                           
CONECT 3959 3958 3960                                                           
CONECT 3960 3959 3961                                                           
CONECT 3961 3960 3962                                                           
CONECT 3962 3961                                                                
CONECT 3963 3964 3965 3966                                                      
CONECT 3964 3963                                                                
CONECT 3965 3963                                                                
CONECT 3966 3963 3967                                                           
CONECT 3967 3966 3968                                                           
CONECT 3968 3967 3969                                                           
CONECT 3969 3968 3970                                                           
CONECT 3970 3969 3971                                                           
CONECT 3971 3970 3972                                                           
CONECT 3972 3971 3973                                                           
CONECT 3973 3972 3974                                                           
CONECT 3974 3973 3975                                                           
CONECT 3975 3974 3976                                                           
CONECT 3976 3975 3977                                                           
CONECT 3977 3976 3978                                                           
CONECT 3978 3977 3979                                                           
CONECT 3979 3978                                                                
CONECT 3980 3981                                                                
CONECT 3981 3980 3982                                                           
CONECT 3982 3981 3983                                                           
CONECT 3983 3982 3984                                                           
CONECT 3984 3983 3985                                                           
CONECT 3985 3984 3986                                                           
CONECT 3986 3985                                                                
CONECT 3987 3988                                                                
CONECT 3988 3987 3989                                                           
CONECT 3989 3988 3990                                                           
CONECT 3990 3989 3991                                                           
CONECT 3991 3990 3992                                                           
CONECT 3992 3991 3993                                                           
CONECT 3993 3992 3994                                                           
CONECT 3994 3993 3995                                                           
CONECT 3995 3994 3996                                                           
CONECT 3996 3995 3997                                                           
CONECT 3997 3996                                                                
CONECT 3998 3999                                                                
CONECT 3999 3998 4000                                                           
CONECT 4000 3999 4001                                                           
CONECT 4001 4000 4002                                                           
CONECT 4002 4001 4003                                                           
CONECT 4003 4002 4004                                                           
CONECT 4004 4003 4005                                                           
CONECT 4005 4004 4006                                                           
CONECT 4006 4005 4007                                                           
CONECT 4007 4006                                                                
CONECT 4008 4009                                                                
CONECT 4009 4008 4010                                                           
CONECT 4010 4009 4011                                                           
CONECT 4011 4010 4012                                                           
CONECT 4012 4011 4013                                                           
CONECT 4013 4012                                                                
CONECT 4014 4015                                                                
CONECT 4015 4014 4016                                                           
CONECT 4016 4015 4017                                                           
CONECT 4017 4016 4018                                                           
CONECT 4018 4017 4019                                                           
CONECT 4019 4018 4020                                                           
CONECT 4020 4019 4021                                                           
CONECT 4021 4020 4022                                                           
CONECT 4022 4021 4023                                                           
CONECT 4023 4022 4024                                                           
CONECT 4024 4023 4025                                                           
CONECT 4025 4024 4026                                                           
CONECT 4026 4025                                                                
CONECT 4027 4028                                                                
CONECT 4028 4027 4029                                                           
CONECT 4029 4028 4030                                                           
CONECT 4030 4029 4031                                                           
CONECT 4031 4030 4032                                                           
CONECT 4032 4031 4033                                                           
CONECT 4033 4032 4034                                                           
CONECT 4034 4033 4035                                                           
CONECT 4035 4034 4036                                                           
CONECT 4036 4035                                                                
CONECT 4037 4038 4039                                                           
CONECT 4038 4037 4040                                                           
CONECT 4039 4037 4042                                                           
CONECT 4040 4038 4043                                                           
CONECT 4041 4052 4054                                                           
CONECT 4042 4039 4044                                                           
CONECT 4043 4040 4045                                                           
CONECT 4044 4042                                                                
CONECT 4045 4043 4046                                                           
CONECT 4046 4045 4047                                                           
CONECT 4047 4046 4048                                                           
CONECT 4048 4047 4049                                                           
CONECT 4049 4048 4051                                                           
CONECT 4050 4052 4056                                                           
CONECT 4051 4049 4053 4056                                                      
CONECT 4052 4041 4050 4055                                                      
CONECT 4053 4051                                                                
CONECT 4054 4041                                                                
CONECT 4055 4052                                                                
CONECT 4056 4050 4051                                                           
CONECT 4057 4058 4059                                                           
CONECT 4058 4057 4060                                                           
CONECT 4059 4057 4063                                                           
CONECT 4060 4058 4064                                                           
CONECT 4061 4075 4077                                                           
CONECT 4062 4065                                                                
CONECT 4063 4059 4066                                                           
CONECT 4064 4060 4067                                                           
CONECT 4065 4062 4068                                                           
CONECT 4066 4063 4068                                                           
CONECT 4067 4064 4069                                                           
CONECT 4068 4065 4066                                                           
CONECT 4069 4067 4070                                                           
CONECT 4070 4069 4071                                                           
CONECT 4071 4070 4072                                                           
CONECT 4072 4071 4074                                                           
CONECT 4073 4075 4079                                                           
CONECT 4074 4072 4076 4079                                                      
CONECT 4075 4061 4073 4078                                                      
CONECT 4076 4074                                                                
CONECT 4077 4061                                                                
CONECT 4078 4075                                                                
CONECT 4079 4073 4074                                                           
CONECT 4080 4081                                                                
CONECT 4081 4080 4082                                                           
CONECT 4082 4081 4084                                                           
CONECT 4083 4092 4094                                                           
CONECT 4084 4082 4085                                                           
CONECT 4085 4084 4086                                                           
CONECT 4086 4085 4087                                                           
CONECT 4087 4086 4088                                                           
CONECT 4088 4087 4089                                                           
CONECT 4089 4088 4091                                                           
CONECT 4090 4092 4096                                                           
CONECT 4091 4089 4093 4096                                                      
CONECT 4092 4083 4090 4095                                                      
CONECT 4093 4091                                                                
CONECT 4094 4083                                                                
CONECT 4095 4092                                                                
CONECT 4096 4090 4091                                                           
CONECT 4097 4098                                                                
CONECT 4098 4097 4099                                                           
CONECT 4099 4098 4101                                                           
CONECT 4100 4109 4111                                                           
CONECT 4101 4099 4102                                                           
CONECT 4102 4101 4103                                                           
CONECT 4103 4102 4104                                                           
CONECT 4104 4103 4105                                                           
CONECT 4105 4104 4106                                                           
CONECT 4106 4105 4108                                                           
CONECT 4107 4109 4113                                                           
CONECT 4108 4106 4110 4113                                                      
CONECT 4109 4100 4107 4112                                                      
CONECT 4110 4108                                                                
CONECT 4111 4100                                                                
CONECT 4112 4109                                                                
CONECT 4113 4107 4108                                                           
CONECT 4114 4116                                                                
CONECT 4115 4124 4126                                                           
CONECT 4116 4114 4117                                                           
CONECT 4117 4116 4118                                                           
CONECT 4118 4117 4119                                                           
CONECT 4119 4118 4120                                                           
CONECT 4120 4119 4121                                                           
CONECT 4121 4120 4123                                                           
CONECT 4122 4124 4128                                                           
CONECT 4123 4121 4125 4128                                                      
CONECT 4124 4115 4122 4127                                                      
CONECT 4125 4123                                                                
CONECT 4126 4115                                                                
CONECT 4127 4124                                                                
CONECT 4128 4122 4123                                                           
CONECT 4129 4130 4131                                                           
CONECT 4130 4129                                                                
CONECT 4131 4129 4132                                                           
CONECT 4132 4131 4133                                                           
CONECT 4133 4132 4134                                                           
CONECT 4134 4133 4135                                                           
CONECT 4135 4134                                                                
CONECT 4136 4137 4138                                                           
CONECT 4137 4136                                                                
CONECT 4138 4136 4139                                                           
CONECT 4139 4138 4140                                                           
CONECT 4140 4139 4141                                                           
CONECT 4141 4140 4142                                                           
CONECT 4142 4141                                                                
CONECT 4143 4144 4145                                                           
CONECT 4144 4143                                                                
CONECT 4145 4143 4146                                                           
CONECT 4146 4145 4147                                                           
CONECT 4147 4146 4148                                                           
CONECT 4148 4147 4149                                                           
CONECT 4149 4148                                                                
CONECT 4150 4151 4152                                                           
CONECT 4151 4150                                                                
CONECT 4152 4150 4153                                                           
CONECT 4153 4152 4154                                                           
CONECT 4154 4153 4155                                                           
CONECT 4155 4154 4156                                                           
CONECT 4156 4155                                                                
CONECT 4157 4158 4159                                                           
CONECT 4158 4157                                                                
CONECT 4159 4157 4160                                                           
CONECT 4160 4159 4161                                                           
CONECT 4161 4160 4162                                                           
CONECT 4162 4161 4163                                                           
CONECT 4163 4162                                                                
CONECT 4164 4165 4166                                                           
CONECT 4165 4164                                                                
CONECT 4166 4164 4167                                                           
CONECT 4167 4166 4168                                                           
CONECT 4168 4167 4169                                                           
CONECT 4169 4168 4170                                                           
CONECT 4170 4169                                                                
CONECT 4171 4172 4173                                                           
CONECT 4172 4171                                                                
CONECT 4173 4171 4174                                                           
CONECT 4174 4173 4175                                                           
CONECT 4175 4174 4176                                                           
CONECT 4176 4175 4177                                                           
CONECT 4177 4176                                                                
CONECT 4178 4179 4180                                                           
CONECT 4179 4178                                                                
CONECT 4180 4178 4181                                                           
CONECT 4181 4180 4182                                                           
CONECT 4182 4181 4183                                                           
CONECT 4183 4182 4184                                                           
CONECT 4184 4183                                                                
CONECT 4185 4186 4187                                                           
CONECT 4186 4185                                                                
CONECT 4187 4185 4188                                                           
CONECT 4188 4187 4189                                                           
CONECT 4189 4188 4190                                                           
CONECT 4190 4189 4191                                                           
CONECT 4191 4190                                                                
CONECT 4192 4193 4194                                                           
CONECT 4193 4192                                                                
CONECT 4194 4192 4195                                                           
CONECT 4195 4194 4196                                                           
CONECT 4196 4195 4197                                                           
CONECT 4197 4196 4198                                                           
CONECT 4198 4197                                                                
CONECT 4199 4200 4201                                                           
CONECT 4200 4199                                                                
CONECT 4201 4199 4202                                                           
CONECT 4202 4201 4203                                                           
CONECT 4203 4202 4204                                                           
CONECT 4204 4203 4205                                                           
CONECT 4205 4204                                                                
CONECT 4206 4207 4208                                                           
CONECT 4207 4206                                                                
CONECT 4208 4206 4209                                                           
CONECT 4209 4208 4210                                                           
CONECT 4210 4209 4211                                                           
CONECT 4211 4210 4212                                                           
CONECT 4212 4211                                                                
CONECT 4213 4214 4215                                                           
CONECT 4214 4213                                                                
CONECT 4215 4213 4216                                                           
CONECT 4216 4215 4217                                                           
CONECT 4217 4216 4218                                                           
CONECT 4218 4217 4219                                                           
CONECT 4219 4218                                                                
CONECT 4220 4221 4222                                                           
CONECT 4221 4220                                                                
CONECT 4222 4220 4223                                                           
CONECT 4223 4222 4224                                                           
CONECT 4224 4223 4225                                                           
CONECT 4225 4224 4226                                                           
CONECT 4226 4225                                                                
CONECT 4227 4228 4229                                                           
CONECT 4228 4227                                                                
CONECT 4229 4227 4230                                                           
CONECT 4230 4229 4231                                                           
CONECT 4231 4230 4232                                                           
CONECT 4232 4231 4233                                                           
CONECT 4233 4232                                                                
CONECT 4234 4235 4236                                                           
CONECT 4235 4234                                                                
CONECT 4236 4234 4237                                                           
CONECT 4237 4236 4238                                                           
CONECT 4238 4237 4239                                                           
CONECT 4239 4238 4240                                                           
CONECT 4240 4239                                                                
CONECT 4241 4242 4243                                                           
CONECT 4242 4241                                                                
CONECT 4243 4241 4244                                                           
CONECT 4244 4243 4245                                                           
CONECT 4245 4244 4246                                                           
CONECT 4246 4245 4247                                                           
CONECT 4247 4246                                                                
CONECT 4248 4249 4250                                                           
CONECT 4249 4248                                                                
CONECT 4250 4248 4251                                                           
CONECT 4251 4250 4252                                                           
CONECT 4252 4251 4253                                                           
CONECT 4253 4252 4254                                                           
CONECT 4254 4253                                                                
CONECT 4255 4256 4257                                                           
CONECT 4256 4255                                                                
CONECT 4257 4255 4258                                                           
CONECT 4258 4257 4259                                                           
CONECT 4259 4258 4260                                                           
CONECT 4260 4259 4261                                                           
CONECT 4261 4260                                                                
CONECT 4262 4263 4264                                                           
CONECT 4263 4262                                                                
CONECT 4264 4262 4265                                                           
CONECT 4265 4264 4266                                                           
CONECT 4266 4265 4267                                                           
CONECT 4267 4266 4268                                                           
CONECT 4268 4267                                                                
CONECT 4269 4270 4271                                                           
CONECT 4270 4269                                                                
CONECT 4271 4269 4272                                                           
CONECT 4272 4271 4273                                                           
CONECT 4273 4272 4274                                                           
CONECT 4274 4273 4275                                                           
CONECT 4275 4274                                                                
CONECT 4276 4277 4278                                                           
CONECT 4277 4276                                                                
CONECT 4278 4276 4279                                                           
CONECT 4279 4278 4280                                                           
CONECT 4280 4279 4281                                                           
CONECT 4281 4280 4282                                                           
CONECT 4282 4281                                                                
CONECT 4283 4284                                                                
CONECT 4284 4283 4285                                                           
CONECT 4285 4284 4287                                                           
CONECT 4286 4295 4297                                                           
CONECT 4287 4285 4288                                                           
CONECT 4288 4287 4289                                                           
CONECT 4289 4288 4290                                                           
CONECT 4290 4289 4291                                                           
CONECT 4291 4290 4292                                                           
CONECT 4292 4291 4294                                                           
CONECT 4293 4295 4299                                                           
CONECT 4294 4292 4296 4299                                                      
CONECT 4295 4286 4293 4298                                                      
CONECT 4296 4294                                                                
CONECT 4297 4286                                                                
CONECT 4298 4295                                                                
CONECT 4299 4293 4294                                                           
CONECT 4300 4305 4307                                                           
CONECT 4301 4302                                                                
CONECT 4302 4301 4304                                                           
CONECT 4303 4305 4309                                                           
CONECT 4304 4302 4306 4309                                                      
CONECT 4305 4300 4303 4308                                                      
CONECT 4306 4304                                                                
CONECT 4307 4300                                                                
CONECT 4308 4305                                                                
CONECT 4309 4303 4304                                                           
CONECT 4310 4311 4312                                                           
CONECT 4311 4310                                                                
CONECT 4312 4310 4313                                                           
CONECT 4313 4312 4314                                                           
CONECT 4314 4313 4315                                                           
CONECT 4315 4314 4316                                                           
CONECT 4316 4315                                                                
CONECT 4317 4318 4319                                                           
CONECT 4318 4317                                                                
CONECT 4319 4317 4320                                                           
CONECT 4320 4319 4321                                                           
CONECT 4321 4320 4322                                                           
CONECT 4322 4321 4323                                                           
CONECT 4323 4322                                                                
MASTER      529    0   44   19    8    0   60    6 4396    1  466   40          
END