HEADER    MEMBRANE PROTEIN                        11-SEP-18   6HLO              
TITLE     CRYSTAL STRUCTURE OF THE NEUROKININ 1 RECEPTOR IN COMPLEX WITH THE    
TITLE    2 SMALL MOLECULE ANTAGONIST APREPITANT                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SUBSTANCE-P RECEPTOR,GLGA GLYCOGEN SYNTHASE,SUBSTANCE-P    
COMPND   3 RECEPTOR;                                                            
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: SPR,NK-1 RECEPTOR,NK-1R,TACHYKININ RECEPTOR 1,GLYCOGEN      
COMPND   6 SYNTHASE,SPR,NK-1 RECEPTOR,NK-1R,TACHYKININ RECEPTOR 1;              
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 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, PAB2292;                                   
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 6HLO    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.    2.40 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) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.44                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 31899                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.190                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1656                            
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 29.4439 -  5.4838    1.00     2704   141  0.1966 0.2086        
REMARK   3     2  5.4838 -  4.3572    1.00     2554   169  0.1809 0.1853        
REMARK   3     3  4.3572 -  3.8077    1.00     2534   141  0.1816 0.2213        
REMARK   3     4  3.8077 -  3.4602    1.00     2508   145  0.1930 0.2061        
REMARK   3     5  3.4602 -  3.2125    1.00     2519   146  0.2058 0.2559        
REMARK   3     6  3.2125 -  3.0233    1.00     2505   139  0.2107 0.2454        
REMARK   3     7  3.0233 -  2.8720    1.00     2497   126  0.2200 0.2995        
REMARK   3     8  2.8720 -  2.7471    1.00     2499   122  0.2213 0.2923        
REMARK   3     9  2.7471 -  2.6414    1.00     2495   127  0.2232 0.2913        
REMARK   3    10  2.6414 -  2.5503    1.00     2470   132  0.2347 0.3046        
REMARK   3    11  2.5503 -  2.4706    1.00     2495   136  0.2538 0.3084        
REMARK   3    12  2.4706 -  2.4000    1.00     2463   132  0.2832 0.3595        
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)     : 0.310            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.720           
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      :  0.003           4228                                  
REMARK   3   ANGLE     :  0.578           5652                                  
REMARK   3   CHIRALITY :  0.044            614                                  
REMARK   3   PLANARITY :  0.005            684                                  
REMARK   3   DIHEDRAL  : 13.405           2510                                  
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):   4.0027 -11.0178  58.4780              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4715 T22:   0.4783                                     
REMARK   3      T33:   0.5428 T12:   0.0162                                     
REMARK   3      T13:   0.0015 T23:  -0.0521                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4562 L22:   1.2796                                     
REMARK   3      L33:   3.2033 L12:  -0.1691                                     
REMARK   3      L13:   0.3962 L23:  -1.7452                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0552 S12:  -0.0371 S13:   0.0089                       
REMARK   3      S21:   0.0060 S22:   0.0138 S23:   0.0592                       
REMARK   3      S31:   0.0326 S32:   0.1057 S33:   0.0002                       
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 6HLO 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_1200011869.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUN-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : 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                                  
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   : 32007                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.240                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 26.20                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.49                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 26.40                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
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   (%): 66.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.68                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM CITRATE PH 6.0, 31%        
REMARK 280  (V/V) PEG400, 50-70 MM MGCL2 AND 50 UM APREPITANT, LIPIDIC CUBIC    
REMARK 280  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       31.09450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       83.56200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.22500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       83.56200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.09450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.22500            
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: 7170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 30.0 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     GLN A    27                                                      
REMARK 465     LEU A   279                                                      
REMARK 465     LYS A   280                                                      
REMARK 465     LYS A   281                                                      
REMARK 465     PHE A   325                                                      
REMARK 465     ILE A   326                                                      
REMARK 465     SER A   327                                                      
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     TYR A 278    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     PHE A 282    CG   CD1  CD2  CE1  CE2  CZ                         
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   O5   CIT A  1502     O    HOH A  1601              2.15            
REMARK 500   O2   CIT A  1502     O    HOH A  1602              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A  1610     O    HOH A  1616     3555     2.19            
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 A1413   CA  -  C   -  N   ANGL. DEV. = -18.3 DEGREES          
REMARK 500    SER A1413   O   -  C   -  N   ANGL. DEV. =  16.0 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       46.92    -84.81                                   
REMARK 500    TYR A 205      -72.28   -135.54                                   
REMARK 500    GLN A1262      -80.41   -126.95                                   
REMARK 500    PRO A1335       44.79    -88.06                                   
REMARK 500    ASN A 274      106.94   -165.00                                   
REMARK 500    PRO A 275      -70.30    -53.03                                   
REMARK 500    ASP A 276     -126.15     56.10                                   
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 1504                                                       
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     OLA A 1512                                                       
REMARK 610     OLA A 1513                                                       
REMARK 610     OLA A 1514                                                       
REMARK 610     OLA A 1516                                                       
REMARK 610     OLA A 1517                                                       
REMARK 610     OLA A 1518                                                       
REMARK 610     OLA A 1519                                                       
REMARK 610     OLC A 1520                                                       
REMARK 610     OLC A 1521                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GBQ 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 OLA A 1512                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1513                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1515                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1516                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1517                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1518                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1519                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1520                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1521                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1522                
DBREF  6HLO A    1  1219  UNP    P25103   NK1R_HUMAN       1    228             
DBREF  6HLO A 1220  1413  UNP    Q9V2J8   Q9V2J8_PYRAB   220    413             
DBREF  6HLO A  238   335  UNP    P25103   NK1R_HUMAN     238    335             
SEQADV 6HLO ALA A   74  UNP  P25103    LEU    74 ENGINEERED MUTATION            
SEQADV 6HLO ILE A  116  UNP  P25103    VAL   116 ENGINEERED MUTATION            
SEQADV 6HLO LEU A  144  UNP  P25103    ALA   144 ENGINEERED MUTATION            
SEQADV 6HLO LYS A  181  UNP  P25103    MET   181 ENGINEERED MUTATION            
SEQADV 6HLO LEU A  215  UNP  P25103    ALA   215 ENGINEERED MUTATION            
SEQADV 6HLO ARG A  224  UNP  P25103    TRP   224 ENGINEERED MUTATION            
SEQADV 6HLO GLY A 1218  UNP  P25103    GLU   227 CONFLICT                       
SEQADV 6HLO 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 6HLO YCM A 1221  CYS  MODIFIED RESIDUE                                   
MODRES 6HLO YCM A  322  CYS  MODIFIED RESIDUE                                   
HET    YCM  A1221      10                                                       
HET    YCM  A 322      10                                                       
HET    GBQ  A1501      37                                                       
HET    CIT  A1502      13                                                       
HET    OLA  A1503      20                                                       
HET    OLA  A1504      14                                                       
HET    OLA  A1505      20                                                       
HET    OLA  A1506      10                                                       
HET    OLA  A1507       8                                                       
HET    OLA  A1508       9                                                       
HET    OLA  A1509      11                                                       
HET    OLA  A1510      11                                                       
HET    OLA  A1511      13                                                       
HET    OLA  A1512      13                                                       
HET    OLA  A1513       9                                                       
HET    OLA  A1514       9                                                       
HET    OLA  A1515      20                                                       
HET    OLA  A1516      11                                                       
HET    OLA  A1517      16                                                       
HET    OLA  A1518      11                                                       
HET    OLA  A1519      10                                                       
HET    OLC  A1520      15                                                       
HET    OLC  A1521      10                                                       
HET    OLC  A1522      25                                                       
HETNAM     YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE                                
HETNAM     GBQ 5-[[(2~{R},3~{S})-2-[(1~{R})-1-[3,5-                             
HETNAM   2 GBQ  BIS(TRIFLUOROMETHYL)PHENYL]ETHOXY]-3-(4-FLUOROPHENYL)           
HETNAM   3 GBQ  MORPHOLIN-4-YL]METHYL]-1,2-DIHYDRO-1,2,4-TRIAZOL-3-ONE          
HETNAM     CIT CITRIC ACID                                                      
HETNAM     OLA OLEIC ACID                                                       
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETSYN     YCM CYSTEINE-S-ACETAMIDE                                             
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
FORMUL   1  YCM    2(C5 H10 N2 O3 S)                                            
FORMUL   2  GBQ    C23 H21 F7 N4 O3                                             
FORMUL   3  CIT    C6 H8 O7                                                     
FORMUL   4  OLA    17(C18 H34 O2)                                               
FORMUL  21  OLC    3(C21 H40 O4)                                                
FORMUL  24  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  SER A 1394  1                                  16    
HELIX   17 AB8 LEU A 1398  ASN A  274  1                                  53    
HELIX   18 AB9 ILE A  283  SER A  297  1                                  15    
HELIX   19 AC1 MET A  299  ASN A  309  1                                  11    
HELIX   20 AC2 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  2.04  
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        -8.56                     
SITE     1 AC1 18 ASN A  89  ASN A 109  PRO A 112  ILE A 113                    
SITE     2 AC1 18 ILE A 116  GLN A 165  ILE A 182  TRP A 184                    
SITE     3 AC1 18 GLU A 193  HIS A 197  VAL A 200  THR A 201                    
SITE     4 AC1 18 ILE A 204  TRP A 261  PHE A 264  HIS A 265                    
SITE     5 AC1 18 MET A 291  MET A 295                                          
SITE     1 AC2  9 GLY A 101  LEU A 102  PHE A 103  ARG A 224                    
SITE     2 AC2  9 OLA A1506  HOH A1601  HOH A1602  HOH A1603                    
SITE     3 AC2  9 HOH A1611                                                     
SITE     1 AC3  2 PHE A 110  TYR A 167                                          
SITE     1 AC4  7 GLY A 213  TYR A 216  THR A 217  ARG A 224                    
SITE     2 AC4  7 OLA A1505  OLA A1506  OLC A1520                               
SITE     1 AC5  8 VAL A  88  THR A  91  TYR A 100  ARG A 224                    
SITE     2 AC5  8 OLA A1504  OLA A1508  OLC A1521  OLC A1522                    
SITE     1 AC6  6 TYR A 100  TYR A 104  CIT A1502  OLA A1504                    
SITE     2 AC6  6 OLC A1520  OLC A1521                                          
SITE     1 AC7  2 TYR A 214  OLA A1508                                          
SITE     1 AC8  3 THR A 222  OLA A1505  OLA A1507                               
SITE     1 AC9  3 LEU A  58  ARG A  64  ASN A 274                               
SITE     1 AD1  1 ILE A 266                                                     
SITE     1 AD2  3 GLN A  31  LEU A  34  TRP A  35                               
SITE     1 AD3  1 TYR A 121                                                     
SITE     1 AD4  2 TYR A 131  TYR A 214                                          
SITE     1 AD5  3 LYS A 248  THR A 256  TYR A 300                               
SITE     1 AD6  5 VAL A  44  THR A  45  VAL A  48  GLY A  49                    
SITE     2 AD6  5 PHE A 316                                                     
SITE     1 AD7  5 TYR A  69  VAL A  72  ASN A  73  LYS A 148                    
SITE     2 AD7  5 TRP A 155                                                     
SITE     1 AD8  4 TRP A  55  HIS A 318  ARG A 321  OLA A1519                    
SITE     1 AD9  3 PHE A 320  OLA A1518  OLC A1522                               
SITE     1 AE1  6 GLY A 220  ARG A 224  ARG A 244  OLA A1504                    
SITE     2 AE1  6 OLA A1506  HOH A1601                                          
SITE     1 AE2  6 PHE A 103  TYR A 104  PHE A 107  OLA A1505                    
SITE     2 AE2  6 OLA A1506  OLC A1522                                          
SITE     1 AE3  5 ALA A  83  TYR A 104  OLA A1505  OLA A1519                    
SITE     2 AE3  5 OLC A1521                                                     
CRYST1   62.189   76.450  167.124  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      0.016080  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013080  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005984        0.00000                         
ATOM      1  N   PRO A  28     -18.926   0.109  20.472  1.00106.78           N  
ANISOU    1  N   PRO A  28    12633  14260  13677  -1808  -2085   2422       N  
ATOM      2  CA  PRO A  28     -19.932   0.061  21.539  1.00110.48           C  
ANISOU    2  CA  PRO A  28    12823  14920  14234  -1815  -2076   2649       C  
ATOM      3  C   PRO A  28     -19.741   1.186  22.554  1.00108.37           C  
ANISOU    3  C   PRO A  28    12360  14714  14100  -1510  -1805   2615       C  
ATOM      4  O   PRO A  28     -19.055   1.001  23.560  1.00115.24           O  
ANISOU    4  O   PRO A  28    13282  15496  15007  -1393  -1685   2448       O  
ATOM      5  CB  PRO A  28     -19.695  -1.308  22.178  1.00107.85           C  
ANISOU    5  CB  PRO A  28    12650  14486  13844  -1964  -2187   2569       C  
ATOM      6  CG  PRO A  28     -18.247  -1.582  21.935  1.00101.47           C  
ANISOU    6  CG  PRO A  28    12154  13428  12970  -1876  -2118   2234       C  
ATOM      7  CD  PRO A  28     -17.912  -0.951  20.613  1.00 99.65           C  
ANISOU    7  CD  PRO A  28    12032  13146  12684  -1855  -2123   2178       C  
ATOM      8  N   ALA A  29     -20.355   2.342  22.283  1.00 95.90           N  
ANISOU    8  N   ALA A  29    10577  13280  12582  -1381  -1717   2779       N  
ATOM      9  CA  ALA A  29     -20.089   3.533  23.084  1.00 84.96           C  
ANISOU    9  CA  ALA A  29     9076  11910  11295  -1076  -1461   2726       C  
ATOM     10  C   ALA A  29     -20.512   3.363  24.539  1.00 91.98           C  
ANISOU   10  C   ALA A  29     9801  12898  12249   -976  -1366   2811       C  
ATOM     11  O   ALA A  29     -19.890   3.949  25.434  1.00 93.99           O  
ANISOU   11  O   ALA A  29    10079  13076  12557   -753  -1169   2662       O  
ATOM     12  CB  ALA A  29     -20.790   4.744  22.468  1.00 68.35           C  
ANISOU   12  CB  ALA A  29     6802   9944   9226   -959  -1400   2915       C  
ATOM     13  N   TRP A  30     -21.565   2.583  24.801  1.00 99.48           N  
ANISOU   13  N   TRP A  30    10587  14022  13188  -1143  -1507   3061       N  
ATOM     14  CA  TRP A  30     -21.995   2.386  26.184  1.00106.58           C  
ANISOU   14  CA  TRP A  30    11320  15033  14142  -1048  -1415   3159       C  
ATOM     15  C   TRP A  30     -20.938   1.644  26.994  1.00105.43           C  
ANISOU   15  C   TRP A  30    11379  14691  13990  -1049  -1380   2881       C  
ATOM     16  O   TRP A  30     -20.723   1.944  28.177  1.00110.03           O  
ANISOU   16  O   TRP A  30    11907  15272  14627   -855  -1208   2822       O  
ATOM     17  CB  TRP A  30     -23.330   1.639  26.219  1.00109.28           C  
ANISOU   17  CB  TRP A  30    11437  15619  14466  -1262  -1596   3509       C  
ATOM     18  CG  TRP A  30     -23.303   0.297  25.549  1.00113.54           C  
ANISOU   18  CG  TRP A  30    12150  16079  14912  -1620  -1877   3496       C  
ATOM     19  CD1 TRP A  30     -23.409   0.044  24.211  1.00118.48           C  
ANISOU   19  CD1 TRP A  30    12898  16664  15456  -1837  -2073   3527       C  
ATOM     20  CD2 TRP A  30     -23.177  -0.979  26.188  1.00111.39           C  
ANISOU   20  CD2 TRP A  30    11977  15744  14603  -1801  -1998   3453       C  
ATOM     21  NE1 TRP A  30     -23.349  -1.309  23.978  1.00117.68           N  
ANISOU   21  NE1 TRP A  30    12990  16464  15258  -2139  -2310   3500       N  
ATOM     22  CE2 TRP A  30     -23.208  -1.960  25.176  1.00113.99           C  
ANISOU   22  CE2 TRP A  30    12512  15980  14819  -2124  -2270   3456       C  
ATOM     23  CE3 TRP A  30     -23.038  -1.388  27.518  1.00116.09           C  
ANISOU   23  CE3 TRP A  30    12524  16343  15240  -1721  -1905   3411       C  
ATOM     24  CZ2 TRP A  30     -23.105  -3.322  25.452  1.00114.33           C  
ANISOU   24  CZ2 TRP A  30    12729  15924  14788  -2364  -2452   3418       C  
ATOM     25  CZ3 TRP A  30     -22.935  -2.742  27.791  1.00117.52           C  
ANISOU   25  CZ3 TRP A  30    12851  16442  15361  -1962  -2084   3377       C  
ATOM     26  CH2 TRP A  30     -22.970  -3.692  26.762  1.00116.56           C  
ANISOU   26  CH2 TRP A  30    12948  16217  15124  -2279  -2355   3381       C  
ATOM     27  N   GLN A  31     -20.244   0.690  26.366  1.00101.25           N  
ANISOU   27  N   GLN A  31    11099  13988  13381  -1251  -1536   2707       N  
ATOM     28  CA  GLN A  31     -19.145   0.022  27.051  1.00100.51           C  
ANISOU   28  CA  GLN A  31    11212  13705  13274  -1230  -1492   2438       C  
ATOM     29  C   GLN A  31     -18.017   0.999  27.348  1.00 94.14           C  
ANISOU   29  C   GLN A  31    10495  12764  12512   -974  -1270   2192       C  
ATOM     30  O   GLN A  31     -17.377   0.920  28.404  1.00 94.69           O  
ANISOU   30  O   GLN A  31    10604  12759  12613   -857  -1151   2046       O  
ATOM     31  CB  GLN A  31     -18.628  -1.147  26.213  1.00105.84           C  
ANISOU   31  CB  GLN A  31    12163  14217  13834  -1465  -1693   2311       C  
ATOM     32  CG  GLN A  31     -19.636  -2.253  25.966  1.00113.68           C  
ANISOU   32  CG  GLN A  31    13132  15301  14760  -1762  -1947   2534       C  
ATOM     33  CD  GLN A  31     -18.980  -3.512  25.433  1.00119.28           C  
ANISOU   33  CD  GLN A  31    14183  15799  15340  -1959  -2123   2367       C  
ATOM     34  OE1 GLN A  31     -17.907  -3.905  25.890  1.00120.33           O  
ANISOU   34  OE1 GLN A  31    14505  15760  15455  -1866  -2041   2118       O  
ATOM     35  NE2 GLN A  31     -19.617  -4.145  24.455  1.00124.68           N  
ANISOU   35  NE2 GLN A  31    14961  16493  15920  -2227  -2369   2509       N  
ATOM     36  N   ILE A  32     -17.778   1.947  26.439  1.00 77.22           N  
ANISOU   36  N   ILE A  32     8381  10591  10366   -896  -1220   2158       N  
ATOM     37  CA  ILE A  32     -16.748   2.952  26.677  1.00 77.01           C  
ANISOU   37  CA  ILE A  32     8438  10445  10377   -678  -1027   1954       C  
ATOM     38  C   ILE A  32     -17.143   3.854  27.838  1.00 77.15           C  
ANISOU   38  C   ILE A  32     8291  10547  10475   -453   -843   2032       C  
ATOM     39  O   ILE A  32     -16.300   4.244  28.655  1.00 80.85           O  
ANISOU   39  O   ILE A  32     8843  10908  10970   -306   -701   1857       O  
ATOM     40  CB  ILE A  32     -16.485   3.758  25.392  1.00 73.43           C  
ANISOU   40  CB  ILE A  32     8050   9953   9898   -664  -1030   1926       C  
ATOM     41  CG1 ILE A  32     -16.063   2.823  24.258  1.00 75.26           C  
ANISOU   41  CG1 ILE A  32     8476  10090  10028   -869  -1205   1842       C  
ATOM     42  CG2 ILE A  32     -15.427   4.826  25.632  1.00 62.43           C  
ANISOU   42  CG2 ILE A  32     6743   8439   8538   -464   -847   1737       C  
ATOM     43  CD1 ILE A  32     -14.894   1.928  24.607  1.00 69.83           C  
ANISOU   43  CD1 ILE A  32     8001   9240   9291   -893  -1206   1603       C  
ATOM     44  N   VAL A  33     -18.436   4.168  27.955  1.00 74.63           N  
ANISOU   44  N   VAL A  33     7744  10427  10184   -420   -846   2308       N  
ATOM     45  CA  VAL A  33     -18.893   4.995  29.067  1.00 76.18           C  
ANISOU   45  CA  VAL A  33     7800  10711  10435   -176   -661   2403       C  
ATOM     46  C   VAL A  33     -18.713   4.257  30.389  1.00 67.81           C  
ANISOU   46  C   VAL A  33     6737   9637   9388   -163   -624   2343       C  
ATOM     47  O   VAL A  33     -18.237   4.831  31.381  1.00 61.72           O  
ANISOU   47  O   VAL A  33     6015   8794   8642     35   -456   2230       O  
ATOM     48  CB  VAL A  33     -20.358   5.418  28.847  1.00 68.05           C  
ANISOU   48  CB  VAL A  33     6507   9930   9420   -131   -670   2746       C  
ATOM     49  CG1 VAL A  33     -20.901   6.124  30.080  1.00 86.33           C  
ANISOU   49  CG1 VAL A  33     8683  12349  11769    143   -472   2865       C  
ATOM     50  CG2 VAL A  33     -20.474   6.313  27.624  1.00 66.94           C  
ANISOU   50  CG2 VAL A  33     6375   9792   9269   -104   -678   2795       C  
ATOM     51  N   LEU A  34     -19.066   2.969  30.420  1.00 63.26           N  
ANISOU   51  N   LEU A  34     6128   9119   8789   -385   -789   2416       N  
ATOM     52  CA  LEU A  34     -18.907   2.199  31.652  1.00 72.81           C  
ANISOU   52  CA  LEU A  34     7337  10318  10009   -388   -766   2366       C  
ATOM     53  C   LEU A  34     -17.436   2.051  32.028  1.00 74.29           C  
ANISOU   53  C   LEU A  34     7765  10274  10188   -347   -702   2038       C  
ATOM     54  O   LEU A  34     -17.074   2.135  33.211  1.00 82.19           O  
ANISOU   54  O   LEU A  34     8778  11238  11214   -216   -579   1951       O  
ATOM     55  CB  LEU A  34     -19.565   0.828  31.500  1.00 71.79           C  
ANISOU   55  CB  LEU A  34     7152  10281   9845   -662   -981   2517       C  
ATOM     56  CG  LEU A  34     -21.070   0.820  31.227  1.00 78.86           C  
ANISOU   56  CG  LEU A  34     7776  11443  10744   -745  -1072   2886       C  
ATOM     57  CD1 LEU A  34     -21.560  -0.598  30.984  1.00 84.40           C  
ANISOU   57  CD1 LEU A  34     8480  12195  11394  -1070  -1324   3011       C  
ATOM     58  CD2 LEU A  34     -21.832   1.465  32.375  1.00 74.81           C  
ANISOU   58  CD2 LEU A  34     7025  11118  10282   -507   -892   3076       C  
ATOM     59  N   TRP A  35     -16.565   1.862  31.031  1.00 60.74           N  
ANISOU   59  N   TRP A  35     6237   8411   8430   -449   -778   1865       N  
ATOM     60  CA  TRP A  35     -15.140   1.756  31.318  1.00 61.82           C  
ANISOU   60  CA  TRP A  35     6578   8357   8553   -403   -714   1582       C  
ATOM     61  C   TRP A  35     -14.581   3.073  31.836  1.00 64.72           C  
ANISOU   61  C   TRP A  35     6964   8666   8961   -175   -520   1484       C  
ATOM     62  O   TRP A  35     -13.754   3.082  32.759  1.00 57.89           O  
ANISOU   62  O   TRP A  35     6183   7708   8106    -95   -429   1326       O  
ATOM     63  CB  TRP A  35     -14.376   1.315  30.070  1.00 55.44           C  
ANISOU   63  CB  TRP A  35     5956   7430   7677   -535   -826   1448       C  
ATOM     64  CG  TRP A  35     -14.390  -0.159  29.822  1.00 61.68           C  
ANISOU   64  CG  TRP A  35     6854   8183   8399   -741  -1001   1437       C  
ATOM     65  CD1 TRP A  35     -14.937  -0.807  28.751  1.00 63.56           C  
ANISOU   65  CD1 TRP A  35     7143   8441   8568   -936  -1187   1537       C  
ATOM     66  CD2 TRP A  35     -13.827  -1.175  30.660  1.00 61.73           C  
ANISOU   66  CD2 TRP A  35     6960   8110   8385   -776  -1017   1319       C  
ATOM     67  NE1 TRP A  35     -14.747  -2.161  28.870  1.00 65.90           N  
ANISOU   67  NE1 TRP A  35     7588   8658   8793  -1089  -1320   1485       N  
ATOM     68  CE2 TRP A  35     -14.070  -2.414  30.034  1.00 57.23           C  
ANISOU   68  CE2 TRP A  35     6516   7503   7729   -988  -1214   1352       C  
ATOM     69  CE3 TRP A  35     -13.143  -1.158  31.880  1.00 55.55           C  
ANISOU   69  CE3 TRP A  35     6186   7278   7641   -652   -890   1192       C  
ATOM     70  CZ2 TRP A  35     -13.654  -3.622  30.586  1.00 59.57           C  
ANISOU   70  CZ2 TRP A  35     6948   7708   7976  -1065  -1280   1262       C  
ATOM     71  CZ3 TRP A  35     -12.731  -2.359  32.427  1.00 59.68           C  
ANISOU   71  CZ3 TRP A  35     6819   7731   8126   -731   -952   1107       C  
ATOM     72  CH2 TRP A  35     -12.988  -3.574  31.780  1.00 68.77           C  
ANISOU   72  CH2 TRP A  35     8097   8840   9192   -929  -1142   1142       C  
ATOM     73  N   ALA A  36     -15.030   4.197  31.266  1.00 51.52           N  
ANISOU   73  N   ALA A  36     5228   7042   7304    -76   -462   1582       N  
ATOM     74  CA  ALA A  36     -14.563   5.488  31.751  1.00 52.01           C  
ANISOU   74  CA  ALA A  36     5343   7029   7389    133   -291   1501       C  
ATOM     75  C   ALA A  36     -15.023   5.727  33.182  1.00 59.27           C  
ANISOU   75  C   ALA A  36     6186   8001   8334    297   -166   1565       C  
ATOM     76  O   ALA A  36     -14.278   6.281  34.000  1.00 54.06           O  
ANISOU   76  O   ALA A  36     5641   7225   7673    421    -50   1421       O  
ATOM     77  CB  ALA A  36     -15.054   6.603  30.830  1.00 51.90           C  
ANISOU   77  CB  ALA A  36     5286   7056   7378    210   -261   1613       C  
ATOM     78  N   ALA A  37     -16.228   5.259  33.520  1.00 53.77           N  
ANISOU   78  N   ALA A  37     5299   7482   7649    287   -197   1787       N  
ATOM     79  CA  ALA A  37     -16.696   5.391  34.895  1.00 56.82           C  
ANISOU   79  CA  ALA A  37     5606   7936   8048    451    -74   1862       C  
ATOM     80  C   ALA A  37     -15.856   4.549  35.849  1.00 59.03           C  
ANISOU   80  C   ALA A  37     5988   8115   8325    392    -80   1681       C  
ATOM     81  O   ALA A  37     -15.487   5.012  36.937  1.00 60.31           O  
ANISOU   81  O   ALA A  37     6220   8211   8484    550     52   1596       O  
ATOM     82  CB  ALA A  37     -18.171   5.002  34.986  1.00 55.13           C  
ANISOU   82  CB  ALA A  37     5137   7968   7843    437   -115   2171       C  
ATOM     83  N   ALA A  38     -15.519   3.320  35.447  1.00 52.55           N  
ANISOU   83  N   ALA A  38     5202   7271   7495    169   -235   1619       N  
ATOM     84  CA  ALA A  38     -14.709   2.472  36.319  1.00 60.92           C  
ANISOU   84  CA  ALA A  38     6360   8237   8548    118   -242   1454       C  
ATOM     85  C   ALA A  38     -13.316   3.062  36.528  1.00 53.74           C  
ANISOU   85  C   ALA A  38     5642   7146   7630    196   -154   1206       C  
ATOM     86  O   ALA A  38     -12.785   3.067  37.651  1.00 51.74           O  
ANISOU   86  O   ALA A  38     5448   6833   7379    275    -72   1102       O  
ATOM     87  CB  ALA A  38     -14.618   1.062  35.736  1.00 50.28           C  
ANISOU   87  CB  ALA A  38     5049   6881   7173   -124   -428   1440       C  
ATOM     88  N   TYR A  39     -12.720   3.592  35.459  1.00 52.91           N  
ANISOU   88  N   TYR A  39     5631   6962   7512    169   -175   1122       N  
ATOM     89  CA  TYR A  39     -11.391   4.180  35.582  1.00 54.75           C  
ANISOU   89  CA  TYR A  39     6026   7043   7732    219   -106    917       C  
ATOM     90  C   TYR A  39     -11.415   5.446  36.435  1.00 48.80           C  
ANISOU   90  C   TYR A  39     5307   6249   6985    413     45    915       C  
ATOM     91  O   TYR A  39     -10.488   5.693  37.221  1.00 52.26           O  
ANISOU   91  O   TYR A  39     5864   6581   7411    455    105    772       O  
ATOM     92  CB  TYR A  39     -10.818   4.454  34.189  1.00 49.97           C  
ANISOU   92  CB  TYR A  39     5496   6385   7104    142   -165    858       C  
ATOM     93  CG  TYR A  39     -10.131   3.249  33.574  1.00 49.88           C  
ANISOU   93  CG  TYR A  39     5561   6336   7053    -14   -281    760       C  
ATOM     94  CD1 TYR A  39     -10.867   2.182  33.066  1.00 49.92           C  
ANISOU   94  CD1 TYR A  39     5522   6408   7038   -148   -413    857       C  
ATOM     95  CD2 TYR A  39      -8.743   3.177  33.512  1.00 51.89           C  
ANISOU   95  CD2 TYR A  39     5946   6490   7280    -25   -261    583       C  
ATOM     96  CE1 TYR A  39     -10.237   1.080  32.508  1.00 46.74           C  
ANISOU   96  CE1 TYR A  39     5239   5945   6576   -271   -517    762       C  
ATOM     97  CE2 TYR A  39      -8.106   2.081  32.957  1.00 49.85           C  
ANISOU   97  CE2 TYR A  39     5774   6199   6969   -127   -349    502       C  
ATOM     98  CZ  TYR A  39      -8.856   1.037  32.456  1.00 50.22           C  
ANISOU   98  CZ  TYR A  39     5812   6285   6985   -241   -473    582       C  
ATOM     99  OH  TYR A  39      -8.222  -0.053  31.906  1.00 45.61           O  
ANISOU   99  OH  TYR A  39     5362   5643   6326   -324   -558    496       O  
ATOM    100  N   THR A  40     -12.471   6.258  36.312  1.00 55.90           N  
ANISOU  100  N   THR A  40     6118   7228   7892    537    104   1082       N  
ATOM    101  CA  THR A  40     -12.579   7.424  37.183  1.00 64.78           C  
ANISOU  101  CA  THR A  40     7314   8299   9000    748    253   1088       C  
ATOM    102  C   THR A  40     -12.791   7.025  38.637  1.00 58.28           C  
ANISOU  102  C   THR A  40     6473   7501   8171    833    322   1094       C  
ATOM    103  O   THR A  40     -12.324   7.726  39.544  1.00 60.44           O  
ANISOU  103  O   THR A  40     6890   7664   8411    960    423   1004       O  
ATOM    104  CB  THR A  40     -13.711   8.343  36.723  1.00 64.09           C  
ANISOU  104  CB  THR A  40     7138   8302   8910    895    314   1284       C  
ATOM    105  OG1 THR A  40     -14.920   7.586  36.586  1.00 85.29           O  
ANISOU  105  OG1 THR A  40     9600  11189  11619    858    261   1497       O  
ATOM    106  CG2 THR A  40     -13.370   8.996  35.394  1.00 50.79           C  
ANISOU  106  CG2 THR A  40     5512   6561   7224    839    268   1256       C  
ATOM    107  N   VAL A  41     -13.491   5.914  38.885  1.00 57.16           N  
ANISOU  107  N   VAL A  41     6170   7498   8050    758    261   1206       N  
ATOM    108  CA  VAL A  41     -13.617   5.438  40.260  1.00 58.85           C  
ANISOU  108  CA  VAL A  41     6364   7739   8257    822    319   1206       C  
ATOM    109  C   VAL A  41     -12.247   5.070  40.810  1.00 57.42           C  
ANISOU  109  C   VAL A  41     6347   7404   8066    743    303    972       C  
ATOM    110  O   VAL A  41     -11.914   5.394  41.961  1.00 52.71           O  
ANISOU  110  O   VAL A  41     5845   6740   7443    853    395    901       O  
ATOM    111  CB  VAL A  41     -14.599   4.254  40.337  1.00 52.94           C  
ANISOU  111  CB  VAL A  41     5409   7174   7533    719    234   1384       C  
ATOM    112  CG1 VAL A  41     -14.471   3.540  41.674  1.00 56.12           C  
ANISOU  112  CG1 VAL A  41     5809   7585   7930    734    266   1347       C  
ATOM    113  CG2 VAL A  41     -16.025   4.738  40.134  1.00 52.46           C  
ANISOU  113  CG2 VAL A  41     5158   7301   7474    841    283   1658       C  
ATOM    114  N   ILE A  42     -11.404   4.451  39.975  1.00 49.39           N  
ANISOU  114  N   ILE A  42     5377   6330   7058    564    189    855       N  
ATOM    115  CA  ILE A  42     -10.027   4.188  40.396  1.00 48.21           C  
ANISOU  115  CA  ILE A  42     5370   6053   6893    502    180    651       C  
ATOM    116  C   ILE A  42      -9.338   5.490  40.781  1.00 54.41           C  
ANISOU  116  C   ILE A  42     6312   6712   7649    612    276    556       C  
ATOM    117  O   ILE A  42      -8.753   5.611  41.866  1.00 55.16           O  
ANISOU  117  O   ILE A  42     6505   6734   7720    655    327    465       O  
ATOM    118  CB  ILE A  42      -9.232   3.470  39.293  1.00 53.60           C  
ANISOU  118  CB  ILE A  42     6088   6704   7574    334     64    561       C  
ATOM    119  CG1 ILE A  42      -9.683   2.023  39.119  1.00 57.43           C  
ANISOU  119  CG1 ILE A  42     6491   7265   8063    205    -47    616       C  
ATOM    120  CG2 ILE A  42      -7.740   3.515  39.611  1.00 44.28           C  
ANISOU  120  CG2 ILE A  42     5043   5411   6371    304     77    377       C  
ATOM    121  CD1 ILE A  42      -8.827   1.268  38.113  1.00 52.98           C  
ANISOU  121  CD1 ILE A  42     6011   6648   7470     71   -150    514       C  
ATOM    122  N   VAL A  43      -9.409   6.489  39.897  1.00 48.68           N  
ANISOU  122  N   VAL A  43     5626   5953   6917    649    291    584       N  
ATOM    123  CA  VAL A  43      -8.652   7.721  40.118  1.00 57.79           C  
ANISOU  123  CA  VAL A  43     6961   6964   8031    714    353    492       C  
ATOM    124  C   VAL A  43      -9.082   8.385  41.421  1.00 58.30           C  
ANISOU  124  C   VAL A  43     7114   6983   8055    894    469    517       C  
ATOM    125  O   VAL A  43      -8.248   8.726  42.275  1.00 54.56           O  
ANISOU  125  O   VAL A  43     6800   6390   7539    900    495    401       O  
ATOM    126  CB  VAL A  43      -8.816   8.681  38.926  1.00 47.31           C  
ANISOU  126  CB  VAL A  43     5660   5615   6702    731    349    541       C  
ATOM    127  CG1 VAL A  43      -8.061   9.978  39.185  1.00 47.39           C  
ANISOU  127  CG1 VAL A  43     5881   5464   6662    783    399    458       C  
ATOM    128  CG2 VAL A  43      -8.336   8.034  37.649  1.00 49.32           C  
ANISOU  128  CG2 VAL A  43     5850   5908   6980    563    240    510       C  
ATOM    129  N   VAL A  44     -10.394   8.559  41.603  1.00 49.18           N  
ANISOU  129  N   VAL A  44     5858   5929   6900   1048    539    682       N  
ATOM    130  CA  VAL A  44     -10.872   9.313  42.757  1.00 52.70           C  
ANISOU  130  CA  VAL A  44     6409   6329   7284   1266    671    721       C  
ATOM    131  C   VAL A  44     -10.617   8.545  44.049  1.00 62.65           C  
ANISOU  131  C   VAL A  44     7678   7593   8532   1258    687    660       C  
ATOM    132  O   VAL A  44     -10.149   9.123  45.042  1.00 56.63           O  
ANISOU  132  O   VAL A  44     7111   6702   7703   1344    751    572       O  
ATOM    133  CB  VAL A  44     -12.359   9.687  42.586  1.00 63.56           C  
ANISOU  133  CB  VAL A  44     7650   7844   8656   1458    756    943       C  
ATOM    134  CG1 VAL A  44     -12.552  10.518  41.323  1.00 55.83           C  
ANISOU  134  CG1 VAL A  44     6680   6849   7684   1470    741    999       C  
ATOM    135  CG2 VAL A  44     -13.246   8.452  42.549  1.00 81.19           C  
ANISOU  135  CG2 VAL A  44     9610  10293  10946   1393    707   1092       C  
ATOM    136  N   THR A  45     -10.880   7.231  44.059  1.00 57.42           N  
ANISOU  136  N   THR A  45     6826   7066   7925   1144    618    703       N  
ATOM    137  CA  THR A  45     -10.677   6.477  45.287  1.00 53.09           C  
ANISOU  137  CA  THR A  45     6278   6527   7366   1139    633    654       C  
ATOM    138  C   THR A  45      -9.206   6.453  45.669  1.00 55.54           C  
ANISOU  138  C   THR A  45     6762   6686   7656   1024    589    449       C  
ATOM    139  O   THR A  45      -8.860   6.648  46.841  1.00 48.36           O  
ANISOU  139  O   THR A  45     5978   5701   6695   1091    645    382       O  
ATOM    140  CB  THR A  45     -11.209   5.055  45.133  1.00 60.67           C  
ANISOU  140  CB  THR A  45     7020   7646   8383   1015    548    743       C  
ATOM    141  OG1 THR A  45     -12.538   5.095  44.598  1.00 58.81           O  
ANISOU  141  OG1 THR A  45     6604   7572   8168   1081    562    960       O  
ATOM    142  CG2 THR A  45     -11.229   4.348  46.485  1.00 62.78           C  
ANISOU  142  CG2 THR A  45     7274   7942   8636   1043    582    730       C  
ATOM    143  N   SER A  46      -8.320   6.281  44.683  1.00 46.70           N  
ANISOU  143  N   SER A  46     5654   5526   6565    859    492    360       N  
ATOM    144  CA  SER A  46      -6.897   6.229  44.988  1.00 52.03           C  
ANISOU  144  CA  SER A  46     6457   6092   7219    745    448    198       C  
ATOM    145  C   SER A  46      -6.402   7.563  45.524  1.00 50.17           C  
ANISOU  145  C   SER A  46     6448   5703   6911    820    504    136       C  
ATOM    146  O   SER A  46      -5.737   7.605  46.567  1.00 50.62           O  
ANISOU  146  O   SER A  46     6628   5684   6923    808    513     51       O  
ATOM    147  CB  SER A  46      -6.109   5.819  43.746  1.00 52.27           C  
ANISOU  147  CB  SER A  46     6443   6135   7282    582    348    144       C  
ATOM    148  OG  SER A  46      -4.717   5.813  44.010  1.00 50.76           O  
ANISOU  148  OG  SER A  46     6351   5870   7066    482    311     18       O  
ATOM    149  N   VAL A  47      -6.758   8.668  44.862  1.00 54.58           N  
ANISOU  149  N   VAL A  47     7082   6209   7449    896    537    185       N  
ATOM    150  CA  VAL A  47      -6.264   9.966  45.311  1.00 47.81           C  
ANISOU  150  CA  VAL A  47     6483   5177   6506    951    574    126       C  
ATOM    151  C   VAL A  47      -6.784  10.280  46.709  1.00 53.80           C  
ANISOU  151  C   VAL A  47     7374   5879   7189   1129    674    139       C  
ATOM    152  O   VAL A  47      -6.009  10.629  47.609  1.00 49.09           O  
ANISOU  152  O   VAL A  47     6977   5153   6521   1098    666     42       O  
ATOM    153  CB  VAL A  47      -6.637  11.070  44.306  1.00 56.50           C  
ANISOU  153  CB  VAL A  47     7649   6226   7593   1014    592    187       C  
ATOM    154  CG1 VAL A  47      -6.247  12.436  44.852  1.00 49.81           C  
ANISOU  154  CG1 VAL A  47     7113   5175   6639   1083    627    136       C  
ATOM    155  CG2 VAL A  47      -5.947  10.819  42.970  1.00 50.95           C  
ANISOU  155  CG2 VAL A  47     6846   5565   6948    830    491    160       C  
ATOM    156  N   VAL A  48      -8.091  10.106  46.932  1.00 59.36           N  
ANISOU  156  N   VAL A  48     7962   6693   7901   1312    767    270       N  
ATOM    157  CA  VAL A  48      -8.663  10.479  48.223  1.00 50.92           C  
ANISOU  157  CA  VAL A  48     7024   5581   6744   1522    885    302       C  
ATOM    158  C   VAL A  48      -8.098   9.607  49.336  1.00 56.73           C  
ANISOU  158  C   VAL A  48     7759   6323   7473   1442    859    216       C  
ATOM    159  O   VAL A  48      -7.635  10.115  50.366  1.00 64.49           O  
ANISOU  159  O   VAL A  48     8980   7164   8360   1490    890    135       O  
ATOM    160  CB  VAL A  48     -10.199  10.404  48.176  1.00 55.54           C  
ANISOU  160  CB  VAL A  48     7435   6328   7339   1740    994    497       C  
ATOM    161  CG1 VAL A  48     -10.775  10.541  49.577  1.00 55.69           C  
ANISOU  161  CG1 VAL A  48     7551   6342   7265   1963   1124    541       C  
ATOM    162  CG2 VAL A  48     -10.755  11.489  47.263  1.00 53.14           C  
ANISOU  162  CG2 VAL A  48     7185   5994   7014   1865   1041    586       C  
ATOM    163  N   GLY A  49      -8.096   8.285  49.142  1.00 48.99           N  
ANISOU  163  N   GLY A  49     6535   5493   6586   1311    794    231       N  
ATOM    164  CA  GLY A  49      -7.669   7.409  50.216  1.00 48.41           C  
ANISOU  164  CA  GLY A  49     6449   5437   6508   1253    777    167       C  
ATOM    165  C   GLY A  49      -6.189   7.529  50.517  1.00 54.25           C  
ANISOU  165  C   GLY A  49     7353   6042   7216   1087    695      5       C  
ATOM    166  O   GLY A  49      -5.784   7.517  51.683  1.00 53.02           O  
ANISOU  166  O   GLY A  49     7329   5819   6998   1102    712    -59       O  
ATOM    167  N   ASN A  50      -5.359   7.693  49.482  1.00 46.95           N  
ANISOU  167  N   ASN A  50     6425   5086   6327    929    604    -48       N  
ATOM    168  CA  ASN A  50      -3.931   7.804  49.744  1.00 47.15           C  
ANISOU  168  CA  ASN A  50     6575   5017   6321    763    522   -168       C  
ATOM    169  C   ASN A  50      -3.569   9.160  50.338  1.00 47.72           C  
ANISOU  169  C   ASN A  50     6953   4901   6279    805    541   -213       C  
ATOM    170  O   ASN A  50      -2.669   9.236  51.186  1.00 57.23           O  
ANISOU  170  O   ASN A  50     8299   6024   7423    712    495   -291       O  
ATOM    171  CB  ASN A  50      -3.140   7.516  48.469  1.00 45.48           C  
ANISOU  171  CB  ASN A  50     6253   4855   6173    591    427   -190       C  
ATOM    172  CG  ASN A  50      -3.046   6.027  48.177  1.00 57.89           C  
ANISOU  172  CG  ASN A  50     7603   6569   7822    511    381   -188       C  
ATOM    173  OD1 ASN A  50      -2.398   5.281  48.914  1.00 45.99           O  
ANISOU  173  OD1 ASN A  50     6080   5082   6311    446    352   -243       O  
ATOM    174  ND2 ASN A  50      -3.704   5.585  47.110  1.00 43.98           N  
ANISOU  174  ND2 ASN A  50     5689   4899   6122    516    369   -122       N  
ATOM    175  N   VAL A  51      -4.268  10.233  49.950  1.00 48.85           N  
ANISOU  175  N   VAL A  51     7218   4966   6378    944    604   -159       N  
ATOM    176  CA  VAL A  51      -4.025  11.516  50.600  1.00 56.84           C  
ANISOU  176  CA  VAL A  51     8572   5768   7255   1005    624   -201       C  
ATOM    177  C   VAL A  51      -4.446  11.459  52.062  1.00 53.51           C  
ANISOU  177  C   VAL A  51     8289   5298   6744   1158    707   -212       C  
ATOM    178  O   VAL A  51      -3.747  11.976  52.941  1.00 61.78           O  
ANISOU  178  O   VAL A  51     9603   6187   7681   1107    672   -291       O  
ATOM    179  CB  VAL A  51      -4.747  12.651  49.847  1.00 58.26           C  
ANISOU  179  CB  VAL A  51     8866   5871   7400   1149    683   -133       C  
ATOM    180  CG1 VAL A  51      -4.815  13.904  50.709  1.00 54.11           C  
ANISOU  180  CG1 VAL A  51     8734   5116   6709   1286    735   -162       C  
ATOM    181  CG2 VAL A  51      -4.041  12.952  48.537  1.00 50.88           C  
ANISOU  181  CG2 VAL A  51     7879   4933   6521    966    583   -144       C  
ATOM    182  N   VAL A  52      -5.576  10.805  52.354  1.00 57.69           N  
ANISOU  182  N   VAL A  52     8639   5969   7311   1335    811   -124       N  
ATOM    183  CA  VAL A  52      -6.004  10.698  53.745  1.00 56.09           C  
ANISOU  183  CA  VAL A  52     8549   5742   7019   1495    901   -122       C  
ATOM    184  C   VAL A  52      -5.036   9.835  54.542  1.00 57.18           C  
ANISOU  184  C   VAL A  52     8662   5893   7169   1314    816   -217       C  
ATOM    185  O   VAL A  52      -4.783  10.106  55.719  1.00 54.53           O  
ANISOU  185  O   VAL A  52     8550   5446   6722   1358    837   -272       O  
ATOM    186  CB  VAL A  52      -7.448  10.163  53.824  1.00 59.52           C  
ANISOU  186  CB  VAL A  52     8758   6361   7495   1716   1029     28       C  
ATOM    187  CG1 VAL A  52      -7.822   9.831  55.262  1.00 55.89           C  
ANISOU  187  CG1 VAL A  52     8363   5916   6956   1861   1118     39       C  
ATOM    188  CG2 VAL A  52      -8.415  11.185  53.261  1.00 54.05           C  
ANISOU  188  CG2 VAL A  52     8136   5644   6756   1940   1133    137       C  
ATOM    189  N   VAL A  53      -4.446   8.816  53.914  1.00 49.48           N  
ANISOU  189  N   VAL A  53     7437   5045   6316   1113    719   -238       N  
ATOM    190  CA  VAL A  53      -3.451   8.005  54.610  1.00 48.59           C  
ANISOU  190  CA  VAL A  53     7298   4952   6214    946    638   -319       C  
ATOM    191  C   VAL A  53      -2.210   8.834  54.927  1.00 58.83           C  
ANISOU  191  C   VAL A  53     8857   6079   7419    794    545   -412       C  
ATOM    192  O   VAL A  53      -1.656   8.762  56.037  1.00 60.79           O  
ANISOU  192  O   VAL A  53     9244   6262   7591    746    518   -469       O  
ATOM    193  CB  VAL A  53      -3.106   6.762  53.769  1.00 48.79           C  
ANISOU  193  CB  VAL A  53     7022   5142   6375    794    562   -311       C  
ATOM    194  CG1 VAL A  53      -1.746   6.203  54.155  1.00 46.13           C  
ANISOU  194  CG1 VAL A  53     6685   4804   6039    597    459   -396       C  
ATOM    195  CG2 VAL A  53      -4.182   5.703  53.923  1.00 48.97           C  
ANISOU  195  CG2 VAL A  53     6820   5321   6464    896    623   -227       C  
ATOM    196  N   MET A  54      -1.762   9.646  53.964  1.00 57.59           N  
ANISOU  196  N   MET A  54     8773   5850   7259    703    487   -416       N  
ATOM    197  CA  MET A  54      -0.605  10.497  54.215  1.00 61.16           C  
ANISOU  197  CA  MET A  54     9476   6145   7616    531    381   -477       C  
ATOM    198  C   MET A  54      -0.899  11.516  55.308  1.00 55.55           C  
ANISOU  198  C   MET A  54     9140   5226   6739    656    426   -506       C  
ATOM    199  O   MET A  54      -0.025  11.828  56.125  1.00 54.96           O  
ANISOU  199  O   MET A  54     9282   5036   6565    520    340   -563       O  
ATOM    200  CB  MET A  54      -0.173  11.196  52.924  1.00 67.11           C  
ANISOU  200  CB  MET A  54    10230   6870   8397    418    314   -456       C  
ATOM    201  CG  MET A  54       0.381  10.246  51.870  1.00 69.24           C  
ANISOU  201  CG  MET A  54    10180   7327   8801    274    254   -437       C  
ATOM    202  SD  MET A  54       0.974  11.073  50.381  1.00 70.06           S  
ANISOU  202  SD  MET A  54    10283   7409   8925    136    176   -404       S  
ATOM    203  CE  MET A  54      -0.560  11.672  49.682  1.00 62.05           C  
ANISOU  203  CE  MET A  54     9287   6360   7928    377    296   -347       C  
ATOM    204  N   TRP A  55      -2.136  12.018  55.363  1.00 56.43           N  
ANISOU  204  N   TRP A  55     9341   5293   6807    921    562   -458       N  
ATOM    205  CA  TRP A  55      -2.502  12.939  56.436  1.00 60.54           C  
ANISOU  205  CA  TRP A  55    10244   5612   7148   1091    629   -482       C  
ATOM    206  C   TRP A  55      -2.537  12.231  57.784  1.00 60.53           C  
ANISOU  206  C   TRP A  55    10256   5643   7099   1141    665   -513       C  
ATOM    207  O   TRP A  55      -2.081  12.780  58.793  1.00 66.38           O  
ANISOU  207  O   TRP A  55    11329   6206   7687   1118    630   -576       O  
ATOM    208  CB  TRP A  55      -3.856  13.584  56.144  1.00 57.15           C  
ANISOU  208  CB  TRP A  55     9877   5159   6679   1403    788   -398       C  
ATOM    209  CG  TRP A  55      -4.407  14.360  57.309  1.00 72.15           C  
ANISOU  209  CG  TRP A  55    12151   6879   8384   1650    896   -408       C  
ATOM    210  CD1 TRP A  55      -4.133  15.657  57.628  1.00 77.68           C  
ANISOU  210  CD1 TRP A  55    13313   7301   8900   1684    872   -458       C  
ATOM    211  CD2 TRP A  55      -5.319  13.886  58.312  1.00 75.26           C  
ANISOU  211  CD2 TRP A  55    12511   7353   8731   1903   1044   -361       C  
ATOM    212  NE1 TRP A  55      -4.817  16.022  58.764  1.00 67.13           N  
ANISOU  212  NE1 TRP A  55    12254   5856   7397   1961   1004   -453       N  
ATOM    213  CE2 TRP A  55      -5.552  14.953  59.204  1.00 69.47           C  
ANISOU  213  CE2 TRP A  55    12237   6381   7776   2105   1118   -390       C  
ATOM    214  CE3 TRP A  55      -5.958  12.664  58.542  1.00 78.05           C  
ANISOU  214  CE3 TRP A  55    12503   7955   9199   1975   1118   -290       C  
ATOM    215  CZ2 TRP A  55      -6.400  14.836  60.308  1.00 73.27           C  
ANISOU  215  CZ2 TRP A  55    12813   6880   8147   2397   1278   -347       C  
ATOM    216  CZ3 TRP A  55      -6.800  12.549  59.640  1.00 65.33           C  
ANISOU  216  CZ3 TRP A  55    10964   6370   7488   2242   1267   -238       C  
ATOM    217  CH2 TRP A  55      -7.012  13.629  60.509  1.00 64.13           C  
ANISOU  217  CH2 TRP A  55    11260   5992   7115   2461   1353   -266       C  
ATOM    218  N   ILE A  56      -3.064  11.006  57.816  1.00 55.37           N  
ANISOU  218  N   ILE A  56     9260   5208   6568   1197    724   -466       N  
ATOM    219  CA  ILE A  56      -3.154  10.267  59.071  1.00 55.85           C  
ANISOU  219  CA  ILE A  56     9310   5317   6593   1249    763   -484       C  
ATOM    220  C   ILE A  56      -1.765  10.019  59.633  1.00 56.55           C  
ANISOU  220  C   ILE A  56     9482   5350   6654    982    613   -576       C  
ATOM    221  O   ILE A  56      -1.526  10.181  60.836  1.00 65.16           O  
ANISOU  221  O   ILE A  56    10804   6335   7618    999    610   -624       O  
ATOM    222  CB  ILE A  56      -3.913   8.944  58.854  1.00 65.21           C  
ANISOU  222  CB  ILE A  56    10096   6753   7927   1313    827   -404       C  
ATOM    223  CG1 ILE A  56      -5.403   9.197  58.620  1.00 64.06           C  
ANISOU  223  CG1 ILE A  56     9880   6681   7778   1601    986   -279       C  
ATOM    224  CG2 ILE A  56      -3.701   7.999  60.031  1.00 53.12           C  
ANISOU  224  CG2 ILE A  56     8510   5287   6386   1286    825   -432       C  
ATOM    225  CD1 ILE A  56      -6.128   7.999  58.032  1.00 51.93           C  
ANISOU  225  CD1 ILE A  56     7937   5395   6401   1603   1008   -175       C  
ATOM    226  N   ILE A  57      -0.817   9.667  58.768  1.00 56.19           N  
ANISOU  226  N   ILE A  57     9258   5378   6712    739    487   -591       N  
ATOM    227  CA  ILE A  57       0.514   9.335  59.264  1.00 52.90           C  
ANISOU  227  CA  ILE A  57     8865   4957   6279    488    348   -646       C  
ATOM    228  C   ILE A  57       1.307  10.595  59.595  1.00 61.27           C  
ANISOU  228  C   ILE A  57    10305   5792   7182    354    243   -688       C  
ATOM    229  O   ILE A  57       1.880  10.714  60.684  1.00 54.24           O  
ANISOU  229  O   ILE A  57     9623   4809   6178    269    180   -731       O  
ATOM    230  CB  ILE A  57       1.259   8.451  58.250  1.00 53.60           C  
ANISOU  230  CB  ILE A  57     8619   5226   6521    302    264   -626       C  
ATOM    231  CG1 ILE A  57       0.552   7.098  58.106  1.00 56.44           C  
ANISOU  231  CG1 ILE A  57     8655   5780   7009    406    342   -592       C  
ATOM    232  CG2 ILE A  57       2.711   8.278  58.668  1.00 49.84           C  
ANISOU  232  CG2 ILE A  57     8168   4755   6013     46    119   -654       C  
ATOM    233  CD1 ILE A  57       1.221   6.143  57.139  1.00 50.73           C  
ANISOU  233  CD1 ILE A  57     7640   5219   6415    259    272   -577       C  
ATOM    234  N   LEU A  58       1.339  11.562  58.673  1.00 66.44           N  
ANISOU  234  N   LEU A  58    11073   6351   7820    324    213   -670       N  
ATOM    235  CA  LEU A  58       2.237  12.703  58.821  1.00 62.40           C  
ANISOU  235  CA  LEU A  58    10904   5635   7169    134     76   -695       C  
ATOM    236  C   LEU A  58       1.757  13.713  59.856  1.00 70.06           C  
ANISOU  236  C   LEU A  58    12343   6346   7932    284    119   -737       C  
ATOM    237  O   LEU A  58       2.584  14.337  60.530  1.00 81.04           O  
ANISOU  237  O   LEU A  58    14049   7566   9176    103    -13   -772       O  
ATOM    238  CB  LEU A  58       2.430  13.397  57.469  1.00 57.24           C  
ANISOU  238  CB  LEU A  58    10223   4963   6564     47     26   -655       C  
ATOM    239  CG  LEU A  58       3.142  12.592  56.376  1.00 61.00           C  
ANISOU  239  CG  LEU A  58    10303   5665   7208   -132    -40   -611       C  
ATOM    240  CD1 LEU A  58       3.172  13.369  55.072  1.00 66.13           C  
ANISOU  240  CD1 LEU A  58    10955   6284   7889   -179    -69   -569       C  
ATOM    241  CD2 LEU A  58       4.553  12.219  56.809  1.00 56.66           C  
ANISOU  241  CD2 LEU A  58     9704   5180   6643   -417   -196   -606       C  
ATOM    242  N   ALA A  59       0.446  13.895  60.002  1.00 69.69           N  
ANISOU  242  N   ALA A  59    12358   6267   7854    612    298   -723       N  
ATOM    243  CA  ALA A  59      -0.079  14.934  60.881  1.00 60.60           C  
ANISOU  243  CA  ALA A  59    11682   4858   6485    807    363   -755       C  
ATOM    244  C   ALA A  59      -0.185  14.501  62.338  1.00 74.54           C  
ANISOU  244  C   ALA A  59    13581   6598   8145    895    407   -797       C  
ATOM    245  O   ALA A  59      -0.529  15.332  63.186  1.00 76.20           O  
ANISOU  245  O   ALA A  59    14226   6580   8146   1056    455   -830       O  
ATOM    246  CB  ALA A  59      -1.450  15.405  60.388  1.00 61.24           C  
ANISOU  246  CB  ALA A  59    11782   4927   6560   1154    551   -697       C  
ATOM    247  N   HIS A  60       0.092  13.239  62.656  1.00 68.36           N  
ANISOU  247  N   HIS A  60    12457   6029   7486    806    394   -794       N  
ATOM    248  CA  HIS A  60      -0.053  12.725  64.013  1.00 62.14           C  
ANISOU  248  CA  HIS A  60    11754   5243   6614    894    442   -825       C  
ATOM    249  C   HIS A  60       1.274  12.132  64.465  1.00 72.86           C  
ANISOU  249  C   HIS A  60    13037   6652   7994    565    263   -862       C  
ATOM    250  O   HIS A  60       1.764  11.169  63.866  1.00 73.78           O  
ANISOU  250  O   HIS A  60    12757   6984   8291    409    209   -834       O  
ATOM    251  CB  HIS A  60      -1.177  11.690  64.082  1.00 68.26           C  
ANISOU  251  CB  HIS A  60    12181   6246   7511   1145    621   -764       C  
ATOM    252  CG  HIS A  60      -2.498  12.210  63.604  1.00 83.75           C  
ANISOU  252  CG  HIS A  60    14159   8204   9458   1468    798   -692       C  
ATOM    253  ND1 HIS A  60      -2.814  12.327  62.267  1.00 84.47           N  
ANISOU  253  ND1 HIS A  60    14035   8380   9679   1469    810   -635       N  
ATOM    254  CD2 HIS A  60      -3.577  12.664  64.285  1.00 82.11           C  
ANISOU  254  CD2 HIS A  60    14160   7928   9112   1809    974   -654       C  
ATOM    255  CE1 HIS A  60      -4.032  12.821  62.145  1.00 80.34           C  
ANISOU  255  CE1 HIS A  60    13572   7847   9105   1788    980   -560       C  
ATOM    256  NE2 HIS A  60      -4.518  13.035  63.355  1.00 87.00           N  
ANISOU  256  NE2 HIS A  60    14667   8604   9785   2009   1088   -565       N  
ATOM    257  N   LYS A  61       1.836  12.697  65.539  1.00 81.80           N  
ANISOU  257  N   LYS A  61    14562   7587   8933    472    172   -917       N  
ATOM    258  CA  LYS A  61       3.187  12.337  65.960  1.00 86.90           C  
ANISOU  258  CA  LYS A  61    15180   8265   9574    131    -24   -932       C  
ATOM    259  C   LYS A  61       3.293  10.871  66.356  1.00 84.18           C  
ANISOU  259  C   LYS A  61    14442   8173   9371    119      9   -918       C  
ATOM    260  O   LYS A  61       4.356  10.261  66.188  1.00 79.51           O  
ANISOU  260  O   LYS A  61    13626   7716   8867   -143   -126   -896       O  
ATOM    261  CB  LYS A  61       3.623  13.231  67.124  1.00101.34           C  
ANISOU  261  CB  LYS A  61    17541   9820  11145     49   -126   -986       C  
ATOM    262  CG  LYS A  61       3.799  14.695  66.751  1.00109.35           C  
ANISOU  262  CG  LYS A  61    18993  10556  11999    -21   -215   -999       C  
ATOM    263  CD  LYS A  61       4.037  15.563  67.977  1.00120.38           C  
ANISOU  263  CD  LYS A  61    20980  11650  13110    -56   -300  -1059       C  
ATOM    264  CE  LYS A  61       4.658  16.898  67.592  1.00123.87           C  
ANISOU  264  CE  LYS A  61    21844  11825  13398   -275   -479  -1058       C  
ATOM    265  NZ  LYS A  61       4.022  17.487  66.379  1.00132.24           N  
ANISOU  265  NZ  LYS A  61    22858  12857  14530   -123   -386  -1031       N  
ATOM    266  N   ARG A  62       2.213  10.288  66.881  1.00 83.60           N  
ANISOU  266  N   ARG A  62    14278   8171   9314    403    187   -917       N  
ATOM    267  CA  ARG A  62       2.249   8.875  67.242  1.00 78.21           C  
ANISOU  267  CA  ARG A  62    13234   7719   8765    394    216   -899       C  
ATOM    268  C   ARG A  62       2.425   7.986  66.018  1.00 78.91           C  
ANISOU  268  C   ARG A  62    12865   8036   9081    306    202   -849       C  
ATOM    269  O   ARG A  62       2.971   6.882  66.128  1.00 78.66           O  
ANISOU  269  O   ARG A  62    12558   8175   9155    188    155   -837       O  
ATOM    270  CB  ARG A  62       0.974   8.486  67.992  1.00 94.53           C  
ANISOU  270  CB  ARG A  62    15295   9824  10799    717    411   -884       C  
ATOM    271  CG  ARG A  62       0.849   9.089  69.383  1.00121.11           C  
ANISOU  271  CG  ARG A  62    19090  12995  13932    822    437   -934       C  
ATOM    272  CD  ARG A  62      -0.431   8.625  70.061  1.00127.48           C  
ANISOU  272  CD  ARG A  62    19835  13885  14716   1157    645   -893       C  
ATOM    273  NE  ARG A  62      -0.536   9.103  71.436  1.00125.40           N  
ANISOU  273  NE  ARG A  62    19978  13448  14221   1276    682   -939       N  
ATOM    274  CZ  ARG A  62      -1.557   8.832  72.243  1.00134.87           C  
ANISOU  274  CZ  ARG A  62    21198  14698  15350   1576    862   -900       C  
ATOM    275  NH1 ARG A  62      -2.564   8.084  71.814  1.00133.28           N  
ANISOU  275  NH1 ARG A  62    20618  14724  15299   1765   1010   -802       N  
ATOM    276  NH2 ARG A  62      -1.570   9.308  73.481  1.00142.80           N  
ANISOU  276  NH2 ARG A  62    22605  15528  16123   1681    889   -948       N  
ATOM    277  N   MET A  63       1.970   8.444  64.850  1.00 71.74           N  
ANISOU  277  N   MET A  63    11889   7128   8241    371    244   -819       N  
ATOM    278  CA  MET A  63       2.003   7.630  63.642  1.00 71.57           C  
ANISOU  278  CA  MET A  63    11466   7309   8419    318    244   -774       C  
ATOM    279  C   MET A  63       3.347   7.655  62.927  1.00 61.80           C  
ANISOU  279  C   MET A  63    10134   6115   7232     27     79   -766       C  
ATOM    280  O   MET A  63       3.529   6.887  61.979  1.00 55.93           O  
ANISOU  280  O   MET A  63     9069   5543   6639    -23     72   -731       O  
ATOM    281  CB  MET A  63       0.906   8.078  62.670  1.00 63.20           C  
ANISOU  281  CB  MET A  63    10358   6247   7408    514    359   -732       C  
ATOM    282  CG  MET A  63      -0.507   7.858  63.183  1.00 60.32           C  
ANISOU  282  CG  MET A  63     9976   5917   7025    816    537   -693       C  
ATOM    283  SD  MET A  63      -0.862   6.128  63.560  1.00 68.81           S  
ANISOU  283  SD  MET A  63    10668   7237   8238    845    584   -653       S  
ATOM    284  CE  MET A  63      -0.822   5.397  61.924  1.00 55.21           C  
ANISOU  284  CE  MET A  63     8569   5691   6719    743    543   -605       C  
ATOM    285  N   ARG A  64       4.289   8.501  63.342  1.00 57.54           N  
ANISOU  285  N   ARG A  64     9867   5432   6562   -167    -56   -785       N  
ATOM    286  CA  ARG A  64       5.550   8.652  62.613  1.00 65.16           C  
ANISOU  286  CA  ARG A  64    10737   6456   7566   -446   -213   -744       C  
ATOM    287  C   ARG A  64       6.513   7.559  63.058  1.00 63.72           C  
ANISOU  287  C   ARG A  64    10320   6452   7439   -602   -291   -719       C  
ATOM    288  O   ARG A  64       7.319   7.737  63.973  1.00 70.48           O  
ANISOU  288  O   ARG A  64    11334   7257   8188   -768   -405   -718       O  
ATOM    289  CB  ARG A  64       6.136  10.041  62.824  1.00 68.13           C  
ANISOU  289  CB  ARG A  64    11502   6610   7773   -613   -343   -749       C  
ATOM    290  CG  ARG A  64       5.213  11.161  62.391  1.00 67.15           C  
ANISOU  290  CG  ARG A  64    11643   6292   7578   -443   -265   -772       C  
ATOM    291  CD  ARG A  64       5.980  12.451  62.179  1.00 83.60           C  
ANISOU  291  CD  ARG A  64    14049   8185   9530   -666   -425   -755       C  
ATOM    292  NE  ARG A  64       5.085  13.598  62.067  1.00 97.83           N  
ANISOU  292  NE  ARG A  64    16204   9749  11216   -479   -349   -789       N  
ATOM    293  CZ  ARG A  64       4.939  14.521  63.011  1.00104.06           C  
ANISOU  293  CZ  ARG A  64    17477  10271  11790   -442   -376   -837       C  
ATOM    294  NH1 ARG A  64       5.643  14.437  64.132  1.00110.19           N  
ANISOU  294  NH1 ARG A  64    18434  10985  12447   -605   -491   -859       N  
ATOM    295  NH2 ARG A  64       4.101  15.532  62.831  1.00103.45           N  
ANISOU  295  NH2 ARG A  64    17717   9983  11605   -237   -291   -859       N  
ATOM    296  N   THR A  65       6.430   6.413  62.393  1.00 53.29           N  
ANISOU  296  N   THR A  65     8632   5337   6278   -547   -233   -693       N  
ATOM    297  CA  THR A  65       7.310   5.279  62.624  1.00 49.61           C  
ANISOU  297  CA  THR A  65     7915   5057   5877   -658   -288   -659       C  
ATOM    298  C   THR A  65       7.998   4.900  61.317  1.00 60.63           C  
ANISOU  298  C   THR A  65     9035   6618   7385   -751   -326   -594       C  
ATOM    299  O   THR A  65       7.657   5.398  60.240  1.00 52.06           O  
ANISOU  299  O   THR A  65     7930   5509   6341   -716   -299   -583       O  
ATOM    300  CB  THR A  65       6.536   4.078  63.186  1.00 50.80           C  
ANISOU  300  CB  THR A  65     7912   5295   6096   -475   -173   -688       C  
ATOM    301  OG1 THR A  65       5.612   3.597  62.200  1.00 50.86           O  
ANISOU  301  OG1 THR A  65     7727   5375   6225   -314    -66   -682       O  
ATOM    302  CG2 THR A  65       5.764   4.475  64.439  1.00 50.19           C  
ANISOU  302  CG2 THR A  65     8101   5067   5900   -349   -113   -741       C  
ATOM    303  N   VAL A  66       8.984   4.006  61.430  1.00 49.27           N  
ANISOU  303  N   VAL A  66     7384   5350   5985   -858   -385   -542       N  
ATOM    304  CA  VAL A  66       9.682   3.490  60.252  1.00 58.98           C  
ANISOU  304  CA  VAL A  66     8342   6760   7307   -911   -403   -470       C  
ATOM    305  C   VAL A  66       8.686   2.889  59.265  1.00 55.90           C  
ANISOU  305  C   VAL A  66     7800   6408   7031   -715   -280   -502       C  
ATOM    306  O   VAL A  66       8.645   3.250  58.073  1.00 64.86           O  
ANISOU  306  O   VAL A  66     8874   7561   8208   -715   -272   -477       O  
ATOM    307  CB  VAL A  66      10.730   2.450  60.692  1.00 52.31           C  
ANISOU  307  CB  VAL A  66     7299   6099   6479   -989   -451   -408       C  
ATOM    308  CG1 VAL A  66      11.201   1.614  59.512  1.00 59.41           C  
ANISOU  308  CG1 VAL A  66     7911   7189   7473   -948   -420   -346       C  
ATOM    309  CG2 VAL A  66      11.896   3.126  61.414  1.00 50.31           C  
ANISOU  309  CG2 VAL A  66     7156   5846   6113  -1233   -603   -335       C  
ATOM    310  N   THR A  67       7.834   1.993  59.769  1.00 45.31           N  
ANISOU  310  N   THR A  67     6407   5075   5733   -557   -191   -551       N  
ATOM    311  CA  THR A  67       6.873   1.304  58.921  1.00 64.89           C  
ANISOU  311  CA  THR A  67     8742   7599   8313   -397    -95   -565       C  
ATOM    312  C   THR A  67       5.916   2.289  58.268  1.00 55.65           C  
ANISOU  312  C   THR A  67     7687   6314   7142   -321    -47   -581       C  
ATOM    313  O   THR A  67       5.647   2.201  57.063  1.00 54.52           O  
ANISOU  313  O   THR A  67     7432   6217   7067   -283    -23   -561       O  
ATOM    314  CB  THR A  67       6.104   0.276  59.756  1.00 47.43           C  
ANISOU  314  CB  THR A  67     6484   5407   6129   -271    -27   -596       C  
ATOM    315  OG1 THR A  67       6.956  -0.841  60.043  1.00 58.95           O  
ANISOU  315  OG1 THR A  67     7795   6993   7610   -317    -62   -574       O  
ATOM    316  CG2 THR A  67       4.854  -0.204  59.028  1.00 42.76           C  
ANISOU  316  CG2 THR A  67     5799   4828   5619   -121     59   -598       C  
ATOM    317  N   ASN A  68       5.425   3.259  59.040  1.00 46.13           N  
ANISOU  317  N   ASN A  68     6724   4956   5849   -290    -33   -612       N  
ATOM    318  CA  ASN A  68       4.496   4.233  58.486  1.00 55.47           C  
ANISOU  318  CA  ASN A  68     8033   6025   7017   -190     24   -617       C  
ATOM    319  C   ASN A  68       5.169   5.164  57.487  1.00 53.43           C  
ANISOU  319  C   ASN A  68     7820   5734   6746   -319    -49   -589       C  
ATOM    320  O   ASN A  68       4.505   5.651  56.569  1.00 50.75           O  
ANISOU  320  O   ASN A  68     7482   5361   6439   -242     -4   -578       O  
ATOM    321  CB  ASN A  68       3.839   5.035  59.606  1.00 47.05           C  
ANISOU  321  CB  ASN A  68     7247   4795   5837    -94     69   -653       C  
ATOM    322  CG  ASN A  68       2.791   4.238  60.354  1.00 61.22           C  
ANISOU  322  CG  ASN A  68     8977   6630   7653     89    178   -659       C  
ATOM    323  OD1 ASN A  68       2.202   3.300  59.813  1.00 60.24           O  
ANISOU  323  OD1 ASN A  68     8622   6630   7637    166    230   -629       O  
ATOM    324  ND2 ASN A  68       2.550   4.608  61.604  1.00 55.16           N  
ANISOU  324  ND2 ASN A  68     8427   5759   6774    153    206   -688       N  
ATOM    325  N   TYR A  69       6.470   5.429  57.636  1.00 46.90           N  
ANISOU  325  N   TYR A  69     7021   4929   5869   -522   -167   -561       N  
ATOM    326  CA  TYR A  69       7.149   6.246  56.634  1.00 47.41           C  
ANISOU  326  CA  TYR A  69     7097   4991   5925   -661   -243   -510       C  
ATOM    327  C   TYR A  69       7.231   5.512  55.305  1.00 54.92           C  
ANISOU  327  C   TYR A  69     7772   6105   6991   -626   -210   -472       C  
ATOM    328  O   TYR A  69       6.974   6.100  54.242  1.00 48.24           O  
ANISOU  328  O   TYR A  69     6925   5235   6169   -614   -199   -453       O  
ATOM    329  CB  TYR A  69       8.546   6.640  57.108  1.00 51.88           C  
ANISOU  329  CB  TYR A  69     7728   5576   6409   -906   -387   -456       C  
ATOM    330  CG  TYR A  69       8.576   7.875  57.976  1.00 67.25           C  
ANISOU  330  CG  TYR A  69    10034   7307   8210   -999   -462   -479       C  
ATOM    331  CD1 TYR A  69       7.402   8.467  58.423  1.00 74.18           C  
ANISOU  331  CD1 TYR A  69    11160   7994   9032   -824   -376   -554       C  
ATOM    332  CD2 TYR A  69       9.780   8.457  58.340  1.00 73.69           C  
ANISOU  332  CD2 TYR A  69    10955   8112   8932  -1260   -622   -413       C  
ATOM    333  CE1 TYR A  69       7.431   9.599  59.217  1.00 78.53           C  
ANISOU  333  CE1 TYR A  69    12089   8324   9425   -889   -441   -580       C  
ATOM    334  CE2 TYR A  69       9.819   9.587  59.130  1.00 80.65           C  
ANISOU  334  CE2 TYR A  69    12213   8771   9660  -1363   -709   -436       C  
ATOM    335  CZ  TYR A  69       8.643  10.155  59.565  1.00 77.77           C  
ANISOU  335  CZ  TYR A  69    12125   8194   9231  -1167   -615   -529       C  
ATOM    336  OH  TYR A  69       8.680  11.282  60.352  1.00 88.31           O  
ANISOU  336  OH  TYR A  69    13882   9284  10390  -1248   -698   -557       O  
ATOM    337  N   PHE A  70       7.557   4.215  55.342  1.00 45.81           N  
ANISOU  337  N   PHE A  70     6399   5107   5898   -598   -191   -462       N  
ATOM    338  CA  PHE A  70       7.538   3.463  54.092  1.00 47.34           C  
ANISOU  338  CA  PHE A  70     6374   5431   6180   -537   -152   -435       C  
ATOM    339  C   PHE A  70       6.126   3.390  53.517  1.00 54.95           C  
ANISOU  339  C   PHE A  70     7338   6337   7202   -372    -62   -472       C  
ATOM    340  O   PHE A  70       5.936   3.462  52.293  1.00 59.21           O  
ANISOU  340  O   PHE A  70     7798   6911   7786   -347    -46   -449       O  
ATOM    341  CB  PHE A  70       8.116   2.065  54.301  1.00 47.94           C  
ANISOU  341  CB  PHE A  70     6263   5660   6291   -516   -147   -419       C  
ATOM    342  CG  PHE A  70       9.603   2.048  54.489  1.00 44.32           C  
ANISOU  342  CG  PHE A  70     5732   5321   5788   -668   -230   -342       C  
ATOM    343  CD1 PHE A  70      10.446   2.408  53.450  1.00 44.75           C  
ANISOU  343  CD1 PHE A  70     5691   5475   5838   -753   -269   -258       C  
ATOM    344  CD2 PHE A  70      10.160   1.661  55.697  1.00 46.23           C  
ANISOU  344  CD2 PHE A  70     5985   5593   5988   -726   -270   -335       C  
ATOM    345  CE1 PHE A  70      11.818   2.396  53.615  1.00 45.64           C  
ANISOU  345  CE1 PHE A  70     5706   5730   5904   -893   -346   -152       C  
ATOM    346  CE2 PHE A  70      11.534   1.642  55.870  1.00 49.67           C  
ANISOU  346  CE2 PHE A  70     6330   6163   6379   -872   -352   -235       C  
ATOM    347  CZ  PHE A  70      12.366   2.011  54.826  1.00 53.34           C  
ANISOU  347  CZ  PHE A  70     6684   6742   6839   -956   -390   -136       C  
ATOM    348  N   LEU A  71       5.115   3.292  54.388  1.00 43.58           N  
ANISOU  348  N   LEU A  71     5985   4818   5755   -259     -2   -514       N  
ATOM    349  CA  LEU A  71       3.738   3.264  53.904  1.00 43.21           C  
ANISOU  349  CA  LEU A  71     5920   4741   5758   -107     80   -517       C  
ATOM    350  C   LEU A  71       3.329   4.593  53.271  1.00 47.23           C  
ANISOU  350  C   LEU A  71     6564   5142   6238    -92     90   -504       C  
ATOM    351  O   LEU A  71       2.591   4.604  52.281  1.00 47.71           O  
ANISOU  351  O   LEU A  71     6549   5226   6353    -18    129   -479       O  
ATOM    352  CB  LEU A  71       2.787   2.900  55.046  1.00 43.28           C  
ANISOU  352  CB  LEU A  71     5978   4715   5754     15    147   -537       C  
ATOM    353  CG  LEU A  71       2.934   1.503  55.662  1.00 42.56           C  
ANISOU  353  CG  LEU A  71     5752   4722   5697     22    147   -545       C  
ATOM    354  CD1 LEU A  71       1.913   1.287  56.778  1.00 42.82           C  
ANISOU  354  CD1 LEU A  71     5838   4722   5710    144    217   -549       C  
ATOM    355  CD2 LEU A  71       2.816   0.415  54.607  1.00 41.62           C  
ANISOU  355  CD2 LEU A  71     5440   4713   5661     35    143   -522       C  
ATOM    356  N   VAL A  72       3.805   5.715  53.817  1.00 45.05           N  
ANISOU  356  N   VAL A  72     6502   4744   5870   -170     46   -516       N  
ATOM    357  CA  VAL A  72       3.517   7.016  53.221  1.00 45.90           C  
ANISOU  357  CA  VAL A  72     6772   4732   5938   -164     45   -502       C  
ATOM    358  C   VAL A  72       4.197   7.140  51.867  1.00 47.51           C  
ANISOU  358  C   VAL A  72     6851   5014   6188   -274    -10   -460       C  
ATOM    359  O   VAL A  72       3.624   7.692  50.921  1.00 45.64           O  
ANISOU  359  O   VAL A  72     6621   4745   5974   -218     19   -438       O  
ATOM    360  CB  VAL A  72       3.939   8.157  54.170  1.00 56.85           C  
ANISOU  360  CB  VAL A  72     8463   5944   7192   -240    -10   -525       C  
ATOM    361  CG1 VAL A  72       4.409   9.377  53.382  1.00 48.44           C  
ANISOU  361  CG1 VAL A  72     7538   4786   6081   -357    -81   -495       C  
ATOM    362  CG2 VAL A  72       2.788   8.557  55.052  1.00 54.75           C  
ANISOU  362  CG2 VAL A  72     8392   5550   6862    -46     87   -555       C  
ATOM    363  N   ASN A  73       5.418   6.614  51.744  1.00 45.32           N  
ANISOU  363  N   ASN A  73     6448   4854   5919   -419    -84   -435       N  
ATOM    364  CA  ASN A  73       6.088   6.661  50.448  1.00 45.13           C  
ANISOU  364  CA  ASN A  73     6289   4929   5929   -503   -122   -380       C  
ATOM    365  C   ASN A  73       5.319   5.852  49.409  1.00 59.65           C  
ANISOU  365  C   ASN A  73     7954   6853   7857   -371    -51   -381       C  
ATOM    366  O   ASN A  73       5.127   6.303  48.269  1.00 50.21           O  
ANISOU  366  O   ASN A  73     6733   5660   6683   -366    -46   -352       O  
ATOM    367  CB  ASN A  73       7.520   6.142  50.577  1.00 45.25           C  
ANISOU  367  CB  ASN A  73     6178   5085   5928   -650   -197   -330       C  
ATOM    368  CG  ASN A  73       8.345   6.392  49.332  1.00 55.00           C  
ANISOU  368  CG  ASN A  73     7296   6428   7172   -744   -238   -250       C  
ATOM    369  OD1 ASN A  73       8.316   7.485  48.766  1.00 56.77           O  
ANISOU  369  OD1 ASN A  73     7625   6574   7370   -809   -271   -222       O  
ATOM    370  ND2 ASN A  73       9.084   5.377  48.895  1.00 48.09           N  
ANISOU  370  ND2 ASN A  73     6210   5735   6325   -738   -231   -205       N  
ATOM    371  N   ALA A  74       4.834   4.669  49.799  1.00 43.20           N  
ANISOU  371  N   ALA A  74     5765   4830   5818   -274     -4   -409       N  
ATOM    372  CA  ALA A  74       4.062   3.854  48.865  1.00 48.66           C  
ANISOU  372  CA  ALA A  74     6321   5589   6579   -173     42   -404       C  
ATOM    373  C   ALA A  74       2.737   4.519  48.510  1.00 47.91           C  
ANISOU  373  C   ALA A  74     6292   5410   6503    -70     94   -395       C  
ATOM    374  O   ALA A  74       2.300   4.477  47.350  1.00 50.87           O  
ANISOU  374  O   ALA A  74     6594   5818   6916    -40    103   -367       O  
ATOM    375  CB  ALA A  74       3.827   2.461  49.452  1.00 41.67           C  
ANISOU  375  CB  ALA A  74     5339   4770   5724   -112     64   -427       C  
ATOM    376  N   ALA A  75       2.091   5.155  49.490  1.00 43.16           N  
ANISOU  376  N   ALA A  75     5834   4703   5864     -5    131   -409       N  
ATOM    377  CA  ALA A  75       0.832   5.838  49.219  1.00 54.24           C  
ANISOU  377  CA  ALA A  75     7297   6039   7271    121    195   -380       C  
ATOM    378  C   ALA A  75       1.037   7.017  48.277  1.00 55.62           C  
ANISOU  378  C   ALA A  75     7561   6148   7425     79    172   -357       C  
ATOM    379  O   ALA A  75       0.212   7.261  47.389  1.00 47.26           O  
ANISOU  379  O   ALA A  75     6458   5099   6401    155    206   -315       O  
ATOM    380  CB  ALA A  75       0.196   6.303  50.530  1.00 44.41           C  
ANISOU  380  CB  ALA A  75     6211   4696   5966    227    254   -393       C  
ATOM    381  N   PHE A  76       2.152   7.734  48.430  1.00 44.76           N  
ANISOU  381  N   PHE A  76     6302   4714   5991    -57    104   -372       N  
ATOM    382  CA  PHE A  76       2.442   8.841  47.529  1.00 60.32           C  
ANISOU  382  CA  PHE A  76     8360   6623   7937   -123     68   -342       C  
ATOM    383  C   PHE A  76       2.706   8.338  46.118  1.00 58.98           C  
ANISOU  383  C   PHE A  76     7993   6582   7833   -163     50   -306       C  
ATOM    384  O   PHE A  76       2.206   8.915  45.143  1.00 44.81           O  
ANISOU  384  O   PHE A  76     6204   4765   6055   -126     65   -273       O  
ATOM    385  CB  PHE A  76       3.636   9.642  48.052  1.00 46.37           C  
ANISOU  385  CB  PHE A  76     6756   4778   6085   -296    -24   -345       C  
ATOM    386  CG  PHE A  76       4.199  10.617  47.056  1.00 60.44           C  
ANISOU  386  CG  PHE A  76     8591   6528   7844   -414    -86   -297       C  
ATOM    387  CD1 PHE A  76       3.610  11.857  46.873  1.00 61.74           C  
ANISOU  387  CD1 PHE A  76     8971   6529   7958   -366    -74   -289       C  
ATOM    388  CD2 PHE A  76       5.323  10.296  46.309  1.00 68.71           C  
ANISOU  388  CD2 PHE A  76     9479   7716   8914   -561   -152   -248       C  
ATOM    389  CE1 PHE A  76       4.126  12.756  45.959  1.00 66.72           C  
ANISOU  389  CE1 PHE A  76     9658   7125   8566   -484   -138   -240       C  
ATOM    390  CE2 PHE A  76       5.843  11.189  45.392  1.00 67.45           C  
ANISOU  390  CE2 PHE A  76     9355   7542   8730   -676   -210   -188       C  
ATOM    391  CZ  PHE A  76       5.244  12.422  45.218  1.00 72.53           C  
ANISOU  391  CZ  PHE A  76    10217   8012   9330   -648   -209   -187       C  
ATOM    392  N   ALA A  77       3.457   7.242  45.990  1.00 46.46           N  
ANISOU  392  N   ALA A  77     6244   5131   6277   -221     24   -310       N  
ATOM    393  CA  ALA A  77       3.738   6.713  44.660  1.00 50.38           C  
ANISOU  393  CA  ALA A  77     6583   5744   6813   -237     14   -278       C  
ATOM    394  C   ALA A  77       2.459   6.259  43.967  1.00 45.47           C  
ANISOU  394  C   ALA A  77     5893   5137   6247   -113     64   -271       C  
ATOM    395  O   ALA A  77       2.239   6.558  42.785  1.00 42.83           O  
ANISOU  395  O   ALA A  77     5524   4821   5928   -109     62   -237       O  
ATOM    396  CB  ALA A  77       4.735   5.558  44.759  1.00 42.84           C  
ANISOU  396  CB  ALA A  77     5494   4924   5861   -283     -8   -279       C  
ATOM    397  N   GLU A  78       1.582   5.569  44.701  1.00 49.10           N  
ANISOU  397  N   GLU A  78     6331   5594   6732    -21    104   -289       N  
ATOM    398  CA  GLU A  78       0.365   5.051  44.085  1.00 49.13           C  
ANISOU  398  CA  GLU A  78     6250   5633   6783     69    132   -256       C  
ATOM    399  C   GLU A  78      -0.617   6.170  43.758  1.00 46.73           C  
ANISOU  399  C   GLU A  78     6017   5258   6480    145    171   -209       C  
ATOM    400  O   GLU A  78      -1.253   6.153  42.694  1.00 49.10           O  
ANISOU  400  O   GLU A  78     6249   5597   6811    170    170   -160       O  
ATOM    401  CB  GLU A  78      -0.271   4.004  44.997  1.00 42.92           C  
ANISOU  401  CB  GLU A  78     5410   4880   6019    128    154   -265       C  
ATOM    402  CG  GLU A  78       0.581   2.749  45.149  1.00 56.70           C  
ANISOU  402  CG  GLU A  78     7083   6698   7764     72    117   -304       C  
ATOM    403  CD  GLU A  78       0.087   1.824  46.245  1.00 72.71           C  
ANISOU  403  CD  GLU A  78     9083   8740   9804    115    133   -315       C  
ATOM    404  OE1 GLU A  78      -1.049   2.021  46.724  1.00 82.97           O  
ANISOU  404  OE1 GLU A  78    10387  10019  11118    191    174   -276       O  
ATOM    405  OE2 GLU A  78       0.839   0.904  46.630  1.00 87.30           O  
ANISOU  405  OE2 GLU A  78    10900  10629  11642     81    110   -350       O  
ATOM    406  N   ALA A  79      -0.749   7.161  44.645  1.00 43.62           N  
ANISOU  406  N   ALA A  79     5776   4756   6041    188    205   -218       N  
ATOM    407  CA  ALA A  79      -1.629   8.285  44.349  1.00 44.48           C  
ANISOU  407  CA  ALA A  79     5980   4787   6134    288    252   -168       C  
ATOM    408  C   ALA A  79      -1.118   9.081  43.158  1.00 52.09           C  
ANISOU  408  C   ALA A  79     6974   5726   7091    210    210   -151       C  
ATOM    409  O   ALA A  79      -1.908   9.529  42.320  1.00 44.99           O  
ANISOU  409  O   ALA A  79     6055   4829   6212    277    234    -93       O  
ATOM    410  CB  ALA A  79      -1.764   9.189  45.575  1.00 45.49           C  
ANISOU  410  CB  ALA A  79     6319   4780   6187    362    296   -189       C  
ATOM    411  N   SER A  80       0.204   9.234  43.039  1.00 44.61           N  
ANISOU  411  N   SER A  80     6059   4774   6116     63    145   -186       N  
ATOM    412  CA  SER A  80       0.747   9.960  41.898  1.00 44.89           C  
ANISOU  412  CA  SER A  80     6109   4804   6143    -22    102   -155       C  
ATOM    413  C   SER A  80       0.507   9.205  40.599  1.00 49.76           C  
ANISOU  413  C   SER A  80     6548   5544   6815    -16     97   -124       C  
ATOM    414  O   SER A  80       0.153   9.814  39.581  1.00 47.33           O  
ANISOU  414  O   SER A  80     6243   5225   6514     -3     97    -80       O  
ATOM    415  CB  SER A  80       2.240  10.218  42.100  1.00 47.79           C  
ANISOU  415  CB  SER A  80     6520   5173   6464   -191     29   -168       C  
ATOM    416  OG  SER A  80       2.463  11.080  43.201  1.00 55.07           O  
ANISOU  416  OG  SER A  80     7652   5955   7317   -224     11   -190       O  
ATOM    417  N   MET A  81       0.664   7.876  40.613  1.00 44.14           N  
ANISOU  417  N   MET A  81     5701   4937   6131    -21     89   -146       N  
ATOM    418  CA  MET A  81       0.419   7.132  39.382  1.00 47.37           C  
ANISOU  418  CA  MET A  81     5988   5440   6569    -15     75   -121       C  
ATOM    419  C   MET A  81      -1.047   7.214  38.979  1.00 52.46           C  
ANISOU  419  C   MET A  81     6606   6077   7249     80    101    -69       C  
ATOM    420  O   MET A  81      -1.364   7.461  37.807  1.00 51.40           O  
ANISOU  420  O   MET A  81     6440   5967   7123     77     87    -24       O  
ATOM    421  CB  MET A  81       0.848   5.672  39.527  1.00 42.19           C  
ANISOU  421  CB  MET A  81     5240   4873   5917    -27     58   -156       C  
ATOM    422  CG  MET A  81       0.952   4.963  38.180  1.00 58.09           C  
ANISOU  422  CG  MET A  81     7182   6964   7924    -36     31   -140       C  
ATOM    423  SD  MET A  81       1.328   3.204  38.271  1.00 71.45           S  
ANISOU  423  SD  MET A  81     8821   8730   9598    -22     12   -180       S  
ATOM    424  CE  MET A  81      -0.306   2.519  38.525  1.00 77.71           C  
ANISOU  424  CE  MET A  81     9593   9499  10432     23     -1   -157       C  
ATOM    425  N   ALA A  82      -1.958   7.053  39.944  1.00 50.03           N  
ANISOU  425  N   ALA A  82     6303   5749   6957    165    142    -56       N  
ATOM    426  CA  ALA A  82      -3.378   7.124  39.613  1.00 58.67           C  
ANISOU  426  CA  ALA A  82     7341   6869   8081    259    169     29       C  
ATOM    427  C   ALA A  82      -3.766   8.516  39.130  1.00 56.03           C  
ANISOU  427  C   ALA A  82     7090   6466   7732    316    201     80       C  
ATOM    428  O   ALA A  82      -4.594   8.657  38.223  1.00 54.78           O  
ANISOU  428  O   ALA A  82     6866   6352   7596    352    199    160       O  
ATOM    429  CB  ALA A  82      -4.221   6.726  40.824  1.00 43.77           C  
ANISOU  429  CB  ALA A  82     5433   4994   6204    350    217     54       C  
ATOM    430  N   ALA A  83      -3.153   9.556  39.698  1.00 57.05           N  
ANISOU  430  N   ALA A  83     7379   6482   7817    315    221     40       N  
ATOM    431  CA  ALA A  83      -3.515  10.916  39.326  1.00 45.86           C  
ANISOU  431  CA  ALA A  83     6083   4971   6370    379    251     86       C  
ATOM    432  C   ALA A  83      -2.945  11.323  37.974  1.00 50.51           C  
ANISOU  432  C   ALA A  83     6656   5572   6962    280    198     98       C  
ATOM    433  O   ALA A  83      -3.566  12.125  37.267  1.00 54.27           O  
ANISOU  433  O   ALA A  83     7162   6020   7438    341    217    163       O  
ATOM    434  CB  ALA A  83      -3.045  11.897  40.402  1.00 46.67           C  
ANISOU  434  CB  ALA A  83     6410   4920   6402    397    274     39       C  
ATOM    435  N   PHE A  84      -1.780  10.799  37.595  1.00 45.88           N  
ANISOU  435  N   PHE A  84     6021   5038   6375    142    138     50       N  
ATOM    436  CA  PHE A  84      -1.079  11.311  36.427  1.00 52.59           C  
ANISOU  436  CA  PHE A  84     6872   5900   7211     49     94     68       C  
ATOM    437  C   PHE A  84      -0.977  10.331  35.266  1.00 54.57           C  
ANISOU  437  C   PHE A  84     6970   6278   7485     10     63     81       C  
ATOM    438  O   PHE A  84      -0.383  10.684  34.242  1.00 58.14           O  
ANISOU  438  O   PHE A  84     7413   6757   7920    -56     33    102       O  
ATOM    439  CB  PHE A  84       0.323  11.778  36.833  1.00 49.49           C  
ANISOU  439  CB  PHE A  84     6568   5466   6771    -82     51     33       C  
ATOM    440  CG  PHE A  84       0.312  12.859  37.873  1.00 55.77           C  
ANISOU  440  CG  PHE A  84     7571   6103   7516    -70     61     20       C  
ATOM    441  CD1 PHE A  84      -0.604  13.896  37.796  1.00 62.76           C  
ANISOU  441  CD1 PHE A  84     8589   6873   8383     38    101     57       C  
ATOM    442  CD2 PHE A  84       1.197  12.827  38.939  1.00 68.17           C  
ANISOU  442  CD2 PHE A  84     9219   7636   9046   -157     28    -25       C  
ATOM    443  CE1 PHE A  84      -0.628  14.893  38.752  1.00 72.81           C  
ANISOU  443  CE1 PHE A  84    10102   7976   9587     69    112     41       C  
ATOM    444  CE2 PHE A  84       1.178  13.820  39.902  1.00 71.59           C  
ANISOU  444  CE2 PHE A  84     9886   7903   9413   -151     26    -41       C  
ATOM    445  CZ  PHE A  84       0.263  14.854  39.808  1.00 75.45           C  
ANISOU  445  CZ  PHE A  84    10538   8258   9873    -32     70    -13       C  
ATOM    446  N   ASN A  85      -1.535   9.123  35.370  1.00 43.99           N  
ANISOU  446  N   ASN A  85     5529   5012   6173     48     63     73       N  
ATOM    447  CA  ASN A  85      -1.402   8.224  34.231  1.00 45.10           C  
ANISOU  447  CA  ASN A  85     5579   5245   6311     10     22     80       C  
ATOM    448  C   ASN A  85      -2.720   7.604  33.784  1.00 51.69           C  
ANISOU  448  C   ASN A  85     6343   6123   7174     57      7    136       C  
ATOM    449  O   ASN A  85      -2.865   7.250  32.608  1.00 67.58           O  
ANISOU  449  O   ASN A  85     8321   8184   9173     27    -34    164       O  
ATOM    450  CB  ASN A  85      -0.396   7.117  34.556  1.00 54.31           C  
ANISOU  450  CB  ASN A  85     6714   6469   7453    -34      6     17       C  
ATOM    451  CG  ASN A  85       1.009   7.650  34.752  1.00 59.03           C  
ANISOU  451  CG  ASN A  85     7344   7070   8016   -105      5     -3       C  
ATOM    452  OD1 ASN A  85       1.442   7.880  35.880  1.00 59.86           O  
ANISOU  452  OD1 ASN A  85     7493   7136   8117   -125     14    -32       O  
ATOM    453  ND2 ASN A  85       1.726   7.856  33.650  1.00 54.12           N  
ANISOU  453  ND2 ASN A  85     6700   6504   7360   -149    -11     25       N  
ATOM    454  N   THR A  86      -3.672   7.460  34.709  1.00 43.78           N  
ANISOU  454  N   THR A  86     5319   5112   6202    124     35    165       N  
ATOM    455  CA  THR A  86      -4.842   6.627  34.443  1.00 55.95           C  
ANISOU  455  CA  THR A  86     6769   6723   7767    139      2    237       C  
ATOM    456  C   THR A  86      -5.677   7.169  33.288  1.00 54.19           C  
ANISOU  456  C   THR A  86     6508   6531   7552    149    -19    336       C  
ATOM    457  O   THR A  86      -6.127   6.403  32.425  1.00 56.72           O  
ANISOU  457  O   THR A  86     6776   6912   7864     92    -89    380       O  
ATOM    458  CB  THR A  86      -5.702   6.519  35.703  1.00 49.18           C  
ANISOU  458  CB  THR A  86     5879   5871   6937    219     47    277       C  
ATOM    459  OG1 THR A  86      -4.881   6.153  36.818  1.00 53.00           O  
ANISOU  459  OG1 THR A  86     6410   6317   7410    210     69    182       O  
ATOM    460  CG2 THR A  86      -6.792   5.471  35.521  1.00 54.42           C  
ANISOU  460  CG2 THR A  86     6430   6627   7620    197     -7    366       C  
ATOM    461  N   VAL A  87      -5.873   8.488  33.238  1.00 45.09           N  
ANISOU  461  N   VAL A  87     5401   5327   6403    217     34    376       N  
ATOM    462  CA  VAL A  87      -6.802   9.058  32.268  1.00 54.07           C  
ANISOU  462  CA  VAL A  87     6493   6500   7551    250     24    489       C  
ATOM    463  C   VAL A  87      -6.265   8.895  30.851  1.00 51.74           C  
ANISOU  463  C   VAL A  87     6202   6227   7230    152    -42    473       C  
ATOM    464  O   VAL A  87      -6.979   8.446  29.946  1.00 47.61           O  
ANISOU  464  O   VAL A  87     5611   5773   6704    116   -103    549       O  
ATOM    465  CB  VAL A  87      -7.085  10.535  32.597  1.00 61.33           C  
ANISOU  465  CB  VAL A  87     7494   7342   8468    367    105    532       C  
ATOM    466  CG1 VAL A  87      -7.877  11.184  31.474  1.00 51.09           C  
ANISOU  466  CG1 VAL A  87     6155   6082   7177    401     95    648       C  
ATOM    467  CG2 VAL A  87      -7.836  10.648  33.919  1.00 47.10           C  
ANISOU  467  CG2 VAL A  87     5691   5532   6674    498    181    572       C  
ATOM    468  N   VAL A  88      -5.001   9.264  30.634  1.00 45.24           N  
ANISOU  468  N   VAL A  88     5457   5354   6377    105    -36    387       N  
ATOM    469  CA  VAL A  88      -4.442   9.118  29.298  1.00 45.17           C  
ANISOU  469  CA  VAL A  88     5453   5378   6331     32    -85    379       C  
ATOM    470  C   VAL A  88      -4.232   7.652  28.949  1.00 52.26           C  
ANISOU  470  C   VAL A  88     6328   6332   7195    -24   -144    338       C  
ATOM    471  O   VAL A  88      -4.360   7.273  27.780  1.00 48.67           O  
ANISOU  471  O   VAL A  88     5875   5914   6702    -65   -199    364       O  
ATOM    472  CB  VAL A  88      -3.147   9.935  29.155  1.00 48.36           C  
ANISOU  472  CB  VAL A  88     5929   5738   6707     -4    -61    328       C  
ATOM    473  CG1 VAL A  88      -2.590   9.801  27.742  1.00 47.71           C  
ANISOU  473  CG1 VAL A  88     5841   5709   6579    -61    -98    337       C  
ATOM    474  CG2 VAL A  88      -3.429  11.393  29.462  1.00 56.58           C  
ANISOU  474  CG2 VAL A  88     7040   6694   7765     44    -18    371       C  
ATOM    475  N   ASN A  89      -3.951   6.790  29.933  1.00 46.25           N  
ANISOU  475  N   ASN A  89     5567   5570   6438    -24   -139    277       N  
ATOM    476  CA  ASN A  89      -3.866   5.368  29.619  1.00 50.55           C  
ANISOU  476  CA  ASN A  89     6121   6148   6938    -67   -200    245       C  
ATOM    477  C   ASN A  89      -5.197   4.862  29.085  1.00 51.46           C  
ANISOU  477  C   ASN A  89     6198   6296   7057   -101   -276    337       C  
ATOM    478  O   ASN A  89      -5.242   4.172  28.057  1.00 49.36           O  
ANISOU  478  O   ASN A  89     5979   6044   6731   -156   -351    343       O  
ATOM    479  CB  ASN A  89      -3.445   4.571  30.855  1.00 48.55           C  
ANISOU  479  CB  ASN A  89     5873   5882   6691    -55   -181    175       C  
ATOM    480  CG  ASN A  89      -1.966   4.706  31.163  1.00 60.37           C  
ANISOU  480  CG  ASN A  89     7406   7373   8159    -49   -134     94       C  
ATOM    481  OD1 ASN A  89      -1.259   5.499  30.542  1.00 67.64           O  
ANISOU  481  OD1 ASN A  89     8341   8301   9060    -59   -113     99       O  
ATOM    482  ND2 ASN A  89      -1.493   3.934  32.133  1.00 61.82           N  
ANISOU  482  ND2 ASN A  89     7595   7556   8339    -40   -122     36       N  
ATOM    483  N   PHE A  90      -6.299   5.288  29.708  1.00 49.08           N  
ANISOU  483  N   PHE A  90     5816   6015   6816    -66   -260    427       N  
ATOM    484  CA  PHE A  90      -7.613   4.873  29.233  1.00 46.82           C  
ANISOU  484  CA  PHE A  90     5461   5793   6536   -111   -339    554       C  
ATOM    485  C   PHE A  90      -7.908   5.443  27.850  1.00 48.06           C  
ANISOU  485  C   PHE A  90     5620   5970   6669   -139   -380    622       C  
ATOM    486  O   PHE A  90      -8.310   4.708  26.937  1.00 49.14           O  
ANISOU  486  O   PHE A  90     5777   6135   6757   -231   -485    665       O  
ATOM    487  CB  PHE A  90      -8.693   5.304  30.223  1.00 46.24           C  
ANISOU  487  CB  PHE A  90     5278   5765   6526    -37   -291    663       C  
ATOM    488  CG  PHE A  90     -10.087   5.098  29.712  1.00 47.30           C  
ANISOU  488  CG  PHE A  90     5302   5999   6670    -80   -366    839       C  
ATOM    489  CD1 PHE A  90     -10.645   3.833  29.689  1.00 56.46           C  
ANISOU  489  CD1 PHE A  90     6434   7209   7807   -195   -479    894       C  
ATOM    490  CD2 PHE A  90     -10.833   6.162  29.238  1.00 50.02           C  
ANISOU  490  CD2 PHE A  90     5575   6391   7039    -13   -333    964       C  
ATOM    491  CE1 PHE A  90     -11.925   3.632  29.211  1.00 62.38           C  
ANISOU  491  CE1 PHE A  90     7072   8068   8560   -265   -568   1082       C  
ATOM    492  CE2 PHE A  90     -12.117   5.968  28.758  1.00 57.76           C  
ANISOU  492  CE2 PHE A  90     6430   7490   8025    -57   -407   1153       C  
ATOM    493  CZ  PHE A  90     -12.663   4.701  28.745  1.00 52.85           C  
ANISOU  493  CZ  PHE A  90     5766   6931   7383   -194   -531   1218       C  
ATOM    494  N   THR A  91      -7.706   6.751  27.669  1.00 47.26           N  
ANISOU  494  N   THR A  91     5517   5847   6593    -69   -305    633       N  
ATOM    495  CA  THR A  91      -8.086   7.367  26.400  1.00 51.97           C  
ANISOU  495  CA  THR A  91     6104   6469   7173    -88   -340    712       C  
ATOM    496  C   THR A  91      -7.245   6.827  25.250  1.00 47.24           C  
ANISOU  496  C   THR A  91     5600   5855   6496   -166   -399    639       C  
ATOM    497  O   THR A  91      -7.773   6.546  24.168  1.00 52.43           O  
ANISOU  497  O   THR A  91     6264   6547   7112   -231   -484    705       O  
ATOM    498  CB  THR A  91      -7.968   8.892  26.475  1.00 55.25           C  
ANISOU  498  CB  THR A  91     6527   6844   7622      6   -248    734       C  
ATOM    499  OG1 THR A  91      -6.603   9.265  26.706  1.00 67.95           O  
ANISOU  499  OG1 THR A  91     8228   8380   9212      7   -197    610       O  
ATOM    500  CG2 THR A  91      -8.846   9.450  27.587  1.00 47.64           C  
ANISOU  500  CG2 THR A  91     5502   5888   6712    119   -176    814       C  
ATOM    501  N   TYR A  92      -5.935   6.664  25.462  1.00 46.16           N  
ANISOU  501  N   TYR A  92     5537   5675   6327   -155   -354    514       N  
ATOM    502  CA  TYR A  92      -5.089   6.111  24.414  1.00 54.90           C  
ANISOU  502  CA  TYR A  92     6735   6782   7343   -193   -389    455       C  
ATOM    503  C   TYR A  92      -5.409   4.648  24.138  1.00 55.84           C  
ANISOU  503  C   TYR A  92     6923   6901   7393   -253   -486    440       C  
ATOM    504  O   TYR A  92      -5.300   4.207  22.988  1.00 50.66           O  
ANISOU  504  O   TYR A  92     6359   6243   6646   -291   -548    439       O  
ATOM    505  CB  TYR A  92      -3.616   6.282  24.786  1.00 45.61           C  
ANISOU  505  CB  TYR A  92     5595   5590   6146   -154   -311    356       C  
ATOM    506  CG  TYR A  92      -2.667   6.007  23.641  1.00 48.24           C  
ANISOU  506  CG  TYR A  92     6002   5947   6379   -156   -316    323       C  
ATOM    507  CD1 TYR A  92      -2.929   6.501  22.362  1.00 46.43           C  
ANISOU  507  CD1 TYR A  92     5792   5737   6114   -177   -346    380       C  
ATOM    508  CD2 TYR A  92      -1.506   5.265  23.837  1.00 45.65           C  
ANISOU  508  CD2 TYR A  92     5724   5634   5987   -121   -281    245       C  
ATOM    509  CE1 TYR A  92      -2.068   6.258  21.307  1.00 46.80           C  
ANISOU  509  CE1 TYR A  92     5910   5813   6057   -162   -340    358       C  
ATOM    510  CE2 TYR A  92      -0.634   5.018  22.792  1.00 46.10           C  
ANISOU  510  CE2 TYR A  92     5846   5730   5938    -91   -267    232       C  
ATOM    511  CZ  TYR A  92      -0.921   5.517  21.527  1.00 54.78           C  
ANISOU  511  CZ  TYR A  92     6971   6845   6999   -111   -295    286       C  
ATOM    512  OH  TYR A  92      -0.058   5.273  20.484  1.00 53.32           O  
ANISOU  512  OH  TYR A  92     6855   6706   6698    -65   -272    279       O  
ATOM    513  N   ALA A  93      -5.801   3.876  25.161  1.00 48.36           N  
ANISOU  513  N   ALA A  93     5955   5946   6474   -266   -506    431       N  
ATOM    514  CA  ALA A  93      -6.229   2.507  24.898  1.00 47.35           C  
ANISOU  514  CA  ALA A  93     5914   5802   6273   -346   -619    435       C  
ATOM    515  C   ALA A  93      -7.529   2.462  24.103  1.00 51.78           C  
ANISOU  515  C   ALA A  93     6448   6401   6825   -445   -736    570       C  
ATOM    516  O   ALA A  93      -7.738   1.533  23.314  1.00 54.45           O  
ANISOU  516  O   ALA A  93     6913   6711   7064   -535   -853    577       O  
ATOM    517  CB  ALA A  93      -6.382   1.739  26.212  1.00 46.42           C  
ANISOU  517  CB  ALA A  93     5772   5672   6192   -348   -618    409       C  
ATOM    518  N   VAL A  94      -8.404   3.448  24.289  1.00 51.95           N  
ANISOU  518  N   VAL A  94     6318   6485   6935   -427   -709    688       N  
ATOM    519  CA  VAL A  94      -9.687   3.466  23.590  1.00 52.68           C  
ANISOU  519  CA  VAL A  94     6346   6644   7025   -518   -818    850       C  
ATOM    520  C   VAL A  94      -9.566   4.090  22.203  1.00 55.18           C  
ANISOU  520  C   VAL A  94     6710   6964   7293   -531   -840    872       C  
ATOM    521  O   VAL A  94     -10.201   3.629  21.251  1.00 57.82           O  
ANISOU  521  O   VAL A  94     7091   7318   7561   -645   -971    953       O  
ATOM    522  CB  VAL A  94     -10.734   4.198  24.455  1.00 51.93           C  
ANISOU  522  CB  VAL A  94     6058   6637   7038   -462   -767    991       C  
ATOM    523  CG1 VAL A  94     -11.997   4.480  23.658  1.00 60.56           C  
ANISOU  523  CG1 VAL A  94     7047   7830   8133   -532   -858   1188       C  
ATOM    524  CG2 VAL A  94     -11.062   3.373  25.689  1.00 55.29           C  
ANISOU  524  CG2 VAL A  94     6437   7078   7493   -478   -776   1000       C  
ATOM    525  N   HIS A  95      -8.737   5.123  22.062  1.00 49.63           N  
ANISOU  525  N   HIS A  95     6006   6238   6614   -431   -725    807       N  
ATOM    526  CA  HIS A  95      -8.571   5.857  20.808  1.00 49.30           C  
ANISOU  526  CA  HIS A  95     5995   6202   6534   -432   -730    833       C  
ATOM    527  C   HIS A  95      -7.077   5.869  20.501  1.00 48.66           C  
ANISOU  527  C   HIS A  95     6029   6069   6392   -380   -659    689       C  
ATOM    528  O   HIS A  95      -6.315   6.604  21.136  1.00 49.12           O  
ANISOU  528  O   HIS A  95     6051   6111   6501   -302   -550    634       O  
ATOM    529  CB  HIS A  95      -9.141   7.268  20.924  1.00 50.58           C  
ANISOU  529  CB  HIS A  95     6026   6405   6786   -360   -659    937       C  
ATOM    530  CG  HIS A  95      -9.120   8.043  19.644  1.00 54.71           C  
ANISOU  530  CG  HIS A  95     6569   6941   7276   -368   -674    985       C  
ATOM    531  ND1 HIS A  95      -9.990   7.792  18.606  1.00 56.80           N  
ANISOU  531  ND1 HIS A  95     6828   7259   7495   -460   -791   1099       N  
ATOM    532  CD2 HIS A  95      -8.342   9.076  19.242  1.00 55.76           C  
ANISOU  532  CD2 HIS A  95     6729   7044   7413   -308   -593    944       C  
ATOM    533  CE1 HIS A  95      -9.745   8.632  17.616  1.00 52.27           C  
ANISOU  533  CE1 HIS A  95     6275   6685   6899   -442   -773   1118       C  
ATOM    534  NE2 HIS A  95      -8.750   9.423  17.978  1.00 50.47           N  
ANISOU  534  NE2 HIS A  95     6066   6407   6701   -351   -653   1028       N  
ATOM    535  N   ASN A  96      -6.662   5.065  19.522  1.00 49.09           N  
ANISOU  535  N   ASN A  96     6228   6101   6324   -423   -725    643       N  
ATOM    536  CA  ASN A  96      -5.251   4.730  19.360  1.00 50.29           C  
ANISOU  536  CA  ASN A  96     6488   6223   6396   -356   -657    520       C  
ATOM    537  C   ASN A  96      -4.467   5.765  18.557  1.00 53.69           C  
ANISOU  537  C   ASN A  96     6907   6682   6810   -305   -582    521       C  
ATOM    538  O   ASN A  96      -3.691   5.401  17.668  1.00 56.08           O  
ANISOU  538  O   ASN A  96     7324   6988   6996   -277   -576    478       O  
ATOM    539  CB  ASN A  96      -5.113   3.355  18.699  1.00 61.76           C  
ANISOU  539  CB  ASN A  96     8135   7629   7700   -391   -747    470       C  
ATOM    540  CG  ASN A  96      -5.738   2.249  19.522  1.00 79.05           C  
ANISOU  540  CG  ASN A  96    10363   9780   9894   -455   -828    465       C  
ATOM    541  OD1 ASN A  96      -5.990   2.414  20.715  1.00 90.82           O  
ANISOU  541  OD1 ASN A  96    11726  11287  11495   -443   -788    474       O  
ATOM    542  ND2 ASN A  96      -5.988   1.109  18.889  1.00 90.64           N  
ANISOU  542  ND2 ASN A  96    12022  11188  11230   -525   -949    454       N  
ATOM    543  N   GLU A  97      -4.637   7.048  18.874  1.00 48.42           N  
ANISOU  543  N   GLU A  97     6117   6033   6246   -286   -523    574       N  
ATOM    544  CA  GLU A  97      -3.817   8.107  18.301  1.00 62.97           C  
ANISOU  544  CA  GLU A  97     7946   7898   8084   -251   -453    581       C  
ATOM    545  C   GLU A  97      -3.339   9.019  19.419  1.00 47.81           C  
ANISOU  545  C   GLU A  97     5948   5960   6258   -215   -364    564       C  
ATOM    546  O   GLU A  97      -4.118   9.400  20.295  1.00 47.63           O  
ANISOU  546  O   GLU A  97     5864   5910   6325   -205   -358    597       O  
ATOM    547  CB  GLU A  97      -4.585   8.923  17.247  1.00 49.10           C  
ANISOU  547  CB  GLU A  97     6166   6159   6331   -284   -496    683       C  
ATOM    548  CG  GLU A  97      -4.952   8.141  15.999  1.00 61.50           C  
ANISOU  548  CG  GLU A  97     7838   7742   7786   -336   -594    704       C  
ATOM    549  CD  GLU A  97      -5.658   8.998  14.963  1.00 62.18           C  
ANISOU  549  CD  GLU A  97     7891   7856   7877   -371   -637    813       C  
ATOM    550  OE1 GLU A  97      -5.122  10.069  14.612  1.00 64.81           O  
ANISOU  550  OE1 GLU A  97     8192   8203   8231   -337   -570    832       O  
ATOM    551  OE2 GLU A  97      -6.752   8.605  14.508  1.00 63.45           O  
ANISOU  551  OE2 GLU A  97     8059   8030   8020   -443   -745    891       O  
ATOM    552  N   TRP A  98      -2.056   9.363  19.384  1.00 47.67           N  
ANISOU  552  N   TRP A  98     5940   5963   6210   -194   -299    526       N  
ATOM    553  CA  TRP A  98      -1.430  10.128  20.455  1.00 47.26           C  
ANISOU  553  CA  TRP A  98     5844   5889   6224   -187   -234    508       C  
ATOM    554  C   TRP A  98      -1.538  11.623  20.167  1.00 49.43           C  
ANISOU  554  C   TRP A  98     6103   6135   6541   -205   -217    579       C  
ATOM    555  O   TRP A  98      -0.952  12.119  19.198  1.00 53.53           O  
ANISOU  555  O   TRP A  98     6632   6693   7012   -227   -212    616       O  
ATOM    556  CB  TRP A  98       0.031   9.717  20.625  1.00 47.14           C  
ANISOU  556  CB  TRP A  98     5835   5928   6149   -174   -186    458       C  
ATOM    557  CG  TRP A  98       0.629  10.289  21.858  1.00 47.23           C  
ANISOU  557  CG  TRP A  98     5811   5915   6219   -192   -144    440       C  
ATOM    558  CD1 TRP A  98       1.398  11.410  21.954  1.00 48.81           C  
ANISOU  558  CD1 TRP A  98     5996   6118   6431   -240   -119    482       C  
ATOM    559  CD2 TRP A  98       0.478   9.786  23.186  1.00 54.44           C  
ANISOU  559  CD2 TRP A  98     6716   6788   7180   -177   -135    383       C  
ATOM    560  NE1 TRP A  98       1.748  11.631  23.264  1.00 46.83           N  
ANISOU  560  NE1 TRP A  98     5742   5825   6225   -262   -102    452       N  
ATOM    561  CE2 TRP A  98       1.196  10.647  24.042  1.00 53.52           C  
ANISOU  561  CE2 TRP A  98     6589   6648   7097   -215   -104    388       C  
ATOM    562  CE3 TRP A  98      -0.189   8.686  23.736  1.00 45.81           C  
ANISOU  562  CE3 TRP A  98     5633   5676   6099   -147   -157    335       C  
ATOM    563  CZ2 TRP A  98       1.263  10.444  25.420  1.00 45.79           C  
ANISOU  563  CZ2 TRP A  98     5612   5627   6160   -211    -90    339       C  
ATOM    564  CZ3 TRP A  98      -0.118   8.486  25.102  1.00 49.50           C  
ANISOU  564  CZ3 TRP A  98     6084   6109   6614   -139   -136    291       C  
ATOM    565  CH2 TRP A  98       0.604   9.360  25.928  1.00 45.30           C  
ANISOU  565  CH2 TRP A  98     5544   5554   6112   -165    -99    289       C  
ATOM    566  N   TYR A  99      -2.270  12.339  21.022  1.00 47.60           N  
ANISOU  566  N   TYR A  99     5861   5833   6391   -186   -204    603       N  
ATOM    567  CA  TYR A  99      -2.490  13.773  20.871  1.00 48.13           C  
ANISOU  567  CA  TYR A  99     5951   5844   6492   -184   -187    670       C  
ATOM    568  C   TYR A  99      -1.828  14.598  21.968  1.00 48.13           C  
ANISOU  568  C   TYR A  99     6002   5765   6519   -196   -147    644       C  
ATOM    569  O   TYR A  99      -2.037  15.813  22.023  1.00 57.32           O  
ANISOU  569  O   TYR A  99     7229   6850   7702   -189   -136    693       O  
ATOM    570  CB  TYR A  99      -3.990  14.082  20.863  1.00 50.37           C  
ANISOU  570  CB  TYR A  99     6211   6102   6826   -126   -201    744       C  
ATOM    571  CG  TYR A  99      -4.812  13.370  19.812  1.00 56.30           C  
ANISOU  571  CG  TYR A  99     6917   6926   7550   -141   -265    796       C  
ATOM    572  CD1 TYR A  99      -4.385  13.291  18.493  1.00 54.99           C  
ANISOU  572  CD1 TYR A  99     6771   6808   7316   -188   -299    810       C  
ATOM    573  CD2 TYR A  99      -6.029  12.786  20.142  1.00 48.88           C  
ANISOU  573  CD2 TYR A  99     5919   6012   6643   -116   -298    846       C  
ATOM    574  CE1 TYR A  99      -5.146  12.649  17.531  1.00 49.44           C  
ANISOU  574  CE1 TYR A  99     6057   6158   6572   -215   -372    858       C  
ATOM    575  CE2 TYR A  99      -6.794  12.143  19.191  1.00 57.18           C  
ANISOU  575  CE2 TYR A  99     6939   7128   7659   -161   -381    909       C  
ATOM    576  CZ  TYR A  99      -6.348  12.075  17.887  1.00 57.39           C  
ANISOU  576  CZ  TYR A  99     7012   7181   7611   -213   -421    909       C  
ATOM    577  OH  TYR A  99      -7.112  11.431  16.942  1.00 59.10           O  
ANISOU  577  OH  TYR A  99     7227   7450   7779   -271   -517    972       O  
ATOM    578  N   TYR A 100      -1.051  13.975  22.848  1.00 47.62           N  
ANISOU  578  N   TYR A 100     5931   5714   6448   -216   -132    573       N  
ATOM    579  CA  TYR A 100      -0.773  14.555  24.155  1.00 50.34           C  
ANISOU  579  CA  TYR A 100     6336   5970   6821   -221   -108    544       C  
ATOM    580  C   TYR A 100       0.635  15.116  24.310  1.00 49.59           C  
ANISOU  580  C   TYR A 100     6274   5879   6689   -321   -113    547       C  
ATOM    581  O   TYR A 100       0.974  15.597  25.397  1.00 48.11           O  
ANISOU  581  O   TYR A 100     6159   5611   6510   -352   -111    525       O  
ATOM    582  CB  TYR A 100      -1.072  13.503  25.226  1.00 46.94           C  
ANISOU  582  CB  TYR A 100     5874   5546   6417   -176    -94    477       C  
ATOM    583  CG  TYR A 100      -2.407  12.849  24.949  1.00 46.82           C  
ANISOU  583  CG  TYR A 100     5805   5557   6429   -109   -108    504       C  
ATOM    584  CD1 TYR A 100      -3.593  13.536  25.179  1.00 49.68           C  
ANISOU  584  CD1 TYR A 100     6178   5865   6832    -34    -90    568       C  
ATOM    585  CD2 TYR A 100      -2.484  11.568  24.410  1.00 51.45           C  
ANISOU  585  CD2 TYR A 100     6339   6224   6986   -121   -143    481       C  
ATOM    586  CE1 TYR A 100      -4.818  12.959  24.907  1.00 52.65           C  
ANISOU  586  CE1 TYR A 100     6478   6296   7232     11   -112    627       C  
ATOM    587  CE2 TYR A 100      -3.706  10.981  24.133  1.00 46.58           C  
ANISOU  587  CE2 TYR A 100     5679   5634   6385    -96   -181    526       C  
ATOM    588  CZ  TYR A 100      -4.870  11.682  24.385  1.00 51.98           C  
ANISOU  588  CZ  TYR A 100     6339   6291   7121    -39   -168    608       C  
ATOM    589  OH  TYR A 100      -6.093  11.110  24.113  1.00 51.96           O  
ANISOU  589  OH  TYR A 100     6267   6344   7133    -29   -214    685       O  
ATOM    590  N   GLY A 101       1.450  15.098  23.261  1.00 48.23           N  
ANISOU  590  N   GLY A 101     6055   5803   6466   -378   -126    587       N  
ATOM    591  CA  GLY A 101       2.757  15.719  23.299  1.00 48.82           C  
ANISOU  591  CA  GLY A 101     6136   5911   6502   -490   -140    630       C  
ATOM    592  C   GLY A 101       3.876  14.725  23.570  1.00 48.55           C  
ANISOU  592  C   GLY A 101     6010   6009   6428   -510   -125    610       C  
ATOM    593  O   GLY A 101       3.664  13.610  24.054  1.00 47.84           O  
ANISOU  593  O   GLY A 101     5886   5944   6346   -439   -103    540       O  
ATOM    594  N   LEU A 102       5.101  15.149  23.242  1.00 49.30           N  
ANISOU  594  N   LEU A 102     6061   6198   6472   -608   -137    690       N  
ATOM    595  CA  LEU A 102       6.254  14.260  23.361  1.00 58.22           C  
ANISOU  595  CA  LEU A 102     7081   7489   7550   -609   -111    707       C  
ATOM    596  C   LEU A 102       6.652  14.042  24.818  1.00 61.08           C  
ANISOU  596  C   LEU A 102     7451   7820   7936   -650   -122    666       C  
ATOM    597  O   LEU A 102       6.921  12.903  25.237  1.00 54.44           O  
ANISOU  597  O   LEU A 102     6549   7053   7082   -578    -87    618       O  
ATOM    598  CB  LEU A 102       7.429  14.830  22.565  1.00 50.46           C  
ANISOU  598  CB  LEU A 102     6022   6648   6503   -702   -119    840       C  
ATOM    599  CG  LEU A 102       8.763  14.096  22.691  1.00 50.92           C  
ANISOU  599  CG  LEU A 102     5945   6907   6495   -701    -86    904       C  
ATOM    600  CD1 LEU A 102       8.626  12.658  22.212  1.00 50.38           C  
ANISOU  600  CD1 LEU A 102     5836   6925   6381   -522    -14    840       C  
ATOM    601  CD2 LEU A 102       9.854  14.821  21.920  1.00 52.28           C  
ANISOU  601  CD2 LEU A 102     6025   7233   6604   -807    -98   1071       C  
ATOM    602  N   PHE A 103       6.700  15.119  25.607  1.00 49.58           N  
ANISOU  602  N   PHE A 103     6091   6243   6504   -764   -173    685       N  
ATOM    603  CA  PHE A 103       7.116  14.967  26.994  1.00 50.06           C  
ANISOU  603  CA  PHE A 103     6178   6270   6575   -817   -192    651       C  
ATOM    604  C   PHE A 103       6.147  14.085  27.761  1.00 48.38           C  
ANISOU  604  C   PHE A 103     5993   5980   6411   -686   -154    528       C  
ATOM    605  O   PHE A 103       6.562  13.266  28.588  1.00 52.13           O  
ANISOU  605  O   PHE A 103     6419   6504   6883   -671   -141    489       O  
ATOM    606  CB  PHE A 103       7.232  16.324  27.687  1.00 51.62           C  
ANISOU  606  CB  PHE A 103     6530   6314   6768   -962   -265    686       C  
ATOM    607  CG  PHE A 103       7.414  16.212  29.174  1.00 61.16           C  
ANISOU  607  CG  PHE A 103     7811   7447   7982  -1005   -290    633       C  
ATOM    608  CD1 PHE A 103       8.659  15.923  29.705  1.00 63.61           C  
ANISOU  608  CD1 PHE A 103     8032   7884   8254  -1121   -325    694       C  
ATOM    609  CD2 PHE A 103       6.337  16.357  30.038  1.00 63.60           C  
ANISOU  609  CD2 PHE A 103     8265   7572   8327   -918   -273    534       C  
ATOM    610  CE1 PHE A 103       8.835  15.799  31.065  1.00 62.24           C  
ANISOU  610  CE1 PHE A 103     7927   7643   8080  -1167   -354    648       C  
ATOM    611  CE2 PHE A 103       6.508  16.231  31.403  1.00 63.97           C  
ANISOU  611  CE2 PHE A 103     8388   7550   8368   -949   -292    484       C  
ATOM    612  CZ  PHE A 103       7.759  15.952  31.917  1.00 65.97           C  
ANISOU  612  CZ  PHE A 103     8563   7917   8584  -1081   -338    535       C  
ATOM    613  N   TYR A 104       4.848  14.232  27.500  1.00 47.96           N  
ANISOU  613  N   TYR A 104     6008   5817   6400   -594   -137    481       N  
ATOM    614  CA  TYR A 104       3.905  13.360  28.178  1.00 47.07           C  
ANISOU  614  CA  TYR A 104     5898   5656   6329   -480   -106    391       C  
ATOM    615  C   TYR A 104       3.999  11.931  27.667  1.00 66.29           C  
ANISOU  615  C   TYR A 104     8225   8217   8745   -403    -78    360       C  
ATOM    616  O   TYR A 104       3.713  10.999  28.417  1.00 45.81           O  
ANISOU  616  O   TYR A 104     5617   5619   6170   -346    -63    295       O  
ATOM    617  CB  TYR A 104       2.474  13.869  28.050  1.00 47.02           C  
ANISOU  617  CB  TYR A 104     5969   5530   6367   -399    -95    381       C  
ATOM    618  CG  TYR A 104       1.569  13.141  29.011  1.00 59.29           C  
ANISOU  618  CG  TYR A 104     7525   7039   7963   -304    -68    316       C  
ATOM    619  CD1 TYR A 104       1.544  13.480  30.356  1.00 69.72           C  
ANISOU  619  CD1 TYR A 104     8934   8262   9293   -304    -61    280       C  
ATOM    620  CD2 TYR A 104       0.778  12.084  28.588  1.00 63.59           C  
ANISOU  620  CD2 TYR A 104     7993   7642   8527   -225    -58    297       C  
ATOM    621  CE1 TYR A 104       0.737  12.808  31.248  1.00 60.96           C  
ANISOU  621  CE1 TYR A 104     7816   7128   8218   -214    -31    232       C  
ATOM    622  CE2 TYR A 104      -0.029  11.404  29.473  1.00 57.29           C  
ANISOU  622  CE2 TYR A 104     7184   6819   7765   -156    -42    257       C  
ATOM    623  CZ  TYR A 104      -0.050  11.771  30.801  1.00 61.17           C  
ANISOU  623  CZ  TYR A 104     7743   7227   8271   -143    -21    227       C  
ATOM    624  OH  TYR A 104      -0.860  11.096  31.687  1.00 60.33           O  
ANISOU  624  OH  TYR A 104     7616   7109   8197    -68      1    199       O  
ATOM    625  N   CYS A 105       4.409  11.729  26.413  1.00 53.85           N  
ANISOU  625  N   CYS A 105     6593   6747   7122   -395    -71    407       N  
ATOM    626  CA  CYS A 105       4.642  10.367  25.937  1.00 48.13           C  
ANISOU  626  CA  CYS A 105     5810   6127   6348   -311    -44    378       C  
ATOM    627  C   CYS A 105       5.770   9.710  26.723  1.00 46.44           C  
ANISOU  627  C   CYS A 105     5537   6004   6103   -315    -22    372       C  
ATOM    628  O   CYS A 105       5.642   8.561  27.187  1.00 48.63           O  
ANISOU  628  O   CYS A 105     5812   6291   6373   -239     -4    307       O  
ATOM    629  CB  CYS A 105       4.942  10.399  24.434  1.00 46.98           C  
ANISOU  629  CB  CYS A 105     5641   6073   6137   -291    -34    438       C  
ATOM    630  SG  CYS A 105       5.670   8.919  23.664  1.00 53.38           S  
ANISOU  630  SG  CYS A 105     6420   7028   6835   -174     13    429       S  
ATOM    631  N   LYS A 106       6.852  10.457  26.956  1.00 47.13           N  
ANISOU  631  N   LYS A 106     5580   6157   6171   -415    -32    451       N  
ATOM    632  CA  LYS A 106       7.946   9.922  27.760  1.00 47.33           C  
ANISOU  632  CA  LYS A 106     5530   6286   6166   -432    -18    472       C  
ATOM    633  C   LYS A 106       7.504   9.674  29.200  1.00 48.00           C  
ANISOU  633  C   LYS A 106     5667   6262   6308   -440    -33    387       C  
ATOM    634  O   LYS A 106       7.803   8.623  29.775  1.00 49.26           O  
ANISOU  634  O   LYS A 106     5788   6476   6455   -375     -7    347       O  
ATOM    635  CB  LYS A 106       9.144  10.871  27.719  1.00 48.45           C  
ANISOU  635  CB  LYS A 106     5606   6529   6274   -573    -47    604       C  
ATOM    636  CG  LYS A 106       9.760  11.027  26.336  1.00 57.77           C  
ANISOU  636  CG  LYS A 106     6705   7858   7386   -557    -21    712       C  
ATOM    637  CD  LYS A 106      10.993  11.915  26.380  1.00 57.67           C  
ANISOU  637  CD  LYS A 106     6604   7972   7337   -718    -61    871       C  
ATOM    638  CE  LYS A 106      11.665  12.010  25.017  1.00 53.38           C  
ANISOU  638  CE  LYS A 106     5956   7608   6716   -689    -22    999       C  
ATOM    639  NZ  LYS A 106      12.199  10.692  24.558  1.00 52.19           N  
ANISOU  639  NZ  LYS A 106     5711   7632   6486   -501     74   1011       N  
ATOM    640  N   PHE A 107       6.775  10.626  29.796  1.00 48.90           N  
ANISOU  640  N   PHE A 107     5882   6221   6477   -502    -70    360       N  
ATOM    641  CA  PHE A 107       6.335  10.454  31.181  1.00 46.06           C  
ANISOU  641  CA  PHE A 107     5585   5758   6160   -497    -77    285       C  
ATOM    642  C   PHE A 107       5.366   9.286  31.310  1.00 52.61           C  
ANISOU  642  C   PHE A 107     6408   6562   7018   -367    -44    198       C  
ATOM    643  O   PHE A 107       5.405   8.537  32.295  1.00 44.69           O  
ANISOU  643  O   PHE A 107     5397   5556   6027   -338    -34    146       O  
ATOM    644  CB  PHE A 107       5.686  11.745  31.684  1.00 46.42           C  
ANISOU  644  CB  PHE A 107     5769   5632   6234   -555   -110    280       C  
ATOM    645  CG  PHE A 107       5.166  11.663  33.098  1.00 51.99           C  
ANISOU  645  CG  PHE A 107     6561   6224   6969   -530   -107    208       C  
ATOM    646  CD1 PHE A 107       5.989  11.972  34.170  1.00 51.43           C  
ANISOU  646  CD1 PHE A 107     6537   6133   6871   -634   -145    216       C  
ATOM    647  CD2 PHE A 107       3.852  11.291  33.353  1.00 50.30           C  
ANISOU  647  CD2 PHE A 107     6379   5933   6801   -407    -70    148       C  
ATOM    648  CE1 PHE A 107       5.519  11.901  35.473  1.00 46.36           C  
ANISOU  648  CE1 PHE A 107     5989   5383   6242   -603   -139    149       C  
ATOM    649  CE2 PHE A 107       3.373  11.217  34.652  1.00 45.29           C  
ANISOU  649  CE2 PHE A 107     5816   5208   6184   -369    -57     94       C  
ATOM    650  CZ  PHE A 107       4.209  11.527  35.714  1.00 45.71           C  
ANISOU  650  CZ  PHE A 107     5933   5228   6205   -461    -88     86       C  
ATOM    651  N   HIS A 108       4.514   9.103  30.302  1.00 45.98           N  
ANISOU  651  N   HIS A 108     5575   5709   6185   -301    -36    194       N  
ATOM    652  CA  HIS A 108       3.535   8.029  30.283  1.00 47.06           C  
ANISOU  652  CA  HIS A 108     5716   5824   6341   -210    -29    136       C  
ATOM    653  C   HIS A 108       4.208   6.668  30.194  1.00 56.78           C  
ANISOU  653  C   HIS A 108     6907   7151   7518   -155    -11    108       C  
ATOM    654  O   HIS A 108       3.709   5.692  30.765  1.00 43.67           O  
ANISOU  654  O   HIS A 108     5261   5462   5869   -106    -13     51       O  
ATOM    655  CB  HIS A 108       2.572   8.304  29.118  1.00 47.10           C  
ANISOU  655  CB  HIS A 108     5741   5803   6352   -184    -44    164       C  
ATOM    656  CG  HIS A 108       2.019   7.087  28.444  1.00 47.50           C  
ANISOU  656  CG  HIS A 108     5792   5882   6372   -124    -58    139       C  
ATOM    657  ND1 HIS A 108       0.779   6.567  28.749  1.00 43.94           N  
ANISOU  657  ND1 HIS A 108     5356   5377   5961    -98    -84    121       N  
ATOM    658  CD2 HIS A 108       2.505   6.331  27.431  1.00 54.57           C  
ANISOU  658  CD2 HIS A 108     6696   6851   7189    -89    -57    141       C  
ATOM    659  CE1 HIS A 108       0.538   5.523  27.974  1.00 52.64           C  
ANISOU  659  CE1 HIS A 108     6485   6506   7009    -74   -116    110       C  
ATOM    660  NE2 HIS A 108       1.570   5.360  27.165  1.00 51.81           N  
ANISOU  660  NE2 HIS A 108     6392   6467   6826    -57    -96    113       N  
ATOM    661  N   ASN A 109       5.353   6.584  29.514  1.00 44.69           N  
ANISOU  661  N   ASN A 109     5326   5736   5917   -153     10    157       N  
ATOM    662  CA  ASN A 109       6.096   5.326  29.530  1.00 48.41           C  
ANISOU  662  CA  ASN A 109     5773   6301   6321    -69     43    141       C  
ATOM    663  C   ASN A 109       7.088   5.201  30.685  1.00 55.91           C  
ANISOU  663  C   ASN A 109     6660   7313   7272    -97     59    154       C  
ATOM    664  O   ASN A 109       7.583   4.098  30.937  1.00 56.38           O  
ANISOU  664  O   ASN A 109     6704   7435   7284    -13     89    134       O  
ATOM    665  CB  ASN A 109       6.831   5.128  28.204  1.00 45.53           C  
ANISOU  665  CB  ASN A 109     5387   6054   5860     -9     77    201       C  
ATOM    666  CG  ASN A 109       5.894   4.733  27.089  1.00 48.39           C  
ANISOU  666  CG  ASN A 109     5838   6358   6191     45     58    171       C  
ATOM    667  OD1 ASN A 109       4.879   4.080  27.325  1.00 59.13           O  
ANISOU  667  OD1 ASN A 109     7270   7620   7576     62     22    104       O  
ATOM    668  ND2 ASN A 109       6.218   5.137  25.869  1.00 64.22           N  
ANISOU  668  ND2 ASN A 109     7837   8427   8135     59     73    231       N  
ATOM    669  N   PHE A 110       7.377   6.287  31.397  1.00 45.00           N  
ANISOU  669  N   PHE A 110     5259   5908   5933   -214     32    189       N  
ATOM    670  CA  PHE A 110       8.423   6.309  32.411  1.00 45.33           C  
ANISOU  670  CA  PHE A 110     5239   6022   5963   -274     29    226       C  
ATOM    671  C   PHE A 110       7.884   6.155  33.829  1.00 55.90           C  
ANISOU  671  C   PHE A 110     6633   7250   7358   -294      9    148       C  
ATOM    672  O   PHE A 110       8.321   5.268  34.571  1.00 48.79           O  
ANISOU  672  O   PHE A 110     5696   6399   6444   -254     25    126       O  
ATOM    673  CB  PHE A 110       9.210   7.624  32.277  1.00 46.25           C  
ANISOU  673  CB  PHE A 110     5322   6184   6067   -420    -10    334       C  
ATOM    674  CG  PHE A 110      10.169   7.901  33.407  1.00 49.76           C  
ANISOU  674  CG  PHE A 110     5724   6681   6502   -536    -46    388       C  
ATOM    675  CD1 PHE A 110       9.755   8.593  34.539  1.00 54.90           C  
ANISOU  675  CD1 PHE A 110     6482   7183   7195   -634    -99    341       C  
ATOM    676  CD2 PHE A 110      11.497   7.507  33.318  1.00 53.60           C  
ANISOU  676  CD2 PHE A 110     6068   7373   6925   -544    -29    500       C  
ATOM    677  CE1 PHE A 110      10.638   8.860  35.571  1.00 52.29           C  
ANISOU  677  CE1 PHE A 110     6134   6890   6842   -759   -149    394       C  
ATOM    678  CE2 PHE A 110      12.387   7.776  34.344  1.00 50.89           C  
ANISOU  678  CE2 PHE A 110     5674   7093   6569   -672    -78    572       C  
ATOM    679  CZ  PHE A 110      11.957   8.452  35.472  1.00 51.08           C  
ANISOU  679  CZ  PHE A 110     5822   6951   6635   -792   -146    513       C  
ATOM    680  N   PHE A 111       6.955   7.021  34.225  1.00 46.97           N  
ANISOU  680  N   PHE A 111     5594   5972   6282   -342    -19    112       N  
ATOM    681  CA  PHE A 111       6.556   7.093  35.627  1.00 49.43           C  
ANISOU  681  CA  PHE A 111     5968   6183   6631   -364    -33     55       C  
ATOM    682  C   PHE A 111       6.001   5.798  36.206  1.00 45.36           C  
ANISOU  682  C   PHE A 111     5441   5658   6136   -263     -7    -19       C  
ATOM    683  O   PHE A 111       6.345   5.488  37.358  1.00 43.97           O  
ANISOU  683  O   PHE A 111     5265   5480   5962   -282    -10    -44       O  
ATOM    684  CB  PHE A 111       5.558   8.232  35.846  1.00 50.16           C  
ANISOU  684  CB  PHE A 111     6180   6119   6762   -387    -48     39       C  
ATOM    685  CG  PHE A 111       5.366   8.565  37.294  1.00 44.29           C  
ANISOU  685  CG  PHE A 111     5528   5271   6028   -415    -60     -2       C  
ATOM    686  CD1 PHE A 111       6.412   9.099  38.031  1.00 45.74           C  
ANISOU  686  CD1 PHE A 111     5745   5461   6173   -539   -105     32       C  
ATOM    687  CD2 PHE A 111       4.162   8.318  37.930  1.00 43.81           C  
ANISOU  687  CD2 PHE A 111     5521   5118   6008   -320    -29    -59       C  
ATOM    688  CE1 PHE A 111       6.254   9.395  39.369  1.00 46.57           C  
ANISOU  688  CE1 PHE A 111     5964   5459   6270   -566   -121    -10       C  
ATOM    689  CE2 PHE A 111       3.996   8.613  39.271  1.00 49.97           C  
ANISOU  689  CE2 PHE A 111     6399   5805   6783   -326    -29    -95       C  
ATOM    690  CZ  PHE A 111       5.043   9.151  39.992  1.00 45.75           C  
ANISOU  690  CZ  PHE A 111     5925   5256   6202   -447    -76    -79       C  
ATOM    691  N   PRO A 112       5.114   5.045  35.538  1.00 44.46           N  
ANISOU  691  N   PRO A 112     5331   5528   6033   -174      8    -53       N  
ATOM    692  CA  PRO A 112       4.545   3.866  36.218  1.00 45.79           C  
ANISOU  692  CA  PRO A 112     5507   5674   6218   -108     14   -113       C  
ATOM    693  C   PRO A 112       5.595   2.875  36.690  1.00 45.92           C  
ANISOU  693  C   PRO A 112     5478   5780   6191    -80     30   -122       C  
ATOM    694  O   PRO A 112       5.439   2.291  37.770  1.00 45.30           O  
ANISOU  694  O   PRO A 112     5407   5674   6131    -66     30   -164       O  
ATOM    695  CB  PRO A 112       3.637   3.247  35.142  1.00 42.82           C  
ANISOU  695  CB  PRO A 112     5151   5284   5836    -50      4   -120       C  
ATOM    696  CG  PRO A 112       3.298   4.372  34.239  1.00 42.52           C  
ANISOU  696  CG  PRO A 112     5124   5223   5810    -83     -4    -74       C  
ATOM    697  CD  PRO A 112       4.520   5.241  34.204  1.00 43.01           C  
ANISOU  697  CD  PRO A 112     5159   5340   5845   -147      4    -30       C  
ATOM    698  N   ILE A 113       6.685   2.709  35.944  1.00 46.25           N  
ANISOU  698  N   ILE A 113     5466   5938   6169    -63     48    -70       N  
ATOM    699  CA  ILE A 113       7.738   1.794  36.369  1.00 46.76           C  
ANISOU  699  CA  ILE A 113     5477   6109   6181    -11     75    -56       C  
ATOM    700  C   ILE A 113       8.391   2.297  37.653  1.00 47.97           C  
ANISOU  700  C   ILE A 113     5588   6283   6356   -103     58    -33       C  
ATOM    701  O   ILE A 113       8.548   1.546  38.624  1.00 48.56           O  
ANISOU  701  O   ILE A 113     5656   6362   6433    -76     63    -66       O  
ATOM    702  CB  ILE A 113       8.764   1.600  35.236  1.00 48.18           C  
ANISOU  702  CB  ILE A 113     5599   6432   6276     51    114     22       C  
ATOM    703  CG1 ILE A 113       8.159   0.738  34.122  1.00 59.15           C  
ANISOU  703  CG1 ILE A 113     7074   7786   7616    166    129    -19       C  
ATOM    704  CG2 ILE A 113      10.045   0.981  35.759  1.00 44.54           C  
ANISOU  704  CG2 ILE A 113     5049   6117   5757     99    150     80       C  
ATOM    705  CD1 ILE A 113       9.015   0.627  32.879  1.00 48.81           C  
ANISOU  705  CD1 ILE A 113     5737   6603   6207    251    177     55       C  
ATOM    706  N   ALA A 114       8.734   3.588  37.695  1.00 46.42           N  
ANISOU  706  N   ALA A 114     5383   6085   6170   -226     26     23       N  
ATOM    707  CA  ALA A 114       9.362   4.145  38.891  1.00 50.80           C  
ANISOU  707  CA  ALA A 114     5931   6643   6728   -341    -12     51       C  
ATOM    708  C   ALA A 114       8.416   4.113  40.085  1.00 45.80           C  
ANISOU  708  C   ALA A 114     5396   5862   6145   -341    -24    -42       C  
ATOM    709  O   ALA A 114       8.834   3.814  41.209  1.00 47.00           O  
ANISOU  709  O   ALA A 114     5541   6027   6290   -370    -37    -51       O  
ATOM    710  CB  ALA A 114       9.828   5.575  38.620  1.00 44.95           C  
ANISOU  710  CB  ALA A 114     5205   5899   5973   -490    -62    132       C  
ATOM    711  N   ALA A 115       7.129   4.365  39.853  1.00 42.95           N  
ANISOU  711  N   ALA A 115     5116   5375   5828   -296    -14    -99       N  
ATOM    712  CA  ALA A 115       6.176   4.427  40.954  1.00 50.79           C  
ANISOU  712  CA  ALA A 115     6193   6245   6860   -277    -12   -164       C  
ATOM    713  C   ALA A 115       5.924   3.044  41.539  1.00 54.81           C  
ANISOU  713  C   ALA A 115     6666   6779   7380   -194     10   -214       C  
ATOM    714  O   ALA A 115       5.920   2.866  42.767  1.00 46.32           O  
ANISOU  714  O   ALA A 115     5617   5672   6311   -205      7   -244       O  
ATOM    715  CB  ALA A 115       4.869   5.059  40.477  1.00 42.42           C  
ANISOU  715  CB  ALA A 115     5202   5077   5836   -235      0   -179       C  
ATOM    716  N   ILE A 116       5.706   2.049  40.674  1.00 41.63           N  
ANISOU  716  N   ILE A 116     4957   5157   5705   -114     26   -222       N  
ATOM    717  CA  ILE A 116       5.499   0.692  41.160  1.00 46.31           C  
ANISOU  717  CA  ILE A 116     5541   5760   6295    -44     35   -264       C  
ATOM    718  C   ILE A 116       6.759   0.166  41.837  1.00 51.61           C  
ANISOU  718  C   ILE A 116     6159   6525   6926    -47     42   -248       C  
ATOM    719  O   ILE A 116       6.681  -0.530  42.858  1.00 46.24           O  
ANISOU  719  O   ILE A 116     5485   5829   6254    -27     43   -283       O  
ATOM    720  CB  ILE A 116       5.045  -0.222  40.008  1.00 47.74           C  
ANISOU  720  CB  ILE A 116     5736   5949   6453     30     34   -271       C  
ATOM    721  CG1 ILE A 116       3.699   0.259  39.458  1.00 44.32           C  
ANISOU  721  CG1 ILE A 116     5339   5437   6064     20     16   -269       C  
ATOM    722  CG2 ILE A 116       4.955  -1.672  40.469  1.00 40.94           C  
ANISOU  722  CG2 ILE A 116     4898   5086   5571     94     31   -309       C  
ATOM    723  CD1 ILE A 116       2.665   0.553  40.532  1.00 40.73           C  
ANISOU  723  CD1 ILE A 116     4900   4909   5669     10     16   -282       C  
ATOM    724  N   PHE A 117       7.939   0.528  41.317  1.00 42.09           N  
ANISOU  724  N   PHE A 117     4890   5430   5675    -76     46   -179       N  
ATOM    725  CA  PHE A 117       9.179   0.129  41.974  1.00 48.02           C  
ANISOU  725  CA  PHE A 117     5564   6299   6384    -85     51   -131       C  
ATOM    726  C   PHE A 117       9.250   0.709  43.378  1.00 55.15           C  
ANISOU  726  C   PHE A 117     6492   7152   7312   -191     14   -142       C  
ATOM    727  O   PHE A 117       9.514  -0.012  44.352  1.00 51.95           O  
ANISOU  727  O   PHE A 117     6069   6768   6900   -170     16   -160       O  
ATOM    728  CB  PHE A 117      10.376   0.588  41.137  1.00 46.10           C  
ANISOU  728  CB  PHE A 117     5224   6206   6085   -112     59    -20       C  
ATOM    729  CG  PHE A 117      11.711   0.140  41.672  1.00 45.82           C  
ANISOU  729  CG  PHE A 117     5075   6336   5997   -110     69     68       C  
ATOM    730  CD1 PHE A 117      12.329   0.825  42.708  1.00 46.55           C  
ANISOU  730  CD1 PHE A 117     5134   6460   6094   -256     14    121       C  
ATOM    731  CD2 PHE A 117      12.356  -0.954  41.123  1.00 52.43           C  
ANISOU  731  CD2 PHE A 117     5852   7299   6769     44    131    110       C  
ATOM    732  CE1 PHE A 117      13.558   0.420  43.193  1.00 50.28           C  
ANISOU  732  CE1 PHE A 117     5482   7107   6517   -265     15    226       C  
ATOM    733  CE2 PHE A 117      13.588  -1.366  41.602  1.00 52.78           C  
ANISOU  733  CE2 PHE A 117     5774   7519   6760     68    150    214       C  
ATOM    734  CZ  PHE A 117      14.189  -0.680  42.641  1.00 50.05           C  
ANISOU  734  CZ  PHE A 117     5363   7224   6431    -94     89    278       C  
ATOM    735  N   ALA A 118       8.985   2.014  43.502  1.00 42.80           N  
ANISOU  735  N   ALA A 118     4992   5507   5765   -299    -22   -135       N  
ATOM    736  CA  ALA A 118       9.086   2.662  44.802  1.00 43.08           C  
ANISOU  736  CA  ALA A 118     5097   5474   5798   -401    -64   -145       C  
ATOM    737  C   ALA A 118       8.104   2.056  45.794  1.00 45.63           C  
ANISOU  737  C   ALA A 118     5484   5697   6155   -328    -40   -234       C  
ATOM    738  O   ALA A 118       8.463   1.790  46.948  1.00 49.49           O  
ANISOU  738  O   ALA A 118     5983   6191   6629   -359    -57   -244       O  
ATOM    739  CB  ALA A 118       8.847   4.165  44.655  1.00 43.63           C  
ANISOU  739  CB  ALA A 118     5276   5439   5862   -507   -104   -129       C  
ATOM    740  N   SER A 119       6.883   1.758  45.344  1.00 41.74           N  
ANISOU  740  N   SER A 119     5023   5132   5705   -234     -6   -284       N  
ATOM    741  CA  SER A 119       5.879   1.239  46.267  1.00 56.27           C  
ANISOU  741  CA  SER A 119     6909   6895   7577   -171     15   -343       C  
ATOM    742  C   SER A 119       6.204  -0.187  46.702  1.00 48.19           C  
ANISOU  742  C   SER A 119     5821   5940   6548   -117     24   -360       C  
ATOM    743  O   SER A 119       6.159  -0.508  47.900  1.00 47.66           O  
ANISOU  743  O   SER A 119     5775   5852   6481   -119     23   -386       O  
ATOM    744  CB  SER A 119       4.489   1.309  45.629  1.00 40.92           C  
ANISOU  744  CB  SER A 119     4990   4882   5674   -101     39   -357       C  
ATOM    745  OG  SER A 119       4.515   0.840  44.295  1.00 78.33           O  
ANISOU  745  OG  SER A 119     9675   9675  10414    -71     38   -337       O  
ATOM    746  N   ILE A 120       6.531  -1.066  45.747  1.00 45.13           N  
ANISOU  746  N   ILE A 120     5375   5626   6144    -59     34   -346       N  
ATOM    747  CA  ILE A 120       6.781  -2.450  46.132  1.00 43.43           C  
ANISOU  747  CA  ILE A 120     5136   5455   5912     10     43   -363       C  
ATOM    748  C   ILE A 120       8.040  -2.560  46.983  1.00 49.00           C  
ANISOU  748  C   ILE A 120     5787   6251   6582    -23     38   -330       C  
ATOM    749  O   ILE A 120       8.101  -3.391  47.897  1.00 49.27           O  
ANISOU  749  O   ILE A 120     5819   6289   6612      7     41   -352       O  
ATOM    750  CB  ILE A 120       6.840  -3.374  44.899  1.00 45.14           C  
ANISOU  750  CB  ILE A 120     5351   5706   6094     98     55   -358       C  
ATOM    751  CG1 ILE A 120       6.782  -4.842  45.336  1.00 43.64           C  
ANISOU  751  CG1 ILE A 120     5191   5510   5882    177     57   -388       C  
ATOM    752  CG2 ILE A 120       8.091  -3.122  44.074  1.00 43.43           C  
ANISOU  752  CG2 ILE A 120     5071   5609   5821    112     74   -293       C  
ATOM    753  CD1 ILE A 120       5.532  -5.209  46.110  1.00 40.07           C  
ANISOU  753  CD1 ILE A 120     4784   4961   5480    159     34   -429       C  
ATOM    754  N   TYR A 121       9.049  -1.718  46.746  1.00 48.36           N  
ANISOU  754  N   TYR A 121     5655   6251   6471   -100     23   -262       N  
ATOM    755  CA  TYR A 121      10.217  -1.804  47.611  1.00 50.79           C  
ANISOU  755  CA  TYR A 121     5897   6661   6741   -154      4   -206       C  
ATOM    756  C   TYR A 121      10.007  -1.123  48.956  1.00 51.65           C  
ANISOU  756  C   TYR A 121     6078   6686   6861   -260    -38   -234       C  
ATOM    757  O   TYR A 121      10.653  -1.514  49.933  1.00 50.18           O  
ANISOU  757  O   TYR A 121     5859   6556   6651   -289    -56   -212       O  
ATOM    758  CB  TYR A 121      11.450  -1.260  46.892  1.00 43.17           C  
ANISOU  758  CB  TYR A 121     4830   5844   5728   -209     -8    -90       C  
ATOM    759  CG  TYR A 121      12.035  -2.313  45.988  1.00 48.26           C  
ANISOU  759  CG  TYR A 121     5391   6617   6328    -62     50    -44       C  
ATOM    760  CD1 TYR A 121      12.917  -3.264  46.482  1.00 53.96           C  
ANISOU  760  CD1 TYR A 121     6033   7464   7005     12     74      9       C  
ATOM    761  CD2 TYR A 121      11.661  -2.396  44.655  1.00 54.03           C  
ANISOU  761  CD2 TYR A 121     6145   7335   7051     20     84    -55       C  
ATOM    762  CE1 TYR A 121      13.437  -4.247  45.665  1.00 52.01           C  
ANISOU  762  CE1 TYR A 121     5743   7321   6697    183    140     51       C  
ATOM    763  CE2 TYR A 121      12.174  -3.374  43.832  1.00 47.19           C  
ANISOU  763  CE2 TYR A 121     5244   6565   6120    176    142    -19       C  
ATOM    764  CZ  TYR A 121      13.062  -4.298  44.342  1.00 54.94           C  
ANISOU  764  CZ  TYR A 121     6161   7664   7049    267    175     34       C  
ATOM    765  OH  TYR A 121      13.576  -5.276  43.523  1.00 65.61           O  
ANISOU  765  OH  TYR A 121     7508   9103   8317    455    245     73       O  
ATOM    766  N   SER A 122       9.086  -0.162  49.056  1.00 48.83           N  
ANISOU  766  N   SER A 122     5831   6191   6529   -303    -49   -280       N  
ATOM    767  CA  SER A 122       8.693   0.301  50.381  1.00 51.38           C  
ANISOU  767  CA  SER A 122     6263   6412   6847   -354    -70   -322       C  
ATOM    768  C   SER A 122       8.002  -0.814  51.163  1.00 51.26           C  
ANISOU  768  C   SER A 122     6247   6370   6858   -256    -34   -381       C  
ATOM    769  O   SER A 122       8.251  -0.992  52.366  1.00 52.16           O  
ANISOU  769  O   SER A 122     6389   6478   6951   -287    -50   -392       O  
ATOM    770  CB  SER A 122       7.787   1.524  50.253  1.00 42.36           C  
ANISOU  770  CB  SER A 122     5257   5125   5712   -375    -70   -352       C  
ATOM    771  OG  SER A 122       8.460   2.581  49.591  1.00 51.81           O  
ANISOU  771  OG  SER A 122     6472   6335   6878   -485   -116   -293       O  
ATOM    772  N   MET A 123       7.165  -1.605  50.484  1.00 41.49           N  
ANISOU  772  N   MET A 123     4982   5121   5662   -150      5   -409       N  
ATOM    773  CA  MET A 123       6.556  -2.757  51.147  1.00 48.30           C  
ANISOU  773  CA  MET A 123     5839   5968   6545    -74     25   -446       C  
ATOM    774  C   MET A 123       7.610  -3.786  51.539  1.00 54.65           C  
ANISOU  774  C   MET A 123     6575   6873   7318    -58     18   -426       C  
ATOM    775  O   MET A 123       7.526  -4.403  52.613  1.00 45.41           O  
ANISOU  775  O   MET A 123     5414   5694   6147    -44     18   -447       O  
ATOM    776  CB  MET A 123       5.504  -3.398  50.241  1.00 39.94           C  
ANISOU  776  CB  MET A 123     4775   4878   5522      3     43   -460       C  
ATOM    777  CG  MET A 123       4.338  -2.490  49.912  1.00 52.00           C  
ANISOU  777  CG  MET A 123     6350   6326   7083      6     57   -461       C  
ATOM    778  SD  MET A 123       3.586  -1.810  51.400  1.00 66.25           S  
ANISOU  778  SD  MET A 123     8234   8050   8889     10     82   -479       S  
ATOM    779  CE  MET A 123       2.278  -0.818  50.691  1.00 61.02           C  
ANISOU  779  CE  MET A 123     7610   7320   8254     56    114   -452       C  
ATOM    780  N   THR A 124       8.623  -3.966  50.685  1.00 42.15           N  
ANISOU  780  N   THR A 124     4918   5395   5702    -47     18   -374       N  
ATOM    781  CA  THR A 124       9.704  -4.893  51.000  1.00 51.52           C  
ANISOU  781  CA  THR A 124     6030   6698   6847     -5     23   -331       C  
ATOM    782  C   THR A 124      10.479  -4.434  52.228  1.00 58.20           C  
ANISOU  782  C   THR A 124     6853   7591   7670   -108    -14   -295       C  
ATOM    783  O   THR A 124      10.853  -5.252  53.078  1.00 53.86           O  
ANISOU  783  O   THR A 124     6276   7085   7105    -78    -13   -290       O  
ATOM    784  CB  THR A 124      10.639  -5.023  49.799  1.00 49.51           C  
ANISOU  784  CB  THR A 124     5697   6567   6549     46     45   -258       C  
ATOM    785  OG1 THR A 124       9.906  -5.523  48.675  1.00 49.41           O  
ANISOU  785  OG1 THR A 124     5736   6495   6542    141     71   -298       O  
ATOM    786  CG2 THR A 124      11.795  -5.966  50.111  1.00 45.95           C  
ANISOU  786  CG2 THR A 124     5160   6257   6043    121     66   -191       C  
ATOM    787  N   ALA A 125      10.704  -3.123  52.350  1.00 50.65           N  
ANISOU  787  N   ALA A 125     5926   6614   6703   -238    -56   -269       N  
ATOM    788  CA  ALA A 125      11.387  -2.597  53.527  1.00 51.88           C  
ANISOU  788  CA  ALA A 125     6098   6791   6822   -365   -114   -233       C  
ATOM    789  C   ALA A 125      10.546  -2.782  54.784  1.00 55.31           C  
ANISOU  789  C   ALA A 125     6640   7107   7270   -353   -110   -316       C  
ATOM    790  O   ALA A 125      11.084  -3.081  55.856  1.00 49.11           O  
ANISOU  790  O   ALA A 125     5845   6360   6453   -396   -139   -298       O  
ATOM    791  CB  ALA A 125      11.732  -1.123  53.324  1.00 43.62           C  
ANISOU  791  CB  ALA A 125     5108   5718   5747   -522   -175   -188       C  
ATOM    792  N   VAL A 126       9.222  -2.635  54.668  1.00 49.71           N  
ANISOU  792  N   VAL A 126     6020   6267   6601   -287    -72   -393       N  
ATOM    793  CA  VAL A 126       8.364  -2.872  55.829  1.00 48.18           C  
ANISOU  793  CA  VAL A 126     5910   5981   6414   -252    -53   -453       C  
ATOM    794  C   VAL A 126       8.467  -4.326  56.279  1.00 54.40           C  
ANISOU  794  C   VAL A 126     6622   6833   7215   -175    -35   -458       C  
ATOM    795  O   VAL A 126       8.619  -4.622  57.477  1.00 50.66           O  
ANISOU  795  O   VAL A 126     6172   6358   6719   -193    -47   -468       O  
ATOM    796  CB  VAL A 126       6.909  -2.482  55.508  1.00 51.62           C  
ANISOU  796  CB  VAL A 126     6422   6303   6889   -179     -7   -500       C  
ATOM    797  CG1 VAL A 126       5.946  -3.164  56.470  1.00 40.74           C  
ANISOU  797  CG1 VAL A 126     5071   4881   5528   -102     30   -535       C  
ATOM    798  CG2 VAL A 126       6.738  -0.974  55.569  1.00 53.49           C  
ANISOU  798  CG2 VAL A 126     6792   6441   7090   -243    -22   -504       C  
ATOM    799  N   ALA A 127       8.407  -5.254  55.322  1.00 48.45           N  
ANISOU  799  N   ALA A 127     5796   6125   6486    -87     -9   -451       N  
ATOM    800  CA  ALA A 127       8.509  -6.667  55.671  1.00 55.61           C  
ANISOU  800  CA  ALA A 127     6664   7072   7393     -7      4   -455       C  
ATOM    801  C   ALA A 127       9.866  -6.987  56.284  1.00 54.12           C  
ANISOU  801  C   ALA A 127     6404   7001   7156    -33    -17   -399       C  
ATOM    802  O   ALA A 127       9.956  -7.772  57.235  1.00 51.66           O  
ANISOU  802  O   ALA A 127     6090   6702   6837     -8    -18   -405       O  
ATOM    803  CB  ALA A 127       8.262  -7.533  54.434  1.00 41.04           C  
ANISOU  803  CB  ALA A 127     4803   5233   5557     90     25   -456       C  
ATOM    804  N   PHE A 128      10.932  -6.371  55.767  1.00 48.35           N  
ANISOU  804  N   PHE A 128     5605   6371   6393    -90    -37   -326       N  
ATOM    805  CA  PHE A 128      12.261  -6.633  56.308  1.00 52.09           C  
ANISOU  805  CA  PHE A 128     5983   6993   6818   -123    -62   -237       C  
ATOM    806  C   PHE A 128      12.402  -6.086  57.722  1.00 56.64           C  
ANISOU  806  C   PHE A 128     6608   7539   7372   -250   -118   -240       C  
ATOM    807  O   PHE A 128      13.041  -6.712  58.577  1.00 54.69           O  
ANISOU  807  O   PHE A 128     6311   7372   7098   -250   -133   -200       O  
ATOM    808  CB  PHE A 128      13.325  -6.034  55.390  1.00 54.57           C  
ANISOU  808  CB  PHE A 128     6193   7444   7098   -168    -76   -129       C  
ATOM    809  CG  PHE A 128      14.727  -6.401  55.771  1.00 66.92           C  
ANISOU  809  CG  PHE A 128     7618   9204   8607   -182    -94      2       C  
ATOM    810  CD1 PHE A 128      15.248  -7.636  55.425  1.00 70.97           C  
ANISOU  810  CD1 PHE A 128     8047   9827   9093    -10    -32     49       C  
ATOM    811  CD2 PHE A 128      15.524  -5.514  56.478  1.00 74.11           C  
ANISOU  811  CD2 PHE A 128     8491  10188   9480   -367   -177     89       C  
ATOM    812  CE1 PHE A 128      16.539  -7.982  55.777  1.00 82.46           C  
ANISOU  812  CE1 PHE A 128     9354  11485  10491     -1    -38    192       C  
ATOM    813  CE2 PHE A 128      16.817  -5.851  56.832  1.00 65.84           C  
ANISOU  813  CE2 PHE A 128     7289   9348   8380   -391   -201    238       C  
ATOM    814  CZ  PHE A 128      17.325  -7.087  56.482  1.00 71.87           C  
ANISOU  814  CZ  PHE A 128     7940  10242   9123   -197   -124    295       C  
ATOM    815  N   ASP A 129      11.803  -4.925  57.992  1.00 50.03           N  
ANISOU  815  N   ASP A 129     5890   6582   6537   -349   -147   -286       N  
ATOM    816  CA  ASP A 129      11.846  -4.375  59.340  1.00 45.47           C  
ANISOU  816  CA  ASP A 129     5412   5945   5918   -459   -200   -301       C  
ATOM    817  C   ASP A 129      11.095  -5.270  60.319  1.00 59.62           C  
ANISOU  817  C   ASP A 129     7246   7678   7728   -369   -162   -369       C  
ATOM    818  O   ASP A 129      11.548  -5.481  61.454  1.00 51.82           O  
ANISOU  818  O   ASP A 129     6271   6718   6701   -421   -197   -352       O  
ATOM    819  CB  ASP A 129      11.263  -2.962  59.336  1.00 48.59           C  
ANISOU  819  CB  ASP A 129     5970   6198   6294   -546   -226   -342       C  
ATOM    820  CG  ASP A 129      11.336  -2.293  60.695  1.00 52.92           C  
ANISOU  820  CG  ASP A 129     6675   6662   6772   -658   -286   -359       C  
ATOM    821  OD1 ASP A 129      12.450  -1.918  61.119  1.00 64.10           O  
ANISOU  821  OD1 ASP A 129     8079   8152   8125   -813   -377   -279       O  
ATOM    822  OD2 ASP A 129      10.278  -2.134  61.334  1.00 61.45           O  
ANISOU  822  OD2 ASP A 129     7894   7607   7849   -591   -244   -442       O  
ATOM    823  N   ARG A 130       9.969  -5.845  59.882  1.00 55.03           N  
ANISOU  823  N   ARG A 130     6679   7026   7203   -245    -98   -431       N  
ATOM    824  CA  ARG A 130       9.247  -6.765  60.758  1.00 53.28           C  
ANISOU  824  CA  ARG A 130     6481   6763   6998   -170    -67   -475       C  
ATOM    825  C   ARG A 130      10.045  -8.044  60.997  1.00 56.59           C  
ANISOU  825  C   ARG A 130     6801   7291   7409   -120    -70   -434       C  
ATOM    826  O   ARG A 130      10.125  -8.537  62.134  1.00 57.87           O  
ANISOU  826  O   ARG A 130     6976   7460   7553   -124    -80   -438       O  
ATOM    827  CB  ARG A 130       7.875  -7.084  60.163  1.00 59.16           C  
ANISOU  827  CB  ARG A 130     7250   7427   7800    -74    -15   -520       C  
ATOM    828  CG  ARG A 130       6.937  -5.882  60.062  1.00 86.61           C  
ANISOU  828  CG  ARG A 130    10826  10801  11282    -88      5   -549       C  
ATOM    829  CD  ARG A 130       6.678  -5.252  61.426  1.00 92.72           C  
ANISOU  829  CD  ARG A 130    11718  11507  12004   -118      6   -573       C  
ATOM    830  NE  ARG A 130       7.689  -4.259  61.783  1.00 95.18           N  
ANISOU  830  NE  ARG A 130    12103  11813  12247   -241    -55   -559       N  
ATOM    831  CZ  ARG A 130       7.959  -3.882  63.028  1.00 93.50           C  
ANISOU  831  CZ  ARG A 130    12001  11561  11964   -301    -86   -569       C  
ATOM    832  NH1 ARG A 130       7.296  -4.418  64.043  1.00102.05           N  
ANISOU  832  NH1 ARG A 130    13120  12614  13038   -230    -46   -597       N  
ATOM    833  NH2 ARG A 130       8.896  -2.973  63.258  1.00 88.72           N  
ANISOU  833  NH2 ARG A 130    11475  10947  11288   -443   -165   -542       N  
ATOM    834  N   TYR A 131      10.664  -8.577  59.941  1.00 52.19           N  
ANISOU  834  N   TYR A 131     6154   6820   6855    -61    -58   -390       N  
ATOM    835  CA  TYR A 131      11.466  -9.786  60.076  1.00 51.54           C  
ANISOU  835  CA  TYR A 131     5993   6841   6750     21    -48   -341       C  
ATOM    836  C   TYR A 131      12.653  -9.556  60.999  1.00 61.26           C  
ANISOU  836  C   TYR A 131     7157   8190   7930    -65    -93   -263       C  
ATOM    837  O   TYR A 131      13.045 -10.453  61.749  1.00 51.16           O  
ANISOU  837  O   TYR A 131     5843   6964   6630    -20    -92   -238       O  
ATOM    838  CB  TYR A 131      11.933 -10.250  58.696  1.00 41.90           C  
ANISOU  838  CB  TYR A 131     4714   5689   5519    123    -14   -301       C  
ATOM    839  CG  TYR A 131      12.866 -11.451  58.668  1.00 42.49           C  
ANISOU  839  CG  TYR A 131     4721   5876   5546    248     12   -235       C  
ATOM    840  CD1 TYR A 131      14.231 -11.309  58.914  1.00 45.92           C  
ANISOU  840  CD1 TYR A 131     5029   6487   5930    228      1   -117       C  
ATOM    841  CD2 TYR A 131      12.389 -12.720  58.348  1.00 42.26           C  
ANISOU  841  CD2 TYR A 131     4765   5780   5513    388     44   -274       C  
ATOM    842  CE1 TYR A 131      15.086 -12.399  58.874  1.00 53.03           C  
ANISOU  842  CE1 TYR A 131     5864   7505   6780    373     40    -40       C  
ATOM    843  CE2 TYR A 131      13.239 -13.816  58.301  1.00 51.77           C  
ANISOU  843  CE2 TYR A 131     5940   7071   6657    529     77   -214       C  
ATOM    844  CZ  TYR A 131      14.585 -13.648  58.564  1.00 52.26           C  
ANISOU  844  CZ  TYR A 131     5864   7320   6673    537     84    -96       C  
ATOM    845  OH  TYR A 131      15.431 -14.731  58.519  1.00 59.06           O  
ANISOU  845  OH  TYR A 131     6692   8282   7467    707    130    -19       O  
ATOM    846  N   MET A 132      13.235  -8.356  60.971  1.00 56.18           N  
ANISOU  846  N   MET A 132     6500   7588   7259   -203   -144   -214       N  
ATOM    847  CA  MET A 132      14.349  -8.084  61.872  1.00 45.40           C  
ANISOU  847  CA  MET A 132     5076   6338   5836   -323   -211   -121       C  
ATOM    848  C   MET A 132      13.866  -7.938  63.307  1.00 58.27           C  
ANISOU  848  C   MET A 132     6824   7869   7449   -393   -245   -183       C  
ATOM    849  O   MET A 132      14.478  -8.486  64.230  1.00 59.16           O  
ANISOU  849  O   MET A 132     6889   8061   7528   -411   -273   -134       O  
ATOM    850  CB  MET A 132      15.106  -6.833  61.425  1.00 45.11           C  
ANISOU  850  CB  MET A 132     5009   6367   5764   -481   -278    -36       C  
ATOM    851  CG  MET A 132      15.926  -7.027  60.156  1.00 64.33           C  
ANISOU  851  CG  MET A 132     7285   8963   8194   -417   -247     72       C  
ATOM    852  SD  MET A 132      17.140  -8.360  60.272  1.00 68.71           S  
ANISOU  852  SD  MET A 132     7648   9751   8710   -284   -211    210       S  
ATOM    853  CE  MET A 132      18.235  -7.724  61.538  1.00 64.92           C  
ANISOU  853  CE  MET A 132     7102   9401   8165   -512   -334    344       C  
ATOM    854  N   ALA A 133      12.753  -7.227  63.516  1.00 60.03           N  
ANISOU  854  N   ALA A 133     7200   7923   7687   -416   -235   -282       N  
ATOM    855  CA  ALA A 133      12.264  -7.032  64.877  1.00 50.17           C  
ANISOU  855  CA  ALA A 133     6081   6578   6403   -461   -255   -337       C  
ATOM    856  C   ALA A 133      11.856  -8.346  65.529  1.00 55.91           C  
ANISOU  856  C   ALA A 133     6774   7313   7156   -344   -208   -365       C  
ATOM    857  O   ALA A 133      11.980  -8.492  66.749  1.00 73.14           O  
ANISOU  857  O   ALA A 133     9003   9491   9297   -386   -236   -366       O  
ATOM    858  CB  ALA A 133      11.088  -6.055  64.884  1.00 43.53           C  
ANISOU  858  CB  ALA A 133     5410   5565   5563   -460   -229   -424       C  
ATOM    859  N   ILE A 134      11.381  -9.314  64.749  1.00 60.80           N  
ANISOU  859  N   ILE A 134     7329   7936   7835   -208   -147   -383       N  
ATOM    860  CA  ILE A 134      10.878 -10.563  65.313  1.00 55.02           C  
ANISOU  860  CA  ILE A 134     6591   7188   7125   -109   -113   -408       C  
ATOM    861  C   ILE A 134      11.933 -11.666  65.309  1.00 60.21           C  
ANISOU  861  C   ILE A 134     7138   7975   7765    -49   -119   -336       C  
ATOM    862  O   ILE A 134      12.085 -12.380  66.300  1.00 63.67           O  
ANISOU  862  O   ILE A 134     7571   8434   8184    -33   -127   -325       O  
ATOM    863  CB  ILE A 134       9.598 -11.002  64.569  1.00 54.45           C  
ANISOU  863  CB  ILE A 134     6553   7023   7114    -13    -61   -463       C  
ATOM    864  CG1 ILE A 134       8.450 -10.048  64.907  1.00 51.65           C  
ANISOU  864  CG1 ILE A 134     6299   6557   6767    -42    -41   -515       C  
ATOM    865  CG2 ILE A 134       9.229 -12.434  64.926  1.00 55.11           C  
ANISOU  865  CG2 ILE A 134     6626   7100   7214     75    -44   -466       C  
ATOM    866  CD1 ILE A 134       7.164 -10.354  64.177  1.00 62.75           C  
ANISOU  866  CD1 ILE A 134     7714   7897   8230     32      1   -539       C  
ATOM    867  N   ILE A 135      12.673 -11.825  64.216  1.00 65.98           N  
ANISOU  867  N   ILE A 135     7781   8797   8492      0   -107   -278       N  
ATOM    868  CA  ILE A 135      13.633 -12.917  64.104  1.00 63.24           C  
ANISOU  868  CA  ILE A 135     7338   8575   8116    105    -91   -199       C  
ATOM    869  C   ILE A 135      14.986 -12.578  64.733  1.00 66.19           C  
ANISOU  869  C   ILE A 135     7599   9116   8433     19   -140    -81       C  
ATOM    870  O   ILE A 135      15.644 -13.463  65.288  1.00 64.33           O  
ANISOU  870  O   ILE A 135     7299   8977   8167     84   -136    -16       O  
ATOM    871  CB  ILE A 135      13.795 -13.315  62.625  1.00 63.82           C  
ANISOU  871  CB  ILE A 135     7382   8676   8192    231    -42   -179       C  
ATOM    872  CG1 ILE A 135      12.433 -13.621  61.998  1.00 62.34           C  
ANISOU  872  CG1 ILE A 135     7312   8323   8053    284    -16   -283       C  
ATOM    873  CG2 ILE A 135      14.720 -14.514  62.481  1.00 57.77           C  
ANISOU  873  CG2 ILE A 135     6550   8024   7375    388     -6    -97       C  
ATOM    874  CD1 ILE A 135      11.668 -14.715  62.715  1.00 60.17           C  
ANISOU  874  CD1 ILE A 135     7116   7955   7790    338    -14   -331       C  
ATOM    875  N   HIS A 136      15.424 -11.321  64.669  1.00 61.33           N  
ANISOU  875  N   HIS A 136     6963   8543   7798   -137   -196    -38       N  
ATOM    876  CA  HIS A 136      16.705 -10.903  65.245  1.00 46.73           C  
ANISOU  876  CA  HIS A 136     5006   6862   5887   -263   -269     98       C  
ATOM    877  C   HIS A 136      16.504  -9.631  66.061  1.00 48.96           C  
ANISOU  877  C   HIS A 136     5406   7055   6140   -478   -359     66       C  
ATOM    878  O   HIS A 136      16.988  -8.556  65.687  1.00 56.25           O  
ANISOU  878  O   HIS A 136     6321   8017   7034   -623   -422    126       O  
ATOM    879  CB  HIS A 136      17.747 -10.681  64.146  1.00 47.33           C  
ANISOU  879  CB  HIS A 136     4923   7118   5940   -247   -263    236       C  
ATOM    880  CG  HIS A 136      17.820 -11.791  63.144  1.00 65.95           C  
ANISOU  880  CG  HIS A 136     7221   9527   8309    -10   -162    251       C  
ATOM    881  ND1 HIS A 136      18.654 -12.879  63.293  1.00 72.20           N  
ANISOU  881  ND1 HIS A 136     7902  10470   9059    137   -121    356       N  
ATOM    882  CD2 HIS A 136      17.163 -11.979  61.975  1.00 75.83           C  
ANISOU  882  CD2 HIS A 136     8532  10688   9594    111    -95    176       C  
ATOM    883  CE1 HIS A 136      18.504 -13.690  62.261  1.00 75.49           C  
ANISOU  883  CE1 HIS A 136     8336  10872   9474    348    -30    338       C  
ATOM    884  NE2 HIS A 136      17.607 -13.167  61.446  1.00 74.46           N  
ANISOU  884  NE2 HIS A 136     8308  10595   9388    325    -20    228       N  
ATOM    885  N   PRO A 137      15.790  -9.722  67.189  1.00 57.22           N  
ANISOU  885  N   PRO A 137     6583   7978   7181   -500   -369    -25       N  
ATOM    886  CA  PRO A 137      15.504  -8.511  67.982  1.00 56.83           C  
ANISOU  886  CA  PRO A 137     6701   7812   7080   -674   -444    -70       C  
ATOM    887  C   PRO A 137      16.741  -7.769  68.465  1.00 67.93           C  
ANISOU  887  C   PRO A 137     8072   9335   8401   -887   -570     60       C  
ATOM    888  O   PRO A 137      16.691  -6.541  68.620  1.00 70.20           O  
ANISOU  888  O   PRO A 137     8507   9529   8636  -1052   -648     46       O  
ATOM    889  CB  PRO A 137      14.665  -9.047  69.150  1.00 54.48           C  
ANISOU  889  CB  PRO A 137     6516   7404   6780   -617   -414   -163       C  
ATOM    890  CG  PRO A 137      14.991 -10.491  69.234  1.00 52.79           C  
ANISOU  890  CG  PRO A 137     6163   7299   6597   -481   -369   -120       C  
ATOM    891  CD  PRO A 137      15.258 -10.937  67.828  1.00 60.46           C  
ANISOU  891  CD  PRO A 137     7007   8348   7615   -365   -314    -80       C  
ATOM    892  N   LEU A 138      17.841  -8.475  68.745  1.00 74.52           N  
ANISOU  892  N   LEU A 138     8731  10371   9213   -893   -601    197       N  
ATOM    893  CA  LEU A 138      19.040  -7.807  69.247  1.00 72.81           C  
ANISOU  893  CA  LEU A 138     8460  10293   8911  -1120   -738    353       C  
ATOM    894  C   LEU A 138      19.699  -6.925  68.194  1.00 75.92           C  
ANISOU  894  C   LEU A 138     8770  10783   9293  -1235   -789    464       C  
ATOM    895  O   LEU A 138      20.366  -5.945  68.545  1.00 77.71           O  
ANISOU  895  O   LEU A 138     9039  11045   9442  -1483   -929    562       O  
ATOM    896  CB  LEU A 138      20.039  -8.839  69.767  1.00 72.27           C  
ANISOU  896  CB  LEU A 138     8192  10445   8822  -1076   -748    497       C  
ATOM    897  CG  LEU A 138      20.103  -8.998  71.288  1.00 70.33           C  
ANISOU  897  CG  LEU A 138     8038  10168   8516  -1174   -821    488       C  
ATOM    898  CD1 LEU A 138      18.748  -9.416  71.841  1.00 58.01           C  
ANISOU  898  CD1 LEU A 138     6664   8385   6994  -1040   -735    288       C  
ATOM    899  CD2 LEU A 138      21.179  -9.998  71.677  1.00 70.59           C  
ANISOU  899  CD2 LEU A 138     7846  10445   8528  -1125   -830    658       C  
ATOM    900  N   GLN A 139      19.543  -7.253  66.917  1.00 62.27           N  
ANISOU  900  N   GLN A 139     6933   9095   7630  -1073   -688    459       N  
ATOM    901  CA  GLN A 139      20.244  -6.509  65.881  1.00 67.31           C  
ANISOU  901  CA  GLN A 139     7463   9856   8255  -1167   -728    586       C  
ATOM    902  C   GLN A 139      19.617  -5.128  65.697  1.00 64.21           C  
ANISOU  902  C   GLN A 139     7287   9262   7846  -1328   -791    494       C  
ATOM    903  O   GLN A 139      18.390  -4.990  65.759  1.00 68.08           O  
ANISOU  903  O   GLN A 139     7967   9527   8373  -1243   -730    311       O  
ATOM    904  CB  GLN A 139      20.233  -7.283  64.565  1.00 74.27           C  
ANISOU  904  CB  GLN A 139     8192  10829   9197   -929   -594    602       C  
ATOM    905  CG  GLN A 139      20.892  -8.651  64.675  1.00 83.97           C  
ANISOU  905  CG  GLN A 139     9236  12246  10422   -739   -522    700       C  
ATOM    906  CD  GLN A 139      21.210  -9.273  63.327  1.00 99.47           C  
ANISOU  906  CD  GLN A 139    11053  14338  12403   -522   -408    767       C  
ATOM    907  OE1 GLN A 139      21.278  -8.583  62.309  1.00101.78           O  
ANISOU  907  OE1 GLN A 139    11318  14652  12702   -556   -404    798       O  
ATOM    908  NE2 GLN A 139      21.412 -10.587  63.317  1.00102.91           N  
ANISOU  908  NE2 GLN A 139    11413  14853  12837   -288   -314    791       N  
ATOM    909  N   PRO A 140      20.427  -4.088  65.497  1.00 75.63           N  
ANISOU  909  N   PRO A 140     8715  10789   9231  -1563   -917    630       N  
ATOM    910  CA  PRO A 140      19.873  -2.743  65.320  1.00 81.18           C  
ANISOU  910  CA  PRO A 140     9654  11285   9904  -1716   -985    548       C  
ATOM    911  C   PRO A 140      19.010  -2.649  64.070  1.00 74.64           C  
ANISOU  911  C   PRO A 140     8844  10358   9158  -1546   -865    440       C  
ATOM    912  O   PRO A 140      19.282  -3.280  63.047  1.00 72.51           O  
ANISOU  912  O   PRO A 140     8371  10238   8944  -1398   -777    500       O  
ATOM    913  CB  PRO A 140      21.121  -1.860  65.202  1.00 84.34           C  
ANISOU  913  CB  PRO A 140     9975  11847  10223  -2002  -1150    764       C  
ATOM    914  CG  PRO A 140      22.160  -2.772  64.647  1.00 79.96           C  
ANISOU  914  CG  PRO A 140     9070  11617   9696  -1907  -1102    958       C  
ATOM    915  CD  PRO A 140      21.881  -4.124  65.254  1.00 79.56           C  
ANISOU  915  CD  PRO A 140     8956  11587   9684  -1679   -993    886       C  
ATOM    916  N   ARG A 141      17.962  -1.840  64.165  1.00 74.07           N  
ANISOU  916  N   ARG A 141     9030  10031   9081  -1561   -861    286       N  
ATOM    917  CA  ARG A 141      17.077  -1.549  63.050  1.00 77.45           C  
ANISOU  917  CA  ARG A 141     9503  10348   9575  -1434   -768    189       C  
ATOM    918  C   ARG A 141      17.292  -0.112  62.585  1.00 74.13           C  
ANISOU  918  C   ARG A 141     9212   9852   9100  -1635   -870    233       C  
ATOM    919  O   ARG A 141      18.086   0.642  63.154  1.00 77.44           O  
ANISOU  919  O   ARG A 141     9705  10292   9425  -1882  -1021    335       O  
ATOM    920  CB  ARG A 141      15.619  -1.797  63.436  1.00 80.43           C  
ANISOU  920  CB  ARG A 141    10055  10511   9994  -1261   -666     -3       C  
ATOM    921  CG  ARG A 141      15.196  -3.254  63.371  1.00 69.67           C  
ANISOU  921  CG  ARG A 141     8550   9212   8710  -1034   -546    -51       C  
ATOM    922  CD  ARG A 141      13.765  -3.410  63.842  1.00 52.60           C  
ANISOU  922  CD  ARG A 141     6550   6857   6578   -900   -465   -207       C  
ATOM    923  NE  ARG A 141      13.639  -3.123  65.267  1.00 71.35           N  
ANISOU  923  NE  ARG A 141     9094   9137   8877   -979   -516   -245       N  
ATOM    924  CZ  ARG A 141      12.501  -2.786  65.863  1.00 82.85           C  
ANISOU  924  CZ  ARG A 141    10749  10414  10317   -910   -469   -357       C  
ATOM    925  NH1 ARG A 141      12.482  -2.548  67.167  1.00 76.20           N  
ANISOU  925  NH1 ARG A 141    10069   9493   9389   -973   -514   -383       N  
ATOM    926  NH2 ARG A 141      11.385  -2.677  65.154  1.00 90.19           N  
ANISOU  926  NH2 ARG A 141    11711  11250  11306   -771   -375   -431       N  
ATOM    927  N   LEU A 142      16.585   0.254  61.521  1.00 71.47           N  
ANISOU  927  N   LEU A 142     8909   9428   8818  -1537   -797    165       N  
ATOM    928  CA  LEU A 142      16.721   1.586  60.953  1.00 70.65           C  
ANISOU  928  CA  LEU A 142     8930   9244   8668  -1707   -882    203       C  
ATOM    929  C   LEU A 142      16.186   2.658  61.896  1.00 62.59           C  
ANISOU  929  C   LEU A 142     8260   7967   7554  -1830   -964    113       C  
ATOM    930  O   LEU A 142      15.126   2.503  62.508  1.00 66.70           O  
ANISOU  930  O   LEU A 142     8946   8317   8080  -1685   -885    -35       O  
ATOM    931  CB  LEU A 142      15.984   1.665  59.617  1.00 73.43           C  
ANISOU  931  CB  LEU A 142     9244   9553   9102  -1549   -774    141       C  
ATOM    932  CG  LEU A 142      16.486   0.773  58.482  1.00 75.73           C  
ANISOU  932  CG  LEU A 142     9242  10069   9463  -1421   -693    228       C  
ATOM    933  CD1 LEU A 142      15.519   0.823  57.313  1.00 65.51           C  
ANISOU  933  CD1 LEU A 142     7967   8684   8241  -1258   -587    133       C  
ATOM    934  CD2 LEU A 142      17.878   1.201  58.049  1.00 80.41           C  
ANISOU  934  CD2 LEU A 142     9670  10876  10005  -1610   -795    438       C  
ATOM    935  N   SER A 143      16.931   3.756  61.998  1.00 61.29           N  
ANISOU  935  N   SER A 143     8219   7778   7292  -2099  -1125    214       N  
ATOM    936  CA  SER A 143      16.442   5.001  62.567  1.00 62.02           C  
ANISOU  936  CA  SER A 143     8695   7594   7274  -2219  -1210    135       C  
ATOM    937  C   SER A 143      15.591   5.739  61.535  1.00 75.89           C  
ANISOU  937  C   SER A 143    10565   9202   9067  -2120  -1138     57       C  
ATOM    938  O   SER A 143      15.609   5.422  60.343  1.00 70.72           O  
ANISOU  938  O   SER A 143     9683   8677   8510  -2027  -1062     94       O  
ATOM    939  CB  SER A 143      17.605   5.879  63.024  1.00 63.56           C  
ANISOU  939  CB  SER A 143     8999   7813   7337  -2573  -1433    288       C  
ATOM    940  OG  SER A 143      18.500   6.130  61.953  1.00 71.62           O  
ANISOU  940  OG  SER A 143     9797   9030   8386  -2712  -1496    461       O  
ATOM    941  N   LEU A 144      14.816   6.719  62.010  1.00 71.09           N  
ANISOU  941  N   LEU A 144    10326   8315   8370  -2122  -1156    -52       N  
ATOM    942  CA  LEU A 144      13.917   7.439  61.111  1.00 75.10           C  
ANISOU  942  CA  LEU A 144    10959   8670   8906  -2003  -1079   -126       C  
ATOM    943  C   LEU A 144      14.683   8.159  60.003  1.00 73.52           C  
ANISOU  943  C   LEU A 144    10681   8547   8706  -2190  -1176      2       C  
ATOM    944  O   LEU A 144      14.270   8.134  58.833  1.00 69.76           O  
ANISOU  944  O   LEU A 144    10073   8110   8321  -2065  -1083     -8       O  
ATOM    945  CB  LEU A 144      13.067   8.435  61.902  1.00 65.47           C  
ANISOU  945  CB  LEU A 144    10179   7137   7561  -1969  -1087   -243       C  
ATOM    946  CG  LEU A 144      12.039   7.884  62.895  1.00 78.32           C  
ANISOU  946  CG  LEU A 144    11914   8664   9180  -1733   -958   -374       C  
ATOM    947  CD1 LEU A 144      12.656   7.636  64.269  1.00 96.86           C  
ANISOU  947  CD1 LEU A 144    14367  11011  11426  -1869  -1059   -359       C  
ATOM    948  CD2 LEU A 144      10.853   8.829  62.998  1.00 77.31           C  
ANISOU  948  CD2 LEU A 144    12134   8264   8976  -1570   -880   -483       C  
ATOM    949  N   THR A 145      15.810   8.791  60.343  1.00 59.00           N  
ANISOU  949  N   THR A 145     8915   6742   6761  -2503  -1371    138       N  
ATOM    950  CA  THR A 145      16.620   9.432  59.312  1.00 75.93           C  
ANISOU  950  CA  THR A 145    10953   8993   8902  -2702  -1473    291       C  
ATOM    951  C   THR A 145      17.192   8.402  58.345  1.00 73.37           C  
ANISOU  951  C   THR A 145    10173   8997   8708  -2613  -1388    401       C  
ATOM    952  O   THR A 145      17.289   8.653  57.135  1.00 75.42           O  
ANISOU  952  O   THR A 145    10301   9335   9019  -2602  -1360    461       O  
ATOM    953  CB  THR A 145      17.745  10.246  59.953  1.00 77.94           C  
ANISOU  953  CB  THR A 145    11364   9240   9009  -3083  -1718    443       C  
ATOM    954  OG1 THR A 145      18.536   9.396  60.792  1.00 87.30           O  
ANISOU  954  OG1 THR A 145    12363  10623  10184  -3162  -1770    531       O  
ATOM    955  CG2 THR A 145      17.173  11.382  60.788  1.00 67.51           C  
ANISOU  955  CG2 THR A 145    10561   7556   7532  -3168  -1809    330       C  
ATOM    956  N   ALA A 146      17.539   7.218  58.857  1.00 66.32           N  
ANISOU  956  N   ALA A 146     9051   8288   7859  -2527  -1337    424       N  
ATOM    957  CA  ALA A 146      18.013   6.158  57.979  1.00 63.95           C  
ANISOU  957  CA  ALA A 146     8357   8277   7664  -2393  -1236    515       C  
ATOM    958  C   ALA A 146      16.913   5.711  57.027  1.00 60.82           C  
ANISOU  958  C   ALA A 146     7908   7821   7379  -2099  -1051    376       C  
ATOM    959  O   ALA A 146      17.181   5.392  55.863  1.00 61.43           O  
ANISOU  959  O   ALA A 146     7760   8063   7520  -2022   -989    448       O  
ATOM    960  CB  ALA A 146      18.523   4.981  58.808  1.00 55.41           C  
ANISOU  960  CB  ALA A 146     7088   7370   6594  -2339  -1216    556       C  
ATOM    961  N   THR A 147      15.661   5.712  57.492  1.00 56.75           N  
ANISOU  961  N   THR A 147     7604   7078   6880  -1935   -966    190       N  
ATOM    962  CA  THR A 147      14.560   5.350  56.607  1.00 64.63           C  
ANISOU  962  CA  THR A 147     8559   8021   7977  -1683   -810     77       C  
ATOM    963  C   THR A 147      14.316   6.422  55.556  1.00 63.13           C  
ANISOU  963  C   THR A 147     8462   7741   7784  -1732   -828     90       C  
ATOM    964  O   THR A 147      13.978   6.101  54.412  1.00 55.84           O  
ANISOU  964  O   THR A 147     7391   6886   6941  -1594   -734     83       O  
ATOM    965  CB  THR A 147      13.288   5.089  57.410  1.00 64.93           C  
ANISOU  965  CB  THR A 147     8773   7869   8027  -1501   -718    -90       C  
ATOM    966  OG1 THR A 147      12.894   6.287  58.089  1.00 96.45           O  
ANISOU  966  OG1 THR A 147    13105  11624  11918  -1595   -786   -144       O  
ATOM    967  CG2 THR A 147      13.533   4.000  58.418  1.00 62.52           C  
ANISOU  967  CG2 THR A 147     8371   7658   7728  -1455   -701    -99       C  
ATOM    968  N   LYS A 148      14.486   7.699  55.912  1.00 58.06           N  
ANISOU  968  N   LYS A 148     8083   6936   7040  -1931   -953    112       N  
ATOM    969  CA  LYS A 148      14.374   8.736  54.890  1.00 65.03           C  
ANISOU  969  CA  LYS A 148     9053   7743   7913  -1998   -984    143       C  
ATOM    970  C   LYS A 148      15.461   8.573  53.831  1.00 69.51           C  
ANISOU  970  C   LYS A 148     9328   8570   8512  -2107  -1023    316       C  
ATOM    971  O   LYS A 148      15.205   8.735  52.627  1.00 62.33           O  
ANISOU  971  O   LYS A 148     8332   7693   7659  -2029   -962    327       O  
ATOM    972  CB  LYS A 148      14.449  10.125  55.527  1.00 64.65           C  
ANISOU  972  CB  LYS A 148     9377   7458   7728  -2209  -1130    145       C  
ATOM    973  CG  LYS A 148      13.309  10.452  56.481  1.00 71.09           C  
ANISOU  973  CG  LYS A 148    10525   7998   8487  -2067  -1074    -21       C  
ATOM    974  CD  LYS A 148      13.528  11.805  57.140  1.00 84.95           C  
ANISOU  974  CD  LYS A 148    12690   9509  10076  -2285  -1233    -11       C  
ATOM    975  CE  LYS A 148      12.552  12.038  58.281  1.00 95.54           C  
ANISOU  975  CE  LYS A 148    14373  10596  11332  -2133  -1177   -160       C  
ATOM    976  NZ  LYS A 148      12.922  13.241  59.082  1.00 96.62           N  
ANISOU  976  NZ  LYS A 148    14945  10490  11275  -2361  -1352   -147       N  
ATOM    977  N   VAL A 149      16.670   8.201  54.261  1.00 65.39           N  
ANISOU  977  N   VAL A 149     8638   8254   7954  -2270  -1116    465       N  
ATOM    978  CA  VAL A 149      17.746   7.951  53.304  1.00 66.24           C  
ANISOU  978  CA  VAL A 149     8435   8650   8082  -2343  -1134    657       C  
ATOM    979  C   VAL A 149      17.411   6.754  52.421  1.00 68.53           C  
ANISOU  979  C   VAL A 149     8470   9090   8480  -2050   -953    614       C  
ATOM    980  O   VAL A 149      17.641   6.776  51.203  1.00 62.94           O  
ANISOU  980  O   VAL A 149     7604   8508   7804  -2005   -908    690       O  
ATOM    981  CB  VAL A 149      19.080   7.748  54.044  1.00 68.09           C  
ANISOU  981  CB  VAL A 149     8527   9096   8248  -2562  -1266    846       C  
ATOM    982  CG1 VAL A 149      20.136   7.199  53.099  1.00 64.26           C  
ANISOU  982  CG1 VAL A 149     7666   8959   7790  -2553  -1237   1055       C  
ATOM    983  CG2 VAL A 149      19.546   9.052  54.674  1.00 59.15           C  
ANISOU  983  CG2 VAL A 149     7654   7828   6992  -2907  -1481    928       C  
ATOM    984  N   VAL A 150      16.852   5.698  53.016  1.00 62.04           N  
ANISOU  984  N   VAL A 150     7622   8246   7704  -1851   -851    493       N  
ATOM    985  CA  VAL A 150      16.492   4.512  52.245  1.00 53.18           C  
ANISOU  985  CA  VAL A 150     6306   7233   6666  -1584   -695    445       C  
ATOM    986  C   VAL A 150      15.400   4.844  51.238  1.00 52.00           C  
ANISOU  986  C   VAL A 150     6247   6939   6573  -1450   -612    333       C  
ATOM    987  O   VAL A 150      15.398   4.336  50.112  1.00 60.54           O  
ANISOU  987  O   VAL A 150     7172   8132   7696  -1315   -528    357       O  
ATOM    988  CB  VAL A 150      16.062   3.373  53.190  1.00 59.20           C  
ANISOU  988  CB  VAL A 150     7062   7973   7458  -1428   -625    341       C  
ATOM    989  CG1 VAL A 150      15.358   2.261  52.420  1.00 48.15           C  
ANISOU  989  CG1 VAL A 150     5560   6599   6137  -1158   -477    253       C  
ATOM    990  CG2 VAL A 150      17.260   2.819  53.943  1.00 50.71           C  
ANISOU  990  CG2 VAL A 150     5829   7103   6337  -1520   -686    478       C  
ATOM    991  N   ILE A 151      14.469   5.721  51.616  1.00 50.84           N  
ANISOU  991  N   ILE A 151     6361   6542   6414  -1480   -635    220       N  
ATOM    992  CA  ILE A 151      13.402   6.114  50.702  1.00 59.48           C  
ANISOU  992  CA  ILE A 151     7539   7505   7557  -1357   -561    131       C  
ATOM    993  C   ILE A 151      13.966   6.909  49.530  1.00 61.00           C  
ANISOU  993  C   ILE A 151     7673   7769   7734  -1468   -607    245       C  
ATOM    994  O   ILE A 151      13.560   6.717  48.372  1.00 65.28           O  
ANISOU  994  O   ILE A 151     8128   8346   8328  -1342   -527    230       O  
ATOM    995  CB  ILE A 151      12.322   6.903  51.466  1.00 56.99           C  
ANISOU  995  CB  ILE A 151     7520   6918   7215  -1341   -566      6       C  
ATOM    996  CG1 ILE A 151      11.575   5.982  52.436  1.00 49.34           C  
ANISOU  996  CG1 ILE A 151     6573   5899   6276  -1183   -489   -105       C  
ATOM    997  CG2 ILE A 151      11.359   7.571  50.502  1.00 52.44           C  
ANISOU  997  CG2 ILE A 151     7037   6216   6672  -1250   -511    -47       C  
ATOM    998  CD1 ILE A 151      10.612   6.710  53.350  1.00 48.12           C  
ANISOU  998  CD1 ILE A 151     6705   5506   6074  -1149   -484   -206       C  
ATOM    999  N   CYS A 152      14.935   7.790  49.801  1.00 56.51           N  
ANISOU  999  N   CYS A 152     7151   7232   7087  -1720   -745    371       N  
ATOM   1000  CA  CYS A 152      15.569   8.522  48.707  1.00 68.57           C  
ANISOU 1000  CA  CYS A 152     8601   8856   8596  -1848   -798    508       C  
ATOM   1001  C   CYS A 152      16.332   7.581  47.779  1.00 64.51           C  
ANISOU 1001  C   CYS A 152     7761   8635   8114  -1751   -725    626       C  
ATOM   1002  O   CYS A 152      16.282   7.729  46.551  1.00 66.43           O  
ANISOU 1002  O   CYS A 152     7919   8940   8381  -1692   -677    664       O  
ATOM   1003  CB  CYS A 152      16.499   9.599  49.262  1.00 69.67           C  
ANISOU 1003  CB  CYS A 152     8855   8981   8634  -2168   -983    643       C  
ATOM   1004  SG  CYS A 152      15.657  10.984  50.053  1.00 78.23           S  
ANISOU 1004  SG  CYS A 152    10396   9685   9641  -2284  -1077    520       S  
ATOM   1005  N   VAL A 153      17.024   6.589  48.348  1.00 59.14           N  
ANISOU 1005  N   VAL A 153     6908   8134   7427  -1714   -709    686       N  
ATOM   1006  CA  VAL A 153      17.747   5.621  47.524  1.00 52.70           C  
ANISOU 1006  CA  VAL A 153     5806   7594   6624  -1577   -621    800       C  
ATOM   1007  C   VAL A 153      16.770   4.804  46.690  1.00 59.67           C  
ANISOU 1007  C   VAL A 153     6680   8417   7573  -1296   -471    657       C  
ATOM   1008  O   VAL A 153      17.034   4.486  45.521  1.00 56.61           O  
ANISOU 1008  O   VAL A 153     6152   8171   7187  -1186   -399    723       O  
ATOM   1009  CB  VAL A 153      18.626   4.719  48.412  1.00 58.56           C  
ANISOU 1009  CB  VAL A 153     6390   8524   7337  -1574   -630    892       C  
ATOM   1010  CG1 VAL A 153      19.169   3.541  47.615  1.00 52.53           C  
ANISOU 1010  CG1 VAL A 153     5373   8008   6578  -1351   -504    976       C  
ATOM   1011  CG2 VAL A 153      19.762   5.518  49.027  1.00 60.66           C  
ANISOU 1011  CG2 VAL A 153     6618   8905   7526  -1879   -795   1087       C  
ATOM   1012  N   ILE A 154      15.608   4.493  47.265  1.00 53.29           N  
ANISOU 1012  N   ILE A 154     6035   7401   6812  -1187   -428    470       N  
ATOM   1013  CA  ILE A 154      14.595   3.732  46.545  1.00 58.98           C  
ANISOU 1013  CA  ILE A 154     6764   8053   7591   -955   -310    343       C  
ATOM   1014  C   ILE A 154      14.099   4.528  45.348  1.00 58.18           C  
ANISOU 1014  C   ILE A 154     6715   7884   7507   -957   -299    336       C  
ATOM   1015  O   ILE A 154      13.968   4.000  44.237  1.00 47.15           O  
ANISOU 1015  O   ILE A 154     5232   6560   6123   -815   -222    338       O  
ATOM   1016  CB  ILE A 154      13.437   3.359  47.490  1.00 47.59           C  
ANISOU 1016  CB  ILE A 154     5476   6415   6191   -871   -282    176       C  
ATOM   1017  CG1 ILE A 154      13.822   2.179  48.385  1.00 56.50           C  
ANISOU 1017  CG1 ILE A 154     6520   7633   7314   -798   -258    172       C  
ATOM   1018  CG2 ILE A 154      12.169   3.057  46.705  1.00 45.60           C  
ANISOU 1018  CG2 ILE A 154     5281   6048   5996   -705   -200     61       C  
ATOM   1019  CD1 ILE A 154      12.751   1.802  49.390  1.00 45.29           C  
ANISOU 1019  CD1 ILE A 154     5237   6042   5929   -729   -235     28       C  
ATOM   1020  N   TRP A 155      13.823   5.817  45.554  1.00 49.04           N  
ANISOU 1020  N   TRP A 155     5719   6577   6336  -1114   -378    328       N  
ATOM   1021  CA  TRP A 155      13.345   6.633  44.443  1.00 54.96           C  
ANISOU 1021  CA  TRP A 155     6527   7256   7101  -1118   -371    326       C  
ATOM   1022  C   TRP A 155      14.419   6.823  43.377  1.00 51.58           C  
ANISOU 1022  C   TRP A 155     5922   7039   6636  -1183   -386    493       C  
ATOM   1023  O   TRP A 155      14.111   6.848  42.179  1.00 55.86           O  
ANISOU 1023  O   TRP A 155     6425   7603   7196  -1093   -330    493       O  
ATOM   1024  CB  TRP A 155      12.837   7.976  44.957  1.00 56.25           C  
ANISOU 1024  CB  TRP A 155     6932   7197   7242  -1258   -452    285       C  
ATOM   1025  CG  TRP A 155      11.376   7.933  45.258  1.00 54.22           C  
ANISOU 1025  CG  TRP A 155     6835   6734   7031  -1108   -386    126       C  
ATOM   1026  CD1 TRP A 155      10.791   7.939  46.488  1.00 51.23           C  
ANISOU 1026  CD1 TRP A 155     6611   6211   6645  -1085   -389     34       C  
ATOM   1027  CD2 TRP A 155      10.311   7.845  44.305  1.00 50.71           C  
ANISOU 1027  CD2 TRP A 155     6397   6230   6642   -952   -305     60       C  
ATOM   1028  NE1 TRP A 155       9.424   7.877  46.361  1.00 47.80           N  
ANISOU 1028  NE1 TRP A 155     6263   5642   6257   -919   -308    -71       N  
ATOM   1029  CE2 TRP A 155       9.104   7.816  45.030  1.00 46.03           C  
ANISOU 1029  CE2 TRP A 155     5946   5468   6074   -844   -262    -55       C  
ATOM   1030  CE3 TRP A 155      10.262   7.797  42.908  1.00 46.43           C  
ANISOU 1030  CE3 TRP A 155     5753   5767   6123   -896   -267     98       C  
ATOM   1031  CZ2 TRP A 155       7.859   7.741  44.406  1.00 50.81           C  
ANISOU 1031  CZ2 TRP A 155     6575   5999   6732   -694   -190   -116       C  
ATOM   1032  CZ3 TRP A 155       9.027   7.719  42.291  1.00 45.95           C  
ANISOU 1032  CZ3 TRP A 155     5735   5611   6111   -755   -203     21       C  
ATOM   1033  CH2 TRP A 155       7.842   7.693  43.040  1.00 47.26           C  
ANISOU 1033  CH2 TRP A 155     6026   5625   6307   -661   -168    -77       C  
ATOM   1034  N   VAL A 156      15.686   6.930  43.783  1.00 55.74           N  
ANISOU 1034  N   VAL A 156     6330   7740   7107  -1337   -459    650       N  
ATOM   1035  CA  VAL A 156      16.754   7.076  42.796  1.00 55.98           C  
ANISOU 1035  CA  VAL A 156     6162   8011   7096  -1390   -465    842       C  
ATOM   1036  C   VAL A 156      16.858   5.818  41.943  1.00 57.33           C  
ANISOU 1036  C   VAL A 156     6160   8349   7275  -1133   -325    846       C  
ATOM   1037  O   VAL A 156      16.958   5.884  40.709  1.00 61.24           O  
ANISOU 1037  O   VAL A 156     6578   8932   7757  -1060   -273    902       O  
ATOM   1038  CB  VAL A 156      18.090   7.402  43.488  1.00 60.05           C  
ANISOU 1038  CB  VAL A 156     6564   8707   7546  -1616   -579   1040       C  
ATOM   1039  CG1 VAL A 156      19.235   7.304  42.492  1.00 54.75           C  
ANISOU 1039  CG1 VAL A 156     5630   8346   6828  -1624   -558   1268       C  
ATOM   1040  CG2 VAL A 156      18.041   8.791  44.107  1.00 54.42           C  
ANISOU 1040  CG2 VAL A 156     6067   7812   6799  -1898   -738   1053       C  
ATOM   1041  N   LEU A 157      16.814   4.648  42.587  1.00 52.78           N  
ANISOU 1041  N   LEU A 157     5544   7803   6708   -986   -265    782       N  
ATOM   1042  CA  LEU A 157      16.875   3.399  41.834  1.00 51.59           C  
ANISOU 1042  CA  LEU A 157     5285   7774   6544   -729   -137    774       C  
ATOM   1043  C   LEU A 157      15.652   3.234  40.941  1.00 55.10           C  
ANISOU 1043  C   LEU A 157     5857   8048   7031   -585    -73    620       C  
ATOM   1044  O   LEU A 157      15.757   2.717  39.823  1.00 52.32           O  
ANISOU 1044  O   LEU A 157     5445   7789   6647   -429      8    647       O  
ATOM   1045  CB  LEU A 157      17.003   2.212  42.787  1.00 54.72           C  
ANISOU 1045  CB  LEU A 157     5651   8202   6938   -612    -98    729       C  
ATOM   1046  CG  LEU A 157      18.281   2.137  43.623  1.00 57.80           C  
ANISOU 1046  CG  LEU A 157     5881   8802   7278   -719   -149    902       C  
ATOM   1047  CD1 LEU A 157      18.351   0.816  44.372  1.00 50.43           C  
ANISOU 1047  CD1 LEU A 157     4918   7904   6340   -552    -86    852       C  
ATOM   1048  CD2 LEU A 157      19.504   2.328  42.743  1.00 52.57           C  
ANISOU 1048  CD2 LEU A 157     5000   8429   6546   -730   -131   1137       C  
ATOM   1049  N   ALA A 158      14.489   3.698  41.404  1.00 49.68           N  
ANISOU 1049  N   ALA A 158     5350   7120   6406   -633   -108    471       N  
ATOM   1050  CA  ALA A 158      13.283   3.596  40.593  1.00 47.13           C  
ANISOU 1050  CA  ALA A 158     5133   6650   6124   -517    -60    348       C  
ATOM   1051  C   ALA A 158      13.393   4.453  39.342  1.00 47.96           C  
ANISOU 1051  C   ALA A 158     5220   6790   6213   -562    -66    420       C  
ATOM   1052  O   ALA A 158      13.073   3.998  38.235  1.00 46.85           O  
ANISOU 1052  O   ALA A 158     5067   6671   6061   -426     -2    401       O  
ATOM   1053  CB  ALA A 158      12.062   4.008  41.417  1.00 46.84           C  
ANISOU 1053  CB  ALA A 158     5269   6379   6148   -556    -93    210       C  
ATOM   1054  N   LEU A 159      13.865   5.693  39.498  1.00 48.05           N  
ANISOU 1054  N   LEU A 159     5242   6803   6213   -763   -150    511       N  
ATOM   1055  CA  LEU A 159      14.015   6.567  38.341  1.00 55.17           C  
ANISOU 1055  CA  LEU A 159     6125   7740   7097   -824   -164    593       C  
ATOM   1056  C   LEU A 159      15.060   6.024  37.374  1.00 51.14           C  
ANISOU 1056  C   LEU A 159     5419   7489   6522   -740   -103    739       C  
ATOM   1057  O   LEU A 159      14.869   6.075  36.152  1.00 49.61           O  
ANISOU 1057  O   LEU A 159     5210   7326   6314   -656    -55    753       O  
ATOM   1058  CB  LEU A 159      14.382   7.976  38.799  1.00 49.75           C  
ANISOU 1058  CB  LEU A 159     5513   6994   6397  -1076   -283    671       C  
ATOM   1059  CG  LEU A 159      13.358   8.649  39.715  1.00 55.39           C  
ANISOU 1059  CG  LEU A 159     6459   7437   7148  -1138   -333    536       C  
ATOM   1060  CD1 LEU A 159      13.897   9.958  40.270  1.00 57.66           C  
ANISOU 1060  CD1 LEU A 159     6859   7659   7391  -1395   -465    622       C  
ATOM   1061  CD2 LEU A 159      12.044   8.874  38.983  1.00 56.72           C  
ANISOU 1061  CD2 LEU A 159     6743   7441   7366  -1018   -281    420       C  
ATOM   1062  N   LEU A 160      16.147   5.452  37.899  1.00 50.43           N  
ANISOU 1062  N   LEU A 160     5178   7596   6386   -738    -96    854       N  
ATOM   1063  CA  LEU A 160      17.168   4.900  37.014  1.00 51.53           C  
ANISOU 1063  CA  LEU A 160     5124   8005   6449   -619    -18   1013       C  
ATOM   1064  C   LEU A 160      16.641   3.695  36.247  1.00 50.73           C  
ANISOU 1064  C   LEU A 160     5062   7885   6327   -338    104    908       C  
ATOM   1065  O   LEU A 160      16.902   3.554  35.047  1.00 55.09           O  
ANISOU 1065  O   LEU A 160     5560   8550   6822   -220    173    976       O  
ATOM   1066  CB  LEU A 160      18.416   4.523  37.811  1.00 52.75           C  
ANISOU 1066  CB  LEU A 160     5101   8387   6554   -663    -33   1176       C  
ATOM   1067  CG  LEU A 160      19.296   5.686  38.263  1.00 64.06           C  
ANISOU 1067  CG  LEU A 160     6449   9924   7967   -959   -164   1361       C  
ATOM   1068  CD1 LEU A 160      20.424   5.190  39.154  1.00 58.75           C  
ANISOU 1068  CD1 LEU A 160     5599   9476   7249   -999   -185   1520       C  
ATOM   1069  CD2 LEU A 160      19.848   6.433  37.057  1.00 55.52           C  
ANISOU 1069  CD2 LEU A 160     5257   8997   6841  -1023   -167   1533       C  
ATOM   1070  N   LEU A 161      15.890   2.819  36.918  1.00 49.53           N  
ANISOU 1070  N   LEU A 161     5020   7586   6211   -233    127    747       N  
ATOM   1071  CA  LEU A 161      15.332   1.661  36.229  1.00 56.45           C  
ANISOU 1071  CA  LEU A 161     5976   8415   7058      6    218    645       C  
ATOM   1072  C   LEU A 161      14.309   2.078  35.179  1.00 57.25           C  
ANISOU 1072  C   LEU A 161     6200   8370   7184     19    216    556       C  
ATOM   1073  O   LEU A 161      14.220   1.457  34.112  1.00 51.96           O  
ANISOU 1073  O   LEU A 161     5562   7729   6450    185    284    547       O  
ATOM   1074  CB  LEU A 161      14.702   0.705  37.241  1.00 47.88           C  
ANISOU 1074  CB  LEU A 161     4989   7195   6010     76    219    504       C  
ATOM   1075  CG  LEU A 161      14.074  -0.566  36.667  1.00 58.03           C  
ANISOU 1075  CG  LEU A 161     6394   8401   7255    295    288    396       C  
ATOM   1076  CD1 LEU A 161      15.100  -1.368  35.884  1.00 48.70           C  
ANISOU 1076  CD1 LEU A 161     5138   7416   5948    498    387    507       C  
ATOM   1077  CD2 LEU A 161      13.450  -1.414  37.768  1.00 52.16           C  
ANISOU 1077  CD2 LEU A 161     5740   7524   6553    324    270    273       C  
ATOM   1078  N   ALA A 162      13.537   3.131  35.452  1.00 54.17           N  
ANISOU 1078  N   ALA A 162     5890   7819   6875   -148    138    497       N  
ATOM   1079  CA  ALA A 162      12.543   3.578  34.485  1.00 47.10           C  
ANISOU 1079  CA  ALA A 162     5098   6794   6005   -138    133    428       C  
ATOM   1080  C   ALA A 162      13.143   4.397  33.349  1.00 55.96           C  
ANISOU 1080  C   ALA A 162     6142   8036   7082   -185    139    557       C  
ATOM   1081  O   ALA A 162      12.487   4.559  32.315  1.00 53.10           O  
ANISOU 1081  O   ALA A 162     5848   7609   6717   -136    153    519       O  
ATOM   1082  CB  ALA A 162      11.453   4.397  35.181  1.00 46.23           C  
ANISOU 1082  CB  ALA A 162     5107   6471   5987   -263     64    329       C  
ATOM   1083  N   PHE A 163      14.368   4.905  33.512  1.00 49.33           N  
ANISOU 1083  N   PHE A 163     5158   7381   6204   -286    121    721       N  
ATOM   1084  CA  PHE A 163      14.921   5.838  32.531  1.00 53.24           C  
ANISOU 1084  CA  PHE A 163     5574   7991   6662   -370    109    861       C  
ATOM   1085  C   PHE A 163      14.966   5.298  31.106  1.00 60.30           C  
ANISOU 1085  C   PHE A 163     6450   8980   7483   -182    202    887       C  
ATOM   1086  O   PHE A 163      14.537   6.022  30.193  1.00 51.11           O  
ANISOU 1086  O   PHE A 163     5331   7762   6326   -225    186    890       O  
ATOM   1087  CB  PHE A 163      16.309   6.301  32.983  1.00 51.93           C  
ANISOU 1087  CB  PHE A 163     5230   8046   6454   -513     69   1066       C  
ATOM   1088  CG  PHE A 163      16.961   7.266  32.031  1.00 56.29           C  
ANISOU 1088  CG  PHE A 163     5682   8740   6964   -624     46   1241       C  
ATOM   1089  CD1 PHE A 163      17.903   6.829  31.112  1.00 57.11           C  
ANISOU 1089  CD1 PHE A 163     5615   9112   6973   -492    135   1406       C  
ATOM   1090  CD2 PHE A 163      16.629   8.611  32.052  1.00 64.24           C  
ANISOU 1090  CD2 PHE A 163     6779   9614   8016   -848    -61   1249       C  
ATOM   1091  CE1 PHE A 163      18.503   7.718  30.234  1.00 57.48           C  
ANISOU 1091  CE1 PHE A 163     5556   9306   6979   -598    115   1584       C  
ATOM   1092  CE2 PHE A 163      17.225   9.505  31.177  1.00 56.90           C  
ANISOU 1092  CE2 PHE A 163     5762   8811   7045   -965    -92   1418       C  
ATOM   1093  CZ  PHE A 163      18.162   9.057  30.268  1.00 55.90           C  
ANISOU 1093  CZ  PHE A 163     5440   8967   6832   -847     -5   1590       C  
ATOM   1094  N   PRO A 164      15.481   4.089  30.829  1.00 53.75           N  
ANISOU 1094  N   PRO A 164     5572   8284   6568     34    299    912       N  
ATOM   1095  CA  PRO A 164      15.589   3.676  29.418  1.00 55.17           C  
ANISOU 1095  CA  PRO A 164     5763   8549   6651    215    387    947       C  
ATOM   1096  C   PRO A 164      14.263   3.660  28.679  1.00 59.09           C  
ANISOU 1096  C   PRO A 164     6449   8826   7177    251    371    788       C  
ATOM   1097  O   PRO A 164      14.222   3.965  27.482  1.00 58.44           O  
ANISOU 1097  O   PRO A 164     6380   8780   7043    292    397    831       O  
ATOM   1098  CB  PRO A 164      16.202   2.270  29.508  1.00 53.08           C  
ANISOU 1098  CB  PRO A 164     5480   8405   6285    461    491    965       C  
ATOM   1099  CG  PRO A 164      16.879   2.230  30.831  1.00 52.67           C  
ANISOU 1099  CG  PRO A 164     5304   8440   6269    371    460   1029       C  
ATOM   1100  CD  PRO A 164      16.017   3.057  31.735  1.00 51.35           C  
ANISOU 1100  CD  PRO A 164     5217   8058   6235    136    339    915       C  
ATOM   1101  N   GLN A 165      13.176   3.302  29.360  1.00 61.03           N  
ANISOU 1101  N   GLN A 165     6832   8857   7499    232    325    621       N  
ATOM   1102  CA  GLN A 165      11.876   3.241  28.701  1.00 53.46           C  
ANISOU 1102  CA  GLN A 165     6035   7710   6568    254    298    494       C  
ATOM   1103  C   GLN A 165      11.351   4.632  28.361  1.00 51.19           C  
ANISOU 1103  C   GLN A 165     5748   7346   6354     86    233    513       C  
ATOM   1104  O   GLN A 165      10.703   4.823  27.325  1.00 54.14           O  
ANISOU 1104  O   GLN A 165     6197   7660   6714    112    230    488       O  
ATOM   1105  CB  GLN A 165      10.884   2.490  29.589  1.00 55.24           C  
ANISOU 1105  CB  GLN A 165     6377   7757   6854    270    263    345       C  
ATOM   1106  CG  GLN A 165       9.511   2.319  28.986  1.00 60.23           C  
ANISOU 1106  CG  GLN A 165     7159   8215   7510    281    224    239       C  
ATOM   1107  CD  GLN A 165       8.867   1.015  29.400  1.00 55.98           C  
ANISOU 1107  CD  GLN A 165     6743   7571   6956    372    216    131       C  
ATOM   1108  OE1 GLN A 165       9.553   0.028  29.657  1.00 54.87           O  
ANISOU 1108  OE1 GLN A 165     6612   7496   6740    494    265    134       O  
ATOM   1109  NE2 GLN A 165       7.544   1.003  29.469  1.00 66.92           N  
ANISOU 1109  NE2 GLN A 165     8220   8798   8406    314    151     50       N  
ATOM   1110  N   GLY A 166      11.618   5.621  29.216  1.00 50.31           N  
ANISOU 1110  N   GLY A 166     5575   7227   6312    -88    177    559       N  
ATOM   1111  CA  GLY A 166      11.227   6.979  28.892  1.00 48.40           C  
ANISOU 1111  CA  GLY A 166     5359   6908   6122   -239    117    588       C  
ATOM   1112  C   GLY A 166      12.136   7.630  27.875  1.00 56.64           C  
ANISOU 1112  C   GLY A 166     6300   8120   7100   -277    132    744       C  
ATOM   1113  O   GLY A 166      11.686   8.461  27.080  1.00 52.48           O  
ANISOU 1113  O   GLY A 166     5816   7535   6588   -335    106    759       O  
ATOM   1114  N   TYR A 167      13.419   7.259  27.877  1.00 52.99           N  
ANISOU 1114  N   TYR A 167     5691   7881   6562   -240    178    876       N  
ATOM   1115  CA  TYR A 167      14.380   7.865  26.963  1.00 52.18           C  
ANISOU 1115  CA  TYR A 167     5457   7978   6389   -279    197   1060       C  
ATOM   1116  C   TYR A 167      14.084   7.498  25.515  1.00 59.33           C  
ANISOU 1116  C   TYR A 167     6407   8912   7222   -116    268   1049       C  
ATOM   1117  O   TYR A 167      14.259   8.323  24.611  1.00 53.09           O  
ANISOU 1117  O   TYR A 167     5580   8182   6410   -180    258   1145       O  
ATOM   1118  CB  TYR A 167      15.793   7.431  27.353  1.00 53.47           C  
ANISOU 1118  CB  TYR A 167     5432   8404   6480   -252    240   1226       C  
ATOM   1119  CG  TYR A 167      16.891   8.000  26.488  1.00 55.23           C  
ANISOU 1119  CG  TYR A 167     5481   8883   6623   -291    264   1456       C  
ATOM   1120  CD1 TYR A 167      17.470   7.243  25.477  1.00 73.28           C  
ANISOU 1120  CD1 TYR A 167     7688  11368   8789    -63    388   1544       C  
ATOM   1121  CD2 TYR A 167      17.354   9.294  26.685  1.00 61.53           C  
ANISOU 1121  CD2 TYR A 167     6205   9721   7451   -555    160   1594       C  
ATOM   1122  CE1 TYR A 167      18.477   7.762  24.684  1.00 61.26           C  
ANISOU 1122  CE1 TYR A 167     5987  10104   7186    -87    420   1776       C  
ATOM   1123  CE2 TYR A 167      18.358   9.821  25.898  1.00 57.85           C  
ANISOU 1123  CE2 TYR A 167     5566   9506   6911   -610    173   1828       C  
ATOM   1124  CZ  TYR A 167      18.916   9.052  24.900  1.00 62.58           C  
ANISOU 1124  CZ  TYR A 167     6056  10324   7396   -372    309   1923       C  
ATOM   1125  OH  TYR A 167      19.920   9.577  24.115  1.00 81.03           O  
ANISOU 1125  OH  TYR A 167     8200  12934   9652   -416    331   2176       O  
ATOM   1126  N   TYR A 168      13.630   6.271  25.275  1.00 59.08           N  
ANISOU 1126  N   TYR A 168     6473   8831   7145     88    332    935       N  
ATOM   1127  CA  TYR A 168      13.388   5.781  23.926  1.00 52.25           C  
ANISOU 1127  CA  TYR A 168     5687   7983   6184    255    396    920       C  
ATOM   1128  C   TYR A 168      11.959   6.002  23.447  1.00 51.51           C  
ANISOU 1128  C   TYR A 168     5761   7662   6148    220    337    780       C  
ATOM   1129  O   TYR A 168      11.654   5.686  22.293  1.00 58.51           O  
ANISOU 1129  O   TYR A 168     6734   8541   6955    329    369    764       O  
ATOM   1130  CB  TYR A 168      13.753   4.298  23.840  1.00 52.69           C  
ANISOU 1130  CB  TYR A 168     5793   8104   6124    502    491    889       C  
ATOM   1131  CG  TYR A 168      15.245   4.061  23.867  1.00 61.43           C  
ANISOU 1131  CG  TYR A 168     6716   9493   7132    600    582   1074       C  
ATOM   1132  CD1 TYR A 168      16.101   4.822  23.076  1.00 58.57           C  
ANISOU 1132  CD1 TYR A 168     6199   9343   6711    570    616   1265       C  
ATOM   1133  CD2 TYR A 168      15.803   3.092  24.693  1.00 60.97           C  
ANISOU 1133  CD2 TYR A 168     6624   9505   7036    721    633   1078       C  
ATOM   1134  CE1 TYR A 168      17.469   4.617  23.096  1.00 57.35           C  
ANISOU 1134  CE1 TYR A 168     5846   9481   6461    662    702   1470       C  
ATOM   1135  CE2 TYR A 168      17.171   2.879  24.721  1.00 64.99           C  
ANISOU 1135  CE2 TYR A 168     6943  10300   7451    823    722   1274       C  
ATOM   1136  CZ  TYR A 168      17.999   3.644  23.923  1.00 66.34           C  
ANISOU 1136  CZ  TYR A 168     6946  10696   7563    793    756   1477       C  
ATOM   1137  OH  TYR A 168      19.359   3.432  23.951  1.00 65.12           O  
ANISOU 1137  OH  TYR A 168     6575  10858   7311    898    847   1705       O  
ATOM   1138  N   SER A 169      11.075   6.513  24.297  1.00 50.22           N  
ANISOU 1138  N   SER A 169     5650   7321   6110     80    255    689       N  
ATOM   1139  CA  SER A 169       9.733   6.850  23.847  1.00 49.23           C  
ANISOU 1139  CA  SER A 169     5650   7012   6042     42    201    594       C  
ATOM   1140  C   SER A 169       9.775   8.064  22.931  1.00 52.14           C  
ANISOU 1140  C   SER A 169     5987   7409   6414    -52    179    685       C  
ATOM   1141  O   SER A 169      10.511   9.022  23.181  1.00 50.39           O  
ANISOU 1141  O   SER A 169     5667   7265   6213   -179    159    793       O  
ATOM   1142  CB  SER A 169       8.825   7.128  25.043  1.00 59.10           C  
ANISOU 1142  CB  SER A 169     6950   8090   7415    -57    136    499       C  
ATOM   1143  OG  SER A 169       8.832   6.040  25.947  1.00 55.36           O  
ANISOU 1143  OG  SER A 169     6496   7597   6940     17    152    424       O  
ATOM   1144  N   THR A 170       8.965   8.027  21.874  1.00 49.71           N  
ANISOU 1144  N   THR A 170     5771   7033   6082     -4    171    648       N  
ATOM   1145  CA  THR A 170       8.814   9.159  20.969  1.00 50.15           C  
ANISOU 1145  CA  THR A 170     5816   7092   6147    -88    145    721       C  
ATOM   1146  C   THR A 170       7.421   9.133  20.362  1.00 52.46           C  
ANISOU 1146  C   THR A 170     6232   7231   6469    -73    101    638       C  
ATOM   1147  O   THR A 170       6.756   8.094  20.315  1.00 49.13           O  
ANISOU 1147  O   THR A 170     5904   6742   6022     16     96    546       O  
ATOM   1148  CB  THR A 170       9.847   9.162  19.825  1.00 57.64           C  
ANISOU 1148  CB  THR A 170     6691   8236   6974    -19    210    848       C  
ATOM   1149  OG1 THR A 170      10.038   7.826  19.340  1.00 62.26           O  
ANISOU 1149  OG1 THR A 170     7338   8879   7440    177    280    808       O  
ATOM   1150  CG2 THR A 170      11.177   9.758  20.268  1.00 72.19           C  
ANISOU 1150  CG2 THR A 170     8369  10254   8806   -107    227    998       C  
ATOM   1151  N   THR A 171       6.986  10.302  19.907  1.00 49.67           N  
ANISOU 1151  N   THR A 171     5882   6826   6164   -170     60    683       N  
ATOM   1152  CA  THR A 171       5.833  10.403  19.028  1.00 55.29           C  
ANISOU 1152  CA  THR A 171     6681   7443   6882   -154     24    651       C  
ATOM   1153  C   THR A 171       6.297  10.317  17.581  1.00 50.43           C  
ANISOU 1153  C   THR A 171     6070   6940   6150    -93     58    719       C  
ATOM   1154  O   THR A 171       7.320  10.897  17.208  1.00 60.03           O  
ANISOU 1154  O   THR A 171     7199   8286   7323   -121     93    826       O  
ATOM   1155  CB  THR A 171       5.081  11.711  19.265  1.00 55.07           C  
ANISOU 1155  CB  THR A 171     6666   7299   6958   -266    -29    673       C  
ATOM   1156  OG1 THR A 171       5.956  12.818  19.017  1.00 51.76           O  
ANISOU 1156  OG1 THR A 171     6189   6947   6529   -359    -27    780       O  
ATOM   1157  CG2 THR A 171       4.585  11.779  20.695  1.00 48.51           C  
ANISOU 1157  CG2 THR A 171     5854   6355   6224   -299    -51    607       C  
ATOM   1158  N   GLU A 172       5.542   9.584  16.769  1.00 57.73           N  
ANISOU 1158  N   GLU A 172     7102   7817   7014    -17     40    666       N  
ATOM   1159  CA  GLU A 172       5.906   9.411  15.370  1.00 51.43           C  
ANISOU 1159  CA  GLU A 172     6344   7111   6086     59     73    718       C  
ATOM   1160  C   GLU A 172       4.677   8.996  14.580  1.00 51.36           C  
ANISOU 1160  C   GLU A 172     6474   6993   6048     72      7    662       C  
ATOM   1161  O   GLU A 172       3.811   8.278  15.086  1.00 52.93           O  
ANISOU 1161  O   GLU A 172     6748   7084   6279     70    -46    579       O  
ATOM   1162  CB  GLU A 172       7.021   8.370  15.202  1.00 52.20           C  
ANISOU 1162  CB  GLU A 172     6451   7341   6044    210    161    729       C  
ATOM   1163  CG  GLU A 172       6.706   7.022  15.844  1.00 63.40           C  
ANISOU 1163  CG  GLU A 172     7977   8680   7433    298    156    615       C  
ATOM   1164  CD  GLU A 172       7.857   6.037  15.746  1.00 61.50           C  
ANISOU 1164  CD  GLU A 172     7753   8567   7046    473    255    635       C  
ATOM   1165  OE1 GLU A 172       7.759   4.947  16.349  1.00 68.40           O  
ANISOU 1165  OE1 GLU A 172     8718   9381   7890    552    258    550       O  
ATOM   1166  OE2 GLU A 172       8.861   6.350  15.071  1.00 71.37           O  
ANISOU 1166  OE2 GLU A 172     8925   9985   8207    542    335    747       O  
ATOM   1167  N   THR A 173       4.597   9.489  13.348  1.00 52.07           N  
ANISOU 1167  N   THR A 173     6589   7119   6078     69      1    724       N  
ATOM   1168  CA  THR A 173       3.591   9.009  12.414  1.00 57.68           C  
ANISOU 1168  CA  THR A 173     7441   7751   6723     83    -66    689       C  
ATOM   1169  C   THR A 173       3.908   7.569  12.005  1.00 56.84           C  
ANISOU 1169  C   THR A 173     7495   7652   6450    218    -43    628       C  
ATOM   1170  O   THR A 173       5.065   7.217  11.758  1.00 62.68           O  
ANISOU 1170  O   THR A 173     8231   8508   7076    340     54    656       O  
ATOM   1171  CB  THR A 173       3.531   9.952  11.207  1.00 53.03           C  
ANISOU 1171  CB  THR A 173     6838   7207   6105     47    -73    778       C  
ATOM   1172  OG1 THR A 173       2.417   9.621  10.387  1.00 88.08           O  
ANISOU 1172  OG1 THR A 173    11404  11562  10499     27   -160    756       O  
ATOM   1173  CG2 THR A 173       4.805   9.898  10.380  1.00 54.15           C  
ANISOU 1173  CG2 THR A 173     6966   7504   6104    147     21    848       C  
ATOM   1174  N   MET A 174       2.882   6.715  11.970  1.00 52.92           N  
ANISOU 1174  N   MET A 174     7146   7032   5928    200   -133    554       N  
ATOM   1175  CA  MET A 174       3.079   5.274  11.780  1.00 54.76           C  
ANISOU 1175  CA  MET A 174     7579   7225   6001    317   -130    480       C  
ATOM   1176  C   MET A 174       2.040   4.671  10.838  1.00 60.95           C  
ANISOU 1176  C   MET A 174     8578   7899   6682    276   -248    453       C  
ATOM   1177  O   MET A 174       1.177   3.893  11.259  1.00 66.11           O  
ANISOU 1177  O   MET A 174     9337   8438   7346    213   -349    397       O  
ATOM   1178  CB  MET A 174       3.059   4.558  13.132  1.00 55.51           C  
ANISOU 1178  CB  MET A 174     7658   7267   6165    320   -133    408       C  
ATOM   1179  CG  MET A 174       4.102   3.465  13.281  1.00 71.32           C  
ANISOU 1179  CG  MET A 174     9764   9310   8023    494    -45    367       C  
ATOM   1180  SD  MET A 174       5.788   4.094  13.168  1.00 85.86           S  
ANISOU 1180  SD  MET A 174    11428  11371   9825    619    121    468       S  
ATOM   1181  CE  MET A 174       6.722   2.587  13.414  1.00 95.60           C  
ANISOU 1181  CE  MET A 174    12811  12632  10880    849    214    420       C  
ATOM   1182  N   PRO A 175       2.118   4.973   9.532  1.00 55.31           N  
ANISOU 1182  N   PRO A 175     7942   7221   5855    303   -247    501       N  
ATOM   1183  CA  PRO A 175       2.970   5.950   8.857  1.00 58.29           C  
ANISOU 1183  CA  PRO A 175     8198   7736   6214    353   -150    589       C  
ATOM   1184  C   PRO A 175       2.282   7.302   8.677  1.00 55.14           C  
ANISOU 1184  C   PRO A 175     7644   7343   5966    203   -203    663       C  
ATOM   1185  O   PRO A 175       2.956   8.278   8.358  1.00 55.30           O  
ANISOU 1185  O   PRO A 175     7532   7470   6010    207   -132    745       O  
ATOM   1186  CB  PRO A 175       3.227   5.293   7.501  1.00 63.38           C  
ANISOU 1186  CB  PRO A 175     9076   8384   6622    474   -138    586       C  
ATOM   1187  CG  PRO A 175       1.951   4.579   7.215  1.00 57.56           C  
ANISOU 1187  CG  PRO A 175     8546   7482   5840    375   -297    527       C  
ATOM   1188  CD  PRO A 175       1.408   4.121   8.558  1.00 56.43           C  
ANISOU 1188  CD  PRO A 175     8352   7257   5833    295   -354    467       C  
ATOM   1189  N   SER A 176       0.960   7.364   8.867  1.00 54.66           N  
ANISOU 1189  N   SER A 176     7596   7174   5996     75   -326    652       N  
ATOM   1190  CA  SER A 176       0.215   8.595   8.630  1.00 67.15           C  
ANISOU 1190  CA  SER A 176     9054   8758   7704    -40   -373    732       C  
ATOM   1191  C   SER A 176      -0.362   9.233   9.888  1.00 53.18           C  
ANISOU 1191  C   SER A 176     7125   6947   6134   -121   -389    739       C  
ATOM   1192  O   SER A 176      -0.604  10.443   9.883  1.00 61.73           O  
ANISOU 1192  O   SER A 176     8091   8043   7322   -176   -383    809       O  
ATOM   1193  CB  SER A 176      -0.922   8.354   7.623  1.00 56.06           C  
ANISOU 1193  CB  SER A 176     7778   7291   6230   -113   -500    757       C  
ATOM   1194  OG  SER A 176      -1.855   7.407   8.111  1.00 66.92           O  
ANISOU 1194  OG  SER A 176     9243   8573   7611   -176   -608    712       O  
ATOM   1195  N   ARG A 177      -0.566   8.476  10.962  1.00 52.56           N  
ANISOU 1195  N   ARG A 177     7053   6816   6101   -120   -403    671       N  
ATOM   1196  CA  ARG A 177      -1.197   8.998  12.167  1.00 51.61           C  
ANISOU 1196  CA  ARG A 177     6803   6654   6153   -181   -416    678       C  
ATOM   1197  C   ARG A 177      -0.251   8.870  13.356  1.00 50.91           C  
ANISOU 1197  C   ARG A 177     6648   6584   6111   -132   -330    623       C  
ATOM   1198  O   ARG A 177       0.499   7.897  13.463  1.00 51.07           O  
ANISOU 1198  O   ARG A 177     6742   6626   6036    -57   -293    564       O  
ATOM   1199  CB  ARG A 177      -2.517   8.271  12.435  1.00 51.61           C  
ANISOU 1199  CB  ARG A 177     6850   6582   6176   -247   -529    673       C  
ATOM   1200  CG  ARG A 177      -3.271   7.957  11.147  1.00 62.19           C  
ANISOU 1200  CG  ARG A 177     8307   7910   7412   -301   -636    720       C  
ATOM   1201  CD  ARG A 177      -4.586   7.255  11.407  1.00 60.39           C  
ANISOU 1201  CD  ARG A 177     8110   7632   7205   -398   -768    747       C  
ATOM   1202  NE  ARG A 177      -5.614   8.178  11.866  1.00 73.38           N  
ANISOU 1202  NE  ARG A 177     9583   9297   9002   -452   -791    847       N  
ATOM   1203  CZ  ARG A 177      -6.605   8.627  11.105  1.00 64.93           C  
ANISOU 1203  CZ  ARG A 177     8480   8251   7938   -523   -875    959       C  
ATOM   1204  NH1 ARG A 177      -6.705   8.229   9.846  1.00 54.32           N  
ANISOU 1204  NH1 ARG A 177     7275   6906   6458   -571   -959    977       N  
ATOM   1205  NH2 ARG A 177      -7.502   9.469  11.603  1.00 68.34           N  
ANISOU 1205  NH2 ARG A 177     8751   8712   8503   -537   -875   1061       N  
ATOM   1206  N   VAL A 178      -0.280   9.873  14.239  1.00 50.28           N  
ANISOU 1206  N   VAL A 178     6445   6493   6167   -169   -299    650       N  
ATOM   1207  CA  VAL A 178       0.678   9.954  15.338  1.00 49.76           C  
ANISOU 1207  CA  VAL A 178     6312   6449   6144   -147   -226    616       C  
ATOM   1208  C   VAL A 178       0.426   8.850  16.359  1.00 54.14           C  
ANISOU 1208  C   VAL A 178     6897   6959   6716   -124   -241    534       C  
ATOM   1209  O   VAL A 178      -0.721   8.559  16.726  1.00 48.93           O  
ANISOU 1209  O   VAL A 178     6249   6232   6111   -159   -306    526       O  
ATOM   1210  CB  VAL A 178       0.615  11.344  15.999  1.00 49.46           C  
ANISOU 1210  CB  VAL A 178     6185   6380   6229   -205   -209    664       C  
ATOM   1211  CG1 VAL A 178       1.608  11.439  17.154  1.00 49.08           C  
ANISOU 1211  CG1 VAL A 178     6083   6350   6215   -209   -154    636       C  
ATOM   1212  CG2 VAL A 178       0.881  12.432  14.974  1.00 50.13           C  
ANISOU 1212  CG2 VAL A 178     6253   6502   6292   -238   -202    750       C  
ATOM   1213  N   VAL A 179       1.513   8.254  16.853  1.00 49.10           N  
ANISOU 1213  N   VAL A 179     6257   6370   6030    -65   -179    491       N  
ATOM   1214  CA  VAL A 179       1.485   7.297  17.950  1.00 53.77           C  
ANISOU 1214  CA  VAL A 179     6865   6923   6640    -39   -180    416       C  
ATOM   1215  C   VAL A 179       2.649   7.603  18.886  1.00 52.44           C  
ANISOU 1215  C   VAL A 179     6604   6816   6505    -24   -103    415       C  
ATOM   1216  O   VAL A 179       3.638   8.233  18.505  1.00 48.73           O  
ANISOU 1216  O   VAL A 179     6075   6438   6004    -21    -51    475       O  
ATOM   1217  CB  VAL A 179       1.567   5.827  17.471  1.00 49.05           C  
ANISOU 1217  CB  VAL A 179     6416   6316   5906     36   -199    359       C  
ATOM   1218  CG1 VAL A 179       0.350   5.451  16.636  1.00 49.50           C  
ANISOU 1218  CG1 VAL A 179     6584   6300   5922    -15   -305    367       C  
ATOM   1219  CG2 VAL A 179       2.852   5.593  16.691  1.00 53.36           C  
ANISOU 1219  CG2 VAL A 179     6997   6963   6313    144   -117    376       C  
ATOM   1220  N   CYS A 180       2.504   7.169  20.135  1.00 47.60           N  
ANISOU 1220  N   CYS A 180     5971   6157   5956    -29   -105    360       N  
ATOM   1221  CA  CYS A 180       3.596   7.157  21.100  1.00 47.40           C  
ANISOU 1221  CA  CYS A 180     5876   6190   5945    -14    -46    353       C  
ATOM   1222  C   CYS A 180       4.140   5.737  21.178  1.00 47.60           C  
ANISOU 1222  C   CYS A 180     5964   6251   5870     91    -17    300       C  
ATOM   1223  O   CYS A 180       3.376   4.789  21.382  1.00 55.44           O  
ANISOU 1223  O   CYS A 180     7049   7163   6852    109    -63    236       O  
ATOM   1224  CB  CYS A 180       3.115   7.641  22.472  1.00 51.65           C  
ANISOU 1224  CB  CYS A 180     6368   6650   6608    -78    -63    328       C  
ATOM   1225  SG  CYS A 180       4.266   7.454  23.873  1.00 53.21           S  
ANISOU 1225  SG  CYS A 180     6497   6896   6824    -81    -16    308       S  
ATOM   1226  N   LYS A 181       5.453   5.590  21.006  1.00 53.50           N  
ANISOU 1226  N   LYS A 181     6666   7125   6537    161     57    341       N  
ATOM   1227  CA  LYS A 181       6.045   4.268  20.871  1.00 53.47           C  
ANISOU 1227  CA  LYS A 181     6744   7164   6408    302    103    307       C  
ATOM   1228  C   LYS A 181       7.470   4.288  21.404  1.00 56.11           C  
ANISOU 1228  C   LYS A 181     6956   7651   6713    356    188    370       C  
ATOM   1229  O   LYS A 181       8.178   5.293  21.290  1.00 56.53           O  
ANISOU 1229  O   LYS A 181     6878   7812   6790    295    214    468       O  
ATOM   1230  CB  LYS A 181       6.026   3.802  19.407  1.00 57.91           C  
ANISOU 1230  CB  LYS A 181     7439   7742   6822    398    112    317       C  
ATOM   1231  CG  LYS A 181       6.438   2.354  19.200  1.00 72.78           C  
ANISOU 1231  CG  LYS A 181     9479   9622   8550    565    150    268       C  
ATOM   1232  CD  LYS A 181       6.199   1.906  17.765  1.00 83.17           C  
ANISOU 1232  CD  LYS A 181    10984  10908   9708    648    139    263       C  
ATOM   1233  CE  LYS A 181       6.664   0.472  17.551  1.00 87.90           C  
ANISOU 1233  CE  LYS A 181    11789  11484  10125    837    183    213       C  
ATOM   1234  NZ  LYS A 181       6.017  -0.466  18.512  1.00 90.06           N  
ANISOU 1234  NZ  LYS A 181    12164  11618  10436    802    112    118       N  
ATOM   1235  N   ILE A 182       7.877   3.167  21.993  1.00 55.09           N  
ANISOU 1235  N   ILE A 182     6869   7533   6529    463    224    325       N  
ATOM   1236  CA  ILE A 182       9.234   2.990  22.500  1.00 49.82           C  
ANISOU 1236  CA  ILE A 182     6082   7030   5818    538    308    399       C  
ATOM   1237  C   ILE A 182      10.109   2.491  21.357  1.00 51.52           C  
ANISOU 1237  C   ILE A 182     6333   7383   5857    721    400    472       C  
ATOM   1238  O   ILE A 182       9.865   1.413  20.803  1.00 63.70           O  
ANISOU 1238  O   ILE A 182     8064   8861   7278    867    417    407       O  
ATOM   1239  CB  ILE A 182       9.260   2.013  23.684  1.00 51.31           C  
ANISOU 1239  CB  ILE A 182     6300   7171   6025    584    309    326       C  
ATOM   1240  CG1 ILE A 182       8.196   2.398  24.713  1.00 47.99           C  
ANISOU 1240  CG1 ILE A 182     5875   6598   5759    427    221    247       C  
ATOM   1241  CG2 ILE A 182      10.641   1.993  24.326  1.00 49.95           C  
ANISOU 1241  CG2 ILE A 182     5969   7184   5827    634    386    424       C  
ATOM   1242  CD1 ILE A 182       8.053   1.402  25.839  1.00 47.47           C  
ANISOU 1242  CD1 ILE A 182     5853   6469   5713    464    213    170       C  
ATOM   1243  N   GLU A 183      11.138   3.263  21.014  1.00 54.11           N  
ANISOU 1243  N   GLU A 183     6496   7903   6161    714    459    616       N  
ATOM   1244  CA  GLU A 183      11.975   3.001  19.843  1.00 53.71           C  
ANISOU 1244  CA  GLU A 183     6451   8015   5943    890    559    717       C  
ATOM   1245  C   GLU A 183      13.414   2.770  20.296  1.00 54.82           C  
ANISOU 1245  C   GLU A 183     6418   8393   6019    997    662    857       C  
ATOM   1246  O   GLU A 183      14.218   3.702  20.345  1.00 62.72           O  
ANISOU 1246  O   GLU A 183     7208   9572   7051    900    676   1012       O  
ATOM   1247  CB  GLU A 183      11.883   4.157  18.840  1.00 54.05           C  
ANISOU 1247  CB  GLU A 183     6435   8104   5997    791    539    799       C  
ATOM   1248  CG  GLU A 183      10.531   4.273  18.163  1.00 67.50           C  
ANISOU 1248  CG  GLU A 183     8313   9606   7729    727    453    687       C  
ATOM   1249  CD  GLU A 183      10.311   3.193  17.121  1.00 77.51           C  
ANISOU 1249  CD  GLU A 183     9805  10825   8820    919    488    630       C  
ATOM   1250  OE1 GLU A 183      10.557   3.460  15.926  1.00 94.30           O  
ANISOU 1250  OE1 GLU A 183    11961  13029  10841    986    529    699       O  
ATOM   1251  OE2 GLU A 183       9.904   2.074  17.497  1.00 89.29           O  
ANISOU 1251  OE2 GLU A 183    11462  12195  10268   1000    470    521       O  
ATOM   1252  N   TRP A 184      13.732   1.521  20.617  1.00 55.28           N  
ANISOU 1252  N   TRP A 184     6567   8457   5979   1193    727    816       N  
ATOM   1253  CA  TRP A 184      15.099   1.158  20.944  1.00 56.61           C  
ANISOU 1253  CA  TRP A 184     6576   8871   6061   1342    841    965       C  
ATOM   1254  C   TRP A 184      15.969   1.216  19.690  1.00 59.43           C  
ANISOU 1254  C   TRP A 184     6887   9444   6249   1526    961   1123       C  
ATOM   1255  O   TRP A 184      15.468   1.055  18.573  1.00 62.41           O  
ANISOU 1255  O   TRP A 184     7446   9735   6532   1614    972   1068       O  
ATOM   1256  CB  TRP A 184      15.146  -0.240  21.550  1.00 56.71           C  
ANISOU 1256  CB  TRP A 184     6732   8816   6000   1531    885    875       C  
ATOM   1257  CG  TRP A 184      14.658  -0.269  22.956  1.00 57.76           C  
ANISOU 1257  CG  TRP A 184     6834   8821   6292   1365    793    778       C  
ATOM   1258  CD1 TRP A 184      13.368  -0.126  23.380  1.00 53.50           C  
ANISOU 1258  CD1 TRP A 184     6412   8035   5880   1193    671    617       C  
ATOM   1259  CD2 TRP A 184      15.452  -0.439  24.134  1.00 55.25           C  
ANISOU 1259  CD2 TRP A 184     6349   8628   6015   1358    818    848       C  
ATOM   1260  NE1 TRP A 184      13.310  -0.202  24.749  1.00 52.55           N  
ANISOU 1260  NE1 TRP A 184     6218   7874   5873   1092    626    577       N  
ATOM   1261  CE2 TRP A 184      14.576  -0.395  25.237  1.00 53.61           C  
ANISOU 1261  CE2 TRP A 184     6186   8226   5959   1182    709    710       C  
ATOM   1262  CE3 TRP A 184      16.818  -0.631  24.364  1.00 56.74           C  
ANISOU 1262  CE3 TRP A 184     6346   9089   6122   1487    923   1031       C  
ATOM   1263  CZ2 TRP A 184      15.021  -0.534  26.548  1.00 54.42           C  
ANISOU 1263  CZ2 TRP A 184     6168   8379   6130   1127    697    732       C  
ATOM   1264  CZ3 TRP A 184      17.258  -0.770  25.668  1.00 60.89           C  
ANISOU 1264  CZ3 TRP A 184     6740   9673   6722   1421    903   1061       C  
ATOM   1265  CH2 TRP A 184      16.362  -0.720  26.743  1.00 56.76           C  
ANISOU 1265  CH2 TRP A 184     6285   8934   6347   1239    790    905       C  
ATOM   1266  N   PRO A 185      17.276   1.438  19.843  1.00 71.47           N  
ANISOU 1266  N   PRO A 185     8167  11264   7725   1588   1052   1335       N  
ATOM   1267  CA  PRO A 185      18.139   1.506  18.660  1.00 70.70           C  
ANISOU 1267  CA  PRO A 185     8001  11405   7458   1779   1180   1514       C  
ATOM   1268  C   PRO A 185      18.084   0.186  17.913  1.00 70.00           C  
ANISOU 1268  C   PRO A 185     8185  11254   7158   2125   1294   1436       C  
ATOM   1269  O   PRO A 185      17.989  -0.885  18.517  1.00 76.53           O  
ANISOU 1269  O   PRO A 185     9157  11979   7941   2266   1316   1334       O  
ATOM   1270  CB  PRO A 185      19.533   1.764  19.244  1.00 72.87           C  
ANISOU 1270  CB  PRO A 185     7952  12014   7721   1788   1251   1765       C  
ATOM   1271  CG  PRO A 185      19.288   2.326  20.603  1.00 76.28           C  
ANISOU 1271  CG  PRO A 185     8271  12359   8353   1493   1114   1719       C  
ATOM   1272  CD  PRO A 185      18.026   1.680  21.088  1.00 82.08           C  
ANISOU 1272  CD  PRO A 185     9274  12751   9159   1475   1036   1442       C  
ATOM   1273  N   GLU A 186      18.118   0.268  16.587  1.00 84.80           N  
ANISOU 1273  N   GLU A 186    10157  13173   8891   2259   1359   1480       N  
ATOM   1274  CA  GLU A 186      17.827  -0.908  15.782  1.00101.95           C  
ANISOU 1274  CA  GLU A 186    12673  15212  10853   2555   1435   1368       C  
ATOM   1275  C   GLU A 186      18.933  -1.939  15.957  1.00109.48           C  
ANISOU 1275  C   GLU A 186    13621  16355  11622   2905   1610   1482       C  
ATOM   1276  O   GLU A 186      20.095  -1.688  15.616  1.00112.98           O  
ANISOU 1276  O   GLU A 186    13836  17125  11968   3057   1748   1721       O  
ATOM   1277  CB  GLU A 186      17.658  -0.530  14.313  1.00112.23           C  
ANISOU 1277  CB  GLU A 186    14082  16528  12033   2620   1466   1400       C  
ATOM   1278  CG  GLU A 186      16.753  -1.492  13.557  1.00120.88           C  
ANISOU 1278  CG  GLU A 186    15611  17342  12976   2766   1441   1203       C  
ATOM   1279  CD  GLU A 186      15.364  -1.585  14.169  1.00119.83           C  
ANISOU 1279  CD  GLU A 186    15641  16881  13009   2510   1250    978       C  
ATOM   1280  OE1 GLU A 186      14.717  -0.530  14.341  1.00117.23           O  
ANISOU 1280  OE1 GLU A 186    15169  16497  12876   2211   1126    957       O  
ATOM   1281  OE2 GLU A 186      14.924  -2.711  14.488  1.00116.06           O  
ANISOU 1281  OE2 GLU A 186    15435  16205  12458   2613   1224    834       O  
ATOM   1282  N   HIS A 187      18.561  -3.096  16.492  1.00114.58           N  
ANISOU 1282  N   HIS A 187    14517  16803  12217   3033   1602   1325       N  
ATOM   1283  CA  HIS A 187      19.395  -4.262  16.665  1.00124.65           C  
ANISOU 1283  CA  HIS A 187    15882  18180  13300   3394   1759   1386       C  
ATOM   1284  C   HIS A 187      18.709  -5.444  15.993  1.00136.17           C  
ANISOU 1284  C   HIS A 187    17830  19349  14559   3616   1765   1196       C  
ATOM   1285  O   HIS A 187      17.475  -5.524  16.007  1.00135.51           O  
ANISOU 1285  O   HIS A 187    17974  18956  14559   3412   1601    988       O  
ATOM   1286  CB  HIS A 187      19.615  -4.547  18.165  1.00129.65           C  
ANISOU 1286  CB  HIS A 187    16361  18828  14072   3306   1722   1378       C  
ATOM   1287  CG  HIS A 187      20.358  -5.816  18.446  1.00141.23           C  
ANISOU 1287  CG  HIS A 187    17946  20364  15352   3673   1871   1422       C  
ATOM   1288  ND1 HIS A 187      19.729  -7.039  18.543  1.00143.59           N  
ANISOU 1288  ND1 HIS A 187    18645  20370  15544   3825   1850   1222       N  
ATOM   1289  CD2 HIS A 187      21.674  -6.053  18.663  1.00143.95           C  
ANISOU 1289  CD2 HIS A 187    18064  21040  15592   3921   2040   1656       C  
ATOM   1290  CE1 HIS A 187      20.626  -7.975  18.797  1.00141.95           C  
ANISOU 1290  CE1 HIS A 187    18474  20292  15169   4166   2006   1318       C  
ATOM   1291  NE2 HIS A 187      21.813  -7.402  18.879  1.00143.62           N  
ANISOU 1291  NE2 HIS A 187    18297  20893  15381   4239   2130   1586       N  
ATOM   1292  N   PRO A 188      19.468  -6.370  15.396  1.00144.07           N  
ANISOU 1292  N   PRO A 188    19013  20442  15284   4031   1946   1272       N  
ATOM   1293  CA  PRO A 188      18.824  -7.408  14.575  1.00149.74           C  
ANISOU 1293  CA  PRO A 188    20251  20868  15776   4236   1942   1097       C  
ATOM   1294  C   PRO A 188      17.816  -8.265  15.323  1.00155.46           C  
ANISOU 1294  C   PRO A 188    21276  21236  16558   4116   1787    861       C  
ATOM   1295  O   PRO A 188      16.826  -8.699  14.718  1.00156.60           O  
ANISOU 1295  O   PRO A 188    21804  21079  16619   4066   1674    686       O  
ATOM   1296  CB  PRO A 188      20.020  -8.236  14.083  1.00148.72           C  
ANISOU 1296  CB  PRO A 188    20219  20942  15346   4734   2188   1254       C  
ATOM   1297  CG  PRO A 188      21.135  -7.247  14.017  1.00144.90           C  
ANISOU 1297  CG  PRO A 188    19244  20893  14920   4746   2314   1539       C  
ATOM   1298  CD  PRO A 188      20.926  -6.336  15.199  1.00142.09           C  
ANISOU 1298  CD  PRO A 188    18505  20586  14895   4326   2163   1548       C  
ATOM   1299  N   ASN A 189      18.024  -8.527  16.612  1.00156.65           N  
ANISOU 1299  N   ASN A 189    21267  21414  16841   4055   1770    859       N  
ATOM   1300  CA  ASN A 189      17.110  -9.359  17.384  1.00157.44           C  
ANISOU 1300  CA  ASN A 189    21631  21194  16994   3942   1628    654       C  
ATOM   1301  C   ASN A 189      16.375  -8.605  18.487  1.00149.26           C  
ANISOU 1301  C   ASN A 189    20333  20098  16281   3524   1453    585       C  
ATOM   1302  O   ASN A 189      15.618  -9.229  19.239  1.00152.86           O  
ANISOU 1302  O   ASN A 189    20957  20319  16804   3407   1334    435       O  
ATOM   1303  CB  ASN A 189      17.867 -10.549  17.987  1.00164.71           C  
ANISOU 1303  CB  ASN A 189    22678  22143  17762   4268   1755    683       C  
ATOM   1304  CG  ASN A 189      16.951 -11.708  18.333  1.00168.39           C  
ANISOU 1304  CG  ASN A 189    23581  22233  18165   4253   1630    468       C  
ATOM   1305  OD1 ASN A 189      15.931 -11.924  17.677  1.00166.23           O  
ANISOU 1305  OD1 ASN A 189    23641  21683  17835   4137   1495    318       O  
ATOM   1306  ND2 ASN A 189      17.306 -12.455  19.371  1.00172.37           N  
ANISOU 1306  ND2 ASN A 189    24084  22731  18677   4355   1664    464       N  
ATOM   1307  N   LYS A 190      16.573  -7.288  18.603  1.00130.95           N  
ANISOU 1307  N   LYS A 190    17627  17978  14150   3300   1435    696       N  
ATOM   1308  CA  LYS A 190      15.962  -6.488  19.671  1.00113.61           C  
ANISOU 1308  CA  LYS A 190    15188  15735  12242   2929   1286    646       C  
ATOM   1309  C   LYS A 190      16.310  -7.043  21.052  1.00103.97           C  
ANISOU 1309  C   LYS A 190    13870  14536  11096   2943   1294    642       C  
ATOM   1310  O   LYS A 190      15.490  -7.018  21.972  1.00101.83           O  
ANISOU 1310  O   LYS A 190    13600  14095  10996   2709   1158    519       O  
ATOM   1311  CB  LYS A 190      14.441  -6.400  19.500  1.00110.27           C  
ANISOU 1311  CB  LYS A 190    14980  15004  11914   2676   1098    456       C  
ATOM   1312  CG  LYS A 190      13.946  -5.236  18.663  1.00110.94           C  
ANISOU 1312  CG  LYS A 190    14970  15105  12078   2482   1034    478       C  
ATOM   1313  CD  LYS A 190      12.432  -5.300  18.507  1.00107.80           C  
ANISOU 1313  CD  LYS A 190    14792  14413  11753   2262    852    309       C  
ATOM   1314  CE  LYS A 190      11.885  -4.060  17.819  1.00105.70           C  
ANISOU 1314  CE  LYS A 190    14400  14166  11594   2051    782    338       C  
ATOM   1315  NZ  LYS A 190      10.444  -4.214  17.471  1.00101.86           N  
ANISOU 1315  NZ  LYS A 190    14142  13420  11138   1876    616    202       N  
ATOM   1316  N   ILE A 191      17.534  -7.559  21.196  1.00 93.77           N  
ANISOU 1316  N   ILE A 191    12492  13467   9669   3230   1460    788       N  
ATOM   1317  CA  ILE A 191      17.889  -8.277  22.417  1.00 86.31           C  
ANISOU 1317  CA  ILE A 191    11506  12532   8757   3293   1478    783       C  
ATOM   1318  C   ILE A 191      17.921  -7.340  23.622  1.00 71.31           C  
ANISOU 1318  C   ILE A 191     9243  10734   7117   2976   1388    827       C  
ATOM   1319  O   ILE A 191      17.529  -7.728  24.729  1.00 72.60           O  
ANISOU 1319  O   ILE A 191     9426  10770   7387   2868   1310    730       O  
ATOM   1320  CB  ILE A 191      19.227  -9.021  22.236  1.00 93.04           C  
ANISOU 1320  CB  ILE A 191    12336  13625   9390   3700   1689    956       C  
ATOM   1321  CG1 ILE A 191      19.461  -9.981  23.404  1.00 94.83           C  
ANISOU 1321  CG1 ILE A 191    12606  13807   9618   3800   1704    923       C  
ATOM   1322  CG2 ILE A 191      20.391  -8.046  22.125  1.00 91.77           C  
ANISOU 1322  CG2 ILE A 191    11746  13864   9260   3706   1794   1223       C  
ATOM   1323  CD1 ILE A 191      18.390 -11.038  23.548  1.00101.31           C  
ANISOU 1323  CD1 ILE A 191    13859  14244  10391   3801   1598    683       C  
ATOM   1324  N   TYR A 192      18.356  -6.090  23.431  1.00 74.66           N  
ANISOU 1324  N   TYR A 192     9356  11373   7639   2815   1389    974       N  
ATOM   1325  CA  TYR A 192      18.485  -5.188  24.572  1.00 71.37           C  
ANISOU 1325  CA  TYR A 192     8629  11049   7439   2522   1301   1029       C  
ATOM   1326  C   TYR A 192      17.124  -4.816  25.138  1.00 62.35           C  
ANISOU 1326  C   TYR A 192     7586   9618   6486   2218   1123    827       C  
ATOM   1327  O   TYR A 192      16.932  -4.809  26.361  1.00 62.31           O  
ANISOU 1327  O   TYR A 192     7501   9559   6615   2068   1052    778       O  
ATOM   1328  CB  TYR A 192      19.251  -3.926  24.176  1.00 74.08           C  
ANISOU 1328  CB  TYR A 192     8655  11670   7824   2404   1326   1240       C  
ATOM   1329  CG  TYR A 192      20.739  -4.117  24.019  1.00 81.07           C  
ANISOU 1329  CG  TYR A 192     9317  12918   8568   2643   1490   1502       C  
ATOM   1330  CD1 TYR A 192      21.564  -4.222  25.130  1.00 81.32           C  
ANISOU 1330  CD1 TYR A 192     9114  13139   8646   2626   1508   1633       C  
ATOM   1331  CD2 TYR A 192      21.322  -4.173  22.762  1.00 89.12           C  
ANISOU 1331  CD2 TYR A 192    10349  14109   9405   2886   1626   1636       C  
ATOM   1332  CE1 TYR A 192      22.928  -4.389  24.994  1.00 87.50           C  
ANISOU 1332  CE1 TYR A 192     9662  14285   9298   2844   1657   1905       C  
ATOM   1333  CE2 TYR A 192      22.684  -4.340  22.614  1.00100.31           C  
ANISOU 1333  CE2 TYR A 192    11538  15891  10686   3122   1787   1905       C  
ATOM   1334  CZ  TYR A 192      23.482  -4.447  23.733  1.00100.36           C  
ANISOU 1334  CZ  TYR A 192    11295  16094  10745   3098   1801   2046       C  
ATOM   1335  OH  TYR A 192      24.840  -4.612  23.589  1.00113.65           O  
ANISOU 1335  OH  TYR A 192    12723  18169  12289   3334   1961   2345       O  
ATOM   1336  N   GLU A 193      16.163  -4.517  24.262  1.00 57.78           N  
ANISOU 1336  N   GLU A 193     7180   8863   5913   2134   1054    719       N  
ATOM   1337  CA  GLU A 193      14.831  -4.149  24.728  1.00 64.51           C  
ANISOU 1337  CA  GLU A 193     8112   9465   6935   1865    895    554       C  
ATOM   1338  C   GLU A 193      14.159  -5.312  25.447  1.00 60.89           C  
ANISOU 1338  C   GLU A 193     7875   8791   6471   1906    844    399       C  
ATOM   1339  O   GLU A 193      13.498  -5.123  26.477  1.00 62.44           O  
ANISOU 1339  O   GLU A 193     8024   8874   6826   1708    744    318       O  
ATOM   1340  CB  GLU A 193      13.989  -3.684  23.539  1.00 55.56           C  
ANISOU 1340  CB  GLU A 193     7117   8211   5783   1796    840    495       C  
ATOM   1341  CG  GLU A 193      12.518  -3.511  23.834  1.00 53.84           C  
ANISOU 1341  CG  GLU A 193     7020   7736   5702   1572    687    337       C  
ATOM   1342  CD  GLU A 193      11.756  -2.955  22.654  1.00 63.33           C  
ANISOU 1342  CD  GLU A 193     8320   8852   6888   1496    632    309       C  
ATOM   1343  OE1 GLU A 193      10.582  -2.568  22.837  1.00 66.21           O  
ANISOU 1343  OE1 GLU A 193     8725   9053   7378   1296    510    221       O  
ATOM   1344  OE2 GLU A 193      12.331  -2.901  21.543  1.00 73.54           O  
ANISOU 1344  OE2 GLU A 193     9646  10256   8041   1643    715    388       O  
ATOM   1345  N   LYS A 194      14.369  -6.532  24.947  1.00 63.68           N  
ANISOU 1345  N   LYS A 194     8480   9088   6629   2173    915    367       N  
ATOM   1346  CA  LYS A 194      13.762  -7.706  25.562  1.00 63.78           C  
ANISOU 1346  CA  LYS A 194     8736   8884   6613   2213    859    230       C  
ATOM   1347  C   LYS A 194      14.359  -7.976  26.937  1.00 59.09           C  
ANISOU 1347  C   LYS A 194     7972   8384   6097   2219    888    268       C  
ATOM   1348  O   LYS A 194      13.625  -8.235  27.901  1.00 60.83           O  
ANISOU 1348  O   LYS A 194     8230   8451   6433   2068    788    163       O  
ATOM   1349  CB  LYS A 194      13.945  -8.912  24.642  1.00 79.60           C  
ANISOU 1349  CB  LYS A 194    11087  10798   8361   2512    932    197       C  
ATOM   1350  CG  LYS A 194      12.996 -10.070  24.883  1.00 83.81           C  
ANISOU 1350  CG  LYS A 194    11971  11035   8839   2505    826     35       C  
ATOM   1351  CD  LYS A 194      12.995 -10.981  23.670  1.00 91.42           C  
ANISOU 1351  CD  LYS A 194    13328  11871   9536   2748    865     -4       C  
ATOM   1352  CE  LYS A 194      12.757 -10.170  22.399  1.00 97.21           C  
ANISOU 1352  CE  LYS A 194    14063  12636  10235   2698    858     24       C  
ATOM   1353  NZ  LYS A 194      12.924 -10.980  21.159  1.00 93.60           N  
ANISOU 1353  NZ  LYS A 194    13988  12083   9493   2964    917      4       N  
ATOM   1354  N   VAL A 195      15.689  -7.905  27.047  1.00 68.51           N  
ANISOU 1354  N   VAL A 195     8963   9844   7224   2387   1022    434       N  
ATOM   1355  CA  VAL A 195      16.343  -8.114  28.335  1.00 57.22           C  
ANISOU 1355  CA  VAL A 195     7348   8531   5860   2387   1048    494       C  
ATOM   1356  C   VAL A 195      15.925  -7.033  29.321  1.00 56.17           C  
ANISOU 1356  C   VAL A 195     6985   8396   5962   2049    930    479       C  
ATOM   1357  O   VAL A 195      15.708  -7.304  30.510  1.00 62.52           O  
ANISOU 1357  O   VAL A 195     7760   9134   6862   1956    876    423       O  
ATOM   1358  CB  VAL A 195      17.873  -8.158  28.155  1.00 58.92           C  
ANISOU 1358  CB  VAL A 195     7361   9072   5952   2625   1212    715       C  
ATOM   1359  CG1 VAL A 195      18.575  -8.158  29.503  1.00 58.73           C  
ANISOU 1359  CG1 VAL A 195     7093   9204   6018   2572   1219    806       C  
ATOM   1360  CG2 VAL A 195      18.279  -9.378  27.345  1.00 64.36           C  
ANISOU 1360  CG2 VAL A 195     8321   9744   6389   3010   1345    722       C  
ATOM   1361  N   TYR A 196      15.758  -5.799  28.835  1.00 60.72           N  
ANISOU 1361  N   TYR A 196     7422   9026   6623   1867    888    524       N  
ATOM   1362  CA  TYR A 196      15.336  -4.717  29.717  1.00 54.77           C  
ANISOU 1362  CA  TYR A 196     6495   8246   6070   1562    779    508       C  
ATOM   1363  C   TYR A 196      13.931  -4.957  30.248  1.00 51.32           C  
ANISOU 1363  C   TYR A 196     6232   7530   5739   1418    660    319       C  
ATOM   1364  O   TYR A 196      13.667  -4.769  31.445  1.00 59.56           O  
ANISOU 1364  O   TYR A 196     7199   8526   6907   1269    598    279       O  
ATOM   1365  CB  TYR A 196      15.404  -3.382  28.977  1.00 53.00           C  
ANISOU 1365  CB  TYR A 196     6132   8112   5893   1414    757    593       C  
ATOM   1366  CG  TYR A 196      14.751  -2.246  29.728  1.00 51.49           C  
ANISOU 1366  CG  TYR A 196     5846   7829   5887   1114    637    549       C  
ATOM   1367  CD1 TYR A 196      13.476  -1.804  29.391  1.00 52.67           C  
ANISOU 1367  CD1 TYR A 196     6124   7771   6117    982    550    424       C  
ATOM   1368  CD2 TYR A 196      15.403  -1.623  30.784  1.00 51.42           C  
ANISOU 1368  CD2 TYR A 196     5634   7941   5961    968    609    640       C  
ATOM   1369  CE1 TYR A 196      12.876  -0.767  30.082  1.00 49.15           C  
ANISOU 1369  CE1 TYR A 196     5612   7240   5823    745    456    391       C  
ATOM   1370  CE2 TYR A 196      14.812  -0.588  31.478  1.00 50.26           C  
ANISOU 1370  CE2 TYR A 196     5448   7690   5960    714    502    596       C  
ATOM   1371  CZ  TYR A 196      13.549  -0.163  31.123  1.00 50.44           C  
ANISOU 1371  CZ  TYR A 196     5607   7504   6054    618    435    470       C  
ATOM   1372  OH  TYR A 196      12.960   0.870  31.815  1.00 49.47           O  
ANISOU 1372  OH  TYR A 196     5463   7275   6058    401    345    432       O  
ATOM   1373  N   HIS A 197      13.019  -5.394  29.375  1.00 51.25           N  
ANISOU 1373  N   HIS A 197     6460   7343   5672   1459    626    213       N  
ATOM   1374  CA  HIS A 197      11.656  -5.657  29.820  1.00 56.62           C  
ANISOU 1374  CA  HIS A 197     7287   7782   6442   1317    508     65       C  
ATOM   1375  C   HIS A 197      11.614  -6.805  30.823  1.00 49.83           C  
ANISOU 1375  C   HIS A 197     6524   6842   5567   1387    501      1       C  
ATOM   1376  O   HIS A 197      10.915  -6.723  31.845  1.00 56.10           O  
ANISOU 1376  O   HIS A 197     7287   7538   6489   1231    422    -64       O  
ATOM   1377  CB  HIS A 197      10.767  -5.957  28.614  1.00 50.23           C  
ANISOU 1377  CB  HIS A 197     6714   6820   5553   1340    461     -7       C  
ATOM   1378  CG  HIS A 197       9.370  -6.351  28.977  1.00 53.60           C  
ANISOU 1378  CG  HIS A 197     7291   7022   6050   1199    334   -127       C  
ATOM   1379  ND1 HIS A 197       8.632  -7.243  28.231  1.00 51.14           N  
ANISOU 1379  ND1 HIS A 197     7261   6542   5627   1245    274   -200       N  
ATOM   1380  CD2 HIS A 197       8.575  -5.973  30.006  1.00 51.51           C  
ANISOU 1380  CD2 HIS A 197     6937   6686   5948   1012    253   -170       C  
ATOM   1381  CE1 HIS A 197       7.443  -7.401  28.785  1.00 57.35           C  
ANISOU 1381  CE1 HIS A 197     8100   7179   6511   1076    154   -269       C  
ATOM   1382  NE2 HIS A 197       7.383  -6.641  29.864  1.00 58.37           N  
ANISOU 1382  NE2 HIS A 197     8001   7369   6807    948    150   -252       N  
ATOM   1383  N   ILE A 198      12.377  -7.872  30.563  1.00 51.22           N  
ANISOU 1383  N   ILE A 198     6821   7062   5579   1635    590     28       N  
ATOM   1384  CA  ILE A 198      12.397  -9.001  31.489  1.00 56.55           C  
ANISOU 1384  CA  ILE A 198     7603   7658   6226   1717    587    -26       C  
ATOM   1385  C   ILE A 198      12.947  -8.566  32.842  1.00 56.04           C  
ANISOU 1385  C   ILE A 198     7280   7723   6288   1621    596     31       C  
ATOM   1386  O   ILE A 198      12.415  -8.939  33.899  1.00 58.06           O  
ANISOU 1386  O   ILE A 198     7560   7871   6627   1527    531    -43       O  
ATOM   1387  CB  ILE A 198      13.215 -10.166  30.898  1.00 64.45           C  
ANISOU 1387  CB  ILE A 198     8794   8689   7004   2036    698      7       C  
ATOM   1388  CG1 ILE A 198      12.620 -10.640  29.571  1.00 71.56           C  
ANISOU 1388  CG1 ILE A 198    10006   9428   7758   2123    674    -61       C  
ATOM   1389  CG2 ILE A 198      13.290 -11.318  31.887  1.00 53.36           C  
ANISOU 1389  CG2 ILE A 198     7504   7202   5568   2127    697    -41       C  
ATOM   1390  CD1 ILE A 198      11.278 -11.303  29.708  1.00 74.66           C  
ANISOU 1390  CD1 ILE A 198    10660   9539   8169   1986    526   -205       C  
ATOM   1391  N   CYS A 199      13.999  -7.739  32.831  1.00 56.98           N  
ANISOU 1391  N   CYS A 199     7149   8079   6420   1624    666    173       N  
ATOM   1392  CA  CYS A 199      14.603  -7.304  34.084  1.00 57.97           C  
ANISOU 1392  CA  CYS A 199     7042   8335   6647   1518    661    243       C  
ATOM   1393  C   CYS A 199      13.657  -6.416  34.876  1.00 54.82           C  
ANISOU 1393  C   CYS A 199     6584   7816   6429   1237    543    163       C  
ATOM   1394  O   CYS A 199      13.581  -6.527  36.105  1.00 60.62           O  
ANISOU 1394  O   CYS A 199     7266   8524   7243   1152    505    136       O  
ATOM   1395  CB  CYS A 199      15.917  -6.569  33.816  1.00 52.10           C  
ANISOU 1395  CB  CYS A 199     6048   7881   5869   1552    740    438       C  
ATOM   1396  SG  CYS A 199      17.276  -7.621  33.270  1.00 70.83           S  
ANISOU 1396  SG  CYS A 199     8416  10470   8027   1920    909    586       S  
ATOM   1397  N   VAL A 200      12.917  -5.537  34.194  1.00 48.31           N  
ANISOU 1397  N   VAL A 200     5778   6915   5662   1105    490    130       N  
ATOM   1398  CA  VAL A 200      11.973  -4.688  34.915  1.00 51.98           C  
ANISOU 1398  CA  VAL A 200     6207   7262   6283    873    392     62       C  
ATOM   1399  C   VAL A 200      10.862  -5.532  35.523  1.00 52.59           C  
ANISOU 1399  C   VAL A 200     6443   7140   6397    855    332    -69       C  
ATOM   1400  O   VAL A 200      10.474  -5.333  36.684  1.00 55.85           O  
ANISOU 1400  O   VAL A 200     6807   7502   6911    738    285   -106       O  
ATOM   1401  CB  VAL A 200      11.410  -3.591  33.994  1.00 46.61           C  
ANISOU 1401  CB  VAL A 200     5520   6546   5645    761    356     66       C  
ATOM   1402  CG1 VAL A 200      10.308  -2.819  34.708  1.00 45.34           C  
ANISOU 1402  CG1 VAL A 200     5358   6243   5625    567    269     -7       C  
ATOM   1403  CG2 VAL A 200      12.517  -2.648  33.554  1.00 47.49           C  
ANISOU 1403  CG2 VAL A 200     5454   6858   5731    737    401    211       C  
ATOM   1404  N   THR A 201      10.355  -6.511  34.764  1.00 46.43           N  
ANISOU 1404  N   THR A 201     5868   6249   5526    969    326   -130       N  
ATOM   1405  CA  THR A 201       9.297  -7.362  35.295  1.00 50.03           C  
ANISOU 1405  CA  THR A 201     6478   6524   6007    931    252   -232       C  
ATOM   1406  C   THR A 201       9.775  -8.162  36.500  1.00 53.73           C  
ANISOU 1406  C   THR A 201     6929   7012   6473    988    273   -240       C  
ATOM   1407  O   THR A 201       9.009  -8.377  37.447  1.00 46.58           O  
ANISOU 1407  O   THR A 201     6040   6007   5652    886    210   -298       O  
ATOM   1408  CB  THR A 201       8.775  -8.297  34.203  1.00 54.69           C  
ANISOU 1408  CB  THR A 201     7321   6987   6471   1028    226   -282       C  
ATOM   1409  OG1 THR A 201       8.251  -7.519  33.122  1.00 56.16           O  
ANISOU 1409  OG1 THR A 201     7517   7154   6667    957    196   -273       O  
ATOM   1410  CG2 THR A 201       7.673  -9.193  34.745  1.00 50.12           C  
ANISOU 1410  CG2 THR A 201     6904   6228   5914    957    127   -365       C  
ATOM   1411  N   VAL A 202      11.040  -8.580  36.503  1.00 47.23           N  
ANISOU 1411  N   VAL A 202     6058   6333   5556   1155    365   -167       N  
ATOM   1412  CA  VAL A 202      11.562  -9.304  37.661  1.00 46.95           C  
ANISOU 1412  CA  VAL A 202     5990   6332   5517   1214    388   -159       C  
ATOM   1413  C   VAL A 202      11.723  -8.364  38.851  1.00 46.66           C  
ANISOU 1413  C   VAL A 202     5738   6375   5618   1040    361   -128       C  
ATOM   1414  O   VAL A 202      11.315  -8.683  39.975  1.00 50.23           O  
ANISOU 1414  O   VAL A 202     6195   6755   6135    971    319   -179       O  
ATOM   1415  CB  VAL A 202      12.889 -10.000  37.308  1.00 52.71           C  
ANISOU 1415  CB  VAL A 202     6716   7214   6095   1464    504    -66       C  
ATOM   1416  CG1 VAL A 202      13.570 -10.520  38.565  1.00 48.65           C  
ANISOU 1416  CG1 VAL A 202     6110   6783   5594   1510    532    -28       C  
ATOM   1417  CG2 VAL A 202      12.647 -11.136  36.325  1.00 49.58           C  
ANISOU 1417  CG2 VAL A 202     6610   6689   5539   1658    525   -120       C  
ATOM   1418  N   LEU A 203      12.321  -7.191  38.623  1.00 46.18           N  
ANISOU 1418  N   LEU A 203     5501   6455   5591    961    380    -39       N  
ATOM   1419  CA  LEU A 203      12.633  -6.286  39.725  1.00 45.69           C  
ANISOU 1419  CA  LEU A 203     5267   6465   5628    796    347      4       C  
ATOM   1420  C   LEU A 203      11.387  -5.703  40.385  1.00 44.38           C  
ANISOU 1420  C   LEU A 203     5146   6131   5584    617    263    -95       C  
ATOM   1421  O   LEU A 203      11.397  -5.452  41.595  1.00 48.40           O  
ANISOU 1421  O   LEU A 203     5598   6636   6158    519    232   -103       O  
ATOM   1422  CB  LEU A 203      13.546  -5.166  39.233  1.00 46.40           C  
ANISOU 1422  CB  LEU A 203     5188   6733   5709    734    368    135       C  
ATOM   1423  CG  LEU A 203      14.974  -5.621  38.927  1.00 51.52           C  
ANISOU 1423  CG  LEU A 203     5719   7613   6243    899    459    284       C  
ATOM   1424  CD1 LEU A 203      15.801  -4.472  38.379  1.00 48.76           C  
ANISOU 1424  CD1 LEU A 203     5192   7450   5886    810    466    435       C  
ATOM   1425  CD2 LEU A 203      15.618  -6.206  40.176  1.00 54.39           C  
ANISOU 1425  CD2 LEU A 203     6003   8057   6605    923    467    325       C  
ATOM   1426  N   ILE A 204      10.310  -5.472  39.629  1.00 46.69           N  
ANISOU 1426  N   ILE A 204     5541   6296   5904    580    228   -159       N  
ATOM   1427  CA  ILE A 204       9.123  -4.858  40.215  1.00 47.57           C  
ANISOU 1427  CA  ILE A 204     5676   6276   6124    435    163   -225       C  
ATOM   1428  C   ILE A 204       8.014  -5.860  40.488  1.00 46.21           C  
ANISOU 1428  C   ILE A 204     5635   5961   5964    456    123   -308       C  
ATOM   1429  O   ILE A 204       6.945  -5.466  40.975  1.00 47.70           O  
ANISOU 1429  O   ILE A 204     5834   6057   6235    358     78   -345       O  
ATOM   1430  CB  ILE A 204       8.586  -3.703  39.344  1.00 48.75           C  
ANISOU 1430  CB  ILE A 204     5817   6395   6311    350    142   -213       C  
ATOM   1431  CG1 ILE A 204       7.896  -4.241  38.092  1.00 43.89           C  
ANISOU 1431  CG1 ILE A 204     5321   5707   5646    419    132   -245       C  
ATOM   1432  CG2 ILE A 204       9.710  -2.736  38.987  1.00 49.35           C  
ANISOU 1432  CG2 ILE A 204     5772   6614   6365    314    170   -115       C  
ATOM   1433  CD1 ILE A 204       7.227  -3.155  37.259  1.00 44.51           C  
ANISOU 1433  CD1 ILE A 204     5395   5750   5768    336    106   -233       C  
ATOM   1434  N   TYR A 205       8.226  -7.143  40.199  1.00 42.94           N  
ANISOU 1434  N   TYR A 205     5328   5527   5460    584    138   -326       N  
ATOM   1435  CA  TYR A 205       7.186  -8.112  40.513  1.00 45.98           C  
ANISOU 1435  CA  TYR A 205     5848   5772   5850    574     79   -391       C  
ATOM   1436  C   TYR A 205       7.739  -9.375  41.165  1.00 50.64           C  
ANISOU 1436  C   TYR A 205     6507   6360   6375    682     98   -405       C  
ATOM   1437  O   TYR A 205       7.544  -9.587  42.365  1.00 51.83           O  
ANISOU 1437  O   TYR A 205     6618   6493   6583    632     81   -423       O  
ATOM   1438  CB  TYR A 205       6.388  -8.475  39.258  1.00 43.04           C  
ANISOU 1438  CB  TYR A 205     5629   5302   5424    584     33   -413       C  
ATOM   1439  CG  TYR A 205       5.167  -9.309  39.568  1.00 46.80           C  
ANISOU 1439  CG  TYR A 205     6229   5639   5915    517    -56   -454       C  
ATOM   1440  CD1 TYR A 205       4.040  -8.732  40.141  1.00 42.17           C  
ANISOU 1440  CD1 TYR A 205     5566   5016   5442    378   -108   -450       C  
ATOM   1441  CD2 TYR A 205       5.148 -10.675  39.313  1.00 47.81           C  
ANISOU 1441  CD2 TYR A 205     6556   5676   5934    595    -90   -483       C  
ATOM   1442  CE1 TYR A 205       2.923  -9.487  40.440  1.00 42.23           C  
ANISOU 1442  CE1 TYR A 205     5657   4926   5461    305   -193   -455       C  
ATOM   1443  CE2 TYR A 205       4.035 -11.440  39.608  1.00 51.37           C  
ANISOU 1443  CE2 TYR A 205     7121   6003   6393    503   -191   -501       C  
ATOM   1444  CZ  TYR A 205       2.926 -10.842  40.171  1.00 55.06           C  
ANISOU 1444  CZ  TYR A 205     7474   6464   6983    351   -244   -478       C  
ATOM   1445  OH  TYR A 205       1.819 -11.605  40.465  1.00 52.49           O  
ANISOU 1445  OH  TYR A 205     7236   6043   6663    249   -348   -466       O  
ATOM   1446  N   PHE A 206       8.426 -10.222  40.395  1.00 48.56           N  
ANISOU 1446  N   PHE A 206     6357   6112   5981    845    140   -393       N  
ATOM   1447  CA  PHE A 206       8.727 -11.568  40.875  1.00 53.86           C  
ANISOU 1447  CA  PHE A 206     7156   6737   6572    965    149   -414       C  
ATOM   1448  C   PHE A 206       9.695 -11.553  42.054  1.00 50.11           C  
ANISOU 1448  C   PHE A 206     6526   6389   6124   1000    203   -370       C  
ATOM   1449  O   PHE A 206       9.421 -12.160  43.097  1.00 55.60           O  
ANISOU 1449  O   PHE A 206     7245   7029   6850    972    173   -401       O  
ATOM   1450  CB  PHE A 206       9.280 -12.416  39.729  1.00 46.62           C  
ANISOU 1450  CB  PHE A 206     6426   5801   5485   1164    194   -406       C  
ATOM   1451  CG  PHE A 206       8.279 -12.678  38.643  1.00 48.81           C  
ANISOU 1451  CG  PHE A 206     6911   5923   5711   1123    117   -455       C  
ATOM   1452  CD1 PHE A 206       7.263 -13.600  38.834  1.00 53.16           C  
ANISOU 1452  CD1 PHE A 206     7661   6294   6244   1053     13   -512       C  
ATOM   1453  CD2 PHE A 206       8.345 -11.999  37.439  1.00 46.67           C  
ANISOU 1453  CD2 PHE A 206     6636   5691   5406   1137    138   -432       C  
ATOM   1454  CE1 PHE A 206       6.332 -13.841  37.845  1.00 48.16           C  
ANISOU 1454  CE1 PHE A 206     7220   5522   5556    986    -79   -540       C  
ATOM   1455  CE2 PHE A 206       7.417 -12.238  36.444  1.00 57.19           C  
ANISOU 1455  CE2 PHE A 206     8163   6882   6685   1087     57   -470       C  
ATOM   1456  CZ  PHE A 206       6.408 -13.160  36.648  1.00 53.66           C  
ANISOU 1456  CZ  PHE A 206     7915   6257   6218   1005    -57   -522       C  
ATOM   1457  N   LEU A 207      10.840 -10.886  41.904  1.00 50.94           N  
ANISOU 1457  N   LEU A 207     6468   6675   6212   1051    277   -284       N  
ATOM   1458  CA  LEU A 207      11.827 -10.876  42.983  1.00 56.14           C  
ANISOU 1458  CA  LEU A 207     6971   7473   6884   1071    317   -219       C  
ATOM   1459  C   LEU A 207      11.311 -10.260  44.281  1.00 53.07           C  
ANISOU 1459  C   LEU A 207     6485   7053   6626    881    257   -251       C  
ATOM   1460  O   LEU A 207      11.464 -10.896  45.341  1.00 50.36           O  
ANISOU 1460  O   LEU A 207     6139   6706   6289    897    252   -260       O  
ATOM   1461  CB  LEU A 207      13.099 -10.168  42.504  1.00 53.16           C  
ANISOU 1461  CB  LEU A 207     6420   7316   6465   1126    390    -91       C  
ATOM   1462  CG  LEU A 207      14.126  -9.875  43.600  1.00 58.21           C  
ANISOU 1462  CG  LEU A 207     6859   8129   7129   1088    408      8       C  
ATOM   1463  CD1 LEU A 207      14.725 -11.172  44.132  1.00 59.67           C  
ANISOU 1463  CD1 LEU A 207     7090   8350   7230   1272    459     32       C  
ATOM   1464  CD2 LEU A 207      15.212  -8.936  43.105  1.00 56.95           C  
ANISOU 1464  CD2 LEU A 207     6504   8191   6945   1070    448    157       C  
ATOM   1465  N   PRO A 208      10.740  -9.047  44.296  1.00 54.74           N  
ANISOU 1465  N   PRO A 208     6627   7241   6930    715    215   -264       N  
ATOM   1466  CA  PRO A 208      10.207  -8.527  45.566  1.00 50.89           C  
ANISOU 1466  CA  PRO A 208     6088   6706   6542    567    168   -298       C  
ATOM   1467  C   PRO A 208       9.127  -9.405  46.171  1.00 51.22           C  
ANISOU 1467  C   PRO A 208     6247   6603   6613    559    126   -377       C  
ATOM   1468  O   PRO A 208       9.056  -9.519  47.400  1.00 58.05           O  
ANISOU 1468  O   PRO A 208     7078   7461   7518    510    111   -390       O  
ATOM   1469  CB  PRO A 208       9.662  -7.140  45.181  1.00 46.34           C  
ANISOU 1469  CB  PRO A 208     5472   6101   6033    434    141   -300       C  
ATOM   1470  CG  PRO A 208       9.427  -7.210  43.717  1.00 48.50           C  
ANISOU 1470  CG  PRO A 208     5812   6354   6262    498    153   -301       C  
ATOM   1471  CD  PRO A 208      10.505  -8.101  43.183  1.00 55.40           C  
ANISOU 1471  CD  PRO A 208     6696   7329   7025    666    213   -250       C  
ATOM   1472  N   LEU A 209       8.292 -10.038  45.343  1.00 53.43           N  
ANISOU 1472  N   LEU A 209     6665   6771   6864    595     99   -419       N  
ATOM   1473  CA  LEU A 209       7.269 -10.920  45.885  1.00 48.95           C  
ANISOU 1473  CA  LEU A 209     6206   6078   6316    566     43   -470       C  
ATOM   1474  C   LEU A 209       7.884 -12.151  46.530  1.00 57.57           C  
ANISOU 1474  C   LEU A 209     7358   7172   7343    671     58   -472       C  
ATOM   1475  O   LEU A 209       7.429 -12.587  47.590  1.00 55.33           O  
ANISOU 1475  O   LEU A 209     7082   6842   7100    622     27   -492       O  
ATOM   1476  CB  LEU A 209       6.283 -11.328  44.792  1.00 48.10           C  
ANISOU 1476  CB  LEU A 209     6243   5854   6177    554    -13   -494       C  
ATOM   1477  CG  LEU A 209       5.281 -10.248  44.388  1.00 61.39           C  
ANISOU 1477  CG  LEU A 209     7870   7513   7942    433    -46   -489       C  
ATOM   1478  CD1 LEU A 209       4.203 -10.841  43.502  1.00 65.66           C  
ANISOU 1478  CD1 LEU A 209     8555   7943   8452    396   -123   -497       C  
ATOM   1479  CD2 LEU A 209       4.681  -9.574  45.610  1.00 42.71           C  
ANISOU 1479  CD2 LEU A 209     5396   5153   5680    332    -52   -487       C  
ATOM   1480  N   LEU A 210       8.940 -12.705  45.929  1.00 51.36           N  
ANISOU 1480  N   LEU A 210     6614   6449   6451    830    115   -440       N  
ATOM   1481  CA  LEU A 210       9.607 -13.846  46.547  1.00 54.62           C  
ANISOU 1481  CA  LEU A 210     7086   6874   6793    957    142   -430       C  
ATOM   1482  C   LEU A 210      10.255 -13.456  47.867  1.00 58.83           C  
ANISOU 1482  C   LEU A 210     7443   7525   7387    910    165   -392       C  
ATOM   1483  O   LEU A 210      10.180 -14.202  48.854  1.00 54.68           O  
ANISOU 1483  O   LEU A 210     6948   6963   6865    918    148   -408       O  
ATOM   1484  CB  LEU A 210      10.653 -14.421  45.594  1.00 54.49           C  
ANISOU 1484  CB  LEU A 210     7144   6923   6637   1171    219   -384       C  
ATOM   1485  CG  LEU A 210      10.090 -15.116  44.362  1.00 68.82           C  
ANISOU 1485  CG  LEU A 210     9207   8591   8351   1247    191   -430       C  
ATOM   1486  CD1 LEU A 210      11.217 -15.600  43.471  1.00 79.52           C  
ANISOU 1486  CD1 LEU A 210    10637  10025   9551   1494    290   -376       C  
ATOM   1487  CD2 LEU A 210       9.200 -16.269  44.791  1.00 73.98           C  
ANISOU 1487  CD2 LEU A 210    10072   9056   8982   1215    106   -494       C  
ATOM   1488  N   VAL A 211      10.862 -12.269  47.915  1.00 52.45           N  
ANISOU 1488  N   VAL A 211     6458   6850   6620    843    191   -337       N  
ATOM   1489  CA  VAL A 211      11.535 -11.839  49.138  1.00 49.09           C  
ANISOU 1489  CA  VAL A 211     5882   6534   6234    776    195   -291       C  
ATOM   1490  C   VAL A 211      10.516 -11.609  50.248  1.00 54.63           C  
ANISOU 1490  C   VAL A 211     6599   7130   7029    633    137   -357       C  
ATOM   1491  O   VAL A 211      10.671 -12.101  51.376  1.00 55.10           O  
ANISOU 1491  O   VAL A 211     6643   7197   7095    629    129   -358       O  
ATOM   1492  CB  VAL A 211      12.379 -10.580  48.868  1.00 51.42           C  
ANISOU 1492  CB  VAL A 211     6014   6983   6541    706    212   -206       C  
ATOM   1493  CG1 VAL A 211      12.935 -10.022  50.168  1.00 44.51           C  
ANISOU 1493  CG1 VAL A 211     5013   6195   5704    588    186   -159       C  
ATOM   1494  CG2 VAL A 211      13.507 -10.899  47.897  1.00 51.77           C  
ANISOU 1494  CG2 VAL A 211     6013   7175   6483    870    285   -108       C  
ATOM   1495  N   ILE A 212       9.446 -10.870  49.936  1.00 51.69           N  
ANISOU 1495  N   ILE A 212     6254   6664   6720    528    102   -403       N  
ATOM   1496  CA  ILE A 212       8.397 -10.618  50.916  1.00 56.28           C  
ANISOU 1496  CA  ILE A 212     6849   7158   7378    420     62   -450       C  
ATOM   1497  C   ILE A 212       7.721 -11.916  51.331  1.00 51.52           C  
ANISOU 1497  C   ILE A 212     6349   6462   6764    460     35   -484       C  
ATOM   1498  O   ILE A 212       7.329 -12.075  52.494  1.00 53.93           O  
ANISOU 1498  O   ILE A 212     6642   6744   7107    410     18   -497       O  
ATOM   1499  CB  ILE A 212       7.382  -9.607  50.347  1.00 45.93           C  
ANISOU 1499  CB  ILE A 212     5546   5782   6124    334     43   -470       C  
ATOM   1500  CG1 ILE A 212       8.038  -8.239  50.165  1.00 47.13           C  
ANISOU 1500  CG1 ILE A 212     5612   6008   6286    271     59   -435       C  
ATOM   1501  CG2 ILE A 212       6.165  -9.495  51.251  1.00 39.82           C  
ANISOU 1501  CG2 ILE A 212     4792   4925   5413    263     17   -499       C  
ATOM   1502  CD1 ILE A 212       7.132  -7.213  49.503  1.00 42.34           C  
ANISOU 1502  CD1 ILE A 212     5024   5337   5725    208     48   -449       C  
ATOM   1503  N   GLY A 213       7.605 -12.878  50.412  1.00 47.10           N  
ANISOU 1503  N   GLY A 213     5911   5844   6141    547     24   -494       N  
ATOM   1504  CA  GLY A 213       6.980 -14.137  50.764  1.00 43.52           C  
ANISOU 1504  CA  GLY A 213     5585   5286   5663    565    -21   -518       C  
ATOM   1505  C   GLY A 213       7.823 -14.945  51.725  1.00 49.35           C  
ANISOU 1505  C   GLY A 213     6318   6068   6363    644      4   -505       C  
ATOM   1506  O   GLY A 213       7.302 -15.498  52.694  1.00 45.17           O  
ANISOU 1506  O   GLY A 213     5814   5488   5860    600    -30   -517       O  
ATOM   1507  N   TYR A 214       9.144 -14.964  51.518  1.00 42.34           N  
ANISOU 1507  N   TYR A 214     5378   5295   5413    761     66   -463       N  
ATOM   1508  CA  TYR A 214      10.014 -15.610  52.494  1.00 49.44           C  
ANISOU 1508  CA  TYR A 214     6240   6265   6279    837     95   -430       C  
ATOM   1509  C   TYR A 214       9.893 -14.933  53.851  1.00 51.97           C  
ANISOU 1509  C   TYR A 214     6432   6632   6683    704     77   -428       C  
ATOM   1510  O   TYR A 214       9.732 -15.599  54.887  1.00 49.81           O  
ANISOU 1510  O   TYR A 214     6181   6328   6417    697     58   -438       O  
ATOM   1511  CB  TYR A 214      11.471 -15.581  52.030  1.00 47.53           C  
ANISOU 1511  CB  TYR A 214     5919   6182   5959    981    170   -350       C  
ATOM   1512  CG  TYR A 214      12.430 -15.888  53.163  1.00 59.17           C  
ANISOU 1512  CG  TYR A 214     7288   7778   7418   1023    196   -288       C  
ATOM   1513  CD1 TYR A 214      12.717 -17.200  53.513  1.00 60.07           C  
ANISOU 1513  CD1 TYR A 214     7507   7858   7459   1167    214   -281       C  
ATOM   1514  CD2 TYR A 214      13.027 -14.867  53.900  1.00 57.94           C  
ANISOU 1514  CD2 TYR A 214     6943   7761   7312    908    193   -232       C  
ATOM   1515  CE1 TYR A 214      13.576 -17.491  54.553  1.00 70.77           C  
ANISOU 1515  CE1 TYR A 214     8758   9332   8801   1208    236   -215       C  
ATOM   1516  CE2 TYR A 214      13.886 -15.147  54.945  1.00 63.67           C  
ANISOU 1516  CE2 TYR A 214     7571   8603   8019    928    203   -164       C  
ATOM   1517  CZ  TYR A 214      14.157 -16.463  55.267  1.00 72.33           C  
ANISOU 1517  CZ  TYR A 214     8750   9680   9052   1083    229   -154       C  
ATOM   1518  OH  TYR A 214      15.013 -16.755  56.305  1.00 63.13           O  
ANISOU 1518  OH  TYR A 214     7479   8640   7867   1107    239    -77       O  
ATOM   1519  N   LEU A 215       9.960 -13.597  53.856  1.00 44.67           N  
ANISOU 1519  N   LEU A 215     5392   5768   5811    599     80   -416       N  
ATOM   1520  CA  LEU A 215       9.990 -12.866  55.118  1.00 41.26           C  
ANISOU 1520  CA  LEU A 215     4872   5375   5432    483     64   -412       C  
ATOM   1521  C   LEU A 215       8.711 -13.095  55.911  1.00 40.64           C  
ANISOU 1521  C   LEU A 215     4858   5179   5406    415     30   -467       C  
ATOM   1522  O   LEU A 215       8.753 -13.449  57.097  1.00 51.33           O  
ANISOU 1522  O   LEU A 215     6199   6538   6765    397     21   -467       O  
ATOM   1523  CB  LEU A 215      10.206 -11.377  54.852  1.00 41.16           C  
ANISOU 1523  CB  LEU A 215     4778   5413   5446    380     62   -391       C  
ATOM   1524  CG  LEU A 215      11.549 -10.987  54.226  1.00 55.05           C  
ANISOU 1524  CG  LEU A 215     6435   7325   7155    413     88   -304       C  
ATOM   1525  CD1 LEU A 215      11.578  -9.507  53.867  1.00 49.40           C  
ANISOU 1525  CD1 LEU A 215     5672   6630   6467    287     68   -287       C  
ATOM   1526  CD2 LEU A 215      12.698 -11.334  55.156  1.00 47.62           C  
ANISOU 1526  CD2 LEU A 215     5401   6518   6173    429     91   -228       C  
ATOM   1527  N   TYR A 216       7.558 -12.929  55.263  1.00 41.54           N  
ANISOU 1527  N   TYR A 216     5030   5197   5555    381     10   -499       N  
ATOM   1528  CA  TYR A 216       6.300 -13.109  55.969  1.00 39.90           C  
ANISOU 1528  CA  TYR A 216     4856   4910   5396    319    -19   -519       C  
ATOM   1529  C   TYR A 216       5.951 -14.571  56.218  1.00 45.72           C  
ANISOU 1529  C   TYR A 216     5682   5584   6105    359    -53   -520       C  
ATOM   1530  O   TYR A 216       5.210 -14.845  57.157  1.00 41.89           O  
ANISOU 1530  O   TYR A 216     5196   5069   5650    310    -72   -516       O  
ATOM   1531  CB  TYR A 216       5.166 -12.406  55.222  1.00 40.91           C  
ANISOU 1531  CB  TYR A 216     4993   4983   5567    265    -31   -523       C  
ATOM   1532  CG  TYR A 216       5.149 -10.914  55.479  1.00 51.85           C  
ANISOU 1532  CG  TYR A 216     6316   6397   6987    210     -2   -525       C  
ATOM   1533  CD1 TYR A 216       5.591 -10.396  56.695  1.00 51.25           C  
ANISOU 1533  CD1 TYR A 216     6208   6355   6908    178     14   -528       C  
ATOM   1534  CD2 TYR A 216       4.706 -10.024  54.512  1.00 46.00           C  
ANISOU 1534  CD2 TYR A 216     5572   5639   6268    188      3   -521       C  
ATOM   1535  CE1 TYR A 216       5.586  -9.036  56.938  1.00 48.98           C  
ANISOU 1535  CE1 TYR A 216     5914   6065   6630    126     30   -532       C  
ATOM   1536  CE2 TYR A 216       4.698  -8.660  54.747  1.00 43.77           C  
ANISOU 1536  CE2 TYR A 216     5266   5362   6003    144     26   -523       C  
ATOM   1537  CZ  TYR A 216       5.139  -8.172  55.959  1.00 47.85           C  
ANISOU 1537  CZ  TYR A 216     5779   5896   6507    113     37   -530       C  
ATOM   1538  OH  TYR A 216       5.136  -6.818  56.194  1.00 55.08           O  
ANISOU 1538  OH  TYR A 216     6720   6789   7420     66     50   -534       O  
ATOM   1539  N   THR A 217       6.501 -15.522  55.460  1.00 42.79           N  
ANISOU 1539  N   THR A 217     5400   5191   5666    452    -59   -519       N  
ATOM   1540  CA  THR A 217       6.304 -16.919  55.824  1.00 41.16           C  
ANISOU 1540  CA  THR A 217     5310   4910   5417    491    -97   -519       C  
ATOM   1541  C   THR A 217       7.030 -17.236  57.122  1.00 52.30           C  
ANISOU 1541  C   THR A 217     6663   6386   6822    521    -72   -506       C  
ATOM   1542  O   THR A 217       6.441 -17.798  58.055  1.00 49.34           O  
ANISOU 1542  O   THR A 217     6311   5969   6466    475   -104   -504       O  
ATOM   1543  CB  THR A 217       6.781 -17.840  54.700  1.00 43.23           C  
ANISOU 1543  CB  THR A 217     5727   5117   5584    610   -103   -524       C  
ATOM   1544  OG1 THR A 217       5.921 -17.694  53.563  1.00 50.59           O  
ANISOU 1544  OG1 THR A 217     6742   5966   6514    559   -148   -535       O  
ATOM   1545  CG2 THR A 217       6.761 -19.294  55.160  1.00 49.96           C  
ANISOU 1545  CG2 THR A 217     6731   5880   6373    665   -141   -523       C  
ATOM   1546  N   VAL A 218       8.300 -16.832  57.218  1.00 44.29           N  
ANISOU 1546  N   VAL A 218     5559   5488   5781    585    -19   -483       N  
ATOM   1547  CA  VAL A 218       9.049 -17.077  58.446  1.00 42.91           C  
ANISOU 1547  CA  VAL A 218     5316   5391   5596    602     -3   -457       C  
ATOM   1548  C   VAL A 218       8.377 -16.372  59.618  1.00 50.44           C  
ANISOU 1548  C   VAL A 218     6205   6343   6618    473    -20   -472       C  
ATOM   1549  O   VAL A 218       8.132 -16.976  60.672  1.00 48.40           O  
ANISOU 1549  O   VAL A 218     5962   6064   6363    458    -37   -471       O  
ATOM   1550  CB  VAL A 218      10.515 -16.638  58.279  1.00 47.52           C  
ANISOU 1550  CB  VAL A 218     5789   6129   6138    670     45   -398       C  
ATOM   1551  CG1 VAL A 218      11.246 -16.705  59.609  1.00 49.09           C  
ANISOU 1551  CG1 VAL A 218     5897   6423   6331    652     47   -357       C  
ATOM   1552  CG2 VAL A 218      11.214 -17.510  57.248  1.00 44.81           C  
ANISOU 1552  CG2 VAL A 218     5522   5798   5705    846     82   -368       C  
ATOM   1553  N   VAL A 219       7.997 -15.104  59.426  1.00 45.10           N  
ANISOU 1553  N   VAL A 219     5474   5676   5987    388    -14   -485       N  
ATOM   1554  CA  VAL A 219       7.426 -14.337  60.528  1.00 41.68           C  
ANISOU 1554  CA  VAL A 219     5005   5237   5593    296    -16   -498       C  
ATOM   1555  C   VAL A 219       6.055 -14.877  60.924  1.00 44.15           C  
ANISOU 1555  C   VAL A 219     5370   5466   5941    270    -36   -506       C  
ATOM   1556  O   VAL A 219       5.754 -15.015  62.116  1.00 47.16           O  
ANISOU 1556  O   VAL A 219     5742   5850   6328    243    -35   -502       O  
ATOM   1557  CB  VAL A 219       7.369 -12.842  60.164  1.00 46.67           C  
ANISOU 1557  CB  VAL A 219     5602   5882   6247    230     -3   -507       C  
ATOM   1558  CG1 VAL A 219       6.359 -12.115  61.038  1.00 39.71           C  
ANISOU 1558  CG1 VAL A 219     4740   4952   5396    171      5   -525       C  
ATOM   1559  CG2 VAL A 219       8.743 -12.216  60.321  1.00 45.68           C  
ANISOU 1559  CG2 VAL A 219     5411   5860   6085    206     -1   -474       C  
ATOM   1560  N   GLY A 220       5.206 -15.211  59.949  1.00 40.97           N  
ANISOU 1560  N   GLY A 220     5017   4997   5552    269    -60   -505       N  
ATOM   1561  CA  GLY A 220       3.869 -15.657  60.285  1.00 44.78           C  
ANISOU 1561  CA  GLY A 220     5523   5425   6065    221    -91   -480       C  
ATOM   1562  C   GLY A 220       3.864 -17.018  60.943  1.00 46.75           C  
ANISOU 1562  C   GLY A 220     5830   5644   6288    233   -128   -462       C  
ATOM   1563  O   GLY A 220       3.109 -17.252  61.894  1.00 47.08           O  
ANISOU 1563  O   GLY A 220     5851   5686   6350    190   -138   -431       O  
ATOM   1564  N   ILE A 221       4.748 -17.916  60.498  1.00 44.82           N  
ANISOU 1564  N   ILE A 221     5663   5378   5988    307   -143   -475       N  
ATOM   1565  CA  ILE A 221       4.861 -19.207  61.164  1.00 43.18           C  
ANISOU 1565  CA  ILE A 221     5532   5131   5743    332   -177   -460       C  
ATOM   1566  C   ILE A 221       5.375 -19.024  62.584  1.00 47.95           C  
ANISOU 1566  C   ILE A 221     6052   5812   6356    334   -142   -456       C  
ATOM   1567  O   ILE A 221       4.838 -19.610  63.533  1.00 52.40           O  
ANISOU 1567  O   ILE A 221     6626   6357   6927    297   -165   -432       O  
ATOM   1568  CB  ILE A 221       5.762 -20.157  60.357  1.00 41.72           C  
ANISOU 1568  CB  ILE A 221     5472   4903   5478    448   -185   -471       C  
ATOM   1569  CG1 ILE A 221       5.048 -20.612  59.083  1.00 42.11           C  
ANISOU 1569  CG1 ILE A 221     5663   4840   5498    429   -245   -474       C  
ATOM   1570  CG2 ILE A 221       6.170 -21.349  61.209  1.00 50.12           C  
ANISOU 1570  CG2 ILE A 221     6609   5941   6495    502   -201   -456       C  
ATOM   1571  CD1 ILE A 221       5.929 -21.387  58.137  1.00 47.04           C  
ANISOU 1571  CD1 ILE A 221     6441   5410   6021    570   -238   -490       C  
ATOM   1572  N   THR A 222       6.410 -18.193  62.760  1.00 42.71           N  
ANISOU 1572  N   THR A 222     5306   5238   5685    363    -94   -469       N  
ATOM   1573  CA  THR A 222       6.979 -18.028  64.094  1.00 52.69           C  
ANISOU 1573  CA  THR A 222     6507   6572   6942    351    -75   -460       C  
ATOM   1574  C   THR A 222       5.982 -17.388  65.052  1.00 45.45           C  
ANISOU 1574  C   THR A 222     5559   5647   6064    269    -68   -462       C  
ATOM   1575  O   THR A 222       5.953 -17.722  66.241  1.00 49.18           O  
ANISOU 1575  O   THR A 222     6023   6136   6526    256    -69   -449       O  
ATOM   1576  CB  THR A 222       8.261 -17.203  64.028  1.00 59.01           C  
ANISOU 1576  CB  THR A 222     7226   7477   7719    366    -47   -451       C  
ATOM   1577  OG1 THR A 222       8.015 -15.991  63.309  1.00 93.68           O  
ANISOU 1577  OG1 THR A 222    11589  11868  12137    317    -34   -470       O  
ATOM   1578  CG2 THR A 222       9.355 -17.985  63.333  1.00 45.70           C  
ANISOU 1578  CG2 THR A 222     5551   5834   5977    483    -36   -420       C  
ATOM   1579  N   LEU A 223       5.139 -16.483  64.553  1.00 40.57           N  
ANISOU 1579  N   LEU A 223     4927   5006   5482    228    -55   -470       N  
ATOM   1580  CA  LEU A 223       4.154 -15.858  65.428  1.00 40.08           C  
ANISOU 1580  CA  LEU A 223     4844   4944   5442    188    -29   -458       C  
ATOM   1581  C   LEU A 223       3.014 -16.815  65.757  1.00 47.56           C  
ANISOU 1581  C   LEU A 223     5802   5862   6407    170    -56   -406       C  
ATOM   1582  O   LEU A 223       2.568 -16.881  66.909  1.00 47.16           O  
ANISOU 1582  O   LEU A 223     5733   5835   6351    160    -37   -380       O  
ATOM   1583  CB  LEU A 223       3.620 -14.577  64.788  1.00 39.92           C  
ANISOU 1583  CB  LEU A 223     4809   4914   5444    173      2   -468       C  
ATOM   1584  CG  LEU A 223       4.594 -13.398  64.684  1.00 39.88           C  
ANISOU 1584  CG  LEU A 223     4803   4934   5416    161     21   -505       C  
ATOM   1585  CD1 LEU A 223       3.933 -12.231  63.968  1.00 40.93           C  
ANISOU 1585  CD1 LEU A 223     4944   5038   5571    153     48   -511       C  
ATOM   1586  CD2 LEU A 223       5.095 -12.968  66.059  1.00 40.16           C  
ANISOU 1586  CD2 LEU A 223     4857   4994   5407    138     32   -516       C  
ATOM   1587  N   ARG A 224       2.523 -17.568  64.767  1.00 44.76           N  
ANISOU 1587  N   ARG A 224     5485   5457   6064    155   -106   -382       N  
ATOM   1588  CA  ARG A 224       1.442 -18.505  65.051  1.00 48.00           C  
ANISOU 1588  CA  ARG A 224     5910   5843   6485    104   -155   -311       C  
ATOM   1589  C   ARG A 224       1.903 -19.607  65.999  1.00 45.31           C  
ANISOU 1589  C   ARG A 224     5611   5493   6113    114   -181   -304       C  
ATOM   1590  O   ARG A 224       1.147 -20.041  66.876  1.00 41.46           O  
ANISOU 1590  O   ARG A 224     5099   5022   5630     73   -194   -243       O  
ATOM   1591  CB  ARG A 224       0.911 -19.102  63.749  1.00 41.16           C  
ANISOU 1591  CB  ARG A 224     5111   4909   5621     61   -229   -284       C  
ATOM   1592  CG  ARG A 224      -0.305 -19.990  63.933  1.00 43.67           C  
ANISOU 1592  CG  ARG A 224     5441   5206   5945    -32   -304   -184       C  
ATOM   1593  CD  ARG A 224      -1.029 -20.235  62.614  1.00 53.09           C  
ANISOU 1593  CD  ARG A 224     6689   6343   7138   -105   -385   -141       C  
ATOM   1594  NE  ARG A 224      -0.103 -20.452  61.510  1.00 65.09           N  
ANISOU 1594  NE  ARG A 224     8333   7783   8617    -50   -404   -223       N  
ATOM   1595  CZ  ARG A 224      -0.014 -19.664  60.445  1.00 46.06           C  
ANISOU 1595  CZ  ARG A 224     5911   5373   6217    -31   -383   -255       C  
ATOM   1596  NH1 ARG A 224      -0.808 -18.610  60.324  1.00 65.96           N  
ANISOU 1596  NH1 ARG A 224     8311   7961   8791    -63   -347   -214       N  
ATOM   1597  NH2 ARG A 224       0.864 -19.937  59.493  1.00 59.42           N  
ANISOU 1597  NH2 ARG A 224     7717   7001   7858     35   -392   -319       N  
ATOM   1598  N   ALA A 225       3.155 -20.044  65.863  1.00 41.11           N  
ANISOU 1598  N   ALA A 225     5132   4946   5541    177   -184   -353       N  
ATOM   1599  CA  ALA A 225       3.680 -21.090  66.731  1.00 42.55           C  
ANISOU 1599  CA  ALA A 225     5359   5121   5688    204   -204   -343       C  
ATOM   1600  C   ALA A 225       3.902 -20.598  68.154  1.00 47.02           C  
ANISOU 1600  C   ALA A 225     5845   5764   6255    201   -157   -342       C  
ATOM   1601  O   ALA A 225       3.995 -21.417  69.074  1.00 56.79           O  
ANISOU 1601  O   ALA A 225     7102   7002   7472    202   -175   -317       O  
ATOM   1602  CB  ALA A 225       4.984 -21.639  66.152  1.00 41.67           C  
ANISOU 1602  CB  ALA A 225     5315   4992   5525    302   -205   -377       C  
ATOM   1603  N   SER A 226       3.993 -19.289  68.352  1.00 52.96           N  
ANISOU 1603  N   SER A 226     6532   6570   7021    195   -103   -369       N  
ATOM   1604  CA  SER A 226       4.147 -18.721  69.683  1.00 45.61           C  
ANISOU 1604  CA  SER A 226     5565   5693   6071    187    -64   -373       C  
ATOM   1605  C   SER A 226       2.790 -18.296  70.231  1.00 51.77           C  
ANISOU 1605  C   SER A 226     6318   6482   6869    162    -31   -330       C  
ATOM   1606  O   SER A 226       2.690 -17.796  71.350  1.00 54.83           O  
ANISOU 1606  O   SER A 226     6701   6905   7229    170     10   -329       O  
ATOM   1607  CB  SER A 226       5.102 -17.528  69.652  1.00 41.24           C  
ANISOU 1607  CB  SER A 226     4994   5179   5496    189    -35   -420       C  
ATOM   1608  OG  SER A 226       6.354 -17.895  69.099  1.00 50.33           O  
ANISOU 1608  OG  SER A 226     6139   6357   6628    221    -58   -429       O  
ATOM   1609  N   GLY A1218       1.689 -18.455  69.497  1.00 51.32           N  
ANISOU 1609  N   GLY A1218     6245   6404   6849    138    -47   -281       N  
ATOM   1610  CA  GLY A1218       0.465 -18.035  70.152  1.00 41.58           C  
ANISOU 1610  CA  GLY A1218     4960   5215   5622    136     -1   -211       C  
ATOM   1611  C   GLY A1218      -0.100 -19.085  71.087  1.00 56.42           C  
ANISOU 1611  C   GLY A1218     6822   7121   7494    108    -26   -132       C  
ATOM   1612  O   GLY A1218       0.286 -20.252  71.036  1.00 65.32           O  
ANISOU 1612  O   GLY A1218     7993   8208   8617     75    -95   -127       O  
ATOM   1613  N   ILE A1219      -1.023 -18.661  71.946  1.00 54.40           N  
ANISOU 1613  N   ILE A1219     6511   6933   7226    132     36    -62       N  
ATOM   1614  CA  ILE A1219      -1.687 -19.546  72.893  1.00 48.26           C  
ANISOU 1614  CA  ILE A1219     5695   6203   6437    104     22     37       C  
ATOM   1615  C   ILE A1219      -3.115 -19.051  73.069  1.00 45.26           C  
ANISOU 1615  C   ILE A1219     5216   5917   6062    127     82    166       C  
ATOM   1616  O   ILE A1219      -3.398 -17.856  72.943  1.00 45.51           O  
ANISOU 1616  O   ILE A1219     5236   5974   6083    205    167    152       O  
ATOM   1617  CB  ILE A1219      -0.941 -19.603  74.251  1.00 58.75           C  
ANISOU 1617  CB  ILE A1219     7063   7547   7714    144     56     -9       C  
ATOM   1618  CG1 ILE A1219      -1.541 -20.677  75.161  1.00 55.97           C  
ANISOU 1618  CG1 ILE A1219     6675   7239   7351    106     30     95       C  
ATOM   1619  CG2 ILE A1219      -0.961 -18.247  74.944  1.00 43.36           C  
ANISOU 1619  CG2 ILE A1219     5133   5628   5714    229    160    -47       C  
ATOM   1620  CD1 ILE A1219      -0.929 -20.722  76.546  1.00 59.65           C  
ANISOU 1620  CD1 ILE A1219     7176   7727   7760    146     66     61       C  
ATOM   1621  N   ASP A1220      -4.022 -19.983  73.340  1.00 49.32           N  
ANISOU 1621  N   ASP A1220     5662   6489   6589     60     37    305       N  
ATOM   1622  CA  ASP A1220      -5.411 -19.635  73.618  1.00 56.89           C  
ANISOU 1622  CA  ASP A1220     6493   7577   7546     85     96    471       C  
ATOM   1623  C   ASP A1220      -5.583 -19.285  75.097  1.00 55.23           C  
ANISOU 1623  C   ASP A1220     6265   7448   7274    190    205    502       C  
ATOM   1624  O   ASP A1220      -5.737 -20.170  75.938  1.00 46.72           O  
ANISOU 1624  O   ASP A1220     5162   6410   6179    148    177    573       O  
ATOM   1625  CB  ASP A1220      -6.340 -20.786  73.228  1.00 46.52           C  
ANISOU 1625  CB  ASP A1220     5104   6307   6265    -60    -17    638       C  
ATOM   1626  CG  ASP A1220      -7.806 -20.420  73.345  1.00 57.35           C  
ANISOU 1626  CG  ASP A1220     6305   7846   7638    -44     37    847       C  
ATOM   1627  OD1 ASP A1220      -8.110 -19.224  73.539  1.00 59.66           O  
ANISOU 1627  OD1 ASP A1220     6554   8206   7908    104    171    849       O  
ATOM   1628  OD2 ASP A1220      -8.655 -21.330  73.244  1.00 62.28           O  
ANISOU 1628  OD2 ASP A1220     6846   8539   8278   -178    -58   1022       O  
HETATM 1629  N   YCM A1221      -5.560 -17.992  75.406  1.00 51.91           N  
ANISOU 1629  N   YCM A1221     5876   7041   6807    329    327    450       N  
HETATM 1630  CA  YCM A1221      -5.677 -17.520  76.821  1.00 49.09           C  
ANISOU 1630  CA  YCM A1221     5549   6741   6363    454    442    463       C  
HETATM 1631  CB  YCM A1221      -5.294 -16.050  76.941  1.00 57.34           C  
ANISOU 1631  CB  YCM A1221     6716   7728   7342    588    544    350       C  
HETATM 1632  SG  YCM A1221      -3.591 -15.833  76.551  1.00 68.27           S  
ANISOU 1632  SG  YCM A1221     8251   8955   8734    513    463    134       S  
HETATM 1633  CD  YCM A1221      -2.970 -16.712  77.944  1.00 78.70           C  
ANISOU 1633  CD  YCM A1221     9612  10284  10007    482    436    116       C  
HETATM 1634  CE  YCM A1221      -3.150 -15.877  79.189  1.00 84.68           C  
ANISOU 1634  CE  YCM A1221    10465  11060  10648    609    547    111       C  
HETATM 1635  OZ1 YCM A1221      -2.777 -14.717  79.210  1.00 87.99           O  
ANISOU 1635  OZ1 YCM A1221    11017  11410  11004    673    594     22       O  
HETATM 1636  NZ2 YCM A1221      -3.741 -16.477  80.224  1.00 74.53           N  
ANISOU 1636  NZ2 YCM A1221     9130   9864   9325    645    586    214       N  
HETATM 1637  C   YCM A1221      -7.067 -17.709  77.349  1.00 53.31           C  
ANISOU 1637  C   YCM A1221     5938   7439   6877    505    508    676       C  
HETATM 1638  O   YCM A1221      -7.289 -17.634  78.556  1.00 59.68           O  
ANISOU 1638  O   YCM A1221     6753   8313   7610    599    593    723       O  
ATOM   1639  N   SER A1222      -8.018 -17.948  76.454  1.00 59.03           N  
ANISOU 1639  N   SER A1222     6524   8243   7660    444    469    822       N  
ATOM   1640  CA  SER A1222      -9.392 -18.189  76.867  1.00 59.21           C  
ANISOU 1640  CA  SER A1222     6369   8459   7669    473    519   1070       C  
ATOM   1641  C   SER A1222      -9.527 -19.580  77.475  1.00 52.14           C  
ANISOU 1641  C   SER A1222     5416   7609   6787    331    421   1171       C  
ATOM   1642  O   SER A1222     -10.476 -19.851  78.206  1.00 70.08           O  
ANISOU 1642  O   SER A1222     7551  10049   9026    361    472   1372       O  
ATOM   1643  CB  SER A1222     -10.351 -18.031  75.687  1.00 62.50           C  
ANISOU 1643  CB  SER A1222     6646   8959   8142    423    486   1216       C  
ATOM   1644  OG  SER A1222     -10.313 -19.166  74.840  1.00 64.61           O  
ANISOU 1644  OG  SER A1222     6889   9177   8483    197    304   1249       O  
ATOM   1645  N   PHE A1223      -8.581 -20.468  77.163  1.00 50.50           N  
ANISOU 1645  N   PHE A1223     5313   7256   6619    186    284   1044       N  
ATOM   1646  CA  PHE A1223      -8.558 -21.796  77.766  1.00 52.34           C  
ANISOU 1646  CA  PHE A1223     5535   7496   6854     58    185   1116       C  
ATOM   1647  C   PHE A1223      -7.485 -21.941  78.838  1.00 49.45           C  
ANISOU 1647  C   PHE A1223     5297   7052   6441    115    216    966       C  
ATOM   1648  O   PHE A1223      -7.790 -22.340  79.965  1.00 50.23           O  
ANISOU 1648  O   PHE A1223     5353   7237   6494    137    252   1058       O  
ATOM   1649  CB  PHE A1223      -8.356 -22.882  76.702  1.00 49.76           C  
ANISOU 1649  CB  PHE A1223     5257   7059   6589   -144     -1   1111       C  
ATOM   1650  CG  PHE A1223      -8.293 -24.269  77.276  1.00 50.23           C  
ANISOU 1650  CG  PHE A1223     5347   7097   6642   -279   -114   1178       C  
ATOM   1651  CD1 PHE A1223      -9.455 -24.966  77.563  1.00 51.75           C  
ANISOU 1651  CD1 PHE A1223     5401   7428   6833   -395   -170   1425       C  
ATOM   1652  CD2 PHE A1223      -7.073 -24.867  77.556  1.00 53.45           C  
ANISOU 1652  CD2 PHE A1223     5915   7356   7038   -288   -164   1012       C  
ATOM   1653  CE1 PHE A1223      -9.403 -26.237  78.109  1.00 55.48           C  
ANISOU 1653  CE1 PHE A1223     5917   7870   7293   -529   -282   1493       C  
ATOM   1654  CE2 PHE A1223      -7.015 -26.136  78.104  1.00 63.25           C  
ANISOU 1654  CE2 PHE A1223     7199   8567   8265   -399   -264   1075       C  
ATOM   1655  CZ  PHE A1223      -8.182 -26.821  78.383  1.00 57.97           C  
ANISOU 1655  CZ  PHE A1223     6413   8017   7595   -524   -327   1310       C  
ATOM   1656  N   TRP A1224      -6.228 -21.642  78.507  1.00 48.17           N  
ANISOU 1656  N   TRP A1224     5280   6739   6283    134    197    753       N  
ATOM   1657  CA  TRP A1224      -5.127 -21.804  79.456  1.00 56.42           C  
ANISOU 1657  CA  TRP A1224     6438   7717   7283    168    207    623       C  
ATOM   1658  C   TRP A1224      -5.148 -20.607  80.402  1.00 63.35           C  
ANISOU 1658  C   TRP A1224     7350   8644   8077    333    356    585       C  
ATOM   1659  O   TRP A1224      -4.394 -19.640  80.269  1.00 49.82           O  
ANISOU 1659  O   TRP A1224     5744   6852   6334    400    397    439       O  
ATOM   1660  CB  TRP A1224      -3.794 -21.942  78.731  1.00 48.70           C  
ANISOU 1660  CB  TRP A1224     5580   6590   6333    126    128    445       C  
ATOM   1661  CG  TRP A1224      -3.742 -23.105  77.788  1.00 54.55           C  
ANISOU 1661  CG  TRP A1224     6337   7259   7130     -6    -10    472       C  
ATOM   1662  CD1 TRP A1224      -3.893 -23.065  76.435  1.00 52.98           C  
ANISOU 1662  CD1 TRP A1224     6145   7006   6979    -60    -69    463       C  
ATOM   1663  CD2 TRP A1224      -3.529 -24.481  78.128  1.00 50.95           C  
ANISOU 1663  CD2 TRP A1224     5924   6762   6674    -97   -111    512       C  
ATOM   1664  NE1 TRP A1224      -3.785 -24.330  75.909  1.00 46.19           N  
ANISOU 1664  NE1 TRP A1224     5349   6064   6137   -176   -202    490       N  
ATOM   1665  CE2 TRP A1224      -3.562 -25.218  76.927  1.00 49.06           C  
ANISOU 1665  CE2 TRP A1224     5741   6429   6471   -199   -230    521       C  
ATOM   1666  CE3 TRP A1224      -3.313 -25.161  79.329  1.00 46.95           C  
ANISOU 1666  CE3 TRP A1224     5430   6278   6128   -100   -113    541       C  
ATOM   1667  CZ2 TRP A1224      -3.386 -26.602  76.893  1.00 52.61           C  
ANISOU 1667  CZ2 TRP A1224     6282   6793   6913   -297   -352    556       C  
ATOM   1668  CZ3 TRP A1224      -3.138 -26.535  79.295  1.00 49.41           C  
ANISOU 1668  CZ3 TRP A1224     5809   6518   6445   -200   -233    580       C  
ATOM   1669  CH2 TRP A1224      -3.175 -27.240  78.086  1.00 49.47           C  
ANISOU 1669  CH2 TRP A1224     5894   6419   6482   -295   -351    586       C  
ATOM   1670  N   ASN A1225      -6.045 -20.685  81.381  1.00 49.17           N  
ANISOU 1670  N   ASN A1225     5475   6979   6229    396    434    731       N  
ATOM   1671  CA  ASN A1225      -6.305 -19.581  82.291  1.00 49.93           C  
ANISOU 1671  CA  ASN A1225     5620   7129   6221    579    590    727       C  
ATOM   1672  C   ASN A1225      -6.619 -20.165  83.660  1.00 52.05           C  
ANISOU 1672  C   ASN A1225     5859   7494   6423    611    632    827       C  
ATOM   1673  O   ASN A1225      -7.431 -21.088  83.771  1.00 51.62           O  
ANISOU 1673  O   ASN A1225     5657   7552   6402    536    594   1007       O  
ATOM   1674  CB  ASN A1225      -7.469 -18.724  81.772  1.00 50.82           C  
ANISOU 1674  CB  ASN A1225     5637   7345   6328    692    693    852       C  
ATOM   1675  CG  ASN A1225      -7.612 -17.407  82.512  1.00 57.74           C  
ANISOU 1675  CG  ASN A1225     6627   8231   7079    912    860    814       C  
ATOM   1676  OD1 ASN A1225      -7.573 -17.359  83.740  1.00 66.15           O  
ANISOU 1676  OD1 ASN A1225     7761   9328   8046   1004    934    822       O  
ATOM   1677  ND2 ASN A1225      -7.781 -16.326  81.759  1.00 71.86           N  
ANISOU 1677  ND2 ASN A1225     8459   9982   8861   1003    919    774       N  
ATOM   1678  N   GLU A1226      -5.980 -19.621  84.699  1.00 58.48           N  
ANISOU 1678  N   GLU A1226     6820   8263   7136    710    701    720       N  
ATOM   1679  CA  GLU A1226      -6.175 -20.149  86.044  1.00 58.55           C  
ANISOU 1679  CA  GLU A1226     6821   8354   7071    746    741    799       C  
ATOM   1680  C   GLU A1226      -7.595 -19.927  86.548  1.00 53.57           C  
ANISOU 1680  C   GLU A1226     6062   7913   6381    884    877   1015       C  
ATOM   1681  O   GLU A1226      -8.034 -20.637  87.459  1.00 54.47           O  
ANISOU 1681  O   GLU A1226     6098   8138   6460    883    895   1147       O  
ATOM   1682  CB  GLU A1226      -5.167 -19.522  87.008  1.00 69.91           C  
ANISOU 1682  CB  GLU A1226     8468   9696   8398    817    778    635       C  
ATOM   1683  CG  GLU A1226      -4.940 -20.335  88.274  1.00 82.22           C  
ANISOU 1683  CG  GLU A1226    10040  11297   9902    794    764    671       C  
ATOM   1684  CD  GLU A1226      -3.842 -19.764  89.148  1.00 95.71           C  
ANISOU 1684  CD  GLU A1226    11961  12902  11502    828    770    508       C  
ATOM   1685  OE1 GLU A1226      -3.056 -18.935  88.645  1.00101.31           O  
ANISOU 1685  OE1 GLU A1226    12800  13492  12201    817    743    359       O  
ATOM   1686  OE2 GLU A1226      -3.767 -20.139  90.338  1.00105.71           O  
ANISOU 1686  OE2 GLU A1226    13267  14210  12688    852    792    538       O  
ATOM   1687  N   SER A1227      -8.329 -18.983  85.954  1.00 54.15           N  
ANISOU 1687  N   SER A1227     6098   8035   6440   1008    974   1071       N  
ATOM   1688  CA  SER A1227      -9.652 -18.624  86.447  1.00 57.84           C  
ANISOU 1688  CA  SER A1227     6444   8702   6833   1186   1130   1291       C  
ATOM   1689  C   SER A1227     -10.631 -19.789  86.410  1.00 56.86           C  
ANISOU 1689  C   SER A1227     6060   8766   6777   1066   1073   1548       C  
ATOM   1690  O   SER A1227     -11.612 -19.780  87.161  1.00 58.59           O  
ANISOU 1690  O   SER A1227     6158   9182   6922   1194   1193   1758       O  
ATOM   1691  CB  SER A1227     -10.211 -17.458  85.631  1.00 56.44           C  
ANISOU 1691  CB  SER A1227     6264   8538   6641   1331   1229   1310       C  
ATOM   1692  OG  SER A1227      -9.264 -16.412  85.505  1.00 78.50           O  
ANISOU 1692  OG  SER A1227     9309  11138   9381   1399   1248   1073       O  
ATOM   1693  N   TYR A1228     -10.415 -20.768  85.534  1.00 57.19           N  
ANISOU 1693  N   TYR A1228     6025   8756   6949    825    893   1550       N  
ATOM   1694  CA  TYR A1228     -11.311 -21.911  85.434  1.00 62.64           C  
ANISOU 1694  CA  TYR A1228     6501   9599   7699    668    804   1797       C  
ATOM   1695  C   TYR A1228     -10.988 -23.024  86.423  1.00 56.95           C  
ANISOU 1695  C   TYR A1228     5793   8882   6962    565    734   1823       C  
ATOM   1696  O   TYR A1228     -11.766 -23.977  86.528  1.00 76.87           O  
ANISOU 1696  O   TYR A1228     8151  11541   9516    433    663   2048       O  
ATOM   1697  CB  TYR A1228     -11.308 -22.442  83.997  1.00 56.01           C  
ANISOU 1697  CB  TYR A1228     5610   8685   6984    455    633   1798       C  
ATOM   1698  CG  TYR A1228     -11.821 -21.400  83.032  1.00 56.14           C  
ANISOU 1698  CG  TYR A1228     5576   8737   7018    552    703   1820       C  
ATOM   1699  CD1 TYR A1228     -13.168 -21.062  83.006  1.00 58.94           C  
ANISOU 1699  CD1 TYR A1228     5720   9326   7348    641    799   2088       C  
ATOM   1700  CD2 TYR A1228     -10.960 -20.722  82.181  1.00 54.63           C  
ANISOU 1700  CD2 TYR A1228     5538   8360   6860    565    681   1589       C  
ATOM   1701  CE1 TYR A1228     -13.648 -20.097  82.142  1.00 58.15           C  
ANISOU 1701  CE1 TYR A1228     5570   9265   7259    744    869   2119       C  
ATOM   1702  CE2 TYR A1228     -11.432 -19.753  81.311  1.00 54.80           C  
ANISOU 1702  CE2 TYR A1228     5518   8409   6893    656    745   1610       C  
ATOM   1703  CZ  TYR A1228     -12.776 -19.446  81.299  1.00 56.54           C  
ANISOU 1703  CZ  TYR A1228     5537   8855   7090    749    840   1872       C  
ATOM   1704  OH  TYR A1228     -13.255 -18.485  80.442  1.00 64.09           O  
ANISOU 1704  OH  TYR A1228     6450   9846   8056    851    908   1904       O  
ATOM   1705  N   LEU A1229      -9.869 -22.936  87.135  1.00 56.49           N  
ANISOU 1705  N   LEU A1229     5926   8682   6856    607    742   1614       N  
ATOM   1706  CA  LEU A1229      -9.610 -23.828  88.256  1.00 56.64           C  
ANISOU 1706  CA  LEU A1229     5962   8723   6836    556    711   1646       C  
ATOM   1707  C   LEU A1229     -10.415 -23.391  89.476  1.00 64.78           C  
ANISOU 1707  C   LEU A1229     6929   9943   7742    752    889   1802       C  
ATOM   1708  O   LEU A1229     -10.774 -22.219  89.619  1.00 71.15           O  
ANISOU 1708  O   LEU A1229     7771  10799   8463    969   1052   1799       O  
ATOM   1709  CB  LEU A1229      -8.120 -23.846  88.589  1.00 59.63           C  
ANISOU 1709  CB  LEU A1229     6555   8900   7199    536    657   1384       C  
ATOM   1710  CG  LEU A1229      -7.202 -24.158  87.406  1.00 61.38           C  
ANISOU 1710  CG  LEU A1229     6855   8940   7525    391    509   1221       C  
ATOM   1711  CD1 LEU A1229      -5.756 -23.961  87.800  1.00 63.91           C  
ANISOU 1711  CD1 LEU A1229     7363   9107   7812    407    485    991       C  
ATOM   1712  CD2 LEU A1229      -7.435 -25.573  86.898  1.00 54.41           C  
ANISOU 1712  CD2 LEU A1229     5893   8049   6731    181    345   1333       C  
ATOM   1713  N   THR A1230     -10.713 -24.347  90.352  1.00 63.18           N  
ANISOU 1713  N   THR A1230     6644   9845   7518    684    861   1948       N  
ATOM   1714  CA  THR A1230     -11.437 -24.066  91.585  1.00 73.51           C  
ANISOU 1714  CA  THR A1230     7890  11343   8697    871   1029   2109       C  
ATOM   1715  C   THR A1230     -10.578 -24.405  92.796  1.00 72.84           C  
ANISOU 1715  C   THR A1230     7963  11178   8535    886   1028   1985       C  
ATOM   1716  O   THR A1230      -9.765 -25.333  92.764  1.00 67.71           O  
ANISOU 1716  O   THR A1230     7371  10401   7953    699    871   1888       O  
ATOM   1717  CB  THR A1230     -12.758 -24.848  91.661  1.00 77.17           C  
ANISOU 1717  CB  THR A1230     8074  12063   9185    790   1017   2456       C  
ATOM   1718  OG1 THR A1230     -12.490 -26.255  91.627  1.00 76.23           O  
ANISOU 1718  OG1 THR A1230     7922  11892   9150    521    820   2497       O  
ATOM   1719  CG2 THR A1230     -13.665 -24.474  90.498  1.00 87.94           C  
ANISOU 1719  CG2 THR A1230     9267  13532  10614    774   1017   2608       C  
ATOM   1720  N   GLY A1231     -10.761 -23.630  93.864  1.00 78.90           N  
ANISOU 1720  N   GLY A1231     8812  12017   9148   1122   1207   1991       N  
ATOM   1721  CA  GLY A1231     -10.062 -23.874  95.108  1.00 61.63           C  
ANISOU 1721  CA  GLY A1231     6774   9778   6866   1152   1220   1898       C  
ATOM   1722  C   GLY A1231      -8.661 -23.294  95.111  1.00 70.99           C  
ANISOU 1722  C   GLY A1231     8230  10719   8025   1149   1172   1588       C  
ATOM   1723  O   GLY A1231      -8.166 -22.748  94.124  1.00 68.78           O  
ANISOU 1723  O   GLY A1231     8022  10304   7808   1115   1123   1439       O  
ATOM   1724  N   SER A1232      -8.011 -23.422  96.264  1.00 60.28           N  
ANISOU 1724  N   SER A1232     7018   9318   6568   1178   1182   1506       N  
ATOM   1725  CA  SER A1232      -6.635 -22.978  96.415  1.00 61.25           C  
ANISOU 1725  CA  SER A1232     7384   9234   6654   1146   1117   1244       C  
ATOM   1726  C   SER A1232      -5.680 -23.952  95.730  1.00 62.56           C  
ANISOU 1726  C   SER A1232     7516   9281   6972    905    916   1149       C  
ATOM   1727  O   SER A1232      -5.979 -25.137  95.554  1.00 57.28           O  
ANISOU 1727  O   SER A1232     6691   8671   6401    766    825   1275       O  
ATOM   1728  CB  SER A1232      -6.267 -22.838  97.892  1.00 60.04           C  
ANISOU 1728  CB  SER A1232     7397   9080   6334   1242   1181   1205       C  
ATOM   1729  OG  SER A1232      -5.898 -24.088  98.447  1.00 64.55           O  
ANISOU 1729  OG  SER A1232     7896   9677   6954   1091   1073   1251       O  
ATOM   1730  N   ARG A1233      -4.511 -23.432  95.343  1.00 58.79           N  
ANISOU 1730  N   ARG A1233     7201   8633   6504    861    847    935       N  
ATOM   1731  CA  ARG A1233      -3.521 -24.277  94.685  1.00 57.85           C  
ANISOU 1731  CA  ARG A1233     7063   8408   6511    673    676    846       C  
ATOM   1732  C   ARG A1233      -3.055 -25.410  95.592  1.00 54.80           C  
ANISOU 1732  C   ARG A1233     6667   8037   6116    585    600    881       C  
ATOM   1733  O   ARG A1233      -2.768 -26.513  95.109  1.00 54.71           O  
ANISOU 1733  O   ARG A1233     6580   7993   6214    446    476    907       O  
ATOM   1734  CB  ARG A1233      -2.324 -23.438  94.234  1.00 53.68           C  
ANISOU 1734  CB  ARG A1233     6698   7727   5972    655    629    636       C  
ATOM   1735  CG  ARG A1233      -1.398 -24.178  93.282  1.00 52.28           C  
ANISOU 1735  CG  ARG A1233     6479   7457   5926    499    477    562       C  
ATOM   1736  CD  ARG A1233      -0.218 -23.330  92.831  1.00 51.47           C  
ANISOU 1736  CD  ARG A1233     6509   7237   5811    478    431    386       C  
ATOM   1737  NE  ARG A1233       0.477 -23.959  91.711  1.00 51.37           N  
ANISOU 1737  NE  ARG A1233     6434   7159   5925    368    315    341       N  
ATOM   1738  CZ  ARG A1233       0.228 -23.686  90.433  1.00 53.09           C  
ANISOU 1738  CZ  ARG A1233     6601   7341   6228    355    305    324       C  
ATOM   1739  NH1 ARG A1233      -0.691 -22.785  90.114  1.00 50.05           N  
ANISOU 1739  NH1 ARG A1233     6209   6985   5824    441    402    351       N  
ATOM   1740  NH2 ARG A1233       0.900 -24.309  89.475  1.00 48.76           N  
ANISOU 1740  NH2 ARG A1233     6020   6732   5776    272    205    285       N  
ATOM   1741  N   ASP A1234      -2.992 -25.170  96.905  1.00 55.76           N  
ANISOU 1741  N   ASP A1234     6884   8202   6100    673    673    885       N  
ATOM   1742  CA  ASP A1234      -2.541 -26.218  97.817  1.00 64.04           C  
ANISOU 1742  CA  ASP A1234     7927   9270   7135    594    603    922       C  
ATOM   1743  C   ASP A1234      -3.552 -27.355  97.904  1.00 61.36           C  
ANISOU 1743  C   ASP A1234     7402   9056   6858    538    591   1133       C  
ATOM   1744  O   ASP A1234      -3.170 -28.533  97.913  1.00 58.72           O  
ANISOU 1744  O   ASP A1234     7025   8693   6595    405    471   1165       O  
ATOM   1745  CB  ASP A1234      -2.266 -25.629  99.199  1.00 71.01           C  
ANISOU 1745  CB  ASP A1234     8971  10168   7840    701    683    878       C  
ATOM   1746  CG  ASP A1234      -1.010 -24.782  99.229  1.00 94.75           C  
ANISOU 1746  CG  ASP A1234    12179  13037  10785    684    633    679       C  
ATOM   1747  OD1 ASP A1234      -0.503 -24.429  98.143  1.00113.71           O  
ANISOU 1747  OD1 ASP A1234    14584  15349  13273    626    571    581       O  
ATOM   1748  OD2 ASP A1234      -0.524 -24.477 100.337  1.00108.10           O  
ANISOU 1748  OD2 ASP A1234    14024  14713  12335    717    647    629       O  
ATOM   1749  N   GLU A1235      -4.846 -27.029  97.947  1.00 62.52           N  
ANISOU 1749  N   GLU A1235     7439   9345   6973    636    709   1294       N  
ATOM   1750  CA  GLU A1235      -5.858 -28.080  97.955  1.00 68.01           C  
ANISOU 1750  CA  GLU A1235     7937  10177   7727    553    682   1527       C  
ATOM   1751  C   GLU A1235      -5.837 -28.869  96.653  1.00 61.12           C  
ANISOU 1751  C   GLU A1235     6979   9229   7014    371    530   1544       C  
ATOM   1752  O   GLU A1235      -6.000 -30.097  96.658  1.00 63.25           O  
ANISOU 1752  O   GLU A1235     7177   9509   7344    221    417   1659       O  
ATOM   1753  CB  GLU A1235      -7.244 -27.475  98.190  1.00 67.52           C  
ANISOU 1753  CB  GLU A1235     7751  10311   7594    706    847   1720       C  
ATOM   1754  CG  GLU A1235      -7.416 -26.809  99.544  1.00 79.99           C  
ANISOU 1754  CG  GLU A1235     9426  11976   8989    911   1011   1736       C  
ATOM   1755  CD  GLU A1235      -8.794 -26.198  99.724  1.00101.66           C  
ANISOU 1755  CD  GLU A1235    12044  14930  11652   1102   1195   1945       C  
ATOM   1756  OE1 GLU A1235      -9.305 -25.581  98.763  1.00 87.71           O  
ANISOU 1756  OE1 GLU A1235    10212  13181   9932   1151   1235   1969       O  
ATOM   1757  OE2 GLU A1235      -9.369 -26.342 100.827  1.00118.42           O  
ANISOU 1757  OE2 GLU A1235    14127  17210  13658   1214   1303   2097       O  
ATOM   1758  N   ARG A1236      -5.592 -28.185  95.530  1.00 56.68           N  
ANISOU 1758  N   ARG A1236     6452   8574   6511    379    518   1426       N  
ATOM   1759  CA  ARG A1236      -5.535 -28.881  94.250  1.00 55.87           C  
ANISOU 1759  CA  ARG A1236     6300   8385   6543    218    376   1430       C  
ATOM   1760  C   ARG A1236      -4.335 -29.816  94.185  1.00 56.54           C  
ANISOU 1760  C   ARG A1236     6493   8315   6673    103    232   1310       C  
ATOM   1761  O   ARG A1236      -4.457 -30.958  93.724  1.00 67.67           O  
ANISOU 1761  O   ARG A1236     7875   9682   8156    -42    103   1390       O  
ATOM   1762  CB  ARG A1236      -5.498 -27.873  93.099  1.00 55.12           C  
ANISOU 1762  CB  ARG A1236     6225   8228   6490    268    406   1325       C  
ATOM   1763  CG  ARG A1236      -6.716 -26.961  93.028  1.00 56.14           C  
ANISOU 1763  CG  ARG A1236     6245   8510   6577    397    550   1456       C  
ATOM   1764  CD  ARG A1236      -6.851 -26.305  91.667  1.00 55.43           C  
ANISOU 1764  CD  ARG A1236     6138   8363   6560    394    539   1400       C  
ATOM   1765  NE  ARG A1236      -5.697 -25.481  91.324  1.00 54.13           N  
ANISOU 1765  NE  ARG A1236     6144   8038   6386    444    539   1155       N  
ATOM   1766  CZ  ARG A1236      -5.606 -24.178  91.572  1.00 54.33           C  
ANISOU 1766  CZ  ARG A1236     6268   8054   6322    606    664   1064       C  
ATOM   1767  NH1 ARG A1236      -6.602 -23.544  92.172  1.00 55.70           N  
ANISOU 1767  NH1 ARG A1236     6397   8367   6402    768    818   1189       N  
ATOM   1768  NH2 ARG A1236      -4.517 -23.506  91.218  1.00 54.63           N  
ANISOU 1768  NH2 ARG A1236     6458   7944   6354    611    636    858       N  
ATOM   1769  N   LYS A1237      -3.171 -29.361  94.666  1.00 54.19           N  
ANISOU 1769  N   LYS A1237     6329   7937   6323    168    247   1134       N  
ATOM   1770  CA  LYS A1237      -1.996 -30.226  94.643  1.00 53.45           C  
ANISOU 1770  CA  LYS A1237     6321   7723   6264     85    124   1041       C  
ATOM   1771  C   LYS A1237      -2.164 -31.414  95.583  1.00 54.28           C  
ANISOU 1771  C   LYS A1237     6404   7873   6348     20     74   1166       C  
ATOM   1772  O   LYS A1237      -1.755 -32.536  95.254  1.00 58.59           O  
ANISOU 1772  O   LYS A1237     6981   8330   6949    -81    -50   1179       O  
ATOM   1773  CB  LYS A1237      -0.743 -29.431  95.005  1.00 52.77           C  
ANISOU 1773  CB  LYS A1237     6359   7574   6118    155    147    859       C  
ATOM   1774  CG  LYS A1237       0.551 -30.180  94.717  1.00 60.90           C  
ANISOU 1774  CG  LYS A1237     7454   8496   7191     92     28    769       C  
ATOM   1775  CD  LYS A1237       1.785 -29.349  95.031  1.00 59.61           C  
ANISOU 1775  CD  LYS A1237     7384   8298   6967    137     37    621       C  
ATOM   1776  CE  LYS A1237       2.117 -29.378  96.510  1.00 55.75           C  
ANISOU 1776  CE  LYS A1237     6947   7866   6369    161     60    634       C  
ATOM   1777  NZ  LYS A1237       3.345 -28.588  96.812  1.00 57.50           N  
ANISOU 1777  NZ  LYS A1237     7268   8057   6523    171     42    508       N  
ATOM   1778  N   LYS A1238      -2.785 -31.197  96.746  1.00 56.71           N  
ANISOU 1778  N   LYS A1238     6668   8313   6565     86    171   1265       N  
ATOM   1779  CA  LYS A1238      -3.005 -32.310  97.660  1.00 62.17           C  
ANISOU 1779  CA  LYS A1238     7329   9060   7234     19    125   1399       C  
ATOM   1780  C   LYS A1238      -3.965 -33.328  97.060  1.00 56.91           C  
ANISOU 1780  C   LYS A1238     6557   8420   6646   -123     34   1585       C  
ATOM   1781  O   LYS A1238      -3.719 -34.537  97.135  1.00 59.29           O  
ANISOU 1781  O   LYS A1238     6895   8655   6979   -240    -88   1636       O  
ATOM   1782  CB  LYS A1238      -3.533 -31.800  99.001  1.00 66.74           C  
ANISOU 1782  CB  LYS A1238     7882   9789   7687    134    261   1478       C  
ATOM   1783  CG  LYS A1238      -3.847 -32.908  99.995  1.00 69.02           C  
ANISOU 1783  CG  LYS A1238     8123  10156   7947     68    224   1635       C  
ATOM   1784  CD  LYS A1238      -4.511 -32.363 101.249  1.00 79.34           C  
ANISOU 1784  CD  LYS A1238     9396  11631   9120    201    377   1734       C  
ATOM   1785  CE  LYS A1238      -4.848 -33.479 102.227  1.00 83.26           C  
ANISOU 1785  CE  LYS A1238     9831  12216   9586    128    339   1905       C  
ATOM   1786  NZ  LYS A1238      -5.502 -32.952 103.457  1.00 84.98           N  
ANISOU 1786  NZ  LYS A1238    10018  12609   9661    277    500   2011       N  
ATOM   1787  N   SER A1239      -5.047 -32.860  96.432  1.00 57.38           N  
ANISOU 1787  N   SER A1239     6499   8572   6733   -122     83   1695       N  
ATOM   1788  CA  SER A1239      -5.986 -33.786  95.810  1.00 58.22           C  
ANISOU 1788  CA  SER A1239     6505   8709   6907   -289    -26   1891       C  
ATOM   1789  C   SER A1239      -5.338 -34.536  94.651  1.00 71.77           C  
ANISOU 1789  C   SER A1239     8338  10220   8711   -419   -191   1795       C  
ATOM   1790  O   SER A1239      -5.598 -35.728  94.449  1.00 71.93           O  
ANISOU 1790  O   SER A1239     8382  10186   8761   -582   -333   1911       O  
ATOM   1791  CB  SER A1239      -7.227 -33.024  95.337  1.00 58.99           C  
ANISOU 1791  CB  SER A1239     6439   8964   7011   -252     64   2035       C  
ATOM   1792  OG  SER A1239      -8.246 -33.917  94.929  1.00 68.14           O  
ANISOU 1792  OG  SER A1239     7477  10197   8217   -435    -45   2273       O  
ATOM   1793  N   LEU A1240      -4.451 -33.869  93.908  1.00 60.93           N  
ANISOU 1793  N   LEU A1240     7059   8725   7365   -344   -178   1586       N  
ATOM   1794  CA  LEU A1240      -3.785 -34.526  92.789  1.00 56.13           C  
ANISOU 1794  CA  LEU A1240     6574   7928   6823   -429   -315   1492       C  
ATOM   1795  C   LEU A1240      -2.839 -35.618  93.275  1.00 55.35           C  
ANISOU 1795  C   LEU A1240     6608   7714   6707   -461   -408   1447       C  
ATOM   1796  O   LEU A1240      -2.862 -36.753  92.772  1.00 67.36           O  
ANISOU 1796  O   LEU A1240     8221   9116   8255   -582   -547   1503       O  
ATOM   1797  CB  LEU A1240      -3.027 -33.491  91.960  1.00 53.86           C  
ANISOU 1797  CB  LEU A1240     6338   7566   6561   -326   -263   1294       C  
ATOM   1798  CG  LEU A1240      -2.014 -34.094  90.989  1.00 54.03           C  
ANISOU 1798  CG  LEU A1240     6505   7398   6626   -357   -375   1168       C  
ATOM   1799  CD1 LEU A1240      -2.747 -34.878  89.919  1.00 60.49           C  
ANISOU 1799  CD1 LEU A1240     7350   8139   7494   -503   -500   1270       C  
ATOM   1800  CD2 LEU A1240      -1.122 -33.021  90.386  1.00 61.18           C  
ANISOU 1800  CD2 LEU A1240     7444   8258   7542   -246   -312    981       C  
ATOM   1801  N   LEU A1241      -1.997 -35.292  94.259  1.00 54.83           N  
ANISOU 1801  N   LEU A1241     6571   7674   6586   -351   -336   1352       N  
ATOM   1802  CA  LEU A1241      -1.087 -36.296  94.796  1.00 70.87           C  
ANISOU 1802  CA  LEU A1241     8713   9618   8596   -364   -414   1324       C  
ATOM   1803  C   LEU A1241      -1.852 -37.442  95.445  1.00 73.65           C  
ANISOU 1803  C   LEU A1241     9048  10004   8932   -485   -488   1515       C  
ATOM   1804  O   LEU A1241      -1.430 -38.601  95.365  1.00 73.98           O  
ANISOU 1804  O   LEU A1241     9211   9919   8977   -551   -606   1534       O  
ATOM   1805  CB  LEU A1241      -0.127 -35.656  95.795  1.00 59.02           C  
ANISOU 1805  CB  LEU A1241     7227   8167   7030   -243   -328   1211       C  
ATOM   1806  CG  LEU A1241       0.864 -34.658  95.193  1.00 63.17           C  
ANISOU 1806  CG  LEU A1241     7793   8644   7564   -150   -287   1028       C  
ATOM   1807  CD1 LEU A1241       1.723 -34.031  96.277  1.00 56.34           C  
ANISOU 1807  CD1 LEU A1241     6949   7838   6619    -67   -225    946       C  
ATOM   1808  CD2 LEU A1241       1.727 -35.339  94.143  1.00 52.76           C  
ANISOU 1808  CD2 LEU A1241     6573   7176   6299   -160   -386    955       C  
ATOM   1809  N   SER A1242      -2.990 -37.142  96.081  1.00 77.19           N  
ANISOU 1809  N   SER A1242     9351  10624   9353   -510   -419   1672       N  
ATOM   1810  CA  SER A1242      -3.803 -38.200  96.672  1.00 80.19           C  
ANISOU 1810  CA  SER A1242     9690  11061   9717   -644   -494   1885       C  
ATOM   1811  C   SER A1242      -4.406 -39.102  95.602  1.00 83.91           C  
ANISOU 1811  C   SER A1242    10210  11428  10244   -829   -655   1995       C  
ATOM   1812  O   SER A1242      -4.526 -40.317  95.802  1.00 84.07           O  
ANISOU 1812  O   SER A1242    10313  11374  10255   -964   -786   2106       O  
ATOM   1813  CB  SER A1242      -4.902 -37.588  97.539  1.00 70.41           C  
ANISOU 1813  CB  SER A1242     8264  10059   8428   -607   -367   2047       C  
ATOM   1814  OG  SER A1242      -5.859 -38.567  97.897  1.00 90.04           O  
ANISOU 1814  OG  SER A1242    10676  12626  10909   -765   -450   2293       O  
ATOM   1815  N   LYS A1243      -4.790 -38.528  94.460  1.00 78.96           N  
ANISOU 1815  N   LYS A1243     9550  10783   9667   -847   -656   1969       N  
ATOM   1816  CA  LYS A1243      -5.251 -39.354  93.351  1.00 77.16           C  
ANISOU 1816  CA  LYS A1243     9408  10428   9480  -1029   -825   2053       C  
ATOM   1817  C   LYS A1243      -4.126 -40.220  92.805  1.00 85.46           C  
ANISOU 1817  C   LYS A1243    10714  11224  10532  -1029   -942   1907       C  
ATOM   1818  O   LYS A1243      -4.377 -41.333  92.330  1.00 89.46           O  
ANISOU 1818  O   LYS A1243    11368  11590  11034  -1190  -1109   1996       O  
ATOM   1819  CB  LYS A1243      -5.850 -38.478  92.249  1.00 72.80           C  
ANISOU 1819  CB  LYS A1243     8767   9919   8977  -1034   -795   2049       C  
ATOM   1820  CG  LYS A1243      -7.194 -37.870  92.624  1.00 81.49           C  
ANISOU 1820  CG  LYS A1243     9618  11274  10071  -1060   -708   2262       C  
ATOM   1821  CD  LYS A1243      -7.623 -36.792  91.646  1.00 90.29           C  
ANISOU 1821  CD  LYS A1243    10638  12442  11227  -1007   -640   2229       C  
ATOM   1822  CE  LYS A1243      -8.910 -36.121  92.105  1.00 95.17           C  
ANISOU 1822  CE  LYS A1243    10999  13336  11824   -982   -525   2450       C  
ATOM   1823  NZ  LYS A1243      -9.316 -35.002  91.205  1.00103.28           N  
ANISOU 1823  NZ  LYS A1243    11934  14423  12884   -903   -442   2420       N  
ATOM   1824  N   PHE A1244      -2.886 -39.740  92.879  1.00 86.36           N  
ANISOU 1824  N   PHE A1244    10895  11279  10641   -850   -860   1697       N  
ATOM   1825  CA  PHE A1244      -1.737 -40.543  92.480  1.00 77.19           C  
ANISOU 1825  CA  PHE A1244     9956   9907   9465   -804   -943   1575       C  
ATOM   1826  C   PHE A1244      -1.211 -41.436  93.598  1.00 84.26           C  
ANISOU 1826  C   PHE A1244    10924  10780  10309   -788   -972   1611       C  
ATOM   1827  O   PHE A1244      -0.253 -42.183  93.374  1.00 90.13           O  
ANISOU 1827  O   PHE A1244    11857  11360  11030   -729  -1034   1532       O  
ATOM   1828  CB  PHE A1244      -0.617 -39.643  91.957  1.00 72.35           C  
ANISOU 1828  CB  PHE A1244     9360   9261   8868   -625   -850   1363       C  
ATOM   1829  CG  PHE A1244      -0.915 -39.040  90.619  1.00 76.02           C  
ANISOU 1829  CG  PHE A1244     9823   9682   9380   -640   -855   1309       C  
ATOM   1830  CD1 PHE A1244      -1.855 -39.621  89.784  1.00 76.68           C  
ANISOU 1830  CD1 PHE A1244     9965   9689   9480   -806   -977   1423       C  
ATOM   1831  CD2 PHE A1244      -0.266 -37.895  90.194  1.00 79.18           C  
ANISOU 1831  CD2 PHE A1244    10169  10115   9801   -506   -750   1155       C  
ATOM   1832  CE1 PHE A1244      -2.142 -39.073  88.551  1.00 74.12           C  
ANISOU 1832  CE1 PHE A1244     9640   9326   9195   -825   -987   1379       C  
ATOM   1833  CE2 PHE A1244      -0.549 -37.345  88.958  1.00 74.10           C  
ANISOU 1833  CE2 PHE A1244     9523   9431   9201   -520   -755   1109       C  
ATOM   1834  CZ  PHE A1244      -1.489 -37.934  88.139  1.00 69.62           C  
ANISOU 1834  CZ  PHE A1244     9010   8792   8651   -674   -870   1218       C  
ATOM   1835  N   GLY A1245      -1.810 -41.385  94.787  1.00 80.44           N  
ANISOU 1835  N   GLY A1245    10301  10462   9800   -825   -923   1737       N  
ATOM   1836  CA  GLY A1245      -1.370 -42.210  95.893  1.00 81.74           C  
ANISOU 1836  CA  GLY A1245    10525  10618   9915   -817   -949   1781       C  
ATOM   1837  C   GLY A1245      -0.199 -41.674  96.685  1.00 91.15           C  
ANISOU 1837  C   GLY A1245    11699  11860  11076   -637   -840   1638       C  
ATOM   1838  O   GLY A1245       0.381 -42.421  97.481  1.00 97.27           O  
ANISOU 1838  O   GLY A1245    12548  12603  11808   -615   -872   1656       O  
ATOM   1839  N   MET A1246       0.179 -40.415  96.486  1.00 80.50           N  
ANISOU 1839  N   MET A1246    10262  10585   9739   -521   -724   1506       N  
ATOM   1840  CA  MET A1246       1.296 -39.807  97.191  1.00 70.23           C  
ANISOU 1840  CA  MET A1246     8947   9337   8399   -378   -638   1380       C  
ATOM   1841  C   MET A1246       0.808 -38.788  98.213  1.00 66.08           C  
ANISOU 1841  C   MET A1246     8279   8999   7829   -340   -512   1403       C  
ATOM   1842  O   MET A1246      -0.278 -38.215  98.089  1.00 78.30           O  
ANISOU 1842  O   MET A1246     9721  10642   9386   -373   -456   1478       O  
ATOM   1843  CB  MET A1246       2.253 -39.132  96.206  1.00 69.32           C  
ANISOU 1843  CB  MET A1246     8872   9151   8313   -278   -614   1211       C  
ATOM   1844  CG  MET A1246       2.795 -40.069  95.153  1.00 68.87           C  
ANISOU 1844  CG  MET A1246     8977   8909   8282   -274   -718   1181       C  
ATOM   1845  SD  MET A1246       3.629 -39.200  93.819  1.00 74.30           S  
ANISOU 1845  SD  MET A1246     9683   9541   9008   -167   -680   1016       S  
ATOM   1846  CE  MET A1246       4.038 -40.579  92.761  1.00 90.85           C  
ANISOU 1846  CE  MET A1246    12007  11411  11100   -154   -803   1023       C  
ATOM   1847  N   ASP A1247       1.630 -38.578  99.236  1.00 59.99           N  
ANISOU 1847  N   ASP A1247     7517   8281   6996   -262   -467   1348       N  
ATOM   1848  CA  ASP A1247       1.422 -37.515 100.205  1.00 71.90           C  
ANISOU 1848  CA  ASP A1247     8948   9936   8434   -198   -347   1333       C  
ATOM   1849  C   ASP A1247       2.115 -36.235  99.739  1.00 67.22           C  
ANISOU 1849  C   ASP A1247     8367   9338   7836   -111   -284   1168       C  
ATOM   1850  O   ASP A1247       2.897 -36.232  98.786  1.00 62.93           O  
ANISOU 1850  O   ASP A1247     7871   8697   7344    -95   -332   1071       O  
ATOM   1851  CB  ASP A1247       1.913 -37.940 101.591  1.00 72.89           C  
ANISOU 1851  CB  ASP A1247     9098  10118   8480   -178   -346   1367       C  
ATOM   1852  CG  ASP A1247       3.310 -38.520 101.565  1.00 93.28           C  
ANISOU 1852  CG  ASP A1247    11771  12608  11065   -147   -423   1288       C  
ATOM   1853  OD1 ASP A1247       3.721 -39.049 100.510  1.00 97.02           O  
ANISOU 1853  OD1 ASP A1247    12303  12957  11602   -152   -495   1253       O  
ATOM   1854  OD2 ASP A1247       3.995 -38.454 102.609  1.00108.39           O  
ANISOU 1854  OD2 ASP A1247    13699  14579  12906   -109   -408   1271       O  
ATOM   1855  N   GLU A1248       1.813 -35.136 100.429  1.00 71.15           N  
ANISOU 1855  N   GLU A1248     8834   9939   8259    -50   -176   1144       N  
ATOM   1856  CA  GLU A1248       2.203 -33.812  99.961  1.00 73.18           C  
ANISOU 1856  CA  GLU A1248     9116  10189   8502     14   -116   1007       C  
ATOM   1857  C   GLU A1248       3.716 -33.667  99.845  1.00 75.77           C  
ANISOU 1857  C   GLU A1248     9512  10456   8823     30   -173    882       C  
ATOM   1858  O   GLU A1248       4.478 -34.177 100.671  1.00 77.69           O  
ANISOU 1858  O   GLU A1248     9787  10713   9018     25   -215    892       O  
ATOM   1859  CB  GLU A1248       1.654 -32.740 100.903  1.00 83.58           C  
ANISOU 1859  CB  GLU A1248    10440  11610   9707     89      7   1010       C  
ATOM   1860  CG  GLU A1248       0.162 -32.493 100.768  1.00104.46           C  
ANISOU 1860  CG  GLU A1248    12993  14341  12354    114     96   1131       C  
ATOM   1861  CD  GLU A1248      -0.329 -31.395 101.693  1.00123.43           C  
ANISOU 1861  CD  GLU A1248    15433  16841  14623    234    237   1133       C  
ATOM   1862  OE1 GLU A1248      -1.446 -31.526 102.235  1.00132.76           O  
ANISOU 1862  OE1 GLU A1248    16535  18145  15762    273    318   1285       O  
ATOM   1863  OE2 GLU A1248       0.406 -30.402 101.882  1.00129.05           O  
ANISOU 1863  OE2 GLU A1248    16264  17508  15260    290    265    991       O  
ATOM   1864  N   GLY A1249       4.140 -32.958  98.804  1.00 70.87           N  
ANISOU 1864  N   GLY A1249     8900   9781   8246     46   -175    779       N  
ATOM   1865  CA  GLY A1249       5.540 -32.651  98.577  1.00 62.45           C  
ANISOU 1865  CA  GLY A1249     7873   8686   7171     58   -223    681       C  
ATOM   1866  C   GLY A1249       5.658 -31.680  97.423  1.00 65.63           C  
ANISOU 1866  C   GLY A1249     8273   9047   7618     72   -202    587       C  
ATOM   1867  O   GLY A1249       4.671 -31.340  96.766  1.00 68.12           O  
ANISOU 1867  O   GLY A1249     8560   9347   7976     77   -156    595       O  
ATOM   1868  N   VAL A1250       6.888 -31.227  97.183  1.00 62.23           N  
ANISOU 1868  N   VAL A1250     7861   8612   7173     74   -241    511       N  
ATOM   1869  CA  VAL A1250       7.143 -30.319  96.069  1.00 58.15           C  
ANISOU 1869  CA  VAL A1250     7340   8059   6695     80   -232    427       C  
ATOM   1870  C   VAL A1250       7.055 -31.110  94.770  1.00 57.04           C  
ANISOU 1870  C   VAL A1250     7165   7846   6662     96   -266    440       C  
ATOM   1871  O   VAL A1250       7.815 -32.060  94.557  1.00 50.63           O  
ANISOU 1871  O   VAL A1250     6352   7011   5873    117   -325    469       O  
ATOM   1872  CB  VAL A1250       8.505 -29.635  96.220  1.00 54.01           C  
ANISOU 1872  CB  VAL A1250     6834   7570   6116     59   -276    371       C  
ATOM   1873  CG1 VAL A1250       8.712 -28.624  95.098  1.00 50.51           C  
ANISOU 1873  CG1 VAL A1250     6389   7096   5708     54   -267    293       C  
ATOM   1874  CG2 VAL A1250       8.597 -28.966  97.576  1.00 51.90           C  
ANISOU 1874  CG2 VAL A1250     6642   7357   5722     27   -264    363       C  
ATOM   1875  N   THR A1251       6.139 -30.711  93.891  1.00 50.09           N  
ANISOU 1875  N   THR A1251     6271   6926   5836     94   -228    424       N  
ATOM   1876  CA  THR A1251       5.718 -31.541  92.768  1.00 56.26           C  
ANISOU 1876  CA  THR A1251     7046   7627   6705     90   -265    455       C  
ATOM   1877  C   THR A1251       6.254 -30.984  91.454  1.00 62.33           C  
ANISOU 1877  C   THR A1251     7812   8349   7520    114   -272    374       C  
ATOM   1878  O   THR A1251       5.951 -29.843  91.085  1.00 48.72           O  
ANISOU 1878  O   THR A1251     6073   6639   5799    112   -222    318       O  
ATOM   1879  CB  THR A1251       4.194 -31.648  92.725  1.00 59.97           C  
ANISOU 1879  CB  THR A1251     7486   8101   7200     51   -233    530       C  
ATOM   1880  OG1 THR A1251       3.732 -32.248  93.940  1.00 56.06           O  
ANISOU 1880  OG1 THR A1251     6982   7661   6657     30   -228    624       O  
ATOM   1881  CG2 THR A1251       3.750 -32.499  91.546  1.00 51.17           C  
ANISOU 1881  CG2 THR A1251     6389   6892   6162     15   -296    569       C  
ATOM   1882  N   PHE A1252       7.037 -31.800  90.752  1.00 53.83           N  
ANISOU 1882  N   PHE A1252     6764   7217   6474    151   -327    374       N  
ATOM   1883  CA  PHE A1252       7.592 -31.486  89.446  1.00 51.76           C  
ANISOU 1883  CA  PHE A1252     6504   6912   6252    191   -334    315       C  
ATOM   1884  C   PHE A1252       6.865 -32.300  88.385  1.00 56.10           C  
ANISOU 1884  C   PHE A1252     7112   7347   6855    187   -369    339       C  
ATOM   1885  O   PHE A1252       6.523 -33.466  88.614  1.00 49.16           O  
ANISOU 1885  O   PHE A1252     6298   6408   5973    172   -418    407       O  
ATOM   1886  CB  PHE A1252       9.092 -31.794  89.410  1.00 48.82           C  
ANISOU 1886  CB  PHE A1252     6124   6575   5850    263   -362    314       C  
ATOM   1887  CG  PHE A1252       9.879 -31.087  90.476  1.00 51.73           C  
ANISOU 1887  CG  PHE A1252     6441   7059   6155    238   -357    311       C  
ATOM   1888  CD1 PHE A1252      10.006 -31.632  91.747  1.00 55.02           C  
ANISOU 1888  CD1 PHE A1252     6864   7520   6520    224   -375    366       C  
ATOM   1889  CD2 PHE A1252      10.488 -29.873  90.210  1.00 48.80           C  
ANISOU 1889  CD2 PHE A1252     6028   6747   5767    213   -346    259       C  
ATOM   1890  CE1 PHE A1252      10.727 -30.980  92.730  1.00 54.95           C  
ANISOU 1890  CE1 PHE A1252     6826   7612   6440    185   -384    368       C  
ATOM   1891  CE2 PHE A1252      11.211 -29.217  91.186  1.00 49.96           C  
ANISOU 1891  CE2 PHE A1252     6153   6988   5840    162   -364    265       C  
ATOM   1892  CZ  PHE A1252      11.329 -29.770  92.451  1.00 58.30           C  
ANISOU 1892  CZ  PHE A1252     7222   8088   6841    147   -384    318       C  
ATOM   1893  N   MET A1253       6.634 -31.689  87.223  1.00 56.28           N  
ANISOU 1893  N   MET A1253     7129   7333   6921    188   -354    288       N  
ATOM   1894  CA  MET A1253       5.911 -32.339  86.139  1.00 52.36           C  
ANISOU 1894  CA  MET A1253     6703   6724   6467    165   -398    309       C  
ATOM   1895  C   MET A1253       6.676 -32.212  84.829  1.00 48.48           C  
ANISOU 1895  C   MET A1253     6252   6178   5990    240   -403    246       C  
ATOM   1896  O   MET A1253       7.196 -31.142  84.501  1.00 47.21           O  
ANISOU 1896  O   MET A1253     6021   6079   5836    266   -357    184       O  
ATOM   1897  CB  MET A1253       4.499 -31.747  85.967  1.00 56.30           C  
ANISOU 1897  CB  MET A1253     7149   7239   7002     78   -374    337       C  
ATOM   1898  CG  MET A1253       3.965 -31.851  84.543  1.00 70.23           C  
ANISOU 1898  CG  MET A1253     8960   8911   8812     50   -412    330       C  
ATOM   1899  SD  MET A1253       2.205 -31.523  84.353  1.00 70.57           S  
ANISOU 1899  SD  MET A1253     8933   8986   8896    -65   -409    420       S  
ATOM   1900  CE  MET A1253       2.071 -29.922  85.122  1.00 67.35           C  
ANISOU 1900  CE  MET A1253     8398   8719   8472    -18   -283    378       C  
ATOM   1901  N   PHE A1254       6.734 -33.314  84.087  1.00 48.29           N  
ANISOU 1901  N   PHE A1254     6358   6032   5959    275   -461    268       N  
ATOM   1902  CA  PHE A1254       7.200 -33.329  82.709  1.00 48.20           C  
ANISOU 1902  CA  PHE A1254     6417   5944   5951    351   -467    219       C  
ATOM   1903  C   PHE A1254       6.085 -33.859  81.819  1.00 50.15           C  
ANISOU 1903  C   PHE A1254     6781   6056   6218    270   -533    242       C  
ATOM   1904  O   PHE A1254       5.384 -34.803  82.194  1.00 54.24           O  
ANISOU 1904  O   PHE A1254     7387   6500   6722    193   -602    314       O  
ATOM   1905  CB  PHE A1254       8.451 -34.202  82.557  1.00 48.90           C  
ANISOU 1905  CB  PHE A1254     6598   6000   5982    503   -474    229       C  
ATOM   1906  CG  PHE A1254       8.850 -34.457  81.126  1.00 57.96           C  
ANISOU 1906  CG  PHE A1254     7862   7050   7110    607   -478    194       C  
ATOM   1907  CD1 PHE A1254       8.406 -35.589  80.455  1.00 49.99           C  
ANISOU 1907  CD1 PHE A1254     7073   5858   6064    620   -548    213       C  
ATOM   1908  CD2 PHE A1254       9.676 -33.571  80.454  1.00 56.31           C  
ANISOU 1908  CD2 PHE A1254     7559   6928   6907    688   -417    150       C  
ATOM   1909  CE1 PHE A1254       8.772 -35.825  79.142  1.00 50.37           C  
ANISOU 1909  CE1 PHE A1254     7259   5805   6074    729   -548    178       C  
ATOM   1910  CE2 PHE A1254      10.046 -33.804  79.140  1.00 49.93           C  
ANISOU 1910  CE2 PHE A1254     6859   6040   6071    799   -411    125       C  
ATOM   1911  CZ  PHE A1254       9.595 -34.932  78.486  1.00 49.85           C  
ANISOU 1911  CZ  PHE A1254     7082   5841   6017    829   -471    134       C  
ATOM   1912  N   ILE A1255       5.932 -33.266  80.637  1.00 48.03           N  
ANISOU 1912  N   ILE A1255     6516   5757   5977    273   -522    192       N  
ATOM   1913  CA  ILE A1255       5.009 -33.777  79.628  1.00 53.42           C  
ANISOU 1913  CA  ILE A1255     7326   6304   6665    195   -599    215       C  
ATOM   1914  C   ILE A1255       5.648 -33.615  78.254  1.00 49.52           C  
ANISOU 1914  C   ILE A1255     6918   5741   6155    297   -587    144       C  
ATOM   1915  O   ILE A1255       6.140 -32.535  77.912  1.00 53.60           O  
ANISOU 1915  O   ILE A1255     7313   6352   6700    349   -514     86       O  
ATOM   1916  CB  ILE A1255       3.634 -33.078  79.685  1.00 51.48           C  
ANISOU 1916  CB  ILE A1255     6964   6117   6479     43   -603    259       C  
ATOM   1917  CG1 ILE A1255       2.748 -33.557  78.527  1.00 50.06           C  
ANISOU 1917  CG1 ILE A1255     6910   5809   6303    -55   -698    295       C  
ATOM   1918  CG2 ILE A1255       3.780 -31.557  79.677  1.00 55.26           C  
ANISOU 1918  CG2 ILE A1255     7271   6726   7000     73   -502    195       C  
ATOM   1919  CD1 ILE A1255       1.350 -32.980  78.540  1.00 56.62           C  
ANISOU 1919  CD1 ILE A1255     7611   6716   7186   -203   -708    376       C  
ATOM   1920  N   GLY A1256       5.647 -34.686  77.477  1.00 56.23           N  
ANISOU 1920  N   GLY A1256     7995   6422   6949    328   -663    155       N  
ATOM   1921  CA  GLY A1256       6.214 -34.663  76.144  1.00 49.44           C  
ANISOU 1921  CA  GLY A1256     7251   5481   6051    442   -651     96       C  
ATOM   1922  C   GLY A1256       6.569 -36.058  75.689  1.00 53.85           C  
ANISOU 1922  C   GLY A1256     8104   5848   6506    539   -718    111       C  
ATOM   1923  O   GLY A1256       6.507 -37.028  76.449  1.00 55.69           O  
ANISOU 1923  O   GLY A1256     8445   6017   6699    525   -771    164       O  
ATOM   1924  N   ARG A1257       6.948 -36.147  74.416  1.00 54.96           N  
ANISOU 1924  N   ARG A1257     8397   5892   6593    648   -713     63       N  
ATOM   1925  CA  ARG A1257       7.317 -37.430  73.832  1.00 53.03           C  
ANISOU 1925  CA  ARG A1257     8485   5440   6223    773   -768     68       C  
ATOM   1926  C   ARG A1257       8.587 -37.971  74.480  1.00 57.50           C  
ANISOU 1926  C   ARG A1257     9067   6055   6725    997   -692     86       C  
ATOM   1927  O   ARG A1257       9.506 -37.215  74.812  1.00 57.38           O  
ANISOU 1927  O   ARG A1257     8822   6236   6745   1109   -582     79       O  
ATOM   1928  CB  ARG A1257       7.515 -37.288  72.320  1.00 59.94           C  
ANISOU 1928  CB  ARG A1257     9514   6219   7043    868   -760     11       C  
ATOM   1929  CG  ARG A1257       7.685 -38.618  71.590  1.00 73.41           C  
ANISOU 1929  CG  ARG A1257    11633   7665   8594    985   -832     11       C  
ATOM   1930  CD  ARG A1257       7.886 -38.435  70.090  1.00 85.15           C  
ANISOU 1930  CD  ARG A1257    13282   9058  10012   1091   -816    -47       C  
ATOM   1931  NE  ARG A1257       8.983 -37.521  69.781  1.00104.32           N  
ANISOU 1931  NE  ARG A1257    15491  11682  12464   1291   -659    -79       N  
ATOM   1932  CZ  ARG A1257       8.821 -36.301  69.279  1.00117.25           C  
ANISOU 1932  CZ  ARG A1257    16903  13454  14193   1221   -613   -115       C  
ATOM   1933  NH1 ARG A1257       7.602 -35.849  69.019  1.00125.97           N  
ANISOU 1933  NH1 ARG A1257    17967  14523  15373    976   -700   -124       N  
ATOM   1934  NH2 ARG A1257       9.874 -35.534  69.030  1.00111.21           N  
ANISOU 1934  NH2 ARG A1257    15951  12865  13439   1392   -482   -126       N  
ATOM   1935  N   PHE A1258       8.632 -39.290  74.664  1.00 60.40           N  
ANISOU 1935  N   PHE A1258     9713   6244   6992   1055   -761    123       N  
ATOM   1936  CA  PHE A1258       9.838 -39.960  75.146  1.00 55.91           C  
ANISOU 1936  CA  PHE A1258     9206   5698   6340   1301   -690    154       C  
ATOM   1937  C   PHE A1258      10.747 -40.227  73.951  1.00 70.02           C  
ANISOU 1937  C   PHE A1258    11184   7410   8010   1573   -622    125       C  
ATOM   1938  O   PHE A1258      10.406 -41.025  73.071  1.00 75.89           O  
ANISOU 1938  O   PHE A1258    12278   7911   8647   1606   -695    105       O  
ATOM   1939  CB  PHE A1258       9.493 -41.266  75.858  1.00 57.23           C  
ANISOU 1939  CB  PHE A1258     9611   5695   6439   1260   -789    210       C  
ATOM   1940  CG  PHE A1258       8.752 -41.093  77.160  1.00 59.81           C  
ANISOU 1940  CG  PHE A1258     9739   6123   6865   1033   -838    259       C  
ATOM   1941  CD1 PHE A1258       8.409 -39.838  77.640  1.00 54.70           C  
ANISOU 1941  CD1 PHE A1258     8747   5690   6347    893   -788    246       C  
ATOM   1942  CD2 PHE A1258       8.405 -42.206  77.910  1.00 59.55           C  
ANISOU 1942  CD2 PHE A1258     9885   5960   6781    970   -930    323       C  
ATOM   1943  CE1 PHE A1258       7.725 -39.701  78.842  1.00 54.16           C  
ANISOU 1943  CE1 PHE A1258     8518   5713   6349    713   -820    297       C  
ATOM   1944  CE2 PHE A1258       7.727 -42.077  79.108  1.00 63.85           C  
ANISOU 1944  CE2 PHE A1258    10247   6606   7407    774   -968    379       C  
ATOM   1945  CZ  PHE A1258       7.385 -40.825  79.576  1.00 55.26           C  
ANISOU 1945  CZ  PHE A1258     8816   5740   6441    654   -907    367       C  
ATOM   1946  N   ASP A1259      11.907 -39.577  73.918  1.00 69.94           N  
ANISOU 1946  N   ASP A1259    10959   7609   8008   1767   -486    135       N  
ATOM   1947  CA  ASP A1259      12.822 -39.730  72.794  1.00 68.30           C  
ANISOU 1947  CA  ASP A1259    10886   7376   7687   2048   -398    129       C  
ATOM   1948  C   ASP A1259      14.219 -39.316  73.235  1.00 74.10           C  
ANISOU 1948  C   ASP A1259    11359   8378   8420   2263   -259    200       C  
ATOM   1949  O   ASP A1259      14.414 -38.775  74.327  1.00 79.03           O  
ANISOU 1949  O   ASP A1259    11697   9195   9136   2160   -244    237       O  
ATOM   1950  CB  ASP A1259      12.366 -38.912  71.579  1.00 66.24           C  
ANISOU 1950  CB  ASP A1259    10612   7095   7459   1971   -401     60       C  
ATOM   1951  CG  ASP A1259      12.094 -37.458  71.920  1.00 78.16           C  
ANISOU 1951  CG  ASP A1259    11737   8830   9132   1772   -375     40       C  
ATOM   1952  OD1 ASP A1259      12.995 -36.788  72.467  1.00 75.13           O  
ANISOU 1952  OD1 ASP A1259    11075   8682   8790   1846   -283     81       O  
ATOM   1953  OD2 ASP A1259      10.975 -36.982  71.639  1.00 85.41           O  
ANISOU 1953  OD2 ASP A1259    12640   9687  10125   1541   -452     -7       O  
ATOM   1954  N   ARG A1260      15.192 -39.590  72.371  1.00 73.01           N  
ANISOU 1954  N   ARG A1260    11327   8252   8162   2566   -160    232       N  
ATOM   1955  CA  ARG A1260      16.578 -39.214  72.610  1.00 73.91           C  
ANISOU 1955  CA  ARG A1260    11184   8642   8256   2789    -25    333       C  
ATOM   1956  C   ARG A1260      16.950 -38.021  71.739  1.00 72.15           C  
ANISOU 1956  C   ARG A1260    10740   8596   8080   2795     47    325       C  
ATOM   1957  O   ARG A1260      16.651 -38.002  70.540  1.00 76.89           O  
ANISOU 1957  O   ARG A1260    11521   9064   8629   2846     50    265       O  
ATOM   1958  CB  ARG A1260      17.514 -40.392  72.334  1.00 72.37           C  
ANISOU 1958  CB  ARG A1260    11239   8379   7880   3166     56    413       C  
ATOM   1959  CG  ARG A1260      17.224 -41.612  73.197  1.00 75.08           C  
ANISOU 1959  CG  ARG A1260    11824   8539   8165   3176    -16    430       C  
ATOM   1960  CD  ARG A1260      18.332 -42.649  73.108  1.00 95.19           C  
ANISOU 1960  CD  ARG A1260    14559  11074  10535   3581     89    534       C  
ATOM   1961  NE  ARG A1260      18.036 -43.830  73.916  1.00100.96           N  
ANISOU 1961  NE  ARG A1260    15547  11610  11204   3589     14    548       N  
ATOM   1962  CZ  ARG A1260      18.281 -43.925  75.220  1.00 99.65           C  
ANISOU 1962  CZ  ARG A1260    15179  11583  11100   3523      3    619       C  
ATOM   1963  NH1 ARG A1260      18.826 -42.905  75.871  1.00 99.91           N  
ANISOU 1963  NH1 ARG A1260    14765  11945  11252   3437     54    680       N  
ATOM   1964  NH2 ARG A1260      17.978 -45.038  75.873  1.00 95.80           N  
ANISOU 1964  NH2 ARG A1260    14953  10899  10548   3532    -69    632       N  
ATOM   1965  N   GLY A1261      17.586 -37.024  72.349  1.00 67.51           N  
ANISOU 1965  N   GLY A1261     9772   8297   7581   2728     93    388       N  
ATOM   1966  CA  GLY A1261      18.113 -35.896  71.612  1.00 62.30           C  
ANISOU 1966  CA  GLY A1261     8884   7832   6956   2741    162    409       C  
ATOM   1967  C   GLY A1261      17.115 -34.820  71.253  1.00 60.34           C  
ANISOU 1967  C   GLY A1261     8554   7543   6829   2456     96    297       C  
ATOM   1968  O   GLY A1261      17.473 -33.893  70.518  1.00 58.50           O  
ANISOU 1968  O   GLY A1261     8167   7441   6620   2461    146    306       O  
ATOM   1969  N   GLN A1262      15.875 -34.907  71.736  1.00 65.45           N  
ANISOU 1969  N   GLN A1262     9292   8025   7551   2214    -10    208       N  
ATOM   1970  CA  GLN A1262      14.872 -33.914  71.371  1.00 72.69           C  
ANISOU 1970  CA  GLN A1262    10137   8908   8575   1966    -63    116       C  
ATOM   1971  C   GLN A1262      14.210 -33.300  72.602  1.00 68.52           C  
ANISOU 1971  C   GLN A1262     9428   8443   8163   1705   -123     96       C  
ATOM   1972  O   GLN A1262      14.564 -32.187  73.007  1.00 63.11           O  
ANISOU 1972  O   GLN A1262     8486   7948   7546   1611    -97    112       O  
ATOM   1973  CB  GLN A1262      13.818 -34.531  70.446  1.00 77.28           C  
ANISOU 1973  CB  GLN A1262    11029   9217   9119   1927   -135     35       C  
ATOM   1974  CG  GLN A1262      14.389 -35.120  69.159  1.00101.20           C  
ANISOU 1974  CG  GLN A1262    14290  12151  12011   2190    -78     40       C  
ATOM   1975  CD  GLN A1262      13.312 -35.508  68.161  1.00109.96           C  
ANISOU 1975  CD  GLN A1262    15698  12999  13084   2105   -167    -43       C  
ATOM   1976  OE1 GLN A1262      13.121 -36.688  67.861  1.00101.85           O  
ANISOU 1976  OE1 GLN A1262    15016  11746  11936   2204   -214    -51       O  
ATOM   1977  NE2 GLN A1262      12.605 -34.512  67.637  1.00113.68           N  
ANISOU 1977  NE2 GLN A1262    16051  13493  13649   1915   -197   -100       N  
ATOM   1978  N   LYS A1263      13.238 -33.999  73.192  1.00 53.33           N  
ANISOU 1978  N   LYS A1263     7649   6360   6253   1584   -205     69       N  
ATOM   1979  CA  LYS A1263      12.473 -33.447  74.305  1.00 54.72           C  
ANISOU 1979  CA  LYS A1263     7676   6588   6529   1351   -253     54       C  
ATOM   1980  C   LYS A1263      13.137 -33.634  75.663  1.00 50.53           C  
ANISOU 1980  C   LYS A1263     7018   6189   5992   1372   -238    120       C  
ATOM   1981  O   LYS A1263      12.686 -33.023  76.637  1.00 50.39           O  
ANISOU 1981  O   LYS A1263     6858   6246   6043   1200   -261    112       O  
ATOM   1982  CB  LYS A1263      11.063 -34.047  74.325  1.00 58.50           C  
ANISOU 1982  CB  LYS A1263     8335   6867   7026   1193   -352     20       C  
ATOM   1983  CG  LYS A1263      10.196 -33.547  73.181  1.00 58.04           C  
ANISOU 1983  CG  LYS A1263     8335   6717   7001   1096   -383    -39       C  
ATOM   1984  CD  LYS A1263      10.393 -32.050  72.981  1.00 66.59           C  
ANISOU 1984  CD  LYS A1263     9172   7969   8161   1041   -321    -69       C  
ATOM   1985  CE  LYS A1263       9.880 -31.589  71.626  1.00 74.66           C  
ANISOU 1985  CE  LYS A1263    10258   8916   9195   1012   -331   -120       C  
ATOM   1986  NZ  LYS A1263      10.280 -30.181  71.332  1.00 71.15           N  
ANISOU 1986  NZ  LYS A1263     9597   8630   8808    991   -265   -143       N  
ATOM   1987  N   GLY A1264      14.194 -34.442  75.754  1.00 54.48           N  
ANISOU 1987  N   GLY A1264     7571   6726   6405   1586   -196    192       N  
ATOM   1988  CA  GLY A1264      15.021 -34.485  76.945  1.00 55.17           C  
ANISOU 1988  CA  GLY A1264     7499   6980   6483   1618   -174    274       C  
ATOM   1989  C   GLY A1264      14.547 -35.346  78.096  1.00 61.19           C  
ANISOU 1989  C   GLY A1264     8347   7661   7240   1555   -232    292       C  
ATOM   1990  O   GLY A1264      15.050 -35.172  79.213  1.00 54.15           O  
ANISOU 1990  O   GLY A1264     7299   6917   6358   1524   -226    348       O  
ATOM   1991  N   VAL A1265      13.605 -36.269  77.882  1.00 58.41           N  
ANISOU 1991  N   VAL A1265     8243   7084   6868   1520   -296    256       N  
ATOM   1992  CA  VAL A1265      13.151 -37.095  79.001  1.00 55.43           C  
ANISOU 1992  CA  VAL A1265     7942   6636   6484   1448   -356    288       C  
ATOM   1993  C   VAL A1265      14.287 -37.958  79.539  1.00 60.00           C  
ANISOU 1993  C   VAL A1265     8552   7270   6976   1661   -317    377       C  
ATOM   1994  O   VAL A1265      14.299 -38.310  80.725  1.00 54.87           O  
ANISOU 1994  O   VAL A1265     7855   6663   6331   1610   -343    423       O  
ATOM   1995  CB  VAL A1265      11.930 -37.953  78.604  1.00 57.75           C  
ANISOU 1995  CB  VAL A1265     8505   6675   6761   1348   -452    255       C  
ATOM   1996  CG1 VAL A1265      12.355 -39.196  77.835  1.00 58.74           C  
ANISOU 1996  CG1 VAL A1265     8944   6613   6760   1561   -461    272       C  
ATOM   1997  CG2 VAL A1265      11.133 -38.340  79.844  1.00 53.28           C  
ANISOU 1997  CG2 VAL A1265     7927   6086   6231   1174   -522    288       C  
ATOM   1998  N   ASP A1266      15.257 -38.315  78.691  1.00 55.54           N  
ANISOU 1998  N   ASP A1266     8065   6715   6323   1917   -248    414       N  
ATOM   1999  CA  ASP A1266      16.414 -39.057  79.181  1.00 59.59           C  
ANISOU 1999  CA  ASP A1266     8576   7317   6748   2150   -193    522       C  
ATOM   2000  C   ASP A1266      17.233 -38.220  80.157  1.00 58.54           C  
ANISOU 2000  C   ASP A1266     8105   7474   6663   2100   -159    598       C  
ATOM   2001  O   ASP A1266      17.744 -38.741  81.158  1.00 66.43           O  
ANISOU 2001  O   ASP A1266     9059   8552   7632   2154   -159    682       O  
ATOM   2002  CB  ASP A1266      17.275 -39.516  78.004  1.00 58.47           C  
ANISOU 2002  CB  ASP A1266     8574   7150   6491   2460   -108    561       C  
ATOM   2003  CG  ASP A1266      17.460 -38.430  76.958  1.00 72.89           C  
ANISOU 2003  CG  ASP A1266    10262   9080   8354   2453    -57    527       C  
ATOM   2004  OD1 ASP A1266      16.611 -37.515  76.890  1.00 66.99           O  
ANISOU 2004  OD1 ASP A1266     9415   8325   7712   2201   -107    440       O  
ATOM   2005  OD2 ASP A1266      18.448 -38.492  76.197  1.00 78.46           O  
ANISOU 2005  OD2 ASP A1266    10955   9879   8975   2709     39    596       O  
ATOM   2006  N   VAL A1267      17.333 -36.913  79.903  1.00 55.44           N  
ANISOU 2006  N   VAL A1267     7488   7236   6341   1978   -141    573       N  
ATOM   2007  CA  VAL A1267      18.043 -36.033  80.824  1.00 56.29           C  
ANISOU 2007  CA  VAL A1267     7304   7600   6485   1884   -134    643       C  
ATOM   2008  C   VAL A1267      17.316 -35.970  82.160  1.00 56.22           C  
ANISOU 2008  C   VAL A1267     7265   7568   6527   1668   -205    612       C  
ATOM   2009  O   VAL A1267      17.941 -36.000  83.229  1.00 59.76           O  
ANISOU 2009  O   VAL A1267     7585   8163   6959   1656   -214    695       O  
ATOM   2010  CB  VAL A1267      18.204 -34.636  80.196  1.00 56.31           C  
ANISOU 2010  CB  VAL A1267     7121   7733   6541   1779   -116    614       C  
ATOM   2011  CG1 VAL A1267      19.021 -33.729  81.101  1.00 54.22           C  
ANISOU 2011  CG1 VAL A1267     6586   7723   6292   1668   -128    700       C  
ATOM   2012  CG2 VAL A1267      18.839 -34.742  78.817  1.00 55.05           C  
ANISOU 2012  CG2 VAL A1267     7001   7589   6325   1998    -40    647       C  
ATOM   2013  N   LEU A1268      15.981 -35.922  82.125  1.00 57.83           N  
ANISOU 2013  N   LEU A1268     7589   7597   6788   1501   -256    506       N  
ATOM   2014  CA  LEU A1268      15.215 -35.903  83.364  1.00 58.79           C  
ANISOU 2014  CA  LEU A1268     7688   7700   6948   1316   -312    488       C  
ATOM   2015  C   LEU A1268      15.345 -37.218  84.123  1.00 54.73           C  
ANISOU 2015  C   LEU A1268     7300   7118   6378   1406   -336    554       C  
ATOM   2016  O   LEU A1268      15.411 -37.222  85.356  1.00 57.30           O  
ANISOU 2016  O   LEU A1268     7537   7527   6705   1325   -359    594       O  
ATOM   2017  CB  LEU A1268      13.746 -35.601  83.072  1.00 51.68           C  
ANISOU 2017  CB  LEU A1268     6872   6650   6113   1139   -353    392       C  
ATOM   2018  CG  LEU A1268      12.830 -35.718  84.292  1.00 58.78           C  
ANISOU 2018  CG  LEU A1268     7767   7526   7041    971   -400    391       C  
ATOM   2019  CD1 LEU A1268      13.232 -34.712  85.369  1.00 50.86           C  
ANISOU 2019  CD1 LEU A1268     6563   6710   6051    875   -385    404       C  
ATOM   2020  CD2 LEU A1268      11.378 -35.544  83.909  1.00 50.61           C  
ANISOU 2020  CD2 LEU A1268     6806   6362   6061    821   -436    333       C  
ATOM   2021  N   LEU A1269      15.391 -38.344  83.410  1.00 54.86           N  
ANISOU 2021  N   LEU A1269     7543   6971   6330   1576   -334    567       N  
ATOM   2022  CA  LEU A1269      15.526 -39.625  84.096  1.00 57.67           C  
ANISOU 2022  CA  LEU A1269     8051   7241   6622   1671   -361    632       C  
ATOM   2023  C   LEU A1269      16.898 -39.758  84.746  1.00 57.03           C  
ANISOU 2023  C   LEU A1269     7819   7364   6486   1836   -308    749       C  
ATOM   2024  O   LEU A1269      17.012 -40.247  85.880  1.00 57.45           O  
ANISOU 2024  O   LEU A1269     7852   7453   6524   1813   -336    808       O  
ATOM   2025  CB  LEU A1269      15.268 -40.775  83.120  1.00 69.04           C  
ANISOU 2025  CB  LEU A1269     9816   8431   7983   1820   -378    617       C  
ATOM   2026  CG  LEU A1269      13.832 -40.879  82.593  1.00 66.83           C  
ANISOU 2026  CG  LEU A1269     9714   7936   7744   1629   -462    531       C  
ATOM   2027  CD1 LEU A1269      13.660 -42.082  81.672  1.00 69.05           C  
ANISOU 2027  CD1 LEU A1269    10363   7952   7922   1767   -501    524       C  
ATOM   2028  CD2 LEU A1269      12.836 -40.934  83.740  1.00 68.19           C  
ANISOU 2028  CD2 LEU A1269     9840   8094   7976   1391   -537    537       C  
ATOM   2029  N   LYS A1270      17.949 -39.299  84.058  1.00 57.49           N  
ANISOU 2029  N   LYS A1270     7753   7576   6515   1994   -235    800       N  
ATOM   2030  CA  LYS A1270      19.270 -39.288  84.679  1.00 64.17           C  
ANISOU 2030  CA  LYS A1270     8405   8664   7314   2126   -191    942       C  
ATOM   2031  C   LYS A1270      19.299 -38.358  85.887  1.00 66.25           C  
ANISOU 2031  C   LYS A1270     8427   9108   7636   1890   -238    957       C  
ATOM   2032  O   LYS A1270      19.925 -38.673  86.907  1.00 68.41           O  
ANISOU 2032  O   LYS A1270     8608   9509   7876   1915   -249   1060       O  
ATOM   2033  CB  LYS A1270      20.333 -38.872  83.660  1.00 68.35           C  
ANISOU 2033  CB  LYS A1270     8817   9352   7801   2319   -106   1016       C  
ATOM   2034  CG  LYS A1270      20.470 -39.803  82.466  1.00101.78           C  
ANISOU 2034  CG  LYS A1270    13306  13422  11946   2602    -42   1016       C  
ATOM   2035  CD  LYS A1270      21.140 -39.096  81.293  1.00105.18           C  
ANISOU 2035  CD  LYS A1270    13621  13985  12359   2724     37   1047       C  
ATOM   2036  CE  LYS A1270      21.177 -39.973  80.048  1.00 99.71           C  
ANISOU 2036  CE  LYS A1270    13219  13103  11562   3007    102   1030       C  
ATOM   2037  NZ  LYS A1270      21.616 -39.213  78.841  1.00 92.18           N  
ANISOU 2037  NZ  LYS A1270    12168  12257  10600   3095    174   1039       N  
ATOM   2038  N   ALA A1271      18.597 -37.222  85.807  1.00 56.15           N  
ANISOU 2038  N   ALA A1271     7067   7830   6435   1663   -267    856       N  
ATOM   2039  CA  ALA A1271      18.551 -36.311  86.947  1.00 65.04           C  
ANISOU 2039  CA  ALA A1271     8021   9094   7597   1443   -314    857       C  
ATOM   2040  C   ALA A1271      17.816 -36.933  88.129  1.00 66.88           C  
ANISOU 2040  C   ALA A1271     8344   9235   7833   1346   -363    840       C  
ATOM   2041  O   ALA A1271      18.215 -36.747  89.287  1.00 58.34           O  
ANISOU 2041  O   ALA A1271     7149   8286   6730   1267   -393    901       O  
ATOM   2042  CB  ALA A1271      17.892 -34.993  86.536  1.00 54.74           C  
ANISOU 2042  CB  ALA A1271     6657   7781   6360   1252   -325    748       C  
ATOM   2043  N   ILE A1272      16.753 -37.691  87.855  1.00 55.07           N  
ANISOU 2043  N   ILE A1272     7054   7516   6354   1340   -380    772       N  
ATOM   2044  CA  ILE A1272      16.027 -38.354  88.933  1.00 62.38           C  
ANISOU 2044  CA  ILE A1272     8065   8358   7278   1248   -428    775       C  
ATOM   2045  C   ILE A1272      16.903 -39.413  89.588  1.00 66.01           C  
ANISOU 2045  C   ILE A1272     8551   8863   7665   1408   -428    892       C  
ATOM   2046  O   ILE A1272      16.922 -39.551  90.819  1.00 63.51           O  
ANISOU 2046  O   ILE A1272     8179   8616   7337   1329   -459    936       O  
ATOM   2047  CB  ILE A1272      14.713 -38.953  88.396  1.00 62.43           C  
ANISOU 2047  CB  ILE A1272     8282   8125   7312   1191   -462    704       C  
ATOM   2048  CG1 ILE A1272      13.750 -37.841  87.973  1.00 56.47           C  
ANISOU 2048  CG1 ILE A1272     7468   7355   6631   1015   -463    607       C  
ATOM   2049  CG2 ILE A1272      14.065 -39.860  89.434  1.00 55.20           C  
ANISOU 2049  CG2 ILE A1272     7467   7124   6382   1120   -516    741       C  
ATOM   2050  CD1 ILE A1272      12.504 -38.348  87.271  1.00 53.82           C  
ANISOU 2050  CD1 ILE A1272     7314   6812   6323    950   -504    560       C  
ATOM   2051  N   GLU A1273      17.665 -40.157  88.781  1.00 59.56           N  
ANISOU 2051  N   GLU A1273     7823   8016   6790   1649   -385    949       N  
ATOM   2052  CA  GLU A1273      18.570 -41.147  89.357  1.00 59.23           C  
ANISOU 2052  CA  GLU A1273     7805   8031   6670   1837   -371   1075       C  
ATOM   2053  C   GLU A1273      19.675 -40.486  90.175  1.00 59.59           C  
ANISOU 2053  C   GLU A1273     7575   8367   6701   1821   -361   1185       C  
ATOM   2054  O   GLU A1273      20.103 -41.032  91.199  1.00 60.61           O  
ANISOU 2054  O   GLU A1273     7669   8570   6789   1852   -380   1278       O  
ATOM   2055  CB  GLU A1273      19.164 -42.029  88.259  1.00 66.91           C  
ANISOU 2055  CB  GLU A1273     8948   8912   7563   2135   -311   1120       C  
ATOM   2056  CG  GLU A1273      18.175 -43.023  87.681  1.00 70.02           C  
ANISOU 2056  CG  GLU A1273     9680   8989   7933   2159   -349   1042       C  
ATOM   2057  CD  GLU A1273      18.838 -44.074  86.819  1.00 87.04           C  
ANISOU 2057  CD  GLU A1273    12066  11031   9974   2485   -292   1098       C  
ATOM   2058  OE1 GLU A1273      19.905 -43.782  86.239  1.00 94.97           O  
ANISOU 2058  OE1 GLU A1273    12950  12200  10935   2693   -203   1170       O  
ATOM   2059  OE2 GLU A1273      18.296 -45.196  86.727  1.00 93.94           O  
ANISOU 2059  OE2 GLU A1273    13253  11652  10790   2536   -338   1080       O  
ATOM   2060  N   ILE A1274      20.139 -39.308  89.752  1.00 60.59           N  
ANISOU 2060  N   ILE A1274     7508   8658   6855   1757   -342   1183       N  
ATOM   2061  CA  ILE A1274      21.159 -38.603  90.526  1.00 59.57           C  
ANISOU 2061  CA  ILE A1274     7125   8804   6705   1694   -360   1299       C  
ATOM   2062  C   ILE A1274      20.589 -38.131  91.858  1.00 63.24           C  
ANISOU 2062  C   ILE A1274     7548   9286   7193   1442   -434   1255       C  
ATOM   2063  O   ILE A1274      21.229 -38.266  92.909  1.00 72.38           O  
ANISOU 2063  O   ILE A1274     8602  10592   8307   1419   -467   1362       O  
ATOM   2064  CB  ILE A1274      21.729 -37.426  89.712  1.00 63.92           C  
ANISOU 2064  CB  ILE A1274     7502   9512   7275   1656   -340   1312       C  
ATOM   2065  CG1 ILE A1274      22.567 -37.930  88.537  1.00 60.53           C  
ANISOU 2065  CG1 ILE A1274     7072   9130   6796   1944   -254   1404       C  
ATOM   2066  CG2 ILE A1274      22.552 -36.508  90.603  1.00 63.27           C  
ANISOU 2066  CG2 ILE A1274     7178   9688   7173   1495   -396   1416       C  
ATOM   2067  CD1 ILE A1274      23.066 -36.821  87.634  1.00 60.32           C  
ANISOU 2067  CD1 ILE A1274     6881   9251   6789   1911   -231   1423       C  
ATOM   2068  N   LEU A1275      19.375 -37.576  91.838  1.00 58.60           N  
ANISOU 2068  N   LEU A1275     7044   8555   6665   1260   -455   1108       N  
ATOM   2069  CA  LEU A1275      18.758 -37.072  93.060  1.00 58.62           C  
ANISOU 2069  CA  LEU A1275     7027   8569   6676   1044   -508   1064       C  
ATOM   2070  C   LEU A1275      18.331 -38.183  94.009  1.00 66.00           C  
ANISOU 2070  C   LEU A1275     8073   9417   7588   1065   -530   1093       C  
ATOM   2071  O   LEU A1275      18.212 -37.932  95.214  1.00 61.84           O  
ANISOU 2071  O   LEU A1275     7502   8958   7038    932   -570   1108       O  
ATOM   2072  CB  LEU A1275      17.553 -36.199  92.712  1.00 60.27           C  
ANISOU 2072  CB  LEU A1275     7294   8659   6947    883   -507    916       C  
ATOM   2073  CG  LEU A1275      17.870 -34.932  91.918  1.00 54.75           C  
ANISOU 2073  CG  LEU A1275     6493   8040   6270    822   -495    876       C  
ATOM   2074  CD1 LEU A1275      16.598 -34.325  91.362  1.00 53.45           C  
ANISOU 2074  CD1 LEU A1275     6415   7726   6166    721   -478    738       C  
ATOM   2075  CD2 LEU A1275      18.606 -33.935  92.800  1.00 59.87           C  
ANISOU 2075  CD2 LEU A1275     7001   8875   6871    678   -546    928       C  
ATOM   2076  N   SER A1276      18.110 -39.400  93.501  1.00 59.86           N  
ANISOU 2076  N   SER A1276     7457   8485   6804   1225   -511   1106       N  
ATOM   2077  CA  SER A1276      17.482 -40.438  94.315  1.00 58.07           C  
ANISOU 2077  CA  SER A1276     7366   8137   6561   1213   -543   1123       C  
ATOM   2078  C   SER A1276      18.317 -40.804  95.536  1.00 65.48           C  
ANISOU 2078  C   SER A1276     8213   9227   7440   1241   -566   1243       C  
ATOM   2079  O   SER A1276      17.769 -41.270  96.541  1.00 62.51           O  
ANISOU 2079  O   SER A1276     7895   8805   7053   1158   -602   1252       O  
ATOM   2080  CB  SER A1276      17.213 -41.680  93.465  1.00 58.74           C  
ANISOU 2080  CB  SER A1276     7676   8013   6629   1381   -532   1124       C  
ATOM   2081  OG  SER A1276      18.415 -42.200  92.926  1.00 67.23           O  
ANISOU 2081  OG  SER A1276     8747   9153   7645   1631   -486   1218       O  
ATOM   2082  N   SER A1277      19.637 -40.618  95.475  1.00 63.69           N  
ANISOU 2082  N   SER A1277     7834   9195   7170   1354   -548   1352       N  
ATOM   2083  CA  SER A1277      20.479 -40.942  96.621  1.00 63.17           C  
ANISOU 2083  CA  SER A1277     7663   9295   7044   1374   -578   1486       C  
ATOM   2084  C   SER A1277      20.485 -39.856  97.694  1.00 67.36           C  
ANISOU 2084  C   SER A1277     8055   9973   7568   1133   -636   1476       C  
ATOM   2085  O   SER A1277      20.928 -40.122  98.816  1.00 61.51           O  
ANISOU 2085  O   SER A1277     7256   9339   6774   1102   -677   1569       O  
ATOM   2086  CB  SER A1277      21.911 -41.216  96.155  1.00 62.64           C  
ANISOU 2086  CB  SER A1277     7472   9406   6924   1597   -539   1643       C  
ATOM   2087  OG  SER A1277      22.373 -40.193  95.290  1.00 75.53           O  
ANISOU 2087  OG  SER A1277     8965  11155   8577   1575   -517   1637       O  
ATOM   2088  N   LYS A1278      20.016 -38.651  97.380  1.00 62.24           N  
ANISOU 2088  N   LYS A1278     7371   9321   6957    970   -642   1368       N  
ATOM   2089  CA  LYS A1278      20.013 -37.555  98.341  1.00 59.30           C  
ANISOU 2089  CA  LYS A1278     6918   9060   6555    749   -699   1349       C  
ATOM   2090  C   LYS A1278      18.808 -37.631  99.276  1.00 58.64           C  
ANISOU 2090  C   LYS A1278     6958   8853   6472    623   -711   1262       C  
ATOM   2091  O   LYS A1278      17.749 -38.161  98.925  1.00 64.39           O  
ANISOU 2091  O   LYS A1278     7814   9403   7248    651   -677   1187       O  
ATOM   2092  CB  LYS A1278      20.030 -36.213  97.609  1.00 58.88           C  
ANISOU 2092  CB  LYS A1278     6803   9042   6525    640   -700   1275       C  
ATOM   2093  CG  LYS A1278      21.229 -36.052  96.682  1.00 64.24           C  
ANISOU 2093  CG  LYS A1278     7337   9872   7199    752   -687   1380       C  
ATOM   2094  CD  LYS A1278      21.225 -34.711  95.976  1.00 60.54           C  
ANISOU 2094  CD  LYS A1278     6815   9434   6754    626   -697   1312       C  
ATOM   2095  CE  LYS A1278      22.566 -34.445  95.310  1.00 75.33           C  
ANISOU 2095  CE  LYS A1278     8502  11518   8604    700   -703   1459       C  
ATOM   2096  NZ  LYS A1278      22.966 -35.547  94.392  1.00 93.26           N  
ANISOU 2096  NZ  LYS A1278    10770  13775  10887    982   -620   1532       N  
ATOM   2097  N   LYS A1279      18.983 -37.098 100.490  1.00 70.15           N  
ANISOU 2097  N   LYS A1279     8376  10414   7864    478   -765   1286       N  
ATOM   2098  CA  LYS A1279      17.866 -37.024 101.430  1.00 64.09           C  
ANISOU 2098  CA  LYS A1279     7716   9555   7079    365   -765   1213       C  
ATOM   2099  C   LYS A1279      16.768 -36.094 100.929  1.00 66.06           C  
ANISOU 2099  C   LYS A1279     8035   9696   7370    276   -724   1071       C  
ATOM   2100  O   LYS A1279      15.582 -36.346 101.182  1.00 73.07           O  
ANISOU 2100  O   LYS A1279     9016  10469   8278    253   -690   1017       O  
ATOM   2101  CB  LYS A1279      18.356 -36.568 102.804  1.00 59.38           C  
ANISOU 2101  CB  LYS A1279     7085   9093   6384    236   -831   1267       C  
ATOM   2102  CG  LYS A1279      19.054 -35.219 102.805  1.00 67.48           C  
ANISOU 2102  CG  LYS A1279     8045  10238   7358     98   -886   1261       C  
ATOM   2103  CD  LYS A1279      19.146 -34.642 104.212  1.00 77.20           C  
ANISOU 2103  CD  LYS A1279     9321  11538   8473    -64   -955   1274       C  
ATOM   2104  CE  LYS A1279      19.919 -33.332 104.221  1.00 77.00           C  
ANISOU 2104  CE  LYS A1279     9260  11620   8377   -226  -1038   1284       C  
ATOM   2105  NZ  LYS A1279      19.904 -32.693 105.563  1.00 92.94           N  
ANISOU 2105  NZ  LYS A1279    11381  13668  10262   -395  -1112   1277       N  
ATOM   2106  N   GLU A1280      17.138 -35.048 100.184  1.00 61.46           N  
ANISOU 2106  N   GLU A1280     7401   9154   6798    233   -727   1027       N  
ATOM   2107  CA  GLU A1280      16.154 -34.111  99.654  1.00 63.34           C  
ANISOU 2107  CA  GLU A1280     7704   9293   7071    163   -685    899       C  
ATOM   2108  C   GLU A1280      15.170 -34.797  98.719  1.00 60.10           C  
ANISOU 2108  C   GLU A1280     7355   8730   6752    255   -626    850       C  
ATOM   2109  O   GLU A1280      14.049 -34.304  98.542  1.00 63.16           O  
ANISOU 2109  O   GLU A1280     7803   9028   7165    203   -585    766       O  
ATOM   2110  CB  GLU A1280      16.854 -32.965  98.919  1.00 66.64           C  
ANISOU 2110  CB  GLU A1280     8056   9780   7485    108   -707    876       C  
ATOM   2111  CG  GLU A1280      17.693 -32.058  99.808  1.00 73.41           C  
ANISOU 2111  CG  GLU A1280     8882  10771   8238    -38   -789    919       C  
ATOM   2112  CD  GLU A1280      19.080 -32.609 100.078  1.00 84.81           C  
ANISOU 2112  CD  GLU A1280    10190  12386   9646     -5   -853   1077       C  
ATOM   2113  OE1 GLU A1280      19.940 -31.839 100.554  1.00 96.22           O  
ANISOU 2113  OE1 GLU A1280    11584  13965  11012   -140   -940   1140       O  
ATOM   2114  OE2 GLU A1280      19.316 -33.806  99.812  1.00 83.88           O  
ANISOU 2114  OE2 GLU A1280    10026  12272   9570    154   -821   1150       O  
ATOM   2115  N   PHE A1281      15.561 -35.935  98.141  1.00 55.45           N  
ANISOU 2115  N   PHE A1281     6764   8107   6199    391   -623    912       N  
ATOM   2116  CA  PHE A1281      14.670 -36.679  97.261  1.00 66.45           C  
ANISOU 2116  CA  PHE A1281     8250   9337   7660    461   -591    875       C  
ATOM   2117  C   PHE A1281      13.397 -37.092  97.986  1.00 65.96           C  
ANISOU 2117  C   PHE A1281     8271   9189   7601    389   -586    865       C  
ATOM   2118  O   PHE A1281      12.355 -37.280  97.347  1.00 65.36           O  
ANISOU 2118  O   PHE A1281     8262   8993   7580    374   -567    825       O  
ATOM   2119  CB  PHE A1281      15.405 -37.904  96.710  1.00 63.86           C  
ANISOU 2119  CB  PHE A1281     7953   8978   7334    633   -597    954       C  
ATOM   2120  CG  PHE A1281      14.618 -38.695  95.703  1.00 67.61           C  
ANISOU 2120  CG  PHE A1281     8564   9264   7859    700   -584    920       C  
ATOM   2121  CD1 PHE A1281      14.483 -38.246  94.399  1.00 67.47           C  
ANISOU 2121  CD1 PHE A1281     8560   9188   7888    732   -556    853       C  
ATOM   2122  CD2 PHE A1281      14.041 -39.905  96.051  1.00 69.31           C  
ANISOU 2122  CD2 PHE A1281     8910   9358   8067    722   -610    962       C  
ATOM   2123  CE1 PHE A1281      13.769 -38.980  93.467  1.00 71.57           C  
ANISOU 2123  CE1 PHE A1281     9227   9527   8439    778   -560    826       C  
ATOM   2124  CE2 PHE A1281      13.327 -40.645  95.124  1.00 72.68           C  
ANISOU 2124  CE2 PHE A1281     9491   9599   8524    757   -622    941       C  
ATOM   2125  CZ  PHE A1281      13.191 -40.181  93.831  1.00 81.02           C  
ANISOU 2125  CZ  PHE A1281    10568  10596   9621    784   -598    871       C  
ATOM   2126  N   GLN A1282      13.451 -37.220  99.317  1.00 69.92           N  
ANISOU 2126  N   GLN A1282     8763   9761   8041    336   -606    913       N  
ATOM   2127  CA  GLN A1282      12.246 -37.561 100.067  1.00 77.97           C  
ANISOU 2127  CA  GLN A1282     9845  10727   9055    269   -594    922       C  
ATOM   2128  C   GLN A1282      11.166 -36.503  99.891  1.00 64.71           C  
ANISOU 2128  C   GLN A1282     8168   9028   7391    187   -543    843       C  
ATOM   2129  O   GLN A1282       9.973 -36.824  99.847  1.00 64.76           O  
ANISOU 2129  O   GLN A1282     8211   8968   7428    156   -521    855       O  
ATOM   2130  CB  GLN A1282      12.570 -37.723 101.552  1.00 85.48           C  
ANISOU 2130  CB  GLN A1282    10783  11775   9923    230   -618    984       C  
ATOM   2131  CG  GLN A1282      13.029 -39.104 101.974  1.00103.88           C  
ANISOU 2131  CG  GLN A1282    13141  14090  12240    304   -659   1086       C  
ATOM   2132  CD  GLN A1282      13.195 -39.212 103.481  1.00108.40           C  
ANISOU 2132  CD  GLN A1282    13701  14758  12729    251   -681   1145       C  
ATOM   2133  OE1 GLN A1282      13.359 -38.205 104.171  1.00 97.85           O  
ANISOU 2133  OE1 GLN A1282    12334  13516  11328    172   -678   1113       O  
ATOM   2134  NE2 GLN A1282      13.141 -40.434 104.000  1.00114.11           N  
ANISOU 2134  NE2 GLN A1282    14470  15444  13441    290   -709   1233       N  
ATOM   2135  N   GLU A1283      11.564 -35.237  99.776  1.00 54.30           N  
ANISOU 2135  N   GLU A1283     6814   7772   6046    151   -527    774       N  
ATOM   2136  CA  GLU A1283      10.605 -34.141  99.757  1.00 55.76           C  
ANISOU 2136  CA  GLU A1283     7021   7944   6222     94   -471    703       C  
ATOM   2137  C   GLU A1283      10.022 -33.866  98.376  1.00 67.70           C  
ANISOU 2137  C   GLU A1283     8529   9373   7822    114   -440    648       C  
ATOM   2138  O   GLU A1283       9.118 -33.031  98.261  1.00 66.77           O  
ANISOU 2138  O   GLU A1283     8425   9242   7704     85   -385    601       O  
ATOM   2139  CB  GLU A1283      11.265 -32.876 100.306  1.00 60.41           C  
ANISOU 2139  CB  GLU A1283     7619   8613   6723     36   -480    653       C  
ATOM   2140  CG  GLU A1283      11.639 -32.983 101.777  1.00 63.87           C  
ANISOU 2140  CG  GLU A1283     8086   9130   7054     -6   -511    703       C  
ATOM   2141  CD  GLU A1283      12.412 -31.779 102.277  1.00 75.68           C  
ANISOU 2141  CD  GLU A1283     9619  10689   8445    -88   -551    663       C  
ATOM   2142  OE1 GLU A1283      13.609 -31.656 101.939  1.00 79.06           O  
ANISOU 2142  OE1 GLU A1283     9984  11180   8874   -111   -619    689       O  
ATOM   2143  OE2 GLU A1283      11.821 -30.955 103.006  1.00 91.72           O  
ANISOU 2143  OE2 GLU A1283    11753  12711  10384   -128   -516    617       O  
ATOM   2144  N   MET A1284      10.515 -34.530  97.335  1.00 57.42           N  
ANISOU 2144  N   MET A1284     7217   8017   6584    176   -469    657       N  
ATOM   2145  CA  MET A1284      10.100 -34.271  95.966  1.00 52.06           C  
ANISOU 2145  CA  MET A1284     6543   7258   5980    195   -449    603       C  
ATOM   2146  C   MET A1284       9.075 -35.296  95.491  1.00 62.99           C  
ANISOU 2146  C   MET A1284     7984   8531   7419    196   -460    646       C  
ATOM   2147  O   MET A1284       9.011 -36.423  95.990  1.00 64.31           O  
ANISOU 2147  O   MET A1284     8196   8665   7573    205   -497    720       O  
ATOM   2148  CB  MET A1284      11.309 -34.282  95.030  1.00 51.99           C  
ANISOU 2148  CB  MET A1284     6504   7260   5990    269   -472    590       C  
ATOM   2149  CG  MET A1284      12.451 -33.392  95.483  1.00 52.24           C  
ANISOU 2149  CG  MET A1284     6466   7420   5963    244   -488    585       C  
ATOM   2150  SD  MET A1284      13.950 -33.684  94.526  1.00 57.81           S  
ANISOU 2150  SD  MET A1284     7100   8185   6681    353   -512    631       S  
ATOM   2151  CE  MET A1284      15.073 -32.510  95.278  1.00 53.12           C  
ANISOU 2151  CE  MET A1284     6413   7763   6007    254   -555    655       C  
ATOM   2152  N   ARG A1285       8.272 -34.882  94.514  1.00 56.91           N  
ANISOU 2152  N   ARG A1285     7218   7700   6704    173   -437    606       N  
ATOM   2153  CA  ARG A1285       7.334 -35.738  93.804  1.00 58.68           C  
ANISOU 2153  CA  ARG A1285     7503   7814   6981    148   -468    649       C  
ATOM   2154  C   ARG A1285       7.492 -35.457  92.320  1.00 63.47           C  
ANISOU 2154  C   ARG A1285     8132   8346   7639    184   -470    585       C  
ATOM   2155  O   ARG A1285       7.715 -34.311  91.926  1.00 56.34           O  
ANISOU 2155  O   ARG A1285     7169   7491   6746    191   -426    512       O  
ATOM   2156  CB  ARG A1285       5.882 -35.475  94.226  1.00 51.84           C  
ANISOU 2156  CB  ARG A1285     6600   6975   6121     60   -437    698       C  
ATOM   2157  CG  ARG A1285       5.636 -35.487  95.720  1.00 54.57           C  
ANISOU 2157  CG  ARG A1285     6914   7416   6403     35   -410    757       C  
ATOM   2158  CD  ARG A1285       5.728 -36.889  96.288  1.00 54.51           C  
ANISOU 2158  CD  ARG A1285     6964   7368   6380     20   -478    850       C  
ATOM   2159  NE  ARG A1285       5.457 -36.892  97.721  1.00 53.74           N  
ANISOU 2159  NE  ARG A1285     6831   7369   6217     -4   -449    912       N  
ATOM   2160  CZ  ARG A1285       6.381 -36.677  98.652  1.00 56.39           C  
ANISOU 2160  CZ  ARG A1285     7162   7775   6489     33   -440    888       C  
ATOM   2161  NH1 ARG A1285       7.639 -36.447  98.300  1.00 53.58           N  
ANISOU 2161  NH1 ARG A1285     6812   7417   6129     91   -460    821       N  
ATOM   2162  NH2 ARG A1285       6.045 -36.692  99.933  1.00 54.51           N  
ANISOU 2162  NH2 ARG A1285     6908   7621   6184     10   -414    946       N  
ATOM   2163  N   PHE A1286       7.378 -36.495  91.496  1.00 52.58           N  
ANISOU 2163  N   PHE A1286     6857   6838   6282    206   -527    612       N  
ATOM   2164  CA  PHE A1286       7.593 -36.360  90.062  1.00 57.84           C  
ANISOU 2164  CA  PHE A1286     7572   7422   6982    255   -533    555       C  
ATOM   2165  C   PHE A1286       6.436 -36.994  89.307  1.00 57.51           C  
ANISOU 2165  C   PHE A1286     7629   7250   6972    173   -590    593       C  
ATOM   2166  O   PHE A1286       5.995 -38.096  89.649  1.00 64.52           O  
ANISOU 2166  O   PHE A1286     8615   8060   7841    126   -657    674       O  
ATOM   2167  CB  PHE A1286       8.918 -37.004  89.640  1.00 51.51           C  
ANISOU 2167  CB  PHE A1286     6840   6584   6147    399   -547    548       C  
ATOM   2168  CG  PHE A1286      10.132 -36.305  90.183  1.00 57.60           C  
ANISOU 2168  CG  PHE A1286     7492   7505   6888    464   -504    532       C  
ATOM   2169  CD1 PHE A1286      10.745 -35.293  89.461  1.00 51.47           C  
ANISOU 2169  CD1 PHE A1286     6637   6793   6127    498   -466    472       C  
ATOM   2170  CD2 PHE A1286      10.659 -36.658  91.416  1.00 56.51           C  
ANISOU 2170  CD2 PHE A1286     7321   7448   6702    474   -513    588       C  
ATOM   2171  CE1 PHE A1286      11.863 -34.646  89.954  1.00 50.88           C  
ANISOU 2171  CE1 PHE A1286     6451   6864   6018    525   -448    480       C  
ATOM   2172  CE2 PHE A1286      11.777 -36.015  91.917  1.00 56.86           C  
ANISOU 2172  CE2 PHE A1286     7255   7637   6711    507   -493    591       C  
ATOM   2173  CZ  PHE A1286      12.380 -35.008  91.185  1.00 53.72           C  
ANISOU 2173  CZ  PHE A1286     6779   7307   6327    524   -466    542       C  
ATOM   2174  N   ILE A1287       5.951 -36.299  88.280  1.00 53.19           N  
ANISOU 2174  N   ILE A1287     7060   6680   6469    144   -575    546       N  
ATOM   2175  CA  ILE A1287       4.878 -36.792  87.422  1.00 56.55           C  
ANISOU 2175  CA  ILE A1287     7574   6991   6922     50   -642    589       C  
ATOM   2176  C   ILE A1287       5.360 -36.680  85.982  1.00 51.49           C  
ANISOU 2176  C   ILE A1287     7019   6254   6291    124   -650    512       C  
ATOM   2177  O   ILE A1287       5.517 -35.569  85.461  1.00 55.53           O  
ANISOU 2177  O   ILE A1287     7433   6832   6836    150   -588    441       O  
ATOM   2178  CB  ILE A1287       3.568 -36.020  87.625  1.00 58.09           C  
ANISOU 2178  CB  ILE A1287     7639   7274   7156    -70   -613    635       C  
ATOM   2179  CG1 ILE A1287       3.105 -36.137  89.082  1.00 51.30           C  
ANISOU 2179  CG1 ILE A1287     6699   6523   6272   -120   -591    721       C  
ATOM   2180  CG2 ILE A1287       2.494 -36.538  86.678  1.00 51.39           C  
ANISOU 2180  CG2 ILE A1287     6867   6323   6334   -188   -699    703       C  
ATOM   2181  CD1 ILE A1287       2.053 -35.127  89.466  1.00 51.11           C  
ANISOU 2181  CD1 ILE A1287     6525   6631   6264   -173   -516    761       C  
ATOM   2182  N   ILE A1288       5.587 -37.823  85.341  1.00 52.79           N  
ANISOU 2182  N   ILE A1288     7384   6255   6417    162   -726    529       N  
ATOM   2183  CA  ILE A1288       6.183 -37.894  84.013  1.00 51.69           C  
ANISOU 2183  CA  ILE A1288     7367   6013   6261    269   -730    461       C  
ATOM   2184  C   ILE A1288       5.121 -38.409  83.050  1.00 56.84           C  
ANISOU 2184  C   ILE A1288     8175   6507   6915    148   -829    493       C  
ATOM   2185  O   ILE A1288       4.610 -39.523  83.218  1.00 59.15           O  
ANISOU 2185  O   ILE A1288     8635   6673   7168     66   -932    570       O  
ATOM   2186  CB  ILE A1288       7.427 -38.797  84.012  1.00 56.16           C  
ANISOU 2186  CB  ILE A1288     8074   6511   6752    453   -728    458       C  
ATOM   2187  CG1 ILE A1288       8.293 -38.500  85.240  1.00 52.28           C  
ANISOU 2187  CG1 ILE A1288     7425   6186   6254    522   -662    472       C  
ATOM   2188  CG2 ILE A1288       8.224 -38.610  82.731  1.00 54.18           C  
ANISOU 2188  CG2 ILE A1288     7899   6211   6476    608   -691    390       C  
ATOM   2189  CD1 ILE A1288       9.510 -39.382  85.367  1.00 53.92           C  
ANISOU 2189  CD1 ILE A1288     7737   6363   6386    711   -653    498       C  
ATOM   2190  N   ILE A1289       4.739 -37.551  82.115  1.00 51.86           N  
ANISOU 2190  N   ILE A1289     7502   5881   6323    125   -810    441       N  
ATOM   2191  CA  ILE A1289       3.645 -37.846  81.157  1.00 57.61           C  
ANISOU 2191  CA  ILE A1289     8334   6495   7060    -22   -907    482       C  
ATOM   2192  C   ILE A1289       4.193 -37.909  79.736  1.00 57.39           C  
ANISOU 2192  C   ILE A1289     8468   6341   6998     82   -914    401       C  
ATOM   2193  O   ILE A1289       4.852 -36.977  79.324  1.00 57.12           O  
ANISOU 2193  O   ILE A1289     8318   6395   6991    191   -819    319       O  
ATOM   2194  CB  ILE A1289       2.594 -36.744  81.281  1.00 53.85           C  
ANISOU 2194  CB  ILE A1289     7634   6163   6663   -158   -873    517       C  
ATOM   2195  CG1 ILE A1289       2.069 -36.651  82.707  1.00 51.42           C  
ANISOU 2195  CG1 ILE A1289     7176   5991   6372   -233   -849    604       C  
ATOM   2196  CG2 ILE A1289       1.482 -36.949  80.285  1.00 51.95           C  
ANISOU 2196  CG2 ILE A1289     7480   5828   6432   -317   -979    579       C  
ATOM   2197  CD1 ILE A1289       1.253 -35.441  82.958  1.00 50.64           C  
ANISOU 2197  CD1 ILE A1289     6842   6067   6330   -277   -760    619       C  
ATOM   2198  N   GLY A1290       3.879 -38.977  79.016  1.00 56.93           N  
ANISOU 2198  N   GLY A1290     8688   6073   6869     44  -1032    430       N  
ATOM   2199  CA  GLY A1290       4.342 -39.107  77.629  1.00 53.81           C  
ANISOU 2199  CA  GLY A1290     8485   5539   6421    143  -1046    359       C  
ATOM   2200  C   GLY A1290       4.482 -40.544  77.189  1.00 55.60           C  
ANISOU 2200  C   GLY A1290     9090   5512   6524    183  -1158    381       C  
ATOM   2201  O   GLY A1290       4.141 -41.423  77.949  1.00 56.93           O  
ANISOU 2201  O   GLY A1290     9368   5608   6656    107  -1239    458       O  
ATOM   2202  N   LYS A1291       4.934 -40.734  75.959  1.00 56.14           N  
ANISOU 2202  N   LYS A1291     9372   5440   6518    309  -1161    315       N  
ATOM   2203  CA  LYS A1291       5.168 -42.073  75.372  1.00 67.63           C  
ANISOU 2203  CA  LYS A1291    11244   6628   7826    399  -1252    317       C  
ATOM   2204  C   LYS A1291       6.164 -41.945  74.227  1.00 65.24           C  
ANISOU 2204  C   LYS A1291    11083   6260   7447    641  -1172    226       C  
ATOM   2205  O   LYS A1291       6.432 -40.836  73.800  1.00 65.13           O  
ANISOU 2205  O   LYS A1291    10860   6383   7502    669  -1086    171       O  
ATOM   2206  CB  LYS A1291       3.873 -42.787  74.996  1.00 72.18           C  
ANISOU 2206  CB  LYS A1291    12064   7004   8358    128  -1454    394       C  
ATOM   2207  CG  LYS A1291       2.948 -42.058  74.043  1.00 80.41           C  
ANISOU 2207  CG  LYS A1291    13006   8082   9466    -66  -1508    399       C  
ATOM   2208  CD  LYS A1291       1.662 -42.820  73.853  1.00 96.93           C  
ANISOU 2208  CD  LYS A1291    15273  10031  11527   -380  -1722    521       C  
ATOM   2209  CE  LYS A1291       0.552 -42.008  73.222  1.00107.89           C  
ANISOU 2209  CE  LYS A1291    16521  11490  12985   -582  -1776    553       C  
ATOM   2210  NZ  LYS A1291      -0.767 -42.667  73.377  1.00113.91           N  
ANISOU 2210  NZ  LYS A1291    17401  12157  13721   -917  -1994    710       N  
ATOM   2211  N   GLY A1292       6.727 -43.057  73.788  1.00 73.80           N  
ANISOU 2211  N   GLY A1292    12532   7132   8376    829  -1196    216       N  
ATOM   2212  CA  GLY A1292       7.743 -42.969  72.734  1.00 66.49           C  
ANISOU 2212  CA  GLY A1292    11774   6140   7350   1101  -1109    145       C  
ATOM   2213  C   GLY A1292       8.653 -44.165  72.777  1.00 75.14           C  
ANISOU 2213  C   GLY A1292    13204   7069   8275   1390  -1079    154       C  
ATOM   2214  O   GLY A1292       8.153 -45.278  72.812  1.00 82.96           O  
ANISOU 2214  O   GLY A1292    14611   7775   9134   1350  -1214    173       O  
ATOM   2215  N   ASP A1293       9.952 -43.906  72.796  1.00 80.29           N  
ANISOU 2215  N   ASP A1293    13685   7900   8920   1677   -909    154       N  
ATOM   2216  CA  ASP A1293      10.974 -44.974  72.815  1.00 76.39           C  
ANISOU 2216  CA  ASP A1293    13479   7287   8257   2011   -847    177       C  
ATOM   2217  C   ASP A1293      10.656 -45.926  73.965  1.00 78.38           C  
ANISOU 2217  C   ASP A1293    13907   7408   8468   1942   -944    240       C  
ATOM   2218  O   ASP A1293      10.473 -45.471  75.089  1.00 85.89           O  
ANISOU 2218  O   ASP A1293    14552   8543   9540   1812   -935    284       O  
ATOM   2219  CB  ASP A1293      12.343 -44.322  72.952  1.00 79.82           C  
ANISOU 2219  CB  ASP A1293    13598   8011   8718   2294   -647    201       C  
ATOM   2220  CG  ASP A1293      13.489 -45.292  73.065  1.00 85.52           C  
ANISOU 2220  CG  ASP A1293    14581   8655   9257   2693   -550    246       C  
ATOM   2221  OD1 ASP A1293      13.273 -46.376  73.588  1.00 95.10           O  
ANISOU 2221  OD1 ASP A1293    16042   9709  10384   2745   -607    289       O  
ATOM   2222  OD2 ASP A1293      14.581 -44.936  72.631  1.00 93.46           O  
ANISOU 2222  OD2 ASP A1293    15537   9770  10202   2969   -410    251       O  
ATOM   2223  N   PRO A1294      10.615 -47.244  73.693  1.00 80.27           N  
ANISOU 2223  N   PRO A1294    14647   7326   8528   2025  -1040    246       N  
ATOM   2224  CA  PRO A1294      10.279 -48.265  74.670  1.00 72.60           C  
ANISOU 2224  CA  PRO A1294    13864   6210   7511   1938  -1148    312       C  
ATOM   2225  C   PRO A1294      11.353 -48.360  75.751  1.00 74.67           C  
ANISOU 2225  C   PRO A1294    13909   6669   7794   2151  -1017    372       C  
ATOM   2226  O   PRO A1294      11.019 -48.634  76.854  1.00 77.63           O  
ANISOU 2226  O   PRO A1294    14192   7075   8230   1985  -1085    430       O  
ATOM   2227  CB  PRO A1294      10.186 -49.550  73.850  1.00 73.09           C  
ANISOU 2227  CB  PRO A1294    14556   5877   7339   2067  -1248    297       C  
ATOM   2228  CG  PRO A1294      10.063 -49.067  72.445  1.00 71.58           C  
ANISOU 2228  CG  PRO A1294    14483   5606   7106   2067  -1255    221       C  
ATOM   2229  CD  PRO A1294      10.943 -47.845  72.416  1.00 79.06           C  
ANISOU 2229  CD  PRO A1294    14939   6907   8191   2194  -1062    194       C  
ATOM   2230  N   GLU A1295      12.615 -48.192  75.382  1.00 70.68           N  
ANISOU 2230  N   GLU A1295    13310   6310   7235   2514   -835    375       N  
ATOM   2231  CA  GLU A1295      13.609 -48.261  76.447  1.00 81.10           C  
ANISOU 2231  CA  GLU A1295    14395   7845   8574   2706   -717    453       C  
ATOM   2232  C   GLU A1295      13.401 -47.147  77.464  1.00 80.47           C  
ANISOU 2232  C   GLU A1295    13788   8083   8704   2467   -694    469       C  
ATOM   2233  O   GLU A1295      13.536 -47.367  78.674  1.00 73.39           O  
ANISOU 2233  O   GLU A1295    12747   7285   7851   2423   -699    531       O  
ATOM   2234  CB  GLU A1295      15.018 -48.194  75.860  1.00 95.41           C  
ANISOU 2234  CB  GLU A1295    16190   9781  10280   3139   -527    484       C  
ATOM   2235  CG  GLU A1295      15.335 -49.307  74.878  1.00118.98           C  
ANISOU 2235  CG  GLU A1295    19725  12455  13028   3441   -521    474       C  
ATOM   2236  CD  GLU A1295      16.741 -49.206  74.320  1.00136.04           C  
ANISOU 2236  CD  GLU A1295    21833  14779  15079   3898   -311    530       C  
ATOM   2237  OE1 GLU A1295      17.503 -48.329  74.783  1.00138.35           O  
ANISOU 2237  OE1 GLU A1295    21650  15434  15484   3957   -186    593       O  
ATOM   2238  OE2 GLU A1295      17.085 -50.002  73.421  1.00142.09           O  
ANISOU 2238  OE2 GLU A1295    23041  15313  15635   4197   -274    522       O  
ATOM   2239  N   LEU A1296      13.044 -45.948  76.994  1.00 65.70           N  
ANISOU 2239  N   LEU A1296    11648   6359   6954   2312   -673    412       N  
ATOM   2240  CA  LEU A1296      12.762 -44.854  77.916  1.00 65.56           C  
ANISOU 2240  CA  LEU A1296    11181   6611   7116   2084   -658    418       C  
ATOM   2241  C   LEU A1296      11.479 -45.104  78.699  1.00 67.95           C  
ANISOU 2241  C   LEU A1296    11501   6824   7491   1749   -805    430       C  
ATOM   2242  O   LEU A1296      11.394 -44.761  79.885  1.00 67.65           O  
ANISOU 2242  O   LEU A1296    11198   6960   7547   1629   -796    469       O  
ATOM   2243  CB  LEU A1296      12.692 -43.535  77.150  1.00 60.90           C  
ANISOU 2243  CB  LEU A1296    10344   6176   6620   2018   -600    356       C  
ATOM   2244  CG  LEU A1296      13.985 -43.182  76.412  1.00 61.38           C  
ANISOU 2244  CG  LEU A1296    10333   6372   6617   2334   -450    367       C  
ATOM   2245  CD1 LEU A1296      13.856 -41.852  75.692  1.00 63.65           C  
ANISOU 2245  CD1 LEU A1296    10376   6806   7001   2238   -406    309       C  
ATOM   2246  CD2 LEU A1296      15.166 -43.162  77.373  1.00 61.66           C  
ANISOU 2246  CD2 LEU A1296    10136   6643   6649   2513   -347    461       C  
ATOM   2247  N   GLU A1297      10.477 -45.722  78.065  1.00 63.28           N  
ANISOU 2247  N   GLU A1297    11227   5968   6848   1593   -945    411       N  
ATOM   2248  CA  GLU A1297       9.258 -46.062  78.794  1.00 67.05           C  
ANISOU 2248  CA  GLU A1297    11724   6371   7380   1275  -1093    457       C  
ATOM   2249  C   GLU A1297       9.539 -47.097  79.873  1.00 68.88           C  
ANISOU 2249  C   GLU A1297    12077   6543   7552   1328  -1125    533       C  
ATOM   2250  O   GLU A1297       9.012 -47.004  80.990  1.00 72.42           O  
ANISOU 2250  O   GLU A1297    12331   7099   8086   1135  -1165    588       O  
ATOM   2251  CB  GLU A1297       8.191 -46.581  77.831  1.00 76.94           C  
ANISOU 2251  CB  GLU A1297    13311   7353   8572   1087  -1256    447       C  
ATOM   2252  CG  GLU A1297       7.743 -45.582  76.782  1.00 82.00           C  
ANISOU 2252  CG  GLU A1297    13834   8047   9276    995  -1245    383       C  
ATOM   2253  CD  GLU A1297       6.561 -46.085  75.975  1.00 91.68           C  
ANISOU 2253  CD  GLU A1297    15359   9026  10448    752  -1433    398       C  
ATOM   2254  OE1 GLU A1297       5.837 -46.975  76.469  1.00 99.93           O  
ANISOU 2254  OE1 GLU A1297    16594   9921  11454    560  -1586    478       O  
ATOM   2255  OE2 GLU A1297       6.357 -45.594  74.844  1.00 92.84           O  
ANISOU 2255  OE2 GLU A1297    15553   9134  10589    740  -1437    341       O  
ATOM   2256  N   GLY A1298      10.398 -48.071  79.570  1.00 67.16           N  
ANISOU 2256  N   GLY A1298    12177   6160   7179   1611  -1097    542       N  
ATOM   2257  CA  GLY A1298      10.753 -49.060  80.571  1.00 70.94           C  
ANISOU 2257  CA  GLY A1298    12780   6580   7593   1693  -1118    617       C  
ATOM   2258  C   GLY A1298      11.584 -48.468  81.691  1.00 79.04           C  
ANISOU 2258  C   GLY A1298    13404   7921   8708   1792   -986    656       C  
ATOM   2259  O   GLY A1298      11.425 -48.839  82.856  1.00 78.97           O  
ANISOU 2259  O   GLY A1298    13322   7955   8726   1697  -1025    721       O  
ATOM   2260  N   TRP A1299      12.472 -47.529  81.356  1.00 76.91           N  
ANISOU 2260  N   TRP A1299    12868   7876   8477   1967   -839    627       N  
ATOM   2261  CA  TRP A1299      13.249 -46.840  82.380  1.00 75.04           C  
ANISOU 2261  CA  TRP A1299    12239   7951   8323   2021   -732    671       C  
ATOM   2262  C   TRP A1299      12.348 -46.014  83.292  1.00 78.76           C  
ANISOU 2262  C   TRP A1299    12408   8574   8945   1694   -781    664       C  
ATOM   2263  O   TRP A1299      12.546 -45.979  84.515  1.00 81.54           O  
ANISOU 2263  O   TRP A1299    12575   9071   9336   1650   -768    719       O  
ATOM   2264  CB  TRP A1299      14.297 -45.957  81.702  1.00 69.90           C  
ANISOU 2264  CB  TRP A1299    11379   7502   7677   2235   -588    654       C  
ATOM   2265  CG  TRP A1299      15.322 -45.366  82.610  1.00 66.49           C  
ANISOU 2265  CG  TRP A1299    10591   7380   7292   2327   -487    723       C  
ATOM   2266  CD1 TRP A1299      15.492 -45.615  83.941  1.00 68.05           C  
ANISOU 2266  CD1 TRP A1299    10662   7681   7512   2276   -502    793       C  
ATOM   2267  CD2 TRP A1299      16.333 -44.420  82.245  1.00 71.65           C  
ANISOU 2267  CD2 TRP A1299    10971   8286   7967   2470   -367    744       C  
ATOM   2268  NE1 TRP A1299      16.546 -44.879  84.428  1.00 66.93           N  
ANISOU 2268  NE1 TRP A1299    10193   7836   7401   2371   -406    854       N  
ATOM   2269  CE2 TRP A1299      17.078 -44.138  83.406  1.00 70.85           C  
ANISOU 2269  CE2 TRP A1299    10589   8432   7898   2484   -326    832       C  
ATOM   2270  CE3 TRP A1299      16.680 -43.785  81.047  1.00 67.88           C  
ANISOU 2270  CE3 TRP A1299    10459   7854   7480   2578   -297    706       C  
ATOM   2271  CZ2 TRP A1299      18.149 -43.246  83.406  1.00 70.29           C  
ANISOU 2271  CZ2 TRP A1299    10207   8653   7848   2581   -231    893       C  
ATOM   2272  CZ3 TRP A1299      17.742 -42.900  81.049  1.00 73.00           C  
ANISOU 2272  CZ3 TRP A1299    10788   8795   8153   2685   -193    767       C  
ATOM   2273  CH2 TRP A1299      18.465 -42.640  82.221  1.00 74.07           C  
ANISOU 2273  CH2 TRP A1299    10650   9175   8319   2677   -168    864       C  
ATOM   2274  N   ALA A1300      11.326 -45.374  82.718  1.00 71.33           N  
ANISOU 2274  N   ALA A1300    11428   7598   8078   1471   -837    605       N  
ATOM   2275  CA  ALA A1300      10.404 -44.591  83.532  1.00 68.76           C  
ANISOU 2275  CA  ALA A1300    10833   7412   7879   1189   -870    610       C  
ATOM   2276  C   ALA A1300       9.555 -45.489  84.423  1.00 66.99           C  
ANISOU 2276  C   ALA A1300    10733   7076   7643   1011   -987    683       C  
ATOM   2277  O   ALA A1300       9.329 -45.169  85.595  1.00 72.33           O  
ANISOU 2277  O   ALA A1300    11188   7910   8384    895   -977    725       O  
ATOM   2278  CB  ALA A1300       9.521 -43.720  82.639  1.00 59.15           C  
ANISOU 2278  CB  ALA A1300     9550   6189   6734   1021   -894    547       C  
ATOM   2279  N   ARG A1301       9.087 -46.624  83.894  1.00 70.78           N  
ANISOU 2279  N   ARG A1301    11582   7281   8031    984  -1105    707       N  
ATOM   2280  CA  ARG A1301       8.348 -47.566  84.732  1.00 71.43           C  
ANISOU 2280  CA  ARG A1301    11801   7249   8089    812  -1229    795       C  
ATOM   2281  C   ARG A1301       9.233 -48.171  85.816  1.00 69.56           C  
ANISOU 2281  C   ARG A1301    11555   7068   7806    975  -1180    850       C  
ATOM   2282  O   ARG A1301       8.756 -48.438  86.927  1.00 63.46           O  
ANISOU 2282  O   ARG A1301    10699   6346   7064    823  -1230    924       O  
ATOM   2283  CB  ARG A1301       7.735 -48.671  83.874  1.00 69.75           C  
ANISOU 2283  CB  ARG A1301    12030   6707   7767    740  -1384    814       C  
ATOM   2284  CG  ARG A1301       6.637 -48.196  82.939  1.00 81.31           C  
ANISOU 2284  CG  ARG A1301    13508   8110   9274    510  -1471    793       C  
ATOM   2285  CD  ARG A1301       5.457 -47.622  83.707  1.00 78.37           C  
ANISOU 2285  CD  ARG A1301    12846   7907   9026    201  -1521    867       C  
ATOM   2286  NE  ARG A1301       4.438 -47.090  82.806  1.00 81.73           N  
ANISOU 2286  NE  ARG A1301    13246   8310   9496     -3  -1592    865       N  
ATOM   2287  CZ  ARG A1301       3.319 -46.495  83.208  1.00 78.45           C  
ANISOU 2287  CZ  ARG A1301    12580   8047   9180   -256  -1628    940       C  
ATOM   2288  NH1 ARG A1301       3.068 -46.351  84.502  1.00 69.91           N  
ANISOU 2288  NH1 ARG A1301    11263   7142   8157   -333  -1595   1016       N  
ATOM   2289  NH2 ARG A1301       2.452 -46.043  82.312  1.00 77.51           N  
ANISOU 2289  NH2 ARG A1301    12445   7910   9094   -421  -1692    949       N  
ATOM   2290  N   SER A1302      10.521 -48.369  85.524  1.00 67.97           N  
ANISOU 2290  N   SER A1302    11419   6879   7530   1289  -1078    830       N  
ATOM   2291  CA  SER A1302      11.439 -48.888  86.529  1.00 66.71           C  
ANISOU 2291  CA  SER A1302    11221   6802   7326   1463  -1023    896       C  
ATOM   2292  C   SER A1302      11.648 -47.882  87.649  1.00 66.95           C  
ANISOU 2292  C   SER A1302    10825   7144   7468   1380   -948    912       C  
ATOM   2293  O   SER A1302      11.636 -48.245  88.830  1.00 75.28           O  
ANISOU 2293  O   SER A1302    11815   8261   8528   1325   -969    980       O  
ATOM   2294  CB  SER A1302      12.773 -49.251  85.876  1.00 70.28           C  
ANISOU 2294  CB  SER A1302    11811   7228   7666   1836   -918    893       C  
ATOM   2295  OG  SER A1302      13.817 -49.307  86.832  1.00 82.69           O  
ANISOU 2295  OG  SER A1302    13200   8993   9226   2011   -829    965       O  
ATOM   2296  N   LEU A1303      11.825 -46.606  87.300  1.00 76.18           N  
ANISOU 2296  N   LEU A1303    11721   8504   8719   1363   -866    850       N  
ATOM   2297  CA  LEU A1303      11.928 -45.581  88.332  1.00 68.18           C  
ANISOU 2297  CA  LEU A1303    10347   7760   7797   1258   -810    857       C  
ATOM   2298  C   LEU A1303      10.617 -45.417  89.090  1.00 65.02           C  
ANISOU 2298  C   LEU A1303     9873   7365   7465    969   -887    876       C  
ATOM   2299  O   LEU A1303      10.632 -45.095  90.284  1.00 63.21           O  
ANISOU 2299  O   LEU A1303     9451   7298   7269    895   -866    913       O  
ATOM   2300  CB  LEU A1303      12.362 -44.252  87.715  1.00 75.41           C  
ANISOU 2300  CB  LEU A1303    11030   8849   8771   1291   -720    789       C  
ATOM   2301  CG  LEU A1303      13.780 -44.230  87.140  1.00 80.31           C  
ANISOU 2301  CG  LEU A1303    11634   9551   9331   1576   -626    803       C  
ATOM   2302  CD1 LEU A1303      14.166 -42.825  86.699  1.00 90.47           C  
ANISOU 2302  CD1 LEU A1303    12656  11035  10683   1559   -552    753       C  
ATOM   2303  CD2 LEU A1303      14.779 -44.774  88.149  1.00 72.34           C  
ANISOU 2303  CD2 LEU A1303    10566   8654   8266   1726   -593    901       C  
ATOM   2304  N   GLU A1304       9.482 -45.651  88.426  1.00 65.70           N  
ANISOU 2304  N   GLU A1304    10112   7286   7564    805   -976    865       N  
ATOM   2305  CA  GLU A1304       8.191 -45.512  89.092  1.00 64.24           C  
ANISOU 2305  CA  GLU A1304     9839   7131   7439    537  -1045    915       C  
ATOM   2306  C   GLU A1304       7.981 -46.611  90.125  1.00 71.60           C  
ANISOU 2306  C   GLU A1304    10887   7995   8324    482  -1120   1017       C  
ATOM   2307  O   GLU A1304       7.553 -46.342  91.253  1.00 67.90           O  
ANISOU 2307  O   GLU A1304    10234   7670   7895    358  -1112   1070       O  
ATOM   2308  CB  GLU A1304       7.065 -45.526  88.057  1.00 62.97           C  
ANISOU 2308  CB  GLU A1304     9804   6826   7297    371  -1133    906       C  
ATOM   2309  CG  GLU A1304       5.669 -45.476  88.658  1.00 64.16           C  
ANISOU 2309  CG  GLU A1304     9860   7019   7499     96  -1210    996       C  
ATOM   2310  CD  GLU A1304       4.575 -45.602  87.611  1.00 81.56           C  
ANISOU 2310  CD  GLU A1304    12195   9084   9711    -81  -1318   1019       C  
ATOM   2311  OE1 GLU A1304       4.838 -46.182  86.536  1.00 79.19           O  
ANISOU 2311  OE1 GLU A1304    12170   8575   9345    -10  -1378    978       O  
ATOM   2312  OE2 GLU A1304       3.453 -45.116  87.861  1.00 83.59           O  
ANISOU 2312  OE2 GLU A1304    12283   9447  10031   -286  -1344   1087       O  
ATOM   2313  N   GLU A1305       8.254 -47.864  89.753  1.00 79.39           N  
ANISOU 2313  N   GLU A1305    12199   8752   9213    575  -1195   1047       N  
ATOM   2314  CA  GLU A1305       8.161 -48.939  90.736  1.00 80.51           C  
ANISOU 2314  CA  GLU A1305    12470   8820   9302    537  -1268   1147       C  
ATOM   2315  C   GLU A1305       9.233 -48.816  91.814  1.00 81.06           C  
ANISOU 2315  C   GLU A1305    12362   9072   9364    702  -1169   1164       C  
ATOM   2316  O   GLU A1305       8.988 -49.175  92.972  1.00 76.50           O  
ANISOU 2316  O   GLU A1305    11728   8552   8787    612  -1199   1243       O  
ATOM   2317  CB  GLU A1305       8.246 -50.304  90.049  1.00 95.05           C  
ANISOU 2317  CB  GLU A1305    14746  10347  11022    614  -1375   1172       C  
ATOM   2318  CG  GLU A1305       9.548 -50.572  89.309  1.00109.92           C  
ANISOU 2318  CG  GLU A1305    16793  12154  12817    950  -1290   1112       C  
ATOM   2319  CD  GLU A1305       9.707 -52.030  88.918  1.00121.49           C  
ANISOU 2319  CD  GLU A1305    18724  13303  14135   1061  -1385   1151       C  
ATOM   2320  OE1 GLU A1305       9.044 -52.887  89.542  1.00125.13           O  
ANISOU 2320  OE1 GLU A1305    19346  13635  14564    893  -1511   1236       O  
ATOM   2321  OE2 GLU A1305      10.491 -52.318  87.988  1.00123.20           O  
ANISOU 2321  OE2 GLU A1305    19158  13396  14256   1322  -1335   1102       O  
ATOM   2322  N   LYS A1306      10.417 -48.307  91.460  1.00 78.82           N  
ANISOU 2322  N   LYS A1306    11984   8895   9071    933  -1057   1107       N  
ATOM   2323  CA  LYS A1306      11.516 -48.231  92.419  1.00 75.38           C  
ANISOU 2323  CA  LYS A1306    11386   8640   8617   1088   -977   1145       C  
ATOM   2324  C   LYS A1306      11.282 -47.168  93.487  1.00 73.89           C  
ANISOU 2324  C   LYS A1306    10864   8703   8508    934   -934   1145       C  
ATOM   2325  O   LYS A1306      11.809 -47.288  94.598  1.00 79.40           O  
ANISOU 2325  O   LYS A1306    11455   9526   9187    969   -913   1203       O  
ATOM   2326  CB  LYS A1306      12.828 -47.957  91.683  1.00 80.06           C  
ANISOU 2326  CB  LYS A1306    11950   9299   9170   1365   -876   1113       C  
ATOM   2327  CG  LYS A1306      14.079 -48.302  92.475  1.00 88.88           C  
ANISOU 2327  CG  LYS A1306    12988  10551  10230   1572   -815   1193       C  
ATOM   2328  CD  LYS A1306      14.232 -49.807  92.634  1.00103.49           C  
ANISOU 2328  CD  LYS A1306    15157  12190  11974   1705   -869   1268       C  
ATOM   2329  CE  LYS A1306      15.506 -50.159  93.387  1.00102.85           C  
ANISOU 2329  CE  LYS A1306    14987  12258  11832   1935   -802   1364       C  
ATOM   2330  NZ  LYS A1306      15.643 -51.628  93.583  1.00100.56           N  
ANISOU 2330  NZ  LYS A1306    15024  11752  11430   2078   -851   1440       N  
ATOM   2331  N   HIS A1307      10.505 -46.131  93.181  1.00 78.20           N  
ANISOU 2331  N   HIS A1307    11261   9320   9132    774   -920   1085       N  
ATOM   2332  CA  HIS A1307      10.376 -44.972  94.055  1.00 72.16           C  
ANISOU 2332  CA  HIS A1307    10211   8784   8424    668   -863   1068       C  
ATOM   2333  C   HIS A1307       8.911 -44.590  94.188  1.00 70.04           C  
ANISOU 2333  C   HIS A1307     9891   8509   8210    437   -899   1075       C  
ATOM   2334  O   HIS A1307       8.213 -44.438  93.180  1.00 78.41           O  
ANISOU 2334  O   HIS A1307    11019   9472   9303    369   -927   1041       O  
ATOM   2335  CB  HIS A1307      11.181 -43.783  93.517  1.00 66.83           C  
ANISOU 2335  CB  HIS A1307     9364   8253   7777    759   -775    989       C  
ATOM   2336  CG  HIS A1307      12.623 -44.094  93.259  1.00 67.05           C  
ANISOU 2336  CG  HIS A1307     9407   8319   7748    993   -732   1010       C  
ATOM   2337  ND1 HIS A1307      13.499 -44.455  94.261  1.00 65.71           N  
ANISOU 2337  ND1 HIS A1307     9174   8262   7531   1082   -719   1087       N  
ATOM   2338  CD2 HIS A1307      13.344 -44.090  92.113  1.00 62.71           C  
ANISOU 2338  CD2 HIS A1307     8919   7732   7176   1167   -693    981       C  
ATOM   2339  CE1 HIS A1307      14.696 -44.663  93.742  1.00 65.14           C  
ANISOU 2339  CE1 HIS A1307     9109   8229   7411   1303   -673   1116       C  
ATOM   2340  NE2 HIS A1307      14.629 -44.447  92.441  1.00 62.50           N  
ANISOU 2340  NE2 HIS A1307     8852   7807   7089   1365   -652   1053       N  
ATOM   2341  N   GLY A1308       8.459 -44.399  95.427  1.00 58.11           N  
ANISOU 2341  N   GLY A1308     8253   7120   6705    327   -892   1129       N  
ATOM   2342  CA  GLY A1308       7.055 -44.108  95.661  1.00 59.99           C  
ANISOU 2342  CA  GLY A1308     8427   7383   6983    131   -914   1170       C  
ATOM   2343  C   GLY A1308       6.648 -42.684  95.353  1.00 69.16           C  
ANISOU 2343  C   GLY A1308     9410   8670   8198     85   -837   1097       C  
ATOM   2344  O   GLY A1308       5.446 -42.399  95.313  1.00 80.74           O  
ANISOU 2344  O   GLY A1308    10823  10158   9697    -54   -846   1139       O  
ATOM   2345  N   ASN A1309       7.610 -41.790  95.139  1.00 55.80           N  
ANISOU 2345  N   ASN A1309     7625   7067   6510    196   -764   1004       N  
ATOM   2346  CA  ASN A1309       7.338 -40.398  94.810  1.00 59.72           C  
ANISOU 2346  CA  ASN A1309     7981   7665   7047    164   -693    926       C  
ATOM   2347  C   ASN A1309       7.408 -40.115  93.313  1.00 59.23           C  
ANISOU 2347  C   ASN A1309     7970   7511   7024    204   -695    854       C  
ATOM   2348  O   ASN A1309       7.374 -38.947  92.912  1.00 58.73           O  
ANISOU 2348  O   ASN A1309     7801   7521   6992    199   -636    781       O  
ATOM   2349  CB  ASN A1309       8.304 -39.485  95.567  1.00 59.81           C  
ANISOU 2349  CB  ASN A1309     7863   7834   7026    225   -628    879       C  
ATOM   2350  CG  ASN A1309       9.755 -39.812  95.286  1.00 64.36           C  
ANISOU 2350  CG  ASN A1309     8467   8413   7575    369   -634    865       C  
ATOM   2351  OD1 ASN A1309      10.072 -40.865  94.731  1.00 61.25           O  
ANISOU 2351  OD1 ASN A1309     8205   7896   7169    454   -676    896       O  
ATOM   2352  ND2 ASN A1309      10.649 -38.911  95.676  1.00 58.69           N  
ANISOU 2352  ND2 ASN A1309     7631   7835   6834    401   -595    831       N  
ATOM   2353  N   VAL A1310       7.531 -41.148  92.482  1.00 54.89           N  
ANISOU 2353  N   VAL A1310     7601   6793   6462    251   -761    870       N  
ATOM   2354  CA  VAL A1310       7.547 -41.009  91.029  1.00 66.06           C  
ANISOU 2354  CA  VAL A1310     9100   8102   7900    292   -770    807       C  
ATOM   2355  C   VAL A1310       6.291 -41.653  90.456  1.00 67.00           C  
ANISOU 2355  C   VAL A1310     9353   8073   8033    149   -862    862       C  
ATOM   2356  O   VAL A1310       5.904 -42.757  90.861  1.00 75.08           O  
ANISOU 2356  O   VAL A1310    10511   8995   9020     86   -946    950       O  
ATOM   2357  CB  VAL A1310       8.819 -41.638  90.425  1.00 64.21           C  
ANISOU 2357  CB  VAL A1310     8995   7788   7614    490   -767    783       C  
ATOM   2358  CG1 VAL A1310       8.728 -41.698  88.912  1.00 55.23           C  
ANISOU 2358  CG1 VAL A1310     7995   6510   6481    535   -785    729       C  
ATOM   2359  CG2 VAL A1310      10.053 -40.858  90.859  1.00 56.45           C  
ANISOU 2359  CG2 VAL A1310     7841   6985   6622    607   -684    753       C  
ATOM   2360  N   LYS A1311       5.660 -40.966  89.506  1.00 62.50           N  
ANISOU 2360  N   LYS A1311     8748   7490   7510     85   -856    820       N  
ATOM   2361  CA  LYS A1311       4.465 -41.450  88.831  1.00 64.39           C  
ANISOU 2361  CA  LYS A1311     9096   7607   7762    -71   -953    883       C  
ATOM   2362  C   LYS A1311       4.626 -41.234  87.334  1.00 69.35           C  
ANISOU 2362  C   LYS A1311     9828   8123   8397    -21   -965    802       C  
ATOM   2363  O   LYS A1311       5.132 -40.195  86.902  1.00 53.86           O  
ANISOU 2363  O   LYS A1311     7744   6251   6468     68   -875    710       O  
ATOM   2364  CB  LYS A1311       3.208 -40.727  89.342  1.00 59.73           C  
ANISOU 2364  CB  LYS A1311     8311   7161   7223   -233   -932    953       C  
ATOM   2365  CG  LYS A1311       1.966 -40.898  88.476  1.00 63.68           C  
ANISOU 2365  CG  LYS A1311     8859   7587   7749   -402  -1022   1028       C  
ATOM   2366  CD  LYS A1311       1.430 -42.319  88.530  1.00 70.11           C  
ANISOU 2366  CD  LYS A1311     9875   8246   8516   -537  -1175   1151       C  
ATOM   2367  CE  LYS A1311       0.117 -42.435  87.775  1.00 68.91           C  
ANISOU 2367  CE  LYS A1311     9743   8053   8386   -747  -1282   1258       C  
ATOM   2368  NZ  LYS A1311      -0.458 -43.806  87.851  1.00 66.46           N  
ANISOU 2368  NZ  LYS A1311     9643   7589   8021   -919  -1456   1398       N  
ATOM   2369  N   VAL A1312       4.196 -42.218  86.547  1.00 58.08           N  
ANISOU 2369  N   VAL A1312     8643   6493   6930    -85  -1084    842       N  
ATOM   2370  CA  VAL A1312       4.326 -42.178  85.096  1.00 60.62           C  
ANISOU 2370  CA  VAL A1312     9116   6679   7238    -37  -1110    771       C  
ATOM   2371  C   VAL A1312       2.953 -42.402  84.477  1.00 59.45           C  
ANISOU 2371  C   VAL A1312     9041   6443   7104   -266  -1233    850       C  
ATOM   2372  O   VAL A1312       2.169 -43.225  84.961  1.00 59.99           O  
ANISOU 2372  O   VAL A1312     9191   6452   7150   -432  -1345    972       O  
ATOM   2373  CB  VAL A1312       5.341 -43.227  84.590  1.00 60.97           C  
ANISOU 2373  CB  VAL A1312     9452   6530   7183    146  -1141    736       C  
ATOM   2374  CG1 VAL A1312       5.455 -43.184  83.071  1.00 62.89           C  
ANISOU 2374  CG1 VAL A1312     9872   6628   7394    209  -1162    664       C  
ATOM   2375  CG2 VAL A1312       6.705 -42.997  85.230  1.00 56.75           C  
ANISOU 2375  CG2 VAL A1312     8807   6121   6634    369  -1021    692       C  
ATOM   2376  N   ILE A1313       2.666 -41.666  83.404  1.00 61.34           N  
ANISOU 2376  N   ILE A1313     9244   6682   7379   -285  -1218    796       N  
ATOM   2377  CA  ILE A1313       1.375 -41.707  82.721  1.00 60.29           C  
ANISOU 2377  CA  ILE A1313     9145   6499   7266   -505  -1331    879       C  
ATOM   2378  C   ILE A1313       1.657 -41.793  81.224  1.00 58.94           C  
ANISOU 2378  C   ILE A1313     9188   6153   7053   -447  -1373    793       C  
ATOM   2379  O   ILE A1313       1.993 -40.786  80.592  1.00 66.56           O  
ANISOU 2379  O   ILE A1313    10030   7199   8063   -350  -1275    698       O  
ATOM   2380  CB  ILE A1313       0.510 -40.482  83.041  1.00 63.17           C  
ANISOU 2380  CB  ILE A1313     9185   7093   7724   -602  -1254    921       C  
ATOM   2381  CG1 ILE A1313       0.352 -40.304  84.553  1.00 55.43           C  
ANISOU 2381  CG1 ILE A1313     8003   6291   6767   -615  -1186    991       C  
ATOM   2382  CG2 ILE A1313      -0.845 -40.593  82.362  1.00 63.99           C  
ANISOU 2382  CG2 ILE A1313     9302   7168   7844   -835  -1377   1043       C  
ATOM   2383  CD1 ILE A1313      -0.300 -38.988  84.941  1.00 60.55           C  
ANISOU 2383  CD1 ILE A1313     8354   7168   7485   -639  -1072   1012       C  
ATOM   2384  N   THR A1314       1.535 -42.992  80.651  1.00 67.24           N  
ANISOU 2384  N   THR A1314    10582   6957   8008   -504  -1521    828       N  
ATOM   2385  CA  THR A1314       1.709 -43.161  79.212  1.00 59.04           C  
ANISOU 2385  CA  THR A1314     9795   5731   6908   -457  -1575    756       C  
ATOM   2386  C   THR A1314       0.414 -43.019  78.420  1.00 62.66           C  
ANISOU 2386  C   THR A1314    10270   6153   7387   -717  -1708    838       C  
ATOM   2387  O   THR A1314       0.469 -42.904  77.191  1.00 72.47           O  
ANISOU 2387  O   THR A1314    11669   7275   8591   -692  -1740    773       O  
ATOM   2388  CB  THR A1314       2.339 -44.525  78.902  1.00 67.13           C  
ANISOU 2388  CB  THR A1314    11243   6475   7787   -351  -1665    739       C  
ATOM   2389  OG1 THR A1314       1.539 -45.567  79.475  1.00 71.17           O  
ANISOU 2389  OG1 THR A1314    11915   6872   8253   -570  -1832    875       O  
ATOM   2390  CG2 THR A1314       3.754 -44.599  79.462  1.00 61.90           C  
ANISOU 2390  CG2 THR A1314    10560   5863   7096    -49  -1518    660       C  
ATOM   2391  N   GLU A1315      -0.741 -43.028  79.078  1.00 66.66           N  
ANISOU 2391  N   GLU A1315    10613   6771   7945   -962  -1784    992       N  
ATOM   2392  CA  GLU A1315      -2.001 -42.865  78.367  1.00 69.94           C  
ANISOU 2392  CA  GLU A1315    11004   7190   8381  -1220  -1912   1105       C  
ATOM   2393  C   GLU A1315      -2.198 -41.412  77.949  1.00 71.44           C  
ANISOU 2393  C   GLU A1315    10885   7585   8674  -1169  -1778   1051       C  
ATOM   2394  O   GLU A1315      -1.700 -40.483  78.593  1.00 67.97           O  
ANISOU 2394  O   GLU A1315    10184   7335   8305  -1009  -1599    979       O  
ATOM   2395  CB  GLU A1315      -3.171 -43.332  79.235  1.00 82.02           C  
ANISOU 2395  CB  GLU A1315    12424   8810   9928  -1490  -2030   1322       C  
ATOM   2396  CG  GLU A1315      -3.079 -42.904  80.693  1.00 97.11           C  
ANISOU 2396  CG  GLU A1315    14030  10958  11909  -1418  -1889   1358       C  
ATOM   2397  CD  GLU A1315      -4.229 -43.431  81.531  1.00102.84           C  
ANISOU 2397  CD  GLU A1315    14653  11780  12640  -1676  -2003   1590       C  
ATOM   2398  OE1 GLU A1315      -5.293 -43.738  80.955  1.00105.17           O  
ANISOU 2398  OE1 GLU A1315    14994  12045  12920  -1934  -2168   1746       O  
ATOM   2399  OE2 GLU A1315      -4.066 -43.543  82.766  1.00105.26           O  
ANISOU 2399  OE2 GLU A1315    14832  12202  12962  -1628  -1932   1630       O  
ATOM   2400  N   MET A1316      -2.920 -41.220  76.847  1.00 83.90           N  
ANISOU 2400  N   MET A1316    12517   9112  10250  -1313  -1874   1089       N  
ATOM   2401  CA  MET A1316      -3.239 -39.873  76.396  1.00 84.84           C  
ANISOU 2401  CA  MET A1316    12356   9416  10462  -1284  -1761   1059       C  
ATOM   2402  C   MET A1316      -4.170 -39.190  77.391  1.00 78.78           C  
ANISOU 2402  C   MET A1316    11223   8924   9785  -1385  -1697   1203       C  
ATOM   2403  O   MET A1316      -5.056 -39.821  77.973  1.00 81.81           O  
ANISOU 2403  O   MET A1316    11580   9348  10158  -1588  -1809   1388       O  
ATOM   2404  CB  MET A1316      -3.876 -39.906  75.005  1.00 94.33           C  
ANISOU 2404  CB  MET A1316    13706  10503  11634  -1433  -1896   1089       C  
ATOM   2405  CG  MET A1316      -4.300 -38.537  74.479  1.00106.19           C  
ANISOU 2405  CG  MET A1316    14926  12193  13230  -1416  -1791   1075       C  
ATOM   2406  SD  MET A1316      -3.793 -38.227  72.777  1.00114.28           S  
ANISOU 2406  SD  MET A1316    16161  13050  14211  -1325  -1805    923       S  
ATOM   2407  CE  MET A1316      -2.011 -38.308  72.935  1.00112.19           C  
ANISOU 2407  CE  MET A1316    16032  12692  13902   -981  -1650    703       C  
ATOM   2408  N   LEU A1317      -3.956 -37.892  77.590  1.00 74.50           N  
ANISOU 2408  N   LEU A1317    10413   8573   9322  -1236  -1513   1125       N  
ATOM   2409  CA  LEU A1317      -4.739 -37.099  78.524  1.00 74.99           C  
ANISOU 2409  CA  LEU A1317    10145   8895   9453  -1268  -1415   1241       C  
ATOM   2410  C   LEU A1317      -5.486 -36.000  77.781  1.00 65.18           C  
ANISOU 2410  C   LEU A1317     8714   7782   8269  -1300  -1368   1277       C  
ATOM   2411  O   LEU A1317      -5.046 -35.527  76.729  1.00 54.49           O  
ANISOU 2411  O   LEU A1317     7436   6347   6921  -1223  -1348   1149       O  
ATOM   2412  CB  LEU A1317      -3.850 -36.471  79.604  1.00 65.16           C  
ANISOU 2412  CB  LEU A1317     8765   7762   8230  -1053  -1231   1126       C  
ATOM   2413  CG  LEU A1317      -2.977 -37.411  80.436  1.00 65.84           C  
ANISOU 2413  CG  LEU A1317     9001   7751   8263   -983  -1247   1082       C  
ATOM   2414  CD1 LEU A1317      -2.044 -36.609  81.331  1.00 62.90           C  
ANISOU 2414  CD1 LEU A1317     8487   7499   7912   -777  -1070    961       C  
ATOM   2415  CD2 LEU A1317      -3.832 -38.358  81.264  1.00 62.60           C  
ANISOU 2415  CD2 LEU A1317     8591   7365   7828  -1168  -1358   1276       C  
ATOM   2416  N   SER A1318      -6.628 -35.606  78.336  1.00 62.32           N  
ANISOU 2416  N   SER A1318     8103   7631   7944  -1403  -1347   1464       N  
ATOM   2417  CA  SER A1318      -7.342 -34.444  77.836  1.00 55.44           C  
ANISOU 2417  CA  SER A1318     7016   6923   7128  -1390  -1266   1513       C  
ATOM   2418  C   SER A1318      -6.581 -33.170  78.189  1.00 54.29           C  
ANISOU 2418  C   SER A1318     6747   6863   7016  -1137  -1051   1337       C  
ATOM   2419  O   SER A1318      -5.802 -33.123  79.145  1.00 63.68           O  
ANISOU 2419  O   SER A1318     7938   8063   8192  -1004   -957   1243       O  
ATOM   2420  CB  SER A1318      -8.754 -34.383  78.419  1.00 60.31           C  
ANISOU 2420  CB  SER A1318     7387   7767   7761  -1537  -1284   1787       C  
ATOM   2421  OG  SER A1318      -8.716 -34.129  79.813  1.00 67.64           O  
ANISOU 2421  OG  SER A1318     8160   8851   8689  -1424  -1148   1819       O  
ATOM   2422  N   ARG A1319      -6.797 -32.130  77.383  1.00 53.02           N  
ANISOU 2422  N   ARG A1319     6493   6758   6895  -1083   -985   1297       N  
ATOM   2423  CA  ARG A1319      -6.185 -30.841  77.686  1.00 60.39           C  
ANISOU 2423  CA  ARG A1319     7322   7772   7853   -869   -795   1150       C  
ATOM   2424  C   ARG A1319      -6.757 -30.231  78.962  1.00 57.88           C  
ANISOU 2424  C   ARG A1319     6795   7662   7534   -797   -661   1252       C  
ATOM   2425  O   ARG A1319      -6.082 -29.428  79.614  1.00 56.30           O  
ANISOU 2425  O   ARG A1319     6566   7500   7325   -626   -520   1126       O  
ATOM   2426  CB  ARG A1319      -6.349 -29.885  76.504  1.00 55.93           C  
ANISOU 2426  CB  ARG A1319     6718   7209   7324   -836   -762   1097       C  
ATOM   2427  CG  ARG A1319      -7.772 -29.445  76.233  1.00 66.02           C  
ANISOU 2427  CG  ARG A1319     7804   8653   8629   -931   -768   1302       C  
ATOM   2428  CD  ARG A1319      -7.902 -28.884  74.825  1.00 69.87           C  
ANISOU 2428  CD  ARG A1319     8313   9090   9143   -950   -798   1257       C  
ATOM   2429  NE  ARG A1319      -9.013 -27.948  74.693  1.00 66.90           N  
ANISOU 2429  NE  ARG A1319     7713   8910   8799   -941   -724   1408       N  
ATOM   2430  CZ  ARG A1319      -8.872 -26.664  74.379  1.00 68.36           C  
ANISOU 2430  CZ  ARG A1319     7823   9145   9007   -784   -586   1317       C  
ATOM   2431  NH1 ARG A1319      -7.664 -26.162  74.154  1.00 58.62           N  
ANISOU 2431  NH1 ARG A1319     6712   7788   7774   -650   -520   1082       N  
ATOM   2432  NH2 ARG A1319      -9.940 -25.882  74.280  1.00 63.55           N  
ANISOU 2432  NH2 ARG A1319     7016   8716   8415   -763   -518   1475       N  
ATOM   2433  N   GLU A1320      -7.990 -30.590  79.336  1.00 53.79           N  
ANISOU 2433  N   GLU A1320     6138   7287   7014   -925   -706   1490       N  
ATOM   2434  CA  GLU A1320      -8.538 -30.108  80.600  1.00 53.79           C  
ANISOU 2434  CA  GLU A1320     5952   7492   6994   -835   -571   1604       C  
ATOM   2435  C   GLU A1320      -7.783 -30.697  81.785  1.00 62.51           C  
ANISOU 2435  C   GLU A1320     7137   8554   8059   -787   -552   1537       C  
ATOM   2436  O   GLU A1320      -7.469 -29.986  82.749  1.00 62.14           O  
ANISOU 2436  O   GLU A1320     7035   8591   7985   -624   -402   1475       O  
ATOM   2437  CB  GLU A1320     -10.029 -30.438  80.698  1.00 55.64           C  
ANISOU 2437  CB  GLU A1320     5999   7914   7230   -988   -628   1908       C  
ATOM   2438  CG  GLU A1320     -10.913 -29.707  79.691  1.00 75.55           C  
ANISOU 2438  CG  GLU A1320     8385  10534   9784  -1016   -621   2015       C  
ATOM   2439  CD  GLU A1320     -10.870 -30.329  78.305  1.00 79.67           C  
ANISOU 2439  CD  GLU A1320     9055  10886  10330  -1204   -813   1994       C  
ATOM   2440  OE1 GLU A1320     -10.293 -31.427  78.161  1.00 77.73           O  
ANISOU 2440  OE1 GLU A1320     9019  10450  10064  -1321   -959   1928       O  
ATOM   2441  OE2 GLU A1320     -11.413 -29.719  77.359  1.00 84.53           O  
ANISOU 2441  OE2 GLU A1320     9592  11553  10975  -1225   -817   2045       O  
ATOM   2442  N   PHE A1321      -7.459 -31.990  81.722  1.00 54.02           N  
ANISOU 2442  N   PHE A1321     6217   7338   6971   -923   -707   1547       N  
ATOM   2443  CA  PHE A1321      -6.682 -32.592  82.797  1.00 54.61           C  
ANISOU 2443  CA  PHE A1321     6377   7364   7008   -873   -694   1483       C  
ATOM   2444  C   PHE A1321      -5.275 -32.010  82.854  1.00 52.25           C  
ANISOU 2444  C   PHE A1321     6180   6969   6703   -689   -601   1231       C  
ATOM   2445  O   PHE A1321      -4.723 -31.807  83.942  1.00 51.90           O  
ANISOU 2445  O   PHE A1321     6121   6972   6628   -582   -511   1174       O  
ATOM   2446  CB  PHE A1321      -6.632 -34.110  82.624  1.00 54.81           C  
ANISOU 2446  CB  PHE A1321     6575   7238   7011  -1050   -886   1549       C  
ATOM   2447  CG  PHE A1321      -5.954 -34.817  83.758  1.00 71.44           C  
ANISOU 2447  CG  PHE A1321     8759   9306   9077  -1009   -881   1516       C  
ATOM   2448  CD1 PHE A1321      -6.485 -34.761  85.036  1.00 76.31           C  
ANISOU 2448  CD1 PHE A1321     9220  10100   9673   -998   -808   1648       C  
ATOM   2449  CD2 PHE A1321      -4.785 -35.530  83.553  1.00 75.99           C  
ANISOU 2449  CD2 PHE A1321     9562   9681   9629   -965   -943   1364       C  
ATOM   2450  CE1 PHE A1321      -5.865 -35.403  86.089  1.00 76.21           C  
ANISOU 2450  CE1 PHE A1321     9278  10057   9623   -963   -806   1620       C  
ATOM   2451  CE2 PHE A1321      -4.161 -36.179  84.603  1.00 80.07           C  
ANISOU 2451  CE2 PHE A1321    10143  10173  10108   -921   -938   1345       C  
ATOM   2452  CZ  PHE A1321      -4.702 -36.114  85.873  1.00 73.64           C  
ANISOU 2452  CZ  PHE A1321     9173   9529   9280   -929   -875   1469       C  
ATOM   2453  N   VAL A1322      -4.683 -31.716  81.695  1.00 51.39           N  
ANISOU 2453  N   VAL A1322     6171   6736   6618   -658   -624   1092       N  
ATOM   2454  CA  VAL A1322      -3.358 -31.106  81.693  1.00 50.05           C  
ANISOU 2454  CA  VAL A1322     6072   6503   6442   -496   -540    882       C  
ATOM   2455  C   VAL A1322      -3.417 -29.694  82.260  1.00 49.47           C  
ANISOU 2455  C   VAL A1322     5863   6567   6365   -366   -377    838       C  
ATOM   2456  O   VAL A1322      -2.505 -29.263  82.975  1.00 50.12           O  
ANISOU 2456  O   VAL A1322     5970   6654   6417   -257   -302    725       O  
ATOM   2457  CB  VAL A1322      -2.757 -31.129  80.276  1.00 49.45           C  
ANISOU 2457  CB  VAL A1322     6127   6278   6385   -490   -599    765       C  
ATOM   2458  CG1 VAL A1322      -1.465 -30.329  80.236  1.00 48.22           C  
ANISOU 2458  CG1 VAL A1322     5997   6101   6225   -331   -504    581       C  
ATOM   2459  CG2 VAL A1322      -2.504 -32.560  79.838  1.00 50.25           C  
ANISOU 2459  CG2 VAL A1322     6425   6209   6457   -581   -751    784       C  
ATOM   2460  N   ARG A1323      -4.495 -28.956  81.970  1.00 49.85           N  
ANISOU 2460  N   ARG A1323     5778   6728   6434   -375   -326    937       N  
ATOM   2461  CA  ARG A1323      -4.640 -27.636  82.572  1.00 53.20           C  
ANISOU 2461  CA  ARG A1323     6110   7270   6833   -233   -166    908       C  
ATOM   2462  C   ARG A1323      -4.784 -27.747  84.081  1.00 54.68           C  
ANISOU 2462  C   ARG A1323     6253   7561   6961   -182    -95    973       C  
ATOM   2463  O   ARG A1323      -4.266 -26.908  84.828  1.00 49.87           O  
ANISOU 2463  O   ARG A1323     5669   6978   6302    -54     13    876       O  
ATOM   2464  CB  ARG A1323      -5.843 -26.902  81.979  1.00 50.16           C  
ANISOU 2464  CB  ARG A1323     5590   6997   6472   -233   -118   1029       C  
ATOM   2465  CG  ARG A1323      -6.111 -25.554  82.642  1.00 52.51           C  
ANISOU 2465  CG  ARG A1323     5820   7409   6722    -60     57   1017       C  
ATOM   2466  CD  ARG A1323      -7.301 -24.839  82.035  1.00 50.96           C  
ANISOU 2466  CD  ARG A1323     5487   7332   6543    -33    115   1152       C  
ATOM   2467  NE  ARG A1323      -8.540 -25.584  82.214  1.00 52.44           N  
ANISOU 2467  NE  ARG A1323     5521   7665   6738   -139     69   1408       N  
ATOM   2468  CZ  ARG A1323      -9.711 -25.205  81.717  1.00 53.43           C  
ANISOU 2468  CZ  ARG A1323     5489   7934   6881   -146     97   1590       C  
ATOM   2469  NH1 ARG A1323      -9.803 -24.086  81.009  1.00 53.02           N  
ANISOU 2469  NH1 ARG A1323     5425   7882   6839    -39    178   1528       N  
ATOM   2470  NH2 ARG A1323     -10.791 -25.947  81.924  1.00 60.99           N  
ANISOU 2470  NH2 ARG A1323     6292   9040   7840   -266     38   1848       N  
ATOM   2471  N   GLU A1324      -5.464 -28.796  84.548  1.00 51.31           N  
ANISOU 2471  N   GLU A1324     5777   7187   6530   -292   -166   1141       N  
ATOM   2472  CA  GLU A1324      -5.573 -29.012  85.986  1.00 51.97           C  
ANISOU 2472  CA  GLU A1324     5823   7369   6555   -248   -106   1210       C  
ATOM   2473  C   GLU A1324      -4.210 -29.316  86.597  1.00 53.93           C  
ANISOU 2473  C   GLU A1324     6210   7509   6774   -203   -120   1046       C  
ATOM   2474  O   GLU A1324      -3.894 -28.849  87.697  1.00 54.00           O  
ANISOU 2474  O   GLU A1324     6223   7576   6719   -101    -26   1007       O  
ATOM   2475  CB  GLU A1324      -6.554 -30.150  86.268  1.00 53.38           C  
ANISOU 2475  CB  GLU A1324     5920   7623   6738   -401   -200   1438       C  
ATOM   2476  CG  GLU A1324      -7.041 -30.202  87.703  1.00 81.32           C  
ANISOU 2476  CG  GLU A1324     9364  11321  10212   -346   -111   1567       C  
ATOM   2477  CD  GLU A1324      -7.975 -29.056  88.039  1.00 95.14           C  
ANISOU 2477  CD  GLU A1324    10962  13263  11922   -206     56   1670       C  
ATOM   2478  OE1 GLU A1324      -8.643 -28.543  87.115  1.00 99.36           O  
ANISOU 2478  OE1 GLU A1324    11414  13844  12496   -214     66   1732       O  
ATOM   2479  OE2 GLU A1324      -8.039 -28.666  89.225  1.00 92.56           O  
ANISOU 2479  OE2 GLU A1324    10613  13038  11517    -76    180   1691       O  
ATOM   2480  N   LEU A1325      -3.380 -30.078  85.881  1.00 53.56           N  
ANISOU 2480  N   LEU A1325     6284   7306   6760   -267   -236    956       N  
ATOM   2481  CA  LEU A1325      -2.041 -30.382  86.382  1.00 49.97           C  
ANISOU 2481  CA  LEU A1325     5942   6768   6277   -213   -249    821       C  
ATOM   2482  C   LEU A1325      -1.168 -29.137  86.425  1.00 51.61           C  
ANISOU 2482  C   LEU A1325     6170   6977   6462    -90   -154    661       C  
ATOM   2483  O   LEU A1325      -0.448 -28.912  87.405  1.00 48.93           O  
ANISOU 2483  O   LEU A1325     5861   6661   6069    -29   -111    601       O  
ATOM   2484  CB  LEU A1325      -1.380 -31.451  85.515  1.00 54.05           C  
ANISOU 2484  CB  LEU A1325     6592   7124   6821   -277   -380    776       C  
ATOM   2485  CG  LEU A1325      -2.096 -32.794  85.443  1.00 64.28           C  
ANISOU 2485  CG  LEU A1325     7931   8372   8121   -421   -507    925       C  
ATOM   2486  CD1 LEU A1325      -1.304 -33.770  84.605  1.00 69.86           C  
ANISOU 2486  CD1 LEU A1325     8826   8890   8827   -444   -623    855       C  
ATOM   2487  CD2 LEU A1325      -2.305 -33.332  86.835  1.00 58.71           C  
ANISOU 2487  CD2 LEU A1325     7185   7748   7373   -439   -495   1023       C  
ATOM   2488  N   TYR A1326      -1.235 -28.308  85.378  1.00 48.46           N  
ANISOU 2488  N   TYR A1326     5760   6552   6098    -66   -130    599       N  
ATOM   2489  CA  TYR A1326      -0.450 -27.081  85.333  1.00 47.71           C  
ANISOU 2489  CA  TYR A1326     5696   6451   5980     28    -54    458       C  
ATOM   2490  C   TYR A1326      -0.812 -26.146  86.475  1.00 48.17           C  
ANISOU 2490  C   TYR A1326     5731   6610   5964    110     62    472       C  
ATOM   2491  O   TYR A1326       0.047 -25.412  86.977  1.00 47.89           O  
ANISOU 2491  O   TYR A1326     5764   6560   5873    166    100    365       O  
ATOM   2492  CB  TYR A1326      -0.675 -26.356  84.004  1.00 53.00           C  
ANISOU 2492  CB  TYR A1326     6351   7085   6699     32    -47    415       C  
ATOM   2493  CG  TYR A1326       0.083 -26.877  82.806  1.00 47.41           C  
ANISOU 2493  CG  TYR A1326     5712   6263   6040     -4   -137    342       C  
ATOM   2494  CD1 TYR A1326       1.346 -27.439  82.935  1.00 46.28           C  
ANISOU 2494  CD1 TYR A1326     5645   6059   5879     16   -183    267       C  
ATOM   2495  CD2 TYR A1326      -0.464 -26.783  81.534  1.00 46.43           C  
ANISOU 2495  CD2 TYR A1326     5575   6099   5967    -44   -169    359       C  
ATOM   2496  CE1 TYR A1326       2.037 -27.904  81.826  1.00 45.93           C  
ANISOU 2496  CE1 TYR A1326     5671   5920   5862     19   -246    212       C  
ATOM   2497  CE2 TYR A1326       0.217 -27.240  80.425  1.00 54.14           C  
ANISOU 2497  CE2 TYR A1326     6635   6967   6970    -58   -243    292       C  
ATOM   2498  CZ  TYR A1326       1.465 -27.801  80.574  1.00 54.98           C  
ANISOU 2498  CZ  TYR A1326     6823   7015   7051    -16   -275    220       C  
ATOM   2499  OH  TYR A1326       2.137 -28.256  79.463  1.00 58.29           O  
ANISOU 2499  OH  TYR A1326     7333   7335   7481      3   -330    165       O  
ATOM   2500  N   GLY A1327      -2.074 -26.150  86.891  1.00 49.07           N  
ANISOU 2500  N   GLY A1327     5756   6826   6064    119    116    614       N  
ATOM   2501  CA  GLY A1327      -2.535 -25.321  87.978  1.00 49.81           C  
ANISOU 2501  CA  GLY A1327     5841   7017   6066    227    242    646       C  
ATOM   2502  C   GLY A1327      -2.344 -25.898  89.357  1.00 56.28           C  
ANISOU 2502  C   GLY A1327     6683   7883   6818    234    250    686       C  
ATOM   2503  O   GLY A1327      -2.707 -25.250  90.344  1.00 61.68           O  
ANISOU 2503  O   GLY A1327     7385   8645   7407    337    358    713       O  
ATOM   2504  N   SER A1328      -1.789 -27.101  89.463  1.00 50.22           N  
ANISOU 2504  N   SER A1328     5930   7066   6084    140    141    694       N  
ATOM   2505  CA  SER A1328      -1.618 -27.775  90.744  1.00 50.83           C  
ANISOU 2505  CA  SER A1328     6022   7187   6103    135    137    745       C  
ATOM   2506  C   SER A1328      -0.167 -28.051  91.094  1.00 51.32           C  
ANISOU 2506  C   SER A1328     6187   7168   6145    124     76    619       C  
ATOM   2507  O   SER A1328       0.214 -27.918  92.260  1.00 50.62           O  
ANISOU 2507  O   SER A1328     6143   7116   5973    163    110    603       O  
ATOM   2508  CB  SER A1328      -2.401 -29.095  90.751  1.00 51.54           C  
ANISOU 2508  CB  SER A1328     6034   7312   6238     27     60    913       C  
ATOM   2509  OG  SER A1328      -3.759 -28.881  90.406  1.00 66.20           O  
ANISOU 2509  OG  SER A1328     7767   9273   8113     18    103   1065       O  
ATOM   2510  N   VAL A1329       0.663 -28.420  90.114  1.00 52.20           N  
ANISOU 2510  N   VAL A1329     6334   7178   6320     81    -11    540       N  
ATOM   2511  CA  VAL A1329       2.058 -28.735  90.406  1.00 49.27           C  
ANISOU 2511  CA  VAL A1329     6034   6758   5929     83    -66    452       C  
ATOM   2512  C   VAL A1329       2.809 -27.467  90.791  1.00 58.91           C  
ANISOU 2512  C   VAL A1329     7307   7995   7082    135    -13    342       C  
ATOM   2513  O   VAL A1329       2.362 -26.337  90.554  1.00 50.90           O  
ANISOU 2513  O   VAL A1329     6302   6992   6047    175     58    306       O  
ATOM   2514  CB  VAL A1329       2.746 -29.431  89.221  1.00 60.26           C  
ANISOU 2514  CB  VAL A1329     7455   8051   7391     56   -155    411       C  
ATOM   2515  CG1 VAL A1329       1.940 -30.635  88.755  1.00 48.91           C  
ANISOU 2515  CG1 VAL A1329     6015   6566   6003    -14   -225    518       C  
ATOM   2516  CG2 VAL A1329       2.987 -28.429  88.102  1.00 47.74           C  
ANISOU 2516  CG2 VAL A1329     5870   6432   5838     80   -132    319       C  
ATOM   2517  N   ASP A1330       3.948 -27.665  91.451  1.00 48.87           N  
ANISOU 2517  N   ASP A1330     6079   6724   5764    129    -55    301       N  
ATOM   2518  CA  ASP A1330       4.806 -26.536  91.777  1.00 57.88           C  
ANISOU 2518  CA  ASP A1330     7285   7873   6833    139    -41    209       C  
ATOM   2519  C   ASP A1330       5.675 -26.119  90.594  1.00 52.96           C  
ANISOU 2519  C   ASP A1330     6656   7206   6261    125    -83    133       C  
ATOM   2520  O   ASP A1330       5.824 -24.921  90.329  1.00 52.37           O  
ANISOU 2520  O   ASP A1330     6624   7118   6155    125    -56     66       O  
ATOM   2521  CB  ASP A1330       5.663 -26.884  92.991  1.00 51.07           C  
ANISOU 2521  CB  ASP A1330     6460   7051   5893    120    -79    218       C  
ATOM   2522  CG  ASP A1330       4.827 -27.254  94.193  1.00 57.47           C  
ANISOU 2522  CG  ASP A1330     7281   7912   6643    139    -32    295       C  
ATOM   2523  OD1 ASP A1330       3.925 -26.464  94.540  1.00 50.58           O  
ANISOU 2523  OD1 ASP A1330     6441   7062   5714    187     56    301       O  
ATOM   2524  OD2 ASP A1330       5.046 -28.343  94.767  1.00 50.43           O  
ANISOU 2524  OD2 ASP A1330     6365   7042   5755    120    -76    358       O  
ATOM   2525  N   PHE A1331       6.227 -27.082  89.854  1.00 47.78           N  
ANISOU 2525  N   PHE A1331     5960   6520   5673    121   -145    150       N  
ATOM   2526  CA  PHE A1331       7.160 -26.780  88.777  1.00 47.28           C  
ANISOU 2526  CA  PHE A1331     5882   6435   5647    125   -179     96       C  
ATOM   2527  C   PHE A1331       6.898 -27.694  87.592  1.00 54.55           C  
ANISOU 2527  C   PHE A1331     6786   7289   6651    149   -206    117       C  
ATOM   2528  O   PHE A1331       6.439 -28.828  87.748  1.00 47.22           O  
ANISOU 2528  O   PHE A1331     5871   6329   5742    149   -233    180       O  
ATOM   2529  CB  PHE A1331       8.623 -26.941  89.217  1.00 47.60           C  
ANISOU 2529  CB  PHE A1331     5913   6531   5643    119   -234     99       C  
ATOM   2530  CG  PHE A1331       8.992 -26.111  90.405  1.00 53.29           C  
ANISOU 2530  CG  PHE A1331     6676   7307   6264     70   -235     84       C  
ATOM   2531  CD1 PHE A1331       9.480 -24.824  90.244  1.00 48.21           C  
ANISOU 2531  CD1 PHE A1331     6069   6672   5576     22   -242     28       C  
ATOM   2532  CD2 PHE A1331       8.848 -26.614  91.689  1.00 48.75           C  
ANISOU 2532  CD2 PHE A1331     6127   6766   5631     62   -237    129       C  
ATOM   2533  CE1 PHE A1331       9.817 -24.053  91.342  1.00 48.94           C  
ANISOU 2533  CE1 PHE A1331     6245   6794   5557    -39   -260     13       C  
ATOM   2534  CE2 PHE A1331       9.183 -25.850  92.792  1.00 49.41           C  
ANISOU 2534  CE2 PHE A1331     6280   6889   5606     14   -245    112       C  
ATOM   2535  CZ  PHE A1331       9.668 -24.567  92.619  1.00 49.55           C  
ANISOU 2535  CZ  PHE A1331     6357   6901   5570    -40   -261     53       C  
ATOM   2536  N   VAL A1332       7.203 -27.180  86.403  1.00 46.43           N  
ANISOU 2536  N   VAL A1332     5747   6231   5661    163   -206     67       N  
ATOM   2537  CA  VAL A1332       7.141 -27.935  85.159  1.00 46.19           C  
ANISOU 2537  CA  VAL A1332     5731   6128   5692    194   -236     74       C  
ATOM   2538  C   VAL A1332       8.542 -27.983  84.567  1.00 50.19           C  
ANISOU 2538  C   VAL A1332     6225   6657   6189    251   -259     53       C  
ATOM   2539  O   VAL A1332       9.168 -26.937  84.359  1.00 53.77           O  
ANISOU 2539  O   VAL A1332     6638   7163   6628    238   -246     13       O  
ATOM   2540  CB  VAL A1332       6.144 -27.312  84.164  1.00 48.36           C  
ANISOU 2540  CB  VAL A1332     6000   6358   6017    172   -209     49       C  
ATOM   2541  CG1 VAL A1332       6.320 -27.919  82.783  1.00 45.55           C  
ANISOU 2541  CG1 VAL A1332     5680   5921   5705    203   -247     40       C  
ATOM   2542  CG2 VAL A1332       4.722 -27.511  84.656  1.00 46.01           C  
ANISOU 2542  CG2 VAL A1332     5692   6061   5730    129   -189    113       C  
ATOM   2543  N   ILE A1333       9.033 -29.190  84.305  1.00 46.59           N  
ANISOU 2543  N   ILE A1333     5808   6164   5731    318   -295     93       N  
ATOM   2544  CA  ILE A1333      10.375 -29.399  83.774  1.00 54.34           C  
ANISOU 2544  CA  ILE A1333     6769   7188   6691    409   -303    104       C  
ATOM   2545  C   ILE A1333      10.283 -29.582  82.265  1.00 54.33           C  
ANISOU 2545  C   ILE A1333     6817   7103   6722    470   -299     77       C  
ATOM   2546  O   ILE A1333       9.551 -30.454  81.780  1.00 50.39           O  
ANISOU 2546  O   ILE A1333     6423   6484   6238    482   -325     85       O  
ATOM   2547  CB  ILE A1333      11.053 -30.608  84.440  1.00 47.70           C  
ANISOU 2547  CB  ILE A1333     5956   6360   5806    484   -329    174       C  
ATOM   2548  CG1 ILE A1333      11.024 -30.456  85.960  1.00 47.92           C  
ANISOU 2548  CG1 ILE A1333     5944   6464   5799    412   -337    201       C  
ATOM   2549  CG2 ILE A1333      12.481 -30.755  83.943  1.00 48.23           C  
ANISOU 2549  CG2 ILE A1333     5978   6508   5841    603   -322    212       C  
ATOM   2550  CD1 ILE A1333      11.615 -31.631  86.708  1.00 48.74           C  
ANISOU 2550  CD1 ILE A1333     6074   6584   5861    479   -365    275       C  
ATOM   2551  N   ILE A1334      11.049 -28.782  81.527  1.00 47.00           N  
ANISOU 2551  N   ILE A1334     5826   6237   5794    501   -277     54       N  
ATOM   2552  CA  ILE A1334      11.043 -28.800  80.065  1.00 46.36           C  
ANISOU 2552  CA  ILE A1334     5787   6092   5736    565   -266     26       C  
ATOM   2553  C   ILE A1334      12.487 -28.925  79.596  1.00 51.77           C  
ANISOU 2553  C   ILE A1334     6420   6871   6378    691   -247     72       C  
ATOM   2554  O   ILE A1334      13.100 -27.924  79.196  1.00 46.78           O  
ANISOU 2554  O   ILE A1334     5688   6337   5749    673   -228     69       O  
ATOM   2555  CB  ILE A1334      10.375 -27.543  79.482  1.00 45.51           C  
ANISOU 2555  CB  ILE A1334     5641   5977   5674    476   -246    -37       C  
ATOM   2556  CG1 ILE A1334       9.069 -27.231  80.216  1.00 45.14           C  
ANISOU 2556  CG1 ILE A1334     5604   5894   5654    367   -245    -53       C  
ATOM   2557  CG2 ILE A1334      10.099 -27.729  77.995  1.00 45.60           C  
ANISOU 2557  CG2 ILE A1334     5719   5897   5709    528   -243    -65       C  
ATOM   2558  CD1 ILE A1334       8.412 -25.935  79.771  1.00 52.92           C  
ANISOU 2558  CD1 ILE A1334     6555   6880   6672    301   -214   -104       C  
ATOM   2559  N   PRO A1335      13.069 -30.128  79.632  1.00 48.51           N  
ANISOU 2559  N   PRO A1335     6073   6441   5918    827   -249    130       N  
ATOM   2560  CA  PRO A1335      14.501 -30.276  79.347  1.00 53.67           C  
ANISOU 2560  CA  PRO A1335     6650   7223   6517    974   -218    207       C  
ATOM   2561  C   PRO A1335      14.807 -30.470  77.870  1.00 49.01           C  
ANISOU 2561  C   PRO A1335     6124   6589   5909   1118   -179    202       C  
ATOM   2562  O   PRO A1335      15.616 -31.331  77.511  1.00 55.57           O  
ANISOU 2562  O   PRO A1335     7005   7437   6673   1312   -147    269       O  
ATOM   2563  CB  PRO A1335      14.872 -31.523  80.157  1.00 56.47           C  
ANISOU 2563  CB  PRO A1335     7068   7569   6821   1073   -229    276       C  
ATOM   2564  CG  PRO A1335      13.629 -32.370  80.071  1.00 49.43           C  
ANISOU 2564  CG  PRO A1335     6367   6469   5946   1039   -265    223       C  
ATOM   2565  CD  PRO A1335      12.451 -31.410  80.014  1.00 48.25           C  
ANISOU 2565  CD  PRO A1335     6188   6276   5869    853   -282    144       C  
ATOM   2566  N   SER A1336      14.176 -29.676  77.008  1.00 55.98           N  
ANISOU 2566  N   SER A1336     7012   7418   6838   1040   -176    128       N  
ATOM   2567  CA  SER A1336      14.287 -29.891  75.570  1.00 49.81           C  
ANISOU 2567  CA  SER A1336     6321   6569   6035   1166   -145    112       C  
ATOM   2568  C   SER A1336      15.713 -29.669  75.073  1.00 53.13           C  
ANISOU 2568  C   SER A1336     6620   7164   6403   1319    -87    200       C  
ATOM   2569  O   SER A1336      16.385 -28.712  75.463  1.00 52.36           O  
ANISOU 2569  O   SER A1336     6331   7245   6319   1242    -84    248       O  
ATOM   2570  CB  SER A1336      13.335 -28.952  74.827  1.00 47.38           C  
ANISOU 2570  CB  SER A1336     6016   6193   5793   1034   -157     25       C  
ATOM   2571  OG  SER A1336      12.059 -28.921  75.442  1.00 55.64           O  
ANISOU 2571  OG  SER A1336     7109   7139   6891    878   -203    -25       O  
ATOM   2572  N   TYR A1337      16.183 -30.581  74.215  1.00 62.04           N  
ANISOU 2572  N   TYR A1337     7873   8243   7457   1541    -43    235       N  
ATOM   2573  CA  TYR A1337      17.361 -30.290  73.404  1.00 51.88           C  
ANISOU 2573  CA  TYR A1337     6477   7117   6116   1706     29    323       C  
ATOM   2574  C   TYR A1337      17.064 -29.235  72.347  1.00 50.47           C  
ANISOU 2574  C   TYR A1337     6253   6940   5982   1625     38    264       C  
ATOM   2575  O   TYR A1337      17.960 -28.483  71.951  1.00 53.49           O  
ANISOU 2575  O   TYR A1337     6460   7509   6354   1655     77    341       O  
ATOM   2576  CB  TYR A1337      17.873 -31.558  72.723  1.00 52.79           C  
ANISOU 2576  CB  TYR A1337     6775   7162   6120   1998     88    373       C  
ATOM   2577  CG  TYR A1337      18.541 -32.557  73.637  1.00 62.92           C  
ANISOU 2577  CG  TYR A1337     8072   8496   7336   2141    103    471       C  
ATOM   2578  CD1 TYR A1337      17.798 -33.526  74.302  1.00 61.84           C  
ANISOU 2578  CD1 TYR A1337     8132   8171   7194   2110     48    420       C  
ATOM   2579  CD2 TYR A1337      19.919 -32.548  73.816  1.00 63.30           C  
ANISOU 2579  CD2 TYR A1337     7935   8793   7325   2308    171    631       C  
ATOM   2580  CE1 TYR A1337      18.409 -34.452  75.129  1.00 64.53           C  
ANISOU 2580  CE1 TYR A1337     8496   8552   7471   2247     62    511       C  
ATOM   2581  CE2 TYR A1337      20.539 -33.469  74.639  1.00 63.02           C  
ANISOU 2581  CE2 TYR A1337     7907   8814   7225   2452    189    733       C  
ATOM   2582  CZ  TYR A1337      19.780 -34.418  75.293  1.00 67.09           C  
ANISOU 2582  CZ  TYR A1337     8634   9122   7737   2425    135    664       C  
ATOM   2583  OH  TYR A1337      20.396 -35.335  76.111  1.00 74.62           O  
ANISOU 2583  OH  TYR A1337     9602  10125   8623   2572    153    767       O  
ATOM   2584  N   PHE A1338      15.814 -29.165  71.892  1.00 49.59           N  
ANISOU 2584  N   PHE A1338     6288   6634   5920   1515     -2    145       N  
ATOM   2585  CA  PHE A1338      15.435 -28.345  70.745  1.00 48.86           C  
ANISOU 2585  CA  PHE A1338     6194   6510   5860   1467      8     86       C  
ATOM   2586  C   PHE A1338      14.002 -27.886  70.974  1.00 47.54           C  
ANISOU 2586  C   PHE A1338     6077   6206   5780   1248    -57    -19       C  
ATOM   2587  O   PHE A1338      13.081 -28.708  70.971  1.00 54.55           O  
ANISOU 2587  O   PHE A1338     7144   6918   6666   1228   -101    -64       O  
ATOM   2588  CB  PHE A1338      15.574 -29.144  69.445  1.00 49.80           C  
ANISOU 2588  CB  PHE A1338     6505   6520   5895   1677     49     82       C  
ATOM   2589  CG  PHE A1338      15.013 -28.454  68.229  1.00 57.20           C  
ANISOU 2589  CG  PHE A1338     7481   7390   6861   1622     49     11       C  
ATOM   2590  CD1 PHE A1338      15.632 -27.332  67.699  1.00 69.00           C  
ANISOU 2590  CD1 PHE A1338     8789   9051   8378   1606     91     46       C  
ATOM   2591  CD2 PHE A1338      13.880 -28.948  67.599  1.00 60.13           C  
ANISOU 2591  CD2 PHE A1338     8079   7536   7232   1578     -3    -76       C  
ATOM   2592  CE1 PHE A1338      15.121 -26.704  66.574  1.00 74.39           C  
ANISOU 2592  CE1 PHE A1338     9508   9671   9086   1560     92    -16       C  
ATOM   2593  CE2 PHE A1338      13.368 -28.328  66.472  1.00 70.82           C  
ANISOU 2593  CE2 PHE A1338     9466   8833   8608   1527     -8   -132       C  
ATOM   2594  CZ  PHE A1338      13.988 -27.203  65.960  1.00 66.53           C  
ANISOU 2594  CZ  PHE A1338     8735   8453   8091   1526     45   -107       C  
ATOM   2595  N   GLU A1339      13.821 -26.592  71.233  1.00 48.83           N  
ANISOU 2595  N   GLU A1339     6087   6455   6011   1084    -67    -42       N  
ATOM   2596  CA  GLU A1339      12.499 -26.006  71.468  1.00 45.53           C  
ANISOU 2596  CA  GLU A1339     5692   5938   5668    901   -109   -123       C  
ATOM   2597  C   GLU A1339      12.384 -24.688  70.717  1.00 47.63           C  
ANISOU 2597  C   GLU A1339     5873   6247   5977    822    -94   -158       C  
ATOM   2598  O   GLU A1339      12.592 -23.608  71.287  1.00 54.42           O  
ANISOU 2598  O   GLU A1339     6611   7203   6862    711    -97   -154       O  
ATOM   2599  CB  GLU A1339      12.238 -25.821  72.966  1.00 45.23           C  
ANISOU 2599  CB  GLU A1339     5590   5941   5655    782   -136   -117       C  
ATOM   2600  CG  GLU A1339      10.762 -25.744  73.326  1.00 45.10           C  
ANISOU 2600  CG  GLU A1339     5636   5807   5691    652   -169   -172       C  
ATOM   2601  CD  GLU A1339       9.996 -26.989  72.922  1.00 51.88           C  
ANISOU 2601  CD  GLU A1339     6663   6510   6537    689   -206   -175       C  
ATOM   2602  OE1 GLU A1339       9.143 -26.898  72.013  1.00 61.22           O  
ANISOU 2602  OE1 GLU A1339     7918   7598   7747    648   -226   -209       O  
ATOM   2603  OE2 GLU A1339      10.252 -28.063  73.509  1.00 57.83           O  
ANISOU 2603  OE2 GLU A1339     7489   7235   7249    751   -224   -138       O  
ATOM   2604  N   PRO A1340      12.082 -24.734  69.417  1.00 57.92           N  
ANISOU 2604  N   PRO A1340     7258   7471   7277    874    -83   -190       N  
ATOM   2605  CA  PRO A1340      12.035 -23.482  68.640  1.00 57.52           C  
ANISOU 2605  CA  PRO A1340     7126   7464   7264    808    -67   -216       C  
ATOM   2606  C   PRO A1340      11.040 -22.449  69.157  1.00 50.21           C  
ANISOU 2606  C   PRO A1340     6158   6511   6408    633    -90   -268       C  
ATOM   2607  O   PRO A1340      11.312 -21.248  69.032  1.00 46.13           O  
ANISOU 2607  O   PRO A1340     5549   6068   5910    563    -79   -273       O  
ATOM   2608  CB  PRO A1340      11.663 -23.958  67.224  1.00 54.86           C  
ANISOU 2608  CB  PRO A1340     6926   7013   6905    895    -61   -247       C  
ATOM   2609  CG  PRO A1340      11.072 -25.322  67.410  1.00 52.39           C  
ANISOU 2609  CG  PRO A1340     6792   6553   6560    940   -100   -256       C  
ATOM   2610  CD  PRO A1340      11.795 -25.912  68.581  1.00 61.67           C  
ANISOU 2610  CD  PRO A1340     7925   7803   7703    993    -92   -202       C  
ATOM   2611  N   PHE A1341       9.908 -22.856  69.734  1.00 45.71           N  
ANISOU 2611  N   PHE A1341     5657   5843   5867    566   -119   -295       N  
ATOM   2612  CA  PHE A1341       8.855 -21.893  70.034  1.00 51.13           C  
ANISOU 2612  CA  PHE A1341     6313   6505   6608    441   -122   -332       C  
ATOM   2613  C   PHE A1341       8.391 -21.858  71.488  1.00 69.69           C  
ANISOU 2613  C   PHE A1341     8644   8871   8964    371   -129   -323       C  
ATOM   2614  O   PHE A1341       8.018 -20.784  71.967  1.00 80.82           O  
ANISOU 2614  O   PHE A1341    10013  10305  10389    297   -111   -343       O  
ATOM   2615  CB  PHE A1341       7.656 -22.140  69.111  1.00 45.63           C  
ANISOU 2615  CB  PHE A1341     5699   5694   5945    417   -144   -352       C  
ATOM   2616  CG  PHE A1341       8.009 -22.056  67.656  1.00 57.57           C  
ANISOU 2616  CG  PHE A1341     7247   7183   7445    480   -137   -368       C  
ATOM   2617  CD1 PHE A1341       8.371 -20.843  67.091  1.00 66.27           C  
ANISOU 2617  CD1 PHE A1341     8268   8347   8563    461   -105   -386       C  
ATOM   2618  CD2 PHE A1341       8.002 -23.187  66.857  1.00 56.28           C  
ANISOU 2618  CD2 PHE A1341     7218   6926   7239    559   -165   -363       C  
ATOM   2619  CE1 PHE A1341       8.710 -20.757  65.752  1.00 66.52           C  
ANISOU 2619  CE1 PHE A1341     8328   8367   8580    523    -94   -394       C  
ATOM   2620  CE2 PHE A1341       8.334 -23.109  65.518  1.00 58.85           C  
ANISOU 2620  CE2 PHE A1341     7596   7227   7538    631   -152   -377       C  
ATOM   2621  CZ  PHE A1341       8.690 -21.893  64.963  1.00 69.14           C  
ANISOU 2621  CZ  PHE A1341     8791   8611   8866    615   -113   -391       C  
ATOM   2622  N   GLY A1342       8.403 -22.975  72.208  1.00 66.47           N  
ANISOU 2622  N   GLY A1342     8279   8444   8534    400   -151   -292       N  
ATOM   2623  CA  GLY A1342       8.134 -22.888  73.638  1.00 86.94           C  
ANISOU 2623  CA  GLY A1342    10842  11070  11120    342   -151   -278       C  
ATOM   2624  C   GLY A1342       6.712 -22.561  74.056  1.00 79.07           C  
ANISOU 2624  C   GLY A1342     9853  10032  10157    267   -144   -280       C  
ATOM   2625  O   GLY A1342       6.515 -21.804  75.013  1.00 63.87           O  
ANISOU 2625  O   GLY A1342     7896   8151   8220    225   -117   -286       O  
ATOM   2626  N   LEU A1343       5.711 -23.078  73.336  1.00 76.58           N  
ANISOU 2626  N   LEU A1343     9584   9639   9874    251   -167   -264       N  
ATOM   2627  CA  LEU A1343       4.320 -22.907  73.755  1.00 55.67           C  
ANISOU 2627  CA  LEU A1343     6916   6983   7253    185   -161   -227       C  
ATOM   2628  C   LEU A1343       4.025 -23.620  75.076  1.00 50.74           C  
ANISOU 2628  C   LEU A1343     6292   6381   6608    165   -171   -176       C  
ATOM   2629  O   LEU A1343       3.172 -23.166  75.850  1.00 50.68           O  
ANISOU 2629  O   LEU A1343     6238   6415   6602    135   -135   -141       O  
ATOM   2630  CB  LEU A1343       3.389 -23.407  72.646  1.00 47.37           C  
ANISOU 2630  CB  LEU A1343     5908   5856   6233    149   -208   -195       C  
ATOM   2631  CG  LEU A1343       1.931 -23.764  72.951  1.00 50.19           C  
ANISOU 2631  CG  LEU A1343     6243   6213   6614     68   -234   -105       C  
ATOM   2632  CD1 LEU A1343       1.131 -22.559  73.457  1.00 42.86           C  
ANISOU 2632  CD1 LEU A1343     5214   5368   5703     63   -158    -82       C  
ATOM   2633  CD2 LEU A1343       1.268 -24.363  71.725  1.00 43.30           C  
ANISOU 2633  CD2 LEU A1343     5437   5259   5757     11   -311    -68       C  
ATOM   2634  N   VAL A1344       4.713 -24.731  75.353  1.00 43.74           N  
ANISOU 2634  N   VAL A1344     5459   5469   5692    196   -211   -163       N  
ATOM   2635  CA  VAL A1344       4.468 -25.451  76.599  1.00 56.74           C  
ANISOU 2635  CA  VAL A1344     7108   7133   7316    174   -225   -110       C  
ATOM   2636  C   VAL A1344       4.865 -24.602  77.803  1.00 60.61           C  
ANISOU 2636  C   VAL A1344     7537   7714   7778    179   -171   -130       C  
ATOM   2637  O   VAL A1344       4.206 -24.651  78.855  1.00 58.45           O  
ANISOU 2637  O   VAL A1344     7243   7475   7490    151   -153    -87       O  
ATOM   2638  CB  VAL A1344       5.203 -26.807  76.574  1.00 70.09           C  
ANISOU 2638  CB  VAL A1344     8891   8767   8974    223   -279    -94       C  
ATOM   2639  CG1 VAL A1344       6.639 -26.634  76.095  1.00 60.67           C  
ANISOU 2639  CG1 VAL A1344     7698   7601   7753    321   -259   -140       C  
ATOM   2640  CG2 VAL A1344       5.163 -27.475  77.947  1.00 69.89           C  
ANISOU 2640  CG2 VAL A1344     8863   8771   8921    206   -290    -44       C  
ATOM   2641  N   ALA A1345       5.916 -23.787  77.668  1.00 48.19           N  
ANISOU 2641  N   ALA A1345     5942   6182   6185    207   -149   -184       N  
ATOM   2642  CA  ALA A1345       6.291 -22.899  78.764  1.00 53.65           C  
ANISOU 2642  CA  ALA A1345     6611   6941   6832    187   -118   -203       C  
ATOM   2643  C   ALA A1345       5.208 -21.861  79.023  1.00 50.39           C  
ANISOU 2643  C   ALA A1345     6199   6529   6419    165    -63   -212       C  
ATOM   2644  O   ALA A1345       4.903 -21.553  80.178  1.00 47.78           O  
ANISOU 2644  O   ALA A1345     5884   6229   6041    160    -32   -199       O  
ATOM   2645  CB  ALA A1345       7.624 -22.217  78.462  1.00 43.35           C  
ANISOU 2645  CB  ALA A1345     5285   5684   5502    192   -128   -238       C  
ATOM   2646  N   LEU A1346       4.593 -21.333  77.964  1.00 43.15           N  
ANISOU 2646  N   LEU A1346     5272   5579   5544    166    -45   -225       N  
ATOM   2647  CA  LEU A1346       3.507 -20.379  78.155  1.00 44.69           C  
ANISOU 2647  CA  LEU A1346     5465   5781   5733    174     18   -216       C  
ATOM   2648  C   LEU A1346       2.297 -21.049  78.789  1.00 46.49           C  
ANISOU 2648  C   LEU A1346     5662   6036   5968    175     37   -126       C  
ATOM   2649  O   LEU A1346       1.632 -20.457  79.646  1.00 47.00           O  
ANISOU 2649  O   LEU A1346     5730   6141   5988    208    104    -98       O  
ATOM   2650  CB  LEU A1346       3.124 -19.742  76.819  1.00 46.28           C  
ANISOU 2650  CB  LEU A1346     5651   5949   5982    177     29   -237       C  
ATOM   2651  CG  LEU A1346       4.184 -18.861  76.161  1.00 54.91           C  
ANISOU 2651  CG  LEU A1346     6768   7029   7066    171     20   -311       C  
ATOM   2652  CD1 LEU A1346       3.749 -18.460  74.757  1.00 46.11           C  
ANISOU 2652  CD1 LEU A1346     5635   5880   6006    174     24   -322       C  
ATOM   2653  CD2 LEU A1346       4.461 -17.632  77.013  1.00 42.76           C  
ANISOU 2653  CD2 LEU A1346     5291   5500   5456    166     56   -350       C  
ATOM   2654  N   GLU A1347       2.012 -22.295  78.400  1.00 43.66           N  
ANISOU 2654  N   GLU A1347     5284   5654   5649    140    -24    -70       N  
ATOM   2655  CA  GLU A1347       0.885 -23.001  78.997  1.00 47.76           C  
ANISOU 2655  CA  GLU A1347     5763   6210   6173    113    -25     41       C  
ATOM   2656  C   GLU A1347       1.101 -23.210  80.488  1.00 56.82           C  
ANISOU 2656  C   GLU A1347     6920   7406   7261    132      1     59       C  
ATOM   2657  O   GLU A1347       0.181 -23.009  81.289  1.00 49.28           O  
ANISOU 2657  O   GLU A1347     5926   6518   6278    151     58    134       O  
ATOM   2658  CB  GLU A1347       0.673 -24.344  78.296  1.00 44.44           C  
ANISOU 2658  CB  GLU A1347     5364   5731   5791     47   -123     96       C  
ATOM   2659  CG  GLU A1347       0.268 -24.226  76.840  1.00 54.00           C  
ANISOU 2659  CG  GLU A1347     6578   6891   7049     16   -158     96       C  
ATOM   2660  CD  GLU A1347       0.216 -25.570  76.140  1.00 55.54           C  
ANISOU 2660  CD  GLU A1347     6853   6994   7255    -50   -269    135       C  
ATOM   2661  OE1 GLU A1347       0.825 -26.535  76.650  1.00 47.36           O  
ANISOU 2661  OE1 GLU A1347     5888   5918   6190    -45   -313    132       O  
ATOM   2662  OE2 GLU A1347      -0.440 -25.661  75.083  1.00 53.18           O  
ANISOU 2662  OE2 GLU A1347     6565   6656   6983   -107   -318    171       O  
ATOM   2663  N   ALA A1348       2.324 -23.577  80.883  1.00 44.51           N  
ANISOU 2663  N   ALA A1348     5409   5828   5676    136    -35      0       N  
ATOM   2664  CA  ALA A1348       2.590 -23.786  82.303  1.00 51.17           C  
ANISOU 2664  CA  ALA A1348     6266   6717   6458    146    -19     17       C  
ATOM   2665  C   ALA A1348       2.578 -22.467  83.069  1.00 45.17           C  
ANISOU 2665  C   ALA A1348     5539   5994   5629    186     59    -25       C  
ATOM   2666  O   ALA A1348       1.985 -22.378  84.149  1.00 45.80           O  
ANISOU 2666  O   ALA A1348     5625   6122   5653    214    111     23       O  
ATOM   2667  CB  ALA A1348       3.923 -24.508  82.490  1.00 44.84           C  
ANISOU 2667  CB  ALA A1348     5498   5898   5642    143    -80    -18       C  
ATOM   2668  N   MET A1349       3.217 -21.429  82.522  1.00 44.82           N  
ANISOU 2668  N   MET A1349     5533   5921   5573    192     67   -109       N  
ATOM   2669  CA  MET A1349       3.314 -20.158  83.230  1.00 45.22           C  
ANISOU 2669  CA  MET A1349     5669   5976   5538    220    122   -157       C  
ATOM   2670  C   MET A1349       1.960 -19.478  83.381  1.00 48.95           C  
ANISOU 2670  C   MET A1349     6148   6465   5987    294    220   -114       C  
ATOM   2671  O   MET A1349       1.712 -18.818  84.395  1.00 46.47           O  
ANISOU 2671  O   MET A1349     5920   6163   5575    349    283   -117       O  
ATOM   2672  CB  MET A1349       4.298 -19.235  82.510  1.00 44.87           C  
ANISOU 2672  CB  MET A1349     5669   5892   5488    187     90   -241       C  
ATOM   2673  CG  MET A1349       5.726 -19.759  82.494  1.00 49.11           C  
ANISOU 2673  CG  MET A1349     6185   6447   6026    130      7   -259       C  
ATOM   2674  SD  MET A1349       6.772 -18.979  81.250  1.00 48.09           S  
ANISOU 2674  SD  MET A1349     6046   6305   5922     88    -37   -311       S  
ATOM   2675  CE  MET A1349       7.221 -17.455  82.077  1.00 45.05           C  
ANISOU 2675  CE  MET A1349     5798   5900   5418     31    -42   -361       C  
ATOM   2676  N   CYS A1350       1.065 -19.643  82.401  1.00 45.49           N  
ANISOU 2676  N   CYS A1350     5626   6034   5625    304    234    -61       N  
ATOM   2677  CA  CYS A1350      -0.264 -19.051  82.527  1.00 46.16           C  
ANISOU 2677  CA  CYS A1350     5687   6167   5687    388    333     14       C  
ATOM   2678  C   CYS A1350      -1.042 -19.669  83.678  1.00 52.59           C  
ANISOU 2678  C   CYS A1350     6458   7066   6458    425    379    125       C  
ATOM   2679  O   CYS A1350      -1.867 -18.994  84.305  1.00 49.86           O  
ANISOU 2679  O   CYS A1350     6133   6773   6038    533    486    179       O  
ATOM   2680  CB  CYS A1350      -1.044 -19.208  81.221  1.00 54.47           C  
ANISOU 2680  CB  CYS A1350     6637   7227   6833    369    320     73       C  
ATOM   2681  SG  CYS A1350      -0.460 -18.155  79.878  1.00 65.84           S  
ANISOU 2681  SG  CYS A1350     8126   8585   8307    362    306    -38       S  
ATOM   2682  N   LEU A1351      -0.783 -20.939  83.977  1.00 46.89           N  
ANISOU 2682  N   LEU A1351     5686   6359   5771    349    303    166       N  
ATOM   2683  CA  LEU A1351      -1.452 -21.655  85.052  1.00 47.72           C  
ANISOU 2683  CA  LEU A1351     5743   6548   5841    362    330    281       C  
ATOM   2684  C   LEU A1351      -0.688 -21.589  86.370  1.00 51.37           C  
ANISOU 2684  C   LEU A1351     6304   7006   6207    385    342    226       C  
ATOM   2685  O   LEU A1351      -1.038 -22.305  87.313  1.00 51.37           O  
ANISOU 2685  O   LEU A1351     6271   7070   6176    386    352    311       O  
ATOM   2686  CB  LEU A1351      -1.682 -23.111  84.647  1.00 47.60           C  
ANISOU 2686  CB  LEU A1351     5639   6539   5908    255    230    370       C  
ATOM   2687  CG  LEU A1351      -2.957 -23.408  83.851  1.00 52.72           C  
ANISOU 2687  CG  LEU A1351     6169   7244   6619    217    222    509       C  
ATOM   2688  CD1 LEU A1351      -4.181 -22.954  84.633  1.00 49.23           C  
ANISOU 2688  CD1 LEU A1351     5643   6941   6120    307    339    652       C  
ATOM   2689  CD2 LEU A1351      -2.935 -22.774  82.472  1.00 47.38           C  
ANISOU 2689  CD2 LEU A1351     5492   6510   5999    211    209    450       C  
ATOM   2690  N   GLY A1352       0.357 -20.768  86.446  1.00 47.71           N  
ANISOU 2690  N   GLY A1352     5962   6474   5694    388    331     96       N  
ATOM   2691  CA  GLY A1352       1.080 -20.545  87.678  1.00 48.19           C  
ANISOU 2691  CA  GLY A1352     6136   6528   5647    396    332     47       C  
ATOM   2692  C   GLY A1352       2.168 -21.547  87.992  1.00 50.01           C  
ANISOU 2692  C   GLY A1352     6350   6752   5900    306    228     29       C  
ATOM   2693  O   GLY A1352       2.834 -21.402  89.024  1.00 51.63           O  
ANISOU 2693  O   GLY A1352     6641   6960   6015    295    215     -3       O  
ATOM   2694  N   ALA A1353       2.371 -22.555  87.151  1.00 49.26           N  
ANISOU 2694  N   ALA A1353     6161   6645   5909    248    155     53       N  
ATOM   2695  CA  ALA A1353       3.525 -23.427  87.311  1.00 54.90           C  
ANISOU 2695  CA  ALA A1353     6873   7348   6638    192     65     34       C  
ATOM   2696  C   ALA A1353       4.799 -22.673  86.952  1.00 56.81           C  
ANISOU 2696  C   ALA A1353     7166   7562   6858    163     24    -60       C  
ATOM   2697  O   ALA A1353       4.820 -21.865  86.020  1.00 48.12           O  
ANISOU 2697  O   ALA A1353     6074   6426   5784    165     35   -109       O  
ATOM   2698  CB  ALA A1353       3.378 -24.673  86.438  1.00 46.48           C  
ANISOU 2698  CB  ALA A1353     5736   6255   5668    160      3     85       C  
ATOM   2699  N   ILE A1354       5.868 -22.934  87.696  1.00 49.82           N  
ANISOU 2699  N   ILE A1354     6306   6702   5923    128    -30    -69       N  
ATOM   2700  CA  ILE A1354       7.148 -22.267  87.485  1.00 52.10           C  
ANISOU 2700  CA  ILE A1354     6622   6994   6179     78    -85   -123       C  
ATOM   2701  C   ILE A1354       7.989 -23.142  86.558  1.00 46.74           C  
ANISOU 2701  C   ILE A1354     5852   6328   5577     77   -143   -102       C  
ATOM   2702  O   ILE A1354       8.263 -24.301  86.906  1.00 50.22           O  
ANISOU 2702  O   ILE A1354     6257   6792   6031     95   -173    -50       O  
ATOM   2703  CB  ILE A1354       7.875 -22.008  88.808  1.00 51.69           C  
ANISOU 2703  CB  ILE A1354     6643   6980   6016     30   -119   -122       C  
ATOM   2704  CG1 ILE A1354       7.000 -21.156  89.734  1.00 48.26           C  
ANISOU 2704  CG1 ILE A1354     6337   6518   5481     59    -49   -144       C  
ATOM   2705  CG2 ILE A1354       9.206 -21.322  88.554  1.00 47.79           C  
ANISOU 2705  CG2 ILE A1354     6162   6509   5486    -53   -196   -147       C  
ATOM   2706  CD1 ILE A1354       7.560 -21.004  91.131  1.00 58.96           C  
ANISOU 2706  CD1 ILE A1354     7794   7897   6709     15    -84   -141       C  
ATOM   2707  N   PRO A1355       8.364 -22.660  85.376  1.00 45.95           N  
ANISOU 2707  N   PRO A1355     5727   6211   5522     74   -154   -136       N  
ATOM   2708  CA  PRO A1355       9.168 -23.484  84.463  1.00 55.11           C  
ANISOU 2708  CA  PRO A1355     6816   7386   6737    105   -194   -110       C  
ATOM   2709  C   PRO A1355      10.582 -23.744  84.968  1.00 47.47           C  
ANISOU 2709  C   PRO A1355     5808   6508   5722     88   -250    -67       C  
ATOM   2710  O   PRO A1355      11.226 -22.878  85.568  1.00 46.67           O  
ANISOU 2710  O   PRO A1355     5724   6458   5552     12   -281    -71       O  
ATOM   2711  CB  PRO A1355       9.175 -22.666  83.167  1.00 45.14           C  
ANISOU 2711  CB  PRO A1355     5541   6094   5516    104   -181   -155       C  
ATOM   2712  CG  PRO A1355       9.022 -21.250  83.625  1.00 63.40           C  
ANISOU 2712  CG  PRO A1355     7920   8400   7769     43   -165   -202       C  
ATOM   2713  CD  PRO A1355       8.182 -21.284  84.879  1.00 45.75           C  
ANISOU 2713  CD  PRO A1355     5750   6153   5480     48   -129   -195       C  
ATOM   2714  N   ILE A1356      11.075 -24.942  84.662  1.00 47.09           N  
ANISOU 2714  N   ILE A1356     5715   6477   5701    160   -268    -15       N  
ATOM   2715  CA  ILE A1356      12.483 -25.308  84.786  1.00 46.94           C  
ANISOU 2715  CA  ILE A1356     5626   6562   5648    183   -310     52       C  
ATOM   2716  C   ILE A1356      12.871 -25.890  83.435  1.00 48.45           C  
ANISOU 2716  C   ILE A1356     5783   6740   5884    290   -296     69       C  
ATOM   2717  O   ILE A1356      12.479 -27.018  83.107  1.00 48.15           O  
ANISOU 2717  O   ILE A1356     5793   6628   5872    378   -285     80       O  
ATOM   2718  CB  ILE A1356      12.743 -26.322  85.909  1.00 47.53           C  
ANISOU 2718  CB  ILE A1356     5701   6674   5685    207   -332    114       C  
ATOM   2719  CG1 ILE A1356      12.149 -25.843  87.233  1.00 47.69           C  
ANISOU 2719  CG1 ILE A1356     5779   6688   5653    119   -334     91       C  
ATOM   2720  CG2 ILE A1356      14.237 -26.584  86.052  1.00 48.37           C  
ANISOU 2720  CG2 ILE A1356     5714   6916   5749    236   -373    205       C  
ATOM   2721  CD1 ILE A1356      12.410 -26.790  88.388  1.00 48.30           C  
ANISOU 2721  CD1 ILE A1356     5856   6807   5690    133   -359    155       C  
ATOM   2722  N   ALA A1357      13.639 -25.137  82.653  1.00 46.88           N  
ANISOU 2722  N   ALA A1357     5520   6608   5684    281   -301     77       N  
ATOM   2723  CA  ALA A1357      13.773 -25.457  81.240  1.00 52.45           C  
ANISOU 2723  CA  ALA A1357     6217   7285   6429    384   -272     75       C  
ATOM   2724  C   ALA A1357      15.203 -25.283  80.757  1.00 53.94           C  
ANISOU 2724  C   ALA A1357     6289   7622   6584    433   -281    162       C  
ATOM   2725  O   ALA A1357      15.996 -24.529  81.333  1.00 47.97           O  
ANISOU 2725  O   ALA A1357     5451   6990   5786    335   -323    215       O  
ATOM   2726  CB  ALA A1357      12.841 -24.593  80.382  1.00 45.84           C  
ANISOU 2726  CB  ALA A1357     5422   6355   5640    334   -248    -11       C  
ATOM   2727  N   SER A1358      15.523 -26.013  79.692  1.00 47.65           N  
ANISOU 2727  N   SER A1358     5496   6814   5795    585   -245    190       N  
ATOM   2728  CA  SER A1358      16.757 -25.765  78.965  1.00 48.41           C  
ANISOU 2728  CA  SER A1358     5471   7060   5861    656   -232    281       C  
ATOM   2729  C   SER A1358      16.703 -24.384  78.330  1.00 49.38           C  
ANISOU 2729  C   SER A1358     5549   7205   6009    536   -242    243       C  
ATOM   2730  O   SER A1358      15.651 -23.941  77.857  1.00 50.85           O  
ANISOU 2730  O   SER A1358     5823   7255   6243    487   -229    136       O  
ATOM   2731  CB  SER A1358      16.969 -26.827  77.889  1.00 48.83           C  
ANISOU 2731  CB  SER A1358     5580   7070   5902    873   -176    307       C  
ATOM   2732  OG  SER A1358      16.893 -28.135  78.422  1.00 52.43           O  
ANISOU 2732  OG  SER A1358     6125   7466   6330    986   -170    332       O  
ATOM   2733  N   ALA A1359      17.847 -23.702  78.316  1.00 48.76           N  
ANISOU 2733  N   ALA A1359     5329   7306   5892    484   -271    345       N  
ATOM   2734  CA  ALA A1359      17.935 -22.371  77.721  1.00 62.92           C  
ANISOU 2734  CA  ALA A1359     7082   9128   7697    357   -294    328       C  
ATOM   2735  C   ALA A1359      18.217 -22.527  76.230  1.00 60.28           C  
ANISOU 2735  C   ALA A1359     6709   8816   7379    498   -234    351       C  
ATOM   2736  O   ALA A1359      19.334 -22.333  75.746  1.00 54.84           O  
ANISOU 2736  O   ALA A1359     5877   8305   6655    536   -232    479       O  
ATOM   2737  CB  ALA A1359      19.000 -21.537  78.420  1.00 49.61           C  
ANISOU 2737  CB  ALA A1359     5276   7621   5953    198   -375    442       C  
ATOM   2738  N   VAL A1360      17.170 -22.896  75.491  1.00 51.89           N  
ANISOU 2738  N   VAL A1360     5775   7577   6363    574   -188    238       N  
ATOM   2739  CA  VAL A1360      17.232 -23.007  74.038  1.00 56.39           C  
ANISOU 2739  CA  VAL A1360     6354   8128   6943    699   -135    233       C  
ATOM   2740  C   VAL A1360      15.988 -22.363  73.442  1.00 55.83           C  
ANISOU 2740  C   VAL A1360     6389   7890   6934    615   -133     99       C  
ATOM   2741  O   VAL A1360      14.893 -22.457  74.010  1.00 58.08           O  
ANISOU 2741  O   VAL A1360     6775   8041   7253    549   -147     11       O  
ATOM   2742  CB  VAL A1360      17.358 -24.475  73.563  1.00 48.19           C  
ANISOU 2742  CB  VAL A1360     5395   7042   5872    932    -79    259       C  
ATOM   2743  CG1 VAL A1360      18.676 -25.087  74.023  1.00 49.61           C  
ANISOU 2743  CG1 VAL A1360     5455   7413   5983   1055    -63    416       C  
ATOM   2744  CG2 VAL A1360      16.180 -25.311  74.046  1.00 47.53           C  
ANISOU 2744  CG2 VAL A1360     5482   6761   5814    929    -92    161       C  
ATOM   2745  N   GLY A1361      16.173 -21.676  72.316  1.00 55.78           N  
ANISOU 2745  N   GLY A1361     6345   7910   6938    619   -114    100       N  
ATOM   2746  CA  GLY A1361      15.062 -21.250  71.480  1.00 45.37           C  
ANISOU 2746  CA  GLY A1361     5124   6441   5673    586   -101    -10       C  
ATOM   2747  C   GLY A1361      14.039 -20.395  72.203  1.00 52.62           C  
ANISOU 2747  C   GLY A1361     6096   7266   6631    421   -133    -97       C  
ATOM   2748  O   GLY A1361      14.363 -19.452  72.947  1.00 64.12           O  
ANISOU 2748  O   GLY A1361     7509   8785   8070    288   -172    -81       O  
ATOM   2749  N   GLY A1362      12.768 -20.745  71.986  1.00 44.50           N  
ANISOU 2749  N   GLY A1362     5177   6085   5645    432   -120   -179       N  
ATOM   2750  CA  GLY A1362      11.687 -19.972  72.566  1.00 49.79           C  
ANISOU 2750  CA  GLY A1362     5896   6676   6348    315   -130   -246       C  
ATOM   2751  C   GLY A1362      11.661 -20.034  74.078  1.00 53.76           C  
ANISOU 2751  C   GLY A1362     6406   7200   6821    254   -152   -235       C  
ATOM   2752  O   GLY A1362      11.201 -19.093  74.729  1.00 59.24           O  
ANISOU 2752  O   GLY A1362     7131   7870   7506    158   -158   -271       O  
ATOM   2753  N   LEU A1363      12.164 -21.130  74.658  1.00 48.01           N  
ANISOU 2753  N   LEU A1363     5664   6511   6067    319   -161   -185       N  
ATOM   2754  CA  LEU A1363      12.256 -21.217  76.112  1.00 48.12           C  
ANISOU 2754  CA  LEU A1363     5680   6559   6046    261   -185   -166       C  
ATOM   2755  C   LEU A1363      13.184 -20.141  76.659  1.00 56.67           C  
ANISOU 2755  C   LEU A1363     6705   7748   7079    151   -225   -131       C  
ATOM   2756  O   LEU A1363      12.845 -19.441  77.622  1.00 55.70           O  
ANISOU 2756  O   LEU A1363     6637   7601   6925     50   -245   -161       O  
ATOM   2757  CB  LEU A1363      12.751 -22.603  76.529  1.00 46.20           C  
ANISOU 2757  CB  LEU A1363     5428   6346   5779    360   -190   -107       C  
ATOM   2758  CG  LEU A1363      11.922 -23.828  76.140  1.00 47.96           C  
ANISOU 2758  CG  LEU A1363     5745   6448   6028    450   -176   -127       C  
ATOM   2759  CD1 LEU A1363      12.651 -25.096  76.546  1.00 45.28           C  
ANISOU 2759  CD1 LEU A1363     5415   6143   5647    559   -183    -59       C  
ATOM   2760  CD2 LEU A1363      10.544 -23.769  76.783  1.00 44.02           C  
ANISOU 2760  CD2 LEU A1363     5309   5856   5560    371   -178   -172       C  
ATOM   2761  N   ARG A1364      14.358 -19.984  76.037  1.00 54.79           N  
ANISOU 2761  N   ARG A1364     6367   7630   6821    168   -240    -57       N  
ATOM   2762  CA  ARG A1364      15.277 -18.929  76.444  1.00 58.01           C  
ANISOU 2762  CA  ARG A1364     6716   8148   7177     31   -300      1       C  
ATOM   2763  C   ARG A1364      14.688 -17.550  76.182  1.00 63.12           C  
ANISOU 2763  C   ARG A1364     7444   8710   7829    -87   -313    -75       C  
ATOM   2764  O   ARG A1364      14.927 -16.618  76.959  1.00 62.10           O  
ANISOU 2764  O   ARG A1364     7366   8589   7642   -231   -373    -71       O  
ATOM   2765  CB  ARG A1364      16.608 -19.094  75.709  1.00 50.33           C  
ANISOU 2765  CB  ARG A1364     5593   7347   6184     82   -308    126       C  
ATOM   2766  CG  ARG A1364      17.796 -18.343  76.304  1.00 66.95           C  
ANISOU 2766  CG  ARG A1364     7599   9618   8222    -68   -393    244       C  
ATOM   2767  CD  ARG A1364      19.028 -18.516  75.413  1.00 85.06           C  
ANISOU 2767  CD  ARG A1364     9714  12106  10498      5   -384    394       C  
ATOM   2768  NE  ARG A1364      20.248 -17.952  75.989  1.00100.31           N  
ANISOU 2768  NE  ARG A1364    11515  14236  12361   -146   -477    551       N  
ATOM   2769  CZ  ARG A1364      21.234 -18.675  76.515  1.00102.57           C  
ANISOU 2769  CZ  ARG A1364    11664  14705  12603    -93   -492    703       C  
ATOM   2770  NH1 ARG A1364      21.151 -19.997  76.541  1.00101.79           N  
ANISOU 2770  NH1 ARG A1364    11561  14597  12517    123   -414    704       N  
ATOM   2771  NH2 ARG A1364      22.308 -18.076  77.013  1.00 94.98           N  
ANISOU 2771  NH2 ARG A1364    10575  13935  11577   -261   -594    864       N  
ATOM   2772  N   ASP A1365      13.906 -17.401  75.107  1.00 53.70           N  
ANISOU 2772  N   ASP A1365     6285   7424   6693    -28   -262   -141       N  
ATOM   2773  CA  ASP A1365      13.305 -16.097  74.831  1.00 68.28           C  
ANISOU 2773  CA  ASP A1365     8215   9185   8542   -120   -266   -208       C  
ATOM   2774  C   ASP A1365      12.215 -15.726  75.835  1.00 69.67           C  
ANISOU 2774  C   ASP A1365     8528   9246   8699   -154   -251   -284       C  
ATOM   2775  O   ASP A1365      12.063 -14.546  76.170  1.00 68.13           O  
ANISOU 2775  O   ASP A1365     8433   8998   8455   -250   -275   -318       O  
ATOM   2776  CB  ASP A1365      12.748 -16.064  73.410  1.00 60.35           C  
ANISOU 2776  CB  ASP A1365     7203   8124   7602    -43   -216   -247       C  
ATOM   2777  CG  ASP A1365      13.836 -16.168  72.361  1.00 77.25           C  
ANISOU 2777  CG  ASP A1365     9226  10382   9744     -6   -222   -169       C  
ATOM   2778  OD1 ASP A1365      14.974 -15.729  72.643  1.00 74.38           O  
ANISOU 2778  OD1 ASP A1365     8784  10147   9330    -90   -276    -81       O  
ATOM   2779  OD2 ASP A1365      13.556 -16.692  71.262  1.00 89.38           O  
ANISOU 2779  OD2 ASP A1365    10750  11888  11321    105   -175   -185       O  
ATOM   2780  N   ILE A1366      11.455 -16.701  76.326  1.00 65.01           N  
ANISOU 2780  N   ILE A1366     7955   8613   8134    -72   -212   -303       N  
ATOM   2781  CA  ILE A1366      10.297 -16.417  77.174  1.00 64.72           C  
ANISOU 2781  CA  ILE A1366     8027   8484   8079    -73   -177   -357       C  
ATOM   2782  C   ILE A1366      10.687 -16.341  78.642  1.00 63.78           C  
ANISOU 2782  C   ILE A1366     7964   8394   7877   -137   -214   -340       C  
ATOM   2783  O   ILE A1366      10.413 -15.350  79.324  1.00 66.60           O  
ANISOU 2783  O   ILE A1366     8448   8696   8163   -197   -220   -377       O  
ATOM   2784  CB  ILE A1366       9.200 -17.479  76.948  1.00 58.38           C  
ANISOU 2784  CB  ILE A1366     7208   7633   7342     26   -124   -364       C  
ATOM   2785  CG1 ILE A1366       8.625 -17.373  75.535  1.00 59.45           C  
ANISOU 2785  CG1 ILE A1366     7322   7721   7545     69    -95   -385       C  
ATOM   2786  CG2 ILE A1366       8.105 -17.345  77.998  1.00 57.04           C  
ANISOU 2786  CG2 ILE A1366     7116   7414   7144     36    -84   -381       C  
ATOM   2787  CD1 ILE A1366       7.725 -18.532  75.163  1.00 62.50           C  
ANISOU 2787  CD1 ILE A1366     7695   8066   7988    136    -76   -370       C  
ATOM   2788  N   ILE A1367      11.315 -17.398  79.152  1.00 54.38           N  
ANISOU 2788  N   ILE A1367     6699   7280   6681   -115   -240   -284       N  
ATOM   2789  CA  ILE A1367      11.690 -17.447  80.555  1.00 56.56           C  
ANISOU 2789  CA  ILE A1367     7021   7591   6879   -175   -280   -261       C  
ATOM   2790  C   ILE A1367      12.790 -16.433  80.833  1.00 62.37           C  
ANISOU 2790  C   ILE A1367     7781   8382   7533   -318   -366   -228       C  
ATOM   2791  O   ILE A1367      13.719 -16.255  80.034  1.00 62.89           O  
ANISOU 2791  O   ILE A1367     7748   8532   7614   -356   -407   -172       O  
ATOM   2792  CB  ILE A1367      12.121 -18.875  80.928  1.00 54.73           C  
ANISOU 2792  CB  ILE A1367     6697   7432   6667   -109   -287   -198       C  
ATOM   2793  CG1 ILE A1367      10.972 -19.848  80.652  1.00 44.90           C  
ANISOU 2793  CG1 ILE A1367     5457   6112   5491      0   -223   -223       C  
ATOM   2794  CG2 ILE A1367      12.553 -18.950  82.381  1.00 46.41           C  
ANISOU 2794  CG2 ILE A1367     5680   6423   5529   -175   -333   -165       C  
ATOM   2795  CD1 ILE A1367      11.383 -21.290  80.660  1.00 44.98           C  
ANISOU 2795  CD1 ILE A1367     5403   6164   5524     81   -231   -165       C  
ATOM   2796  N   THR A1368      12.684 -15.758  81.970  1.00 58.99           N  
ANISOU 2796  N   THR A1368     7496   7910   7008   -404   -400   -252       N  
ATOM   2797  CA  THR A1368      13.699 -14.840  82.460  1.00 63.66           C  
ANISOU 2797  CA  THR A1368     8151   8540   7497   -575   -510   -211       C  
ATOM   2798  C   THR A1368      14.156 -15.308  83.837  1.00 70.26           C  
ANISOU 2798  C   THR A1368     9012   9431   8253   -628   -565   -165       C  
ATOM   2799  O   THR A1368      13.626 -16.271  84.398  1.00 65.46           O  
ANISOU 2799  O   THR A1368     8380   8821   7671   -525   -508   -174       O  
ATOM   2800  CB  THR A1368      13.167 -13.404  82.519  1.00 66.06           C  
ANISOU 2800  CB  THR A1368     8671   8705   7724   -645   -518   -289       C  
ATOM   2801  OG1 THR A1368      12.183 -13.295  83.556  1.00 65.64           O  
ANISOU 2801  OG1 THR A1368     8792   8546   7604   -584   -461   -357       O  
ATOM   2802  CG2 THR A1368      12.538 -13.009  81.187  1.00 58.19           C  
ANISOU 2802  CG2 THR A1368     7649   7648   6813   -570   -449   -337       C  
ATOM   2803  N   ASN A1369      15.151 -14.609  84.386  1.00 77.65           N  
ANISOU 2803  N   ASN A1369    10001  10417   9085   -807   -687   -106       N  
ATOM   2804  CA  ASN A1369      15.660 -14.971  85.704  1.00 78.20           C  
ANISOU 2804  CA  ASN A1369    10102  10544   9066   -881   -757    -53       C  
ATOM   2805  C   ASN A1369      14.577 -14.853  86.770  1.00 83.53           C  
ANISOU 2805  C   ASN A1369    10987  11081   9671   -825   -699   -151       C  
ATOM   2806  O   ASN A1369      14.606 -15.579  87.771  1.00 72.05           O  
ANISOU 2806  O   ASN A1369     9527   9666   8184   -804   -702   -125       O  
ATOM   2807  CB  ASN A1369      16.857 -14.084  86.054  1.00 77.50           C  
ANISOU 2807  CB  ASN A1369    10059  10524   8864  -1118   -920     36       C  
ATOM   2808  CG  ASN A1369      17.667 -14.624  87.213  1.00 69.72           C  
ANISOU 2808  CG  ASN A1369     9032   9654   7802  -1208  -1011    135       C  
ATOM   2809  OD1 ASN A1369      17.540 -15.790  87.585  1.00 71.89           O  
ANISOU 2809  OD1 ASN A1369     9195   9992   8130  -1079   -950    155       O  
ATOM   2810  ND2 ASN A1369      18.512 -13.777  87.788  1.00 74.20           N  
ANISOU 2810  ND2 ASN A1369     9701  10251   8240  -1442  -1169    206       N  
ATOM   2811  N   GLU A1370      13.621 -13.947  86.573  1.00 80.35           N  
ANISOU 2811  N   GLU A1370    10766  10524   9237   -787   -640   -252       N  
ATOM   2812  CA  GLU A1370      12.542 -13.718  87.523  1.00 72.13           C  
ANISOU 2812  CA  GLU A1370     9932   9360   8114   -703   -565   -331       C  
ATOM   2813  C   GLU A1370      11.299 -14.555  87.245  1.00 60.94           C  
ANISOU 2813  C   GLU A1370     8421   7929   6805   -500   -416   -363       C  
ATOM   2814  O   GLU A1370      10.355 -14.509  88.039  1.00 59.59           O  
ANISOU 2814  O   GLU A1370     8379   7691   6572   -407   -337   -402       O  
ATOM   2815  CB  GLU A1370      12.161 -12.231  87.539  1.00 83.89           C  
ANISOU 2815  CB  GLU A1370    11699  10690   9485   -751   -575   -408       C  
ATOM   2816  CG  GLU A1370      13.298 -11.287  87.938  1.00 98.88           C  
ANISOU 2816  CG  GLU A1370    13753  12571  11244   -987   -746   -373       C  
ATOM   2817  CD  GLU A1370      14.361 -11.147  86.857  1.00118.63           C  
ANISOU 2817  CD  GLU A1370    16069  15183  13823  -1121   -842   -292       C  
ATOM   2818  OE1 GLU A1370      14.050 -11.423  85.677  1.00119.96           O  
ANISOU 2818  OE1 GLU A1370    16066  15382  14130  -1015   -761   -300       O  
ATOM   2819  OE2 GLU A1370      15.507 -10.778  87.191  1.00126.21           O  
ANISOU 2819  OE2 GLU A1370    17048  16209  14698  -1335  -1001   -206       O  
ATOM   2820  N   THR A1371      11.265 -15.314  86.144  1.00 57.25           N  
ANISOU 2820  N   THR A1371     7743   7525   6485   -430   -378   -337       N  
ATOM   2821  CA  THR A1371      10.060 -16.044  85.760  1.00 58.91           C  
ANISOU 2821  CA  THR A1371     7878   7713   6792   -272   -261   -355       C  
ATOM   2822  C   THR A1371      10.323 -17.529  85.532  1.00 63.54           C  
ANISOU 2822  C   THR A1371     8270   8392   7480   -220   -261   -293       C  
ATOM   2823  O   THR A1371       9.514 -18.198  84.881  1.00 61.58           O  
ANISOU 2823  O   THR A1371     7942   8128   7326   -122   -195   -293       O  
ATOM   2824  CB  THR A1371       9.426 -15.429  84.509  1.00 55.53           C  
ANISOU 2824  CB  THR A1371     7444   7223   6433   -220   -205   -397       C  
ATOM   2825  OG1 THR A1371      10.392 -15.382  83.452  1.00 67.61           O  
ANISOU 2825  OG1 THR A1371     8859   8807   8023   -288   -269   -371       O  
ATOM   2826  CG2 THR A1371       8.926 -14.021  84.798  1.00 51.98           C  
ANISOU 2826  CG2 THR A1371     7217   6658   5874   -228   -180   -460       C  
ATOM   2827  N   GLY A1372      11.424 -18.057  86.042  1.00 60.67           N  
ANISOU 2827  N   GLY A1372     7841   8120   7089   -286   -340   -232       N  
ATOM   2828  CA  GLY A1372      11.701 -19.472  85.906  1.00 53.52           C  
ANISOU 2828  CA  GLY A1372     6786   7290   6259   -216   -337   -170       C  
ATOM   2829  C   GLY A1372      13.152 -19.771  86.211  1.00 57.59           C  
ANISOU 2829  C   GLY A1372     7213   7930   6738   -289   -428    -85       C  
ATOM   2830  O   GLY A1372      13.933 -18.891  86.571  1.00 65.43           O  
ANISOU 2830  O   GLY A1372     8253   8959   7648   -420   -508    -64       O  
ATOM   2831  N   ILE A1373      13.496 -21.050  86.062  1.00 56.82           N  
ANISOU 2831  N   ILE A1373     6995   7899   6696   -203   -421    -22       N  
ATOM   2832  CA  ILE A1373      14.866 -21.519  86.234  1.00 55.96           C  
ANISOU 2832  CA  ILE A1373     6767   7934   6562   -228   -489     86       C  
ATOM   2833  C   ILE A1373      15.336 -22.124  84.916  1.00 60.40           C  
ANISOU 2833  C   ILE A1373     7202   8545   7201   -119   -461    131       C  
ATOM   2834  O   ILE A1373      14.653 -22.979  84.339  1.00 61.93           O  
ANISOU 2834  O   ILE A1373     7401   8665   7462      6   -398    100       O  
ATOM   2835  CB  ILE A1373      14.978 -22.533  87.387  1.00 49.33           C  
ANISOU 2835  CB  ILE A1373     5918   7134   5689   -197   -501    137       C  
ATOM   2836  CG1 ILE A1373      14.357 -21.960  88.665  1.00 49.67           C  
ANISOU 2836  CG1 ILE A1373     6111   7115   5648   -281   -511     84       C  
ATOM   2837  CG2 ILE A1373      16.430 -22.903  87.630  1.00 50.35           C  
ANISOU 2837  CG2 ILE A1373     5918   7434   5780   -224   -573    269       C  
ATOM   2838  CD1 ILE A1373      14.207 -22.971  89.781  1.00 54.07           C  
ANISOU 2838  CD1 ILE A1373     6672   7693   6179   -240   -508    122       C  
ATOM   2839  N   LEU A1374      16.495 -21.672  84.439  1.00 52.37           N  
ANISOU 2839  N   LEU A1374     6081   7655   6163   -170   -512    213       N  
ATOM   2840  CA  LEU A1374      17.039 -22.080  83.152  1.00 50.18           C  
ANISOU 2840  CA  LEU A1374     5687   7442   5938    -57   -478    267       C  
ATOM   2841  C   LEU A1374      18.360 -22.809  83.348  1.00 50.30           C  
ANISOU 2841  C   LEU A1374     5551   7645   5917      0   -507    424       C  
ATOM   2842  O   LEU A1374      19.181 -22.415  84.182  1.00 51.34           O  
ANISOU 2842  O   LEU A1374     5626   7901   5979   -126   -589    516       O  
ATOM   2843  CB  LEU A1374      17.244 -20.869  82.237  1.00 49.11           C  
ANISOU 2843  CB  LEU A1374     5535   7316   5808   -144   -496    252       C  
ATOM   2844  CG  LEU A1374      15.984 -20.174  81.719  1.00 54.22           C  
ANISOU 2844  CG  LEU A1374     6312   7789   6498   -157   -450    112       C  
ATOM   2845  CD1 LEU A1374      16.344 -18.937  80.903  1.00 48.19           C  
ANISOU 2845  CD1 LEU A1374     5536   7047   5728   -257   -481    113       C  
ATOM   2846  CD2 LEU A1374      15.152 -21.137  80.892  1.00 47.09           C  
ANISOU 2846  CD2 LEU A1374     5423   6793   5677      8   -365     60       C  
ATOM   2847  N   VAL A1375      18.575 -23.859  82.555  1.00 51.73           N  
ANISOU 2847  N   VAL A1375     5675   7846   6133    194   -442    466       N  
ATOM   2848  CA  VAL A1375      19.788 -24.664  82.632  1.00 51.52           C  
ANISOU 2848  CA  VAL A1375     5507   8001   6067    307   -444    628       C  
ATOM   2849  C   VAL A1375      20.285 -24.971  81.224  1.00 52.04           C  
ANISOU 2849  C   VAL A1375     5497   8125   6151    479   -377    684       C  
ATOM   2850  O   VAL A1375      19.576 -24.798  80.232  1.00 52.18           O  
ANISOU 2850  O   VAL A1375     5594   8013   6218    523   -330    582       O  
ATOM   2851  CB  VAL A1375      19.583 -25.978  83.416  1.00 53.60           C  
ANISOU 2851  CB  VAL A1375     5823   8221   6321    425   -421    640       C  
ATOM   2852  CG1 VAL A1375      19.273 -25.692  84.870  1.00 51.69           C  
ANISOU 2852  CG1 VAL A1375     5636   7960   6044    264   -486    612       C  
ATOM   2853  CG2 VAL A1375      18.485 -26.817  82.777  1.00 51.77           C  
ANISOU 2853  CG2 VAL A1375     5737   7787   6145    563   -350    525       C  
ATOM   2854  N   LYS A1376      21.542 -25.405  81.156  1.00 55.08           N  
ANISOU 2854  N   LYS A1376     5720   8720   6486    582   -372    863       N  
ATOM   2855  CA  LYS A1376      22.110 -25.898  79.910  1.00 56.46           C  
ANISOU 2855  CA  LYS A1376     5828   8969   6654    802   -288    942       C  
ATOM   2856  C   LYS A1376      21.424 -27.193  79.490  1.00 63.32           C  
ANISOU 2856  C   LYS A1376     6867   9655   7538   1029   -206    857       C  
ATOM   2857  O   LYS A1376      21.209 -28.093  80.306  1.00 62.70           O  
ANISOU 2857  O   LYS A1376     6863   9514   7444   1083   -210    851       O  
ATOM   2858  CB  LYS A1376      23.611 -26.126  80.083  1.00 69.30           C  
ANISOU 2858  CB  LYS A1376     7232  10889   8210    881   -294   1182       C  
ATOM   2859  CG  LYS A1376      24.363 -26.519  78.826  1.00 87.88           C  
ANISOU 2859  CG  LYS A1376     9488  13368  10533   1127   -197   1301       C  
ATOM   2860  CD  LYS A1376      25.806 -26.855  79.169  1.00104.37           C  
ANISOU 2860  CD  LYS A1376    11340  15771  12544   1225   -194   1568       C  
ATOM   2861  CE  LYS A1376      26.415 -25.788  80.070  1.00114.40           C  
ANISOU 2861  CE  LYS A1376    12440  17229  13796    919   -331   1682       C  
ATOM   2862  NZ  LYS A1376      27.681 -26.241  80.711  1.00112.60           N  
ANISOU 2862  NZ  LYS A1376    11991  17299  13494    982   -351   1946       N  
ATOM   2863  N   ALA A1377      21.096 -27.292  78.204  1.00 69.18           N  
ANISOU 2863  N   ALA A1377     7684  10303   8300   1152   -142    797       N  
ATOM   2864  CA  ALA A1377      20.453 -28.493  77.689  1.00 56.10           C  
ANISOU 2864  CA  ALA A1377     6225   8453   6639   1349    -82    720       C  
ATOM   2865  C   ALA A1377      21.418 -29.675  77.707  1.00 59.43           C  
ANISOU 2865  C   ALA A1377     6626   8976   6977   1614    -22    865       C  
ATOM   2866  O   ALA A1377      22.620 -29.522  77.473  1.00 69.89           O  
ANISOU 2866  O   ALA A1377     7768  10539   8250   1715     11   1033       O  
ATOM   2867  CB  ALA A1377      19.941 -28.254  76.270  1.00 59.53           C  
ANISOU 2867  CB  ALA A1377     6752   8769   7097   1408    -37    632       C  
ATOM   2868  N   GLY A1378      20.884 -30.861  77.990  1.00 62.94           N  
ANISOU 2868  N   GLY A1378     7263   9247   7403   1730    -10    812       N  
ATOM   2869  CA  GLY A1378      21.666 -32.077  77.907  1.00 61.48           C  
ANISOU 2869  CA  GLY A1378     7124   9108   7127   2017     56    931       C  
ATOM   2870  C   GLY A1378      22.590 -32.354  79.070  1.00 71.95           C  
ANISOU 2870  C   GLY A1378     8289  10638   8413   2036     39   1088       C  
ATOM   2871  O   GLY A1378      23.473 -33.210  78.943  1.00 70.91           O  
ANISOU 2871  O   GLY A1378     8141  10608   8195   2300    108   1229       O  
ATOM   2872  N   ASP A1379      22.421 -31.667  80.201  1.00 70.08           N  
ANISOU 2872  N   ASP A1379     7943  10462   8223   1777    -49   1074       N  
ATOM   2873  CA  ASP A1379      23.299 -31.813  81.362  1.00 67.75           C  
ANISOU 2873  CA  ASP A1379     7484  10371   7887   1753    -84   1228       C  
ATOM   2874  C   ASP A1379      22.449 -32.257  82.545  1.00 64.06           C  
ANISOU 2874  C   ASP A1379     7148   9746   7447   1629   -145   1130       C  
ATOM   2875  O   ASP A1379      21.848 -31.420  83.240  1.00 65.73           O  
ANISOU 2875  O   ASP A1379     7345   9922   7706   1371   -219   1043       O  
ATOM   2876  CB  ASP A1379      24.034 -30.505  81.662  1.00 63.67           C  
ANISOU 2876  CB  ASP A1379     6717  10099   7378   1540   -149   1330       C  
ATOM   2877  CG  ASP A1379      25.142 -30.672  82.693  1.00 79.54           C  
ANISOU 2877  CG  ASP A1379     8530  12364   9327   1530   -191   1535       C  
ATOM   2878  OD1 ASP A1379      25.015 -31.524  83.596  1.00 85.65           O  
ANISOU 2878  OD1 ASP A1379     9377  13086  10082   1580   -201   1540       O  
ATOM   2879  OD2 ASP A1379      26.149 -29.937  82.600  1.00 94.55           O  
ANISOU 2879  OD2 ASP A1379    10199  14528  11199   1460   -221   1705       O  
ATOM   2880  N   PRO A1380      22.367 -33.564  82.809  1.00 57.48           N  
ANISOU 2880  N   PRO A1380     6457   8812   6573   1814   -113   1147       N  
ATOM   2881  CA  PRO A1380      21.542 -34.034  83.933  1.00 59.84           C  
ANISOU 2881  CA  PRO A1380     6876   8966   6894   1695   -171   1067       C  
ATOM   2882  C   PRO A1380      21.956 -33.467  85.278  1.00 66.04           C  
ANISOU 2882  C   PRO A1380     7493   9922   7675   1503   -245   1139       C  
ATOM   2883  O   PRO A1380      21.091 -33.254  86.139  1.00 57.95           O  
ANISOU 2883  O   PRO A1380     6540   8791   6687   1316   -301   1038       O  
ATOM   2884  CB  PRO A1380      21.725 -35.560  83.888  1.00 58.04           C  
ANISOU 2884  CB  PRO A1380     6811   8642   6599   1962   -122   1122       C  
ATOM   2885  CG  PRO A1380      22.249 -35.858  82.521  1.00 61.53           C  
ANISOU 2885  CG  PRO A1380     7300   9090   6990   2218    -32   1166       C  
ATOM   2886  CD  PRO A1380      23.055 -34.667  82.121  1.00 59.21           C  
ANISOU 2886  CD  PRO A1380     6744   9044   6708   2151    -21   1251       C  
ATOM   2887  N   GLY A1381      23.250 -33.219  85.489  1.00 63.22           N  
ANISOU 2887  N   GLY A1381     6919   9836   7268   1544   -248   1322       N  
ATOM   2888  CA  GLY A1381      23.681 -32.710  86.778  1.00 61.68           C  
ANISOU 2888  CA  GLY A1381     6583   9800   7053   1346   -337   1401       C  
ATOM   2889  C   GLY A1381      23.220 -31.288  87.032  1.00 62.10           C  
ANISOU 2889  C   GLY A1381     6607   9843   7145   1044   -415   1303       C  
ATOM   2890  O   GLY A1381      22.782 -30.954  88.138  1.00 65.44           O  
ANISOU 2890  O   GLY A1381     7071  10228   7567    854   -486   1249       O  
ATOM   2891  N   GLU A1382      23.272 -30.439  86.003  1.00 57.94           N  
ANISOU 2891  N   GLU A1382     6033   9336   6645   1008   -400   1276       N  
ATOM   2892  CA  GLU A1382      22.744 -29.090  86.159  1.00 61.18           C  
ANISOU 2892  CA  GLU A1382     6460   9701   7085    740   -468   1169       C  
ATOM   2893  C   GLU A1382      21.236 -29.105  86.363  1.00 65.50           C  
ANISOU 2893  C   GLU A1382     7220   9980   7687    671   -458    960       C  
ATOM   2894  O   GLU A1382      20.707 -28.283  87.120  1.00 66.04           O  
ANISOU 2894  O   GLU A1382     7339   9999   7754    465   -518    881       O  
ATOM   2895  CB  GLU A1382      23.117 -28.230  84.950  1.00 56.24           C  
ANISOU 2895  CB  GLU A1382     5744   9150   6476    728   -451   1191       C  
ATOM   2896  CG  GLU A1382      22.797 -26.754  85.132  1.00 76.45           C  
ANISOU 2896  CG  GLU A1382     8314  11686   9046    449   -534   1114       C  
ATOM   2897  CD  GLU A1382      23.529 -25.863  84.147  1.00 98.14           C  
ANISOU 2897  CD  GLU A1382    10921  14579  11788    405   -544   1202       C  
ATOM   2898  OE1 GLU A1382      24.656 -26.219  83.741  1.00109.24           O  
ANISOU 2898  OE1 GLU A1382    12143  16206  13157    532   -521   1393       O  
ATOM   2899  OE2 GLU A1382      22.975 -24.804  83.778  1.00 98.80           O  
ANISOU 2899  OE2 GLU A1382    11075  14564  11900    251   -573   1090       O  
ATOM   2900  N   LEU A1383      20.533 -30.047  85.730  1.00 54.04           N  
ANISOU 2900  N   LEU A1383     5903   8358   6271    841   -387    883       N  
ATOM   2901  CA  LEU A1383      19.092 -30.144  85.941  1.00 62.55           C  
ANISOU 2901  CA  LEU A1383     7159   9210   7399    770   -384    721       C  
ATOM   2902  C   LEU A1383      18.768 -30.608  87.357  1.00 52.86           C  
ANISOU 2902  C   LEU A1383     5978   7960   6147    701   -423    724       C  
ATOM   2903  O   LEU A1383      17.817 -30.117  87.976  1.00 53.98           O  
ANISOU 2903  O   LEU A1383     6199   8007   6306    556   -444    626       O  
ATOM   2904  CB  LEU A1383      18.471 -31.083  84.908  1.00 52.80           C  
ANISOU 2904  CB  LEU A1383     6064   7803   6195    943   -322    661       C  
ATOM   2905  CG  LEU A1383      16.986 -31.415  85.088  1.00 59.52           C  
ANISOU 2905  CG  LEU A1383     7085   8436   7092    877   -327    535       C  
ATOM   2906  CD1 LEU A1383      16.139 -30.153  85.151  1.00 50.24           C  
ANISOU 2906  CD1 LEU A1383     5908   7222   5961    687   -343    431       C  
ATOM   2907  CD2 LEU A1383      16.505 -32.332  83.971  1.00 65.36           C  
ANISOU 2907  CD2 LEU A1383     7976   9011   7846   1027   -291    497       C  
ATOM   2908  N   ALA A1384      19.552 -31.544  87.894  1.00 53.99           N  
ANISOU 2908  N   ALA A1384     6074   8196   6242    816   -426    845       N  
ATOM   2909  CA  ALA A1384      19.348 -31.952  89.279  1.00 61.12           C  
ANISOU 2909  CA  ALA A1384     7009   9097   7115    745   -468    862       C  
ATOM   2910  C   ALA A1384      19.644 -30.804  90.236  1.00 54.38           C  
ANISOU 2910  C   ALA A1384     6077   8362   6222    527   -542    876       C  
ATOM   2911  O   ALA A1384      18.946 -30.627  91.242  1.00 58.29           O  
ANISOU 2911  O   ALA A1384     6653   8790   6703    406   -571    813       O  
ATOM   2912  CB  ALA A1384      20.220 -33.165  89.602  1.00 55.55           C  
ANISOU 2912  CB  ALA A1384     6265   8480   6361    926   -455   1002       C  
ATOM   2913  N   ASN A1385      20.657 -29.992  89.923  1.00 55.07           N  
ANISOU 2913  N   ASN A1385     6020   8622   6281    468   -577    965       N  
ATOM   2914  CA  ASN A1385      20.940 -28.831  90.760  1.00 55.41           C  
ANISOU 2914  CA  ASN A1385     6029   8755   6271    234   -669    978       C  
ATOM   2915  C   ASN A1385      19.811 -27.809  90.689  1.00 63.57           C  
ANISOU 2915  C   ASN A1385     7205   9622   7328     94   -668    807       C  
ATOM   2916  O   ASN A1385      19.468 -27.182  91.698  1.00 64.01           O  
ANISOU 2916  O   ASN A1385     7344   9646   7330    -64   -721    760       O  
ATOM   2917  CB  ASN A1385      22.266 -28.193  90.348  1.00 56.61           C  
ANISOU 2917  CB  ASN A1385     5995   9132   6384    181   -722   1132       C  
ATOM   2918  CG  ASN A1385      23.465 -28.976  90.840  1.00 61.01           C  
ANISOU 2918  CG  ASN A1385     6389   9905   6887    270   -747   1339       C  
ATOM   2919  OD1 ASN A1385      23.343 -29.834  91.713  1.00 65.16           O  
ANISOU 2919  OD1 ASN A1385     6957  10409   7392    327   -746   1357       O  
ATOM   2920  ND2 ASN A1385      24.636 -28.674  90.293  1.00 73.24           N  
ANISOU 2920  ND2 ASN A1385     7741  11678   8408    284   -770   1512       N  
ATOM   2921  N   ALA A1386      19.212 -27.637  89.508  1.00 53.78           N  
ANISOU 2921  N   ALA A1386     6004   8273   6157    162   -604    717       N  
ATOM   2922  CA  ALA A1386      18.075 -26.730  89.393  1.00 52.16           C  
ANISOU 2922  CA  ALA A1386     5928   7914   5975     59   -589    566       C  
ATOM   2923  C   ALA A1386      16.865 -27.254  90.158  1.00 58.00           C  
ANISOU 2923  C   ALA A1386     6800   8513   6726     73   -554    481       C  
ATOM   2924  O   ALA A1386      16.112 -26.473  90.751  1.00 56.51           O  
ANISOU 2924  O   ALA A1386     6713   8251   6508    -34   -559    399       O  
ATOM   2925  CB  ALA A1386      17.722 -26.512  87.925  1.00 51.34           C  
ANISOU 2925  CB  ALA A1386     5824   7738   5945    136   -530    505       C  
ATOM   2926  N   ILE A1387      16.668 -28.574  90.167  1.00 54.13           N  
ANISOU 2926  N   ILE A1387     6317   7983   6266    211   -519    511       N  
ATOM   2927  CA  ILE A1387      15.565 -29.142  90.937  1.00 51.15           C  
ANISOU 2927  CA  ILE A1387     6046   7494   5894    210   -497    461       C  
ATOM   2928  C   ILE A1387      15.798 -28.942  92.432  1.00 51.85           C  
ANISOU 2928  C   ILE A1387     6148   7652   5900    108   -546    496       C  
ATOM   2929  O   ILE A1387      14.865 -28.635  93.188  1.00 51.59           O  
ANISOU 2929  O   ILE A1387     6211   7550   5843     43   -531    434       O  
ATOM   2930  CB  ILE A1387      15.378 -30.629  90.575  1.00 51.20           C  
ANISOU 2930  CB  ILE A1387     6081   7432   5941    363   -467    497       C  
ATOM   2931  CG1 ILE A1387      14.910 -30.771  89.121  1.00 51.15           C  
ANISOU 2931  CG1 ILE A1387     6113   7320   6003    446   -424    443       C  
ATOM   2932  CG2 ILE A1387      14.396 -31.300  91.519  1.00 51.12           C  
ANISOU 2932  CG2 ILE A1387     6159   7338   5926    341   -463    483       C  
ATOM   2933  CD1 ILE A1387      14.747 -32.210  88.666  1.00 50.83           C  
ANISOU 2933  CD1 ILE A1387     6152   7181   5980    591   -410    475       C  
ATOM   2934  N   LEU A1388      17.051 -29.078  92.877  1.00 56.26           N  
ANISOU 2934  N   LEU A1388     6610   8361   6404     94   -605    607       N  
ATOM   2935  CA  LEU A1388      17.360 -28.810  94.280  1.00 55.30           C  
ANISOU 2935  CA  LEU A1388     6508   8312   6191    -25   -669    646       C  
ATOM   2936  C   LEU A1388      17.168 -27.334  94.618  1.00 53.74           C  
ANISOU 2936  C   LEU A1388     6395   8096   5929   -196   -709    575       C  
ATOM   2937  O   LEU A1388      16.701 -26.993  95.713  1.00 59.08           O  
ANISOU 2937  O   LEU A1388     7184   8733   6530   -278   -726    537       O  
ATOM   2938  CB  LEU A1388      18.788 -29.256  94.596  1.00 59.66           C  
ANISOU 2938  CB  LEU A1388     6921   9050   6698     -9   -733    804       C  
ATOM   2939  CG  LEU A1388      19.045 -30.764  94.634  1.00 63.53           C  
ANISOU 2939  CG  LEU A1388     7365   9559   7214    169   -699    890       C  
ATOM   2940  CD1 LEU A1388      20.530 -31.063  94.480  1.00 56.62           C  
ANISOU 2940  CD1 LEU A1388     6318   8890   6306    232   -736   1063       C  
ATOM   2941  CD2 LEU A1388      18.512 -31.368  95.925  1.00 55.49           C  
ANISOU 2941  CD2 LEU A1388     6429   8496   6157    144   -710    885       C  
ATOM   2942  N   LYS A1389      17.498 -26.443  93.679  1.00 54.35           N  
ANISOU 2942  N   LYS A1389     6439   8186   6023   -242   -722    556       N  
ATOM   2943  CA  LYS A1389      17.254 -25.020  93.892  1.00 59.74           C  
ANISOU 2943  CA  LYS A1389     7241   8818   6640   -397   -760    480       C  
ATOM   2944  C   LYS A1389      15.763 -24.729  93.988  1.00 62.46           C  
ANISOU 2944  C   LYS A1389     7740   8994   6999   -360   -674    345       C  
ATOM   2945  O   LYS A1389      15.332 -23.899  94.799  1.00 60.26           O  
ANISOU 2945  O   LYS A1389     7615   8656   6625   -447   -688    287       O  
ATOM   2946  CB  LYS A1389      17.884 -24.212  92.755  1.00 54.89           C  
ANISOU 2946  CB  LYS A1389     6553   8251   6051   -446   -789    497       C  
ATOM   2947  CG  LYS A1389      17.368 -22.783  92.618  1.00 71.30           C  
ANISOU 2947  CG  LYS A1389     8785  10222   8083   -568   -804    392       C  
ATOM   2948  CD  LYS A1389      18.040 -21.841  93.604  1.00 91.03           C  
ANISOU 2948  CD  LYS A1389    11383  12766  10440   -775   -931    430       C  
ATOM   2949  CE  LYS A1389      17.676 -20.392  93.313  1.00100.85           C  
ANISOU 2949  CE  LYS A1389    12801  13891  11626   -890   -956    336       C  
ATOM   2950  NZ  LYS A1389      18.416 -19.438  94.186  1.00104.37           N  
ANISOU 2950  NZ  LYS A1389    13378  14362  11914  -1117  -1105    380       N  
ATOM   2951  N   ALA A1390      14.956 -25.420  93.180  1.00 52.03           N  
ANISOU 2951  N   ALA A1390     6388   7597   5783   -225   -586    306       N  
ATOM   2952  CA  ALA A1390      13.511 -25.251  93.268  1.00 55.81           C  
ANISOU 2952  CA  ALA A1390     6977   7949   6279   -185   -503    215       C  
ATOM   2953  C   ALA A1390      12.984 -25.747  94.608  1.00 55.41           C  
ANISOU 2953  C   ALA A1390     6995   7891   6166   -180   -490    230       C  
ATOM   2954  O   ALA A1390      12.093 -25.128  95.208  1.00 58.17           O  
ANISOU 2954  O   ALA A1390     7468   8179   6456   -194   -445    174       O  
ATOM   2955  CB  ALA A1390      12.832 -25.988  92.115  1.00 50.11           C  
ANISOU 2955  CB  ALA A1390     6199   7161   5678    -69   -437    198       C  
ATOM   2956  N   LEU A1391      13.547 -26.849  95.112  1.00 58.31           N  
ANISOU 2956  N   LEU A1391     7290   8329   6538   -150   -523    314       N  
ATOM   2957  CA  LEU A1391      13.137 -27.335  96.425  1.00 62.40           C  
ANISOU 2957  CA  LEU A1391     7867   8851   6990   -153   -517    339       C  
ATOM   2958  C   LEU A1391      13.511 -26.343  97.520  1.00 57.54           C  
ANISOU 2958  C   LEU A1391     7363   8265   6233   -272   -571    325       C  
ATOM   2959  O   LEU A1391      12.750 -26.142  98.473  1.00 64.99           O  
ANISOU 2959  O   LEU A1391     8425   9168   7099   -273   -534    296       O  
ATOM   2960  CB  LEU A1391      13.766 -28.698  96.709  1.00 57.02           C  
ANISOU 2960  CB  LEU A1391     7093   8236   6336    -96   -550    438       C  
ATOM   2961  CG  LEU A1391      13.558 -29.216  98.134  1.00 53.47           C  
ANISOU 2961  CG  LEU A1391     6693   7812   5811   -113   -560    480       C  
ATOM   2962  CD1 LEU A1391      12.076 -29.346  98.454  1.00 53.80           C  
ANISOU 2962  CD1 LEU A1391     6813   7766   5862    -76   -477    439       C  
ATOM   2963  CD2 LEU A1391      14.267 -30.543  98.332  1.00 53.88           C  
ANISOU 2963  CD2 LEU A1391     6658   7927   5889    -48   -595    584       C  
ATOM   2964  N   GLU A1392      14.671 -25.697  97.391  1.00 54.04           N  
ANISOU 2964  N   GLU A1392     6895   7894   5744   -376   -664    355       N  
ATOM   2965  CA  GLU A1392      15.045 -24.682  98.372  1.00 59.12           C  
ANISOU 2965  CA  GLU A1392     7683   8545   6236   -519   -740    343       C  
ATOM   2966  C   GLU A1392      14.115 -23.476  98.296  1.00 61.62           C  
ANISOU 2966  C   GLU A1392     8189   8731   6494   -532   -686    225       C  
ATOM   2967  O   GLU A1392      13.723 -22.920  99.328  1.00 58.09           O  
ANISOU 2967  O   GLU A1392     7929   8230   5912   -568   -684    186       O  
ATOM   2968  CB  GLU A1392      16.498 -24.255  98.161  1.00 65.60           C  
ANISOU 2968  CB  GLU A1392     8421   9483   7020   -654   -869    427       C  
ATOM   2969  CG  GLU A1392      17.520 -25.316  98.542  1.00 95.16           C  
ANISOU 2969  CG  GLU A1392    11998  13383  10777   -645   -930    569       C  
ATOM   2970  CD  GLU A1392      18.954 -24.850  98.349  1.00119.22           C  
ANISOU 2970  CD  GLU A1392    14934  16583  13779   -784  -1060    689       C  
ATOM   2971  OE1 GLU A1392      19.205 -24.037  97.432  1.00119.44           O  
ANISOU 2971  OE1 GLU A1392    14945  16608  13830   -840  -1080    673       O  
ATOM   2972  OE2 GLU A1392      19.832 -25.296  99.120  1.00127.44           O  
ANISOU 2972  OE2 GLU A1392    15899  17761  14763   -843  -1144    814       O  
ATOM   2973  N   LEU A1393      13.732 -23.076  97.082  1.00 63.24           N  
ANISOU 2973  N   LEU A1393     8361   8880   6789   -485   -634    172       N  
ATOM   2974  CA  LEU A1393      12.807 -21.957  96.925  1.00 61.16           C  
ANISOU 2974  CA  LEU A1393     8271   8493   6474   -470   -569     69       C  
ATOM   2975  C   LEU A1393      11.434 -22.283  97.497  1.00 63.77           C  
ANISOU 2975  C   LEU A1393     8672   8766   6793   -341   -446     38       C  
ATOM   2976  O   LEU A1393      10.726 -21.384  97.964  1.00 62.98           O  
ANISOU 2976  O   LEU A1393     8762   8583   6584   -316   -392    -24       O  
ATOM   2977  CB  LEU A1393      12.682 -21.573  95.449  1.00 53.14           C  
ANISOU 2977  CB  LEU A1393     7178   7443   5570   -440   -538     31       C  
ATOM   2978  CG  LEU A1393      13.896 -20.945  94.763  1.00 57.81           C  
ANISOU 2978  CG  LEU A1393     7717   8087   6160   -567   -646     61       C  
ATOM   2979  CD1 LEU A1393      13.689 -20.903  93.257  1.00 57.84           C  
ANISOU 2979  CD1 LEU A1393     7609   8071   6296   -500   -595     36       C  
ATOM   2980  CD2 LEU A1393      14.160 -19.549  95.301  1.00 54.67           C  
ANISOU 2980  CD2 LEU A1393     7544   7624   5606   -713   -723     18       C  
ATOM   2981  N   SER A1394      11.046 -23.559  97.480  1.00 66.44           N  
ANISOU 2981  N   SER A1394     8867   9148   7229   -254   -400     93       N  
ATOM   2982  CA  SER A1394       9.717 -23.940  97.948  1.00 58.56           C  
ANISOU 2982  CA  SER A1394     7899   8121   6229   -144   -289     96       C  
ATOM   2983  C   SER A1394       9.551 -23.813  99.460  1.00 66.98           C  
ANISOU 2983  C   SER A1394     9109   9199   7142   -151   -281    107       C  
ATOM   2984  O   SER A1394       8.413 -23.855  99.939  1.00 66.94           O  
ANISOU 2984  O   SER A1394     9155   9179   7101    -52   -176    114       O  
ATOM   2985  CB  SER A1394       9.395 -25.368  97.506  1.00 58.02           C  
ANISOU 2985  CB  SER A1394     7658   8087   6298    -80   -267    164       C  
ATOM   2986  OG  SER A1394      10.326 -26.291  98.037  1.00 68.30           O  
ANISOU 2986  OG  SER A1394     8892   9459   7599   -117   -346    232       O  
ATOM   2987  N   ARG A1395      10.644 -23.683 100.222  1.00 70.33           N  
ANISOU 2987  N   ARG A1395     9592   9661   7468   -262   -390    125       N  
ATOM   2988  CA  ARG A1395      10.512 -23.455 101.660  1.00 71.43           C  
ANISOU 2988  CA  ARG A1395     9902   9798   7439   -276   -390    127       C  
ATOM   2989  C   ARG A1395       9.810 -22.136 101.955  1.00 75.46           C  
ANISOU 2989  C   ARG A1395    10663  10203   7806   -236   -324     42       C  
ATOM   2990  O   ARG A1395       9.097 -22.022 102.959  1.00 88.28           O  
ANISOU 2990  O   ARG A1395    12428  11810   9306   -157   -248     41       O  
ATOM   2991  CB  ARG A1395      11.886 -23.462 102.331  1.00 60.41           C  
ANISOU 2991  CB  ARG A1395     8529   8463   5959   -429   -542    170       C  
ATOM   2992  CG  ARG A1395      12.817 -24.573 101.887  1.00 71.79           C  
ANISOU 2992  CG  ARG A1395     9732  10015   7529   -460   -614    261       C  
ATOM   2993  CD  ARG A1395      12.498 -25.895 102.554  1.00 78.88           C  
ANISOU 2993  CD  ARG A1395    10537  10969   8465   -382   -578    334       C  
ATOM   2994  NE  ARG A1395      13.470 -26.916 102.178  1.00 83.41           N  
ANISOU 2994  NE  ARG A1395    10918  11637   9136   -392   -648    424       N  
ATOM   2995  CZ  ARG A1395      13.365 -28.203 102.489  1.00 78.62           C  
ANISOU 2995  CZ  ARG A1395    10213  11072   8588   -322   -630    497       C  
ATOM   2996  NH1 ARG A1395      12.324 -28.637 103.185  1.00 85.20           N  
ANISOU 2996  NH1 ARG A1395    11101  11872   9399   -257   -553    498       N  
ATOM   2997  NH2 ARG A1395      14.302 -29.058 102.098  1.00 61.86           N  
ANISOU 2997  NH2 ARG A1395     7940   9027   6536   -307   -687    581       N  
ATOM   2998  N   SER A1396      10.009 -21.131 101.109  1.00 73.03           N  
ANISOU 2998  N   SER A1396    10424   9824   7499   -278   -346    -23       N  
ATOM   2999  CA  SER A1396       9.363 -19.834 101.235  1.00 68.26           C  
ANISOU 2999  CA  SER A1396    10079   9100   6758   -225   -282   -106       C  
ATOM   3000  C   SER A1396       8.116 -19.773 100.360  1.00 65.97           C  
ANISOU 3000  C   SER A1396     9709   8785   6571    -59   -130   -122       C  
ATOM   3001  O   SER A1396       7.832 -20.678  99.572  1.00 61.12           O  
ANISOU 3001  O   SER A1396     8851   8235   6136    -20    -99    -74       O  
ATOM   3002  CB  SER A1396      10.333 -18.708 100.865  1.00 66.72           C  
ANISOU 3002  CB  SER A1396    10031   8832   6487   -386   -411   -160       C  
ATOM   3003  OG  SER A1396      11.458 -18.704 101.723  1.00 76.18           O  
ANISOU 3003  OG  SER A1396    11308  10065   7572   -559   -565   -124       O  
ATOM   3004  N   ASP A1397       7.353 -18.694 100.529  1.00 58.29           N  
ANISOU 3004  N   ASP A1397     8962   7715   5470     42    -38   -181       N  
ATOM   3005  CA  ASP A1397       6.200 -18.458  99.671  1.00 65.19           C  
ANISOU 3005  CA  ASP A1397     9770   8573   6426    196    102   -184       C  
ATOM   3006  C   ASP A1397       6.649 -18.256  98.228  1.00 64.21           C  
ANISOU 3006  C   ASP A1397     9513   8429   6453    117     43   -215       C  
ATOM   3007  O   ASP A1397       7.623 -17.549  97.954  1.00 75.18           O  
ANISOU 3007  O   ASP A1397    11004   9760   7801    -20    -72   -267       O  
ATOM   3008  CB  ASP A1397       5.422 -17.236 100.163  1.00 71.14           C  
ANISOU 3008  CB  ASP A1397    10822   9222   6986    337    213   -236       C  
ATOM   3009  CG  ASP A1397       4.045 -17.125  99.536  1.00 87.49           C  
ANISOU 3009  CG  ASP A1397    12802  11318   9122    537    386   -199       C  
ATOM   3010  OD1 ASP A1397       3.704 -17.963  98.674  1.00 90.39           O  
ANISOU 3010  OD1 ASP A1397    12884  11774   9688    537    402   -137       O  
ATOM   3011  OD2 ASP A1397       3.299 -16.197  99.913  1.00 95.80           O  
ANISOU 3011  OD2 ASP A1397    14080  12303  10017    699    504   -222       O  
ATOM   3012  N   LEU A1398       5.931 -18.886  97.299  1.00 54.93           N  
ANISOU 3012  N   LEU A1398     8116   7308   5449    195    115   -171       N  
ATOM   3013  CA  LEU A1398       6.233 -18.796  95.875  1.00 57.46           C  
ANISOU 3013  CA  LEU A1398     8303   7614   5916    143     74   -194       C  
ATOM   3014  C   LEU A1398       5.234 -17.932  95.112  1.00 53.68           C  
ANISOU 3014  C   LEU A1398     7875   7075   5445    261    185   -225       C  
ATOM   3015  O   LEU A1398       5.295 -17.878  93.879  1.00 56.57           O  
ANISOU 3015  O   LEU A1398     8124   7432   5937    236    168   -238       O  
ATOM   3016  CB  LEU A1398       6.292 -20.198  95.261  1.00 52.49           C  
ANISOU 3016  CB  LEU A1398     7402   7073   5468    125     49   -124       C  
ATOM   3017  CG  LEU A1398       7.464 -21.094  95.676  1.00 61.37           C  
ANISOU 3017  CG  LEU A1398     8444   8260   6614     15    -68    -88       C  
ATOM   3018  CD1 LEU A1398       7.264 -22.519  95.181  1.00 51.46           C  
ANISOU 3018  CD1 LEU A1398     6976   7066   5512     42    -68    -15       C  
ATOM   3019  CD2 LEU A1398       8.778 -20.532  95.158  1.00 58.71           C  
ANISOU 3019  CD2 LEU A1398     8123   7911   6274   -116   -188   -124       C  
ATOM   3020  N   SER A1399       4.316 -17.259  95.811  1.00 56.40           N  
ANISOU 3020  N   SER A1399     8395   7384   5650    403    303   -227       N  
ATOM   3021  CA  SER A1399       3.215 -16.579  95.132  1.00 66.55           C  
ANISOU 3021  CA  SER A1399     9697   8643   6947    552    431   -224       C  
ATOM   3022  C   SER A1399       3.707 -15.467  94.212  1.00 63.94           C  
ANISOU 3022  C   SER A1399     9482   8199   6612    493    380   -315       C  
ATOM   3023  O   SER A1399       3.165 -15.280  93.117  1.00 62.30           O  
ANISOU 3023  O   SER A1399     9168   7993   6511    545    430   -307       O  
ATOM   3024  CB  SER A1399       2.234 -16.015  96.162  1.00 72.61           C  
ANISOU 3024  CB  SER A1399    10655   9400   7533    744    578   -199       C  
ATOM   3025  OG  SER A1399       1.533 -17.050  96.826  1.00 87.11           O  
ANISOU 3025  OG  SER A1399    12336  11366   9395    818    648    -85       O  
ATOM   3026  N   LYS A1400       4.728 -14.715  94.635  1.00 61.79           N  
ANISOU 3026  N   LYS A1400     9434   7831   6213    372    272   -392       N  
ATOM   3027  CA  LYS A1400       5.254 -13.659  93.775  1.00 68.96           C  
ANISOU 3027  CA  LYS A1400    10457   8633   7112    289    206   -466       C  
ATOM   3028  C   LYS A1400       5.929 -14.240  92.537  1.00 66.23           C  
ANISOU 3028  C   LYS A1400     9845   8352   6967    163    116   -450       C  
ATOM   3029  O   LYS A1400       5.853 -13.658  91.447  1.00 58.73           O  
ANISOU 3029  O   LYS A1400     8876   7358   6082    161    121   -480       O  
ATOM   3030  CB  LYS A1400       6.224 -12.777  94.559  1.00 71.86           C  
ANISOU 3030  CB  LYS A1400    11130   8887   7286    152     85   -530       C  
ATOM   3031  CG  LYS A1400       5.577 -12.048  95.721  1.00100.04           C  
ANISOU 3031  CG  LYS A1400    15034  12355  10622    293    175   -561       C  
ATOM   3032  CD  LYS A1400       6.604 -11.304  96.558  1.00109.16           C  
ANISOU 3032  CD  LYS A1400    16511  13390  11574    121     23   -617       C  
ATOM   3033  CE  LYS A1400       5.956 -10.662  97.772  1.00113.28           C  
ANISOU 3033  CE  LYS A1400    17399  13800  11842    280    117   -651       C  
ATOM   3034  NZ  LYS A1400       6.932  -9.890  98.587  1.00120.73           N  
ANISOU 3034  NZ  LYS A1400    18705  14602  12564     94    -49   -707       N  
ATOM   3035  N   PHE A1401       6.563 -15.406  92.680  1.00 59.42           N  
ANISOU 3035  N   PHE A1401     8784   7596   6198     76     43   -398       N  
ATOM   3036  CA  PHE A1401       7.202 -16.053  91.539  1.00 54.73           C  
ANISOU 3036  CA  PHE A1401     7952   7066   5778     -9    -27   -374       C  
ATOM   3037  C   PHE A1401       6.162 -16.488  90.512  1.00 51.32           C  
ANISOU 3037  C   PHE A1401     7349   6659   5490    108     73   -348       C  
ATOM   3038  O   PHE A1401       6.308 -16.231  89.308  1.00 54.16           O  
ANISOU 3038  O   PHE A1401     7633   7002   5943     84     55   -368       O  
ATOM   3039  CB  PHE A1401       8.019 -17.251  92.031  1.00 56.13           C  
ANISOU 3039  CB  PHE A1401     7982   7345   5999    -87   -109   -314       C  
ATOM   3040  CG  PHE A1401       9.216 -17.571  91.182  1.00 58.15           C  
ANISOU 3040  CG  PHE A1401     8087   7659   6349   -205   -219   -292       C  
ATOM   3041  CD1 PHE A1401       9.253 -17.230  89.842  1.00 72.37           C  
ANISOU 3041  CD1 PHE A1401     9809   9441   8246   -206   -216   -312       C  
ATOM   3042  CD2 PHE A1401      10.310 -18.216  91.733  1.00 59.10           C  
ANISOU 3042  CD2 PHE A1401     8137   7865   6455   -301   -319   -236       C  
ATOM   3043  CE1 PHE A1401      10.358 -17.528  89.065  1.00 72.00           C  
ANISOU 3043  CE1 PHE A1401     9619   9463   8273   -291   -303   -277       C  
ATOM   3044  CE2 PHE A1401      11.418 -18.516  90.963  1.00 66.49           C  
ANISOU 3044  CE2 PHE A1401     8919   8878   7465   -381   -405   -191       C  
ATOM   3045  CZ  PHE A1401      11.442 -18.173  89.627  1.00 68.45           C  
ANISOU 3045  CZ  PHE A1401     9093   9111   7804   -370   -393   -210       C  
ATOM   3046  N   ARG A1402       5.095 -17.147  90.976  1.00 55.19           N  
ANISOU 3046  N   ARG A1402     7778   7198   5996    227    171   -291       N  
ATOM   3047  CA  ARG A1402       4.022 -17.539  90.071  1.00 50.05           C  
ANISOU 3047  CA  ARG A1402     6970   6579   5466    318    253   -243       C  
ATOM   3048  C   ARG A1402       3.347 -16.322  89.457  1.00 53.37           C  
ANISOU 3048  C   ARG A1402     7493   6932   5854    402    332   -280       C  
ATOM   3049  O   ARG A1402       2.943 -16.360  88.288  1.00 49.54           O  
ANISOU 3049  O   ARG A1402     6887   6453   5483    417    349   -267       O  
ATOM   3050  CB  ARG A1402       2.988 -18.393  90.808  1.00 50.42           C  
ANISOU 3050  CB  ARG A1402     6936   6707   5513    411    336   -146       C  
ATOM   3051  CG  ARG A1402       3.568 -19.500  91.674  1.00 50.44           C  
ANISOU 3051  CG  ARG A1402     6884   6766   5515    345    269   -107       C  
ATOM   3052  CD  ARG A1402       2.481 -20.478  92.088  1.00 50.65           C  
ANISOU 3052  CD  ARG A1402     6789   6879   5578    415    337      8       C  
ATOM   3053  NE  ARG A1402       2.966 -21.491  93.022  1.00 50.83           N  
ANISOU 3053  NE  ARG A1402     6781   6948   5585    362    282     48       N  
ATOM   3054  CZ  ARG A1402       3.559 -22.626  92.664  1.00 55.69           C  
ANISOU 3054  CZ  ARG A1402     7278   7581   6303    280    191     74       C  
ATOM   3055  NH1 ARG A1402       3.755 -22.907  91.382  1.00 49.17           N  
ANISOU 3055  NH1 ARG A1402     6359   6726   5596    242    145     60       N  
ATOM   3056  NH2 ARG A1402       3.961 -23.482  93.593  1.00 52.62           N  
ANISOU 3056  NH2 ARG A1402     6877   7232   5885    248    149    115       N  
ATOM   3057  N   GLU A1403       3.232 -15.229  90.217  1.00 51.59           N  
ANISOU 3057  N   GLU A1403     7508   6631   5461    462    378   -327       N  
ATOM   3058  CA  GLU A1403       2.637 -14.018  89.666  1.00 57.38           C  
ANISOU 3058  CA  GLU A1403     8373   7284   6145    559    455   -364       C  
ATOM   3059  C   GLU A1403       3.502 -13.438  88.555  1.00 53.41           C  
ANISOU 3059  C   GLU A1403     7877   6712   5703    433    357   -433       C  
ATOM   3060  O   GLU A1403       2.983 -12.973  87.534  1.00 59.99           O  
ANISOU 3060  O   GLU A1403     8669   7524   6601    487    403   -437       O  
ATOM   3061  CB  GLU A1403       2.420 -12.986  90.773  1.00 62.80           C  
ANISOU 3061  CB  GLU A1403     9371   7880   6612    658    518   -404       C  
ATOM   3062  CG  GLU A1403       1.710 -11.727  90.304  1.00 78.72           C  
ANISOU 3062  CG  GLU A1403    11558   9801   8551    799    618   -434       C  
ATOM   3063  CD  GLU A1403       1.470 -10.734  91.425  1.00120.20           C  
ANISOU 3063  CD  GLU A1403    17167  14944  13560    925    688   -475       C  
ATOM   3064  OE1 GLU A1403       1.949 -10.972  92.556  1.00130.92           O  
ANISOU 3064  OE1 GLU A1403    18647  16291  14805    876    643   -489       O  
ATOM   3065  OE2 GLU A1403       0.797  -9.712  91.172  1.00134.05           O  
ANISOU 3065  OE2 GLU A1403    19094  16616  15225   1084    791   -490       O  
ATOM   3066  N   ASN A1404       4.827 -13.480  88.727  1.00 51.26           N  
ANISOU 3066  N   ASN A1404     7640   6424   5412    262    218   -472       N  
ATOM   3067  CA  ASN A1404       5.718 -13.015  87.669  1.00 50.68           C  
ANISOU 3067  CA  ASN A1404     7539   6317   5400    133    120   -512       C  
ATOM   3068  C   ASN A1404       5.622 -13.905  86.438  1.00 51.81           C  
ANISOU 3068  C   ASN A1404     7410   6541   5736    133    120   -472       C  
ATOM   3069  O   ASN A1404       5.630 -13.407  85.305  1.00 55.18           O  
ANISOU 3069  O   ASN A1404     7803   6937   6226    121    115   -495       O  
ATOM   3070  CB  ASN A1404       7.161 -12.971  88.167  1.00 51.14           C  
ANISOU 3070  CB  ASN A1404     7656   6381   5394    -53    -31   -523       C  
ATOM   3071  CG  ASN A1404       7.390 -11.888  89.194  1.00 64.40           C  
ANISOU 3071  CG  ASN A1404     9657   7946   6865    -95    -67   -571       C  
ATOM   3072  OD1 ASN A1404       6.610 -10.942  89.305  1.00 72.39           O  
ANISOU 3072  OD1 ASN A1404    10883   8847   7776     16     17   -616       O  
ATOM   3073  ND2 ASN A1404       8.471 -12.018  89.954  1.00 66.88           N  
ANISOU 3073  ND2 ASN A1404    10025   8284   7103   -253   -195   -556       N  
ATOM   3074  N   CYS A1405       5.507 -15.221  86.643  1.00 48.60           N  
ANISOU 3074  N   CYS A1405     6827   6226   5411    147    121   -412       N  
ATOM   3075  CA  CYS A1405       5.363 -16.126  85.506  1.00 47.41           C  
ANISOU 3075  CA  CYS A1405     6464   6129   5420    151    115   -375       C  
ATOM   3076  C   CYS A1405       4.083 -15.826  84.740  1.00 49.39           C  
ANISOU 3076  C   CYS A1405     6678   6362   5725    257    213   -358       C  
ATOM   3077  O   CYS A1405       4.083 -15.750  83.502  1.00 50.00           O  
ANISOU 3077  O   CYS A1405     6675   6429   5896    242    199   -368       O  
ATOM   3078  CB  CYS A1405       5.366 -17.583  85.978  1.00 47.12           C  
ANISOU 3078  CB  CYS A1405     6296   6169   5437    152     98   -311       C  
ATOM   3079  SG  CYS A1405       6.925 -18.170  86.672  1.00 56.51           S  
ANISOU 3079  SG  CYS A1405     7472   7409   6591     39    -20   -303       S  
ATOM   3080  N   LYS A1406       2.984 -15.618  85.470  1.00 47.92           N  
ANISOU 3080  N   LYS A1406     6550   6185   5473    372    316   -321       N  
ATOM   3081  CA  LYS A1406       1.703 -15.347  84.826  1.00 55.89           C  
ANISOU 3081  CA  LYS A1406     7502   7209   6525    483    415   -271       C  
ATOM   3082  C   LYS A1406       1.727 -14.015  84.085  1.00 56.84           C  
ANISOU 3082  C   LYS A1406     7740   7243   6615    508    437   -336       C  
ATOM   3083  O   LYS A1406       1.250 -13.921  82.947  1.00 49.91           O  
ANISOU 3083  O   LYS A1406     6763   6371   5829    526    454   -317       O  
ATOM   3084  CB  LYS A1406       0.591 -15.362  85.874  1.00 59.54           C  
ANISOU 3084  CB  LYS A1406     7996   7725   6902    620    532   -193       C  
ATOM   3085  CG  LYS A1406      -0.812 -15.419  85.311  1.00 69.03           C  
ANISOU 3085  CG  LYS A1406     9069   9000   8161    730    630    -86       C  
ATOM   3086  CD  LYS A1406      -1.837 -15.261  86.422  1.00 77.57           C  
ANISOU 3086  CD  LYS A1406    10191  10153   9130    890    762      7       C  
ATOM   3087  CE  LYS A1406      -1.586 -16.253  87.546  1.00 74.00           C  
ANISOU 3087  CE  LYS A1406     9710   9757   8649    847    731     45       C  
ATOM   3088  NZ  LYS A1406      -1.628 -17.659  87.057  1.00 78.25           N  
ANISOU 3088  NZ  LYS A1406    10033  10365   9333    728    645    119       N  
ATOM   3089  N   LYS A1407       2.307 -12.979  84.703  1.00 48.93           N  
ANISOU 3089  N   LYS A1407     6964   6152   5477    495    423   -411       N  
ATOM   3090  CA  LYS A1407       2.381 -11.677  84.047  1.00 55.05           C  
ANISOU 3090  CA  LYS A1407     7884   6824   6206    507    431   -473       C  
ATOM   3091  C   LYS A1407       3.261 -11.730  82.806  1.00 50.71           C  
ANISOU 3091  C   LYS A1407     7227   6268   5770    370    328   -507       C  
ATOM   3092  O   LYS A1407       2.937 -11.119  81.779  1.00 59.16           O  
ANISOU 3092  O   LYS A1407     8288   7304   6886    397    352   -519       O  
ATOM   3093  CB  LYS A1407       2.903 -10.626  85.027  1.00 50.61           C  
ANISOU 3093  CB  LYS A1407     7626   6149   5456    492    410   -543       C  
ATOM   3094  CG  LYS A1407       1.893 -10.191  86.076  1.00 79.15           C  
ANISOU 3094  CG  LYS A1407    11414   9738   8923    682    544   -519       C  
ATOM   3095  CD  LYS A1407       2.532  -9.289  87.124  1.00 91.56           C  
ANISOU 3095  CD  LYS A1407    13323  11177  10287    646    499   -594       C  
ATOM   3096  CE  LYS A1407       3.051  -7.995  86.514  1.00 96.84           C  
ANISOU 3096  CE  LYS A1407    14212  11696  10889    575    436   -673       C  
ATOM   3097  NZ  LYS A1407       3.649  -7.106  87.550  1.00 96.29           N  
ANISOU 3097  NZ  LYS A1407    14514  11477  10597    518    371   -740       N  
ATOM   3098  N   ARG A1408       4.365 -12.478  82.869  1.00 47.59           N  
ANISOU 3098  N   ARG A1408     6744   5920   5419    236    219   -510       N  
ATOM   3099  CA  ARG A1408       5.248 -12.582  81.715  1.00 46.73           C  
ANISOU 3099  CA  ARG A1408     6524   5826   5405    130    133   -524       C  
ATOM   3100  C   ARG A1408       4.565 -13.320  80.574  1.00 51.17           C  
ANISOU 3100  C   ARG A1408     6895   6436   6110    185    171   -484       C  
ATOM   3101  O   ARG A1408       4.651 -12.897  79.414  1.00 53.78           O  
ANISOU 3101  O   ARG A1408     7190   6744   6499    167    159   -503       O  
ATOM   3102  CB  ARG A1408       6.543 -13.285  82.124  1.00 46.96           C  
ANISOU 3102  CB  ARG A1408     6489   5918   5434      8     25   -509       C  
ATOM   3103  CG  ARG A1408       7.486 -13.619  80.986  1.00 52.19           C  
ANISOU 3103  CG  ARG A1408     7006   6633   6191    -71    -48   -495       C  
ATOM   3104  CD  ARG A1408       7.946 -12.376  80.246  1.00 50.28           C  
ANISOU 3104  CD  ARG A1408     6848   6336   5921   -143    -87   -530       C  
ATOM   3105  NE  ARG A1408       9.059 -12.674  79.352  1.00 73.94           N  
ANISOU 3105  NE  ARG A1408     9704   9410   8982   -226   -163   -497       N  
ATOM   3106  CZ  ARG A1408       9.326 -12.003  78.237  1.00 80.45           C  
ANISOU 3106  CZ  ARG A1408    10509  10218   9838   -263   -181   -505       C  
ATOM   3107  NH1 ARG A1408       8.551 -10.994  77.864  1.00 62.82           N  
ANISOU 3107  NH1 ARG A1408     8397   7886   7587   -228   -133   -553       N  
ATOM   3108  NH2 ARG A1408      10.362 -12.351  77.485  1.00 74.92           N  
ANISOU 3108  NH2 ARG A1408     9668   9611   9186   -319   -239   -456       N  
ATOM   3109  N   ALA A1409       3.856 -14.408  80.890  1.00 45.46           N  
ANISOU 3109  N   ALA A1409     6063   5775   5437    242    209   -424       N  
ATOM   3110  CA  ALA A1409       3.159 -15.152  79.847  1.00 54.11           C  
ANISOU 3110  CA  ALA A1409     7003   6903   6652    270    224   -375       C  
ATOM   3111  C   ALA A1409       2.038 -14.326  79.234  1.00 48.82           C  
ANISOU 3111  C   ALA A1409     6348   6211   5991    354    306   -359       C  
ATOM   3112  O   ALA A1409       1.805 -14.392  78.022  1.00 55.82           O  
ANISOU 3112  O   ALA A1409     7151   7095   6963    344    294   -350       O  
ATOM   3113  CB  ALA A1409       2.613 -16.465  80.411  1.00 44.72           C  
ANISOU 3113  CB  ALA A1409     5717   5777   5496    288    229   -299       C  
ATOM   3114  N   MET A1410       1.350 -13.521  80.048  1.00 46.93           N  
ANISOU 3114  N   MET A1410     6225   5954   5654    451    394   -350       N  
ATOM   3115  CA  MET A1410       0.275 -12.691  79.518  1.00 46.27           C  
ANISOU 3115  CA  MET A1410     6157   5859   5564    561    487   -319       C  
ATOM   3116  C   MET A1410       0.827 -11.594  78.615  1.00 53.05           C  
ANISOU 3116  C   MET A1410     7109   6629   6418    526    459   -398       C  
ATOM   3117  O   MET A1410       0.351 -11.406  77.490  1.00 58.97           O  
ANISOU 3117  O   MET A1410     7779   7383   7244    544    474   -377       O  
ATOM   3118  CB  MET A1410      -0.540 -12.090  80.664  1.00 53.42           C  
ANISOU 3118  CB  MET A1410     7186   6768   6341    709    604   -283       C  
ATOM   3119  CG  MET A1410      -1.374 -13.106  81.435  1.00 88.31           C  
ANISOU 3119  CG  MET A1410    11481  11302  10770    764    653   -168       C  
ATOM   3120  SD  MET A1410      -2.141 -12.437  82.924  1.00102.29           S  
ANISOU 3120  SD  MET A1410    13415  13087  12362    956    798   -125       S  
ATOM   3121  CE  MET A1410      -3.011 -11.022  82.255  1.00103.86           C  
ANISOU 3121  CE  MET A1410    13710  13244  12508   1128    918   -109       C  
ATOM   3122  N   SER A1411       1.846 -10.869  79.085  1.00 47.52           N  
ANISOU 3122  N   SER A1411     6580   5849   5626    460    407   -480       N  
ATOM   3123  CA  SER A1411       2.394  -9.778  78.289  1.00 58.16           C  
ANISOU 3123  CA  SER A1411     8031   7111   6958    408    369   -543       C  
ATOM   3124  C   SER A1411       3.053 -10.283  77.012  1.00 58.04           C  
ANISOU 3124  C   SER A1411     7851   7134   7070    303    288   -547       C  
ATOM   3125  O   SER A1411       3.002  -9.600  75.984  1.00 56.08           O  
ANISOU 3125  O   SER A1411     7609   6847   6853    299    288   -565       O  
ATOM   3126  CB  SER A1411       3.396  -8.968  79.114  1.00 47.35           C  
ANISOU 3126  CB  SER A1411     6886   5654   5453    321    302   -610       C  
ATOM   3127  OG  SER A1411       4.666  -9.596  79.140  1.00 64.82           O  
ANISOU 3127  OG  SER A1411     9014   7916   7700    164    183   -617       O  
ATOM   3128  N   PHE A1412       3.668 -11.470  77.050  1.00 59.60           N  
ANISOU 3128  N   PHE A1412     7912   7403   7330    233    225   -527       N  
ATOM   3129  CA  PHE A1412       4.264 -12.022  75.837  1.00 49.60           C  
ANISOU 3129  CA  PHE A1412     6507   6172   6166    169    164   -524       C  
ATOM   3130  C   PHE A1412       3.201 -12.371  74.803  1.00 53.49           C  
ANISOU 3130  C   PHE A1412     6892   6680   6753    234    210   -484       C  
ATOM   3131  O   PHE A1412       3.416 -12.192  73.598  1.00 45.94           O  
ANISOU 3131  O   PHE A1412     5888   5713   5853    208    185   -497       O  
ATOM   3132  CB  PHE A1412       5.103 -13.254  76.183  1.00 43.40           C  
ANISOU 3132  CB  PHE A1412     5627   5454   5407    116    100   -502       C  
ATOM   3133  CG  PHE A1412       5.770 -13.897  74.998  1.00 43.69           C  
ANISOU 3133  CG  PHE A1412     5547   5528   5526     84     49   -492       C  
ATOM   3134  CD1 PHE A1412       5.116 -14.868  74.256  1.00 43.80           C  
ANISOU 3134  CD1 PHE A1412     5468   5552   5622    129     61   -460       C  
ATOM   3135  CD2 PHE A1412       7.061 -13.543  74.637  1.00 45.05           C  
ANISOU 3135  CD2 PHE A1412     5710   5727   5680      7    -14   -503       C  
ATOM   3136  CE1 PHE A1412       5.729 -15.464  73.167  1.00 45.06           C  
ANISOU 3136  CE1 PHE A1412     5559   5728   5833    120     20   -456       C  
ATOM   3137  CE2 PHE A1412       7.682 -14.140  73.551  1.00 53.18           C  
ANISOU 3137  CE2 PHE A1412     6635   6801   6769      9    -43   -483       C  
ATOM   3138  CZ  PHE A1412       7.014 -15.102  72.814  1.00 43.21           C  
ANISOU 3138  CZ  PHE A1412     5311   5529   5577     77    -21   -468       C  
ATOM   3139  N   SER A1413       2.036 -12.827  75.256  1.00 47.30           N  
ANISOU 3139  N   SER A1413     6067   5927   5976    312    273   -423       N  
ATOM   3140  CA  SER A1413       1.003 -13.349  74.366  1.00 54.80           C  
ANISOU 3140  CA  SER A1413     6898   6912   7013    344    293   -355       C  
ATOM   3141  C   SER A1413       0.340 -12.257  73.533  1.00 57.79           C  
ANISOU 3141  C   SER A1413     7299   7261   7398    399    346   -353       C  
ATOM   3142  O   SER A1413       0.069 -12.443  72.348  1.00 66.80           O  
ANISOU 3142  O   SER A1413     8359   8407   8613    376    322   -332       O  
ATOM   3143  CB  SER A1413      -0.060 -14.103  75.173  1.00 43.61           C  
ANISOU 3143  CB  SER A1413     5417   5562   5593    395    338   -259       C  
ATOM   3144  OG  SER A1413       0.451 -15.330  75.667  1.00 55.73           O  
ANISOU 3144  OG  SER A1413     6909   7121   7143    335    275   -249       O  
ATOM   3145  N   GLU A 238       0.472 -11.275  74.351  1.00 58.72           N  
ANISOU 3145  N   GLU A 238     7558   7334   7418    446    393   -391       N  
ATOM   3146  CA  GLU A 238      -0.123  -9.985  74.038  1.00 56.22           C  
ANISOU 3146  CA  GLU A 238     7338   6967   7057    534    466   -397       C  
ATOM   3147  C   GLU A 238       0.618  -9.295  72.898  1.00 52.65           C  
ANISOU 3147  C   GLU A 238     6918   6452   6634    460    410   -462       C  
ATOM   3148  O   GLU A 238       0.004  -8.831  71.939  1.00 55.90           O  
ANISOU 3148  O   GLU A 238     7294   6858   7087    502    441   -437       O  
ATOM   3149  CB  GLU A 238      -0.124  -9.099  75.277  1.00 64.81           C  
ANISOU 3149  CB  GLU A 238     8627   7995   8003    612    526   -428       C  
ATOM   3150  CG  GLU A 238      -1.108  -7.964  75.209  1.00 80.58           C  
ANISOU 3150  CG  GLU A 238    10731   9952   9932    769    638   -400       C  
ATOM   3151  CD  GLU A 238      -1.790  -7.743  76.535  1.00111.06           C  
ANISOU 3151  CD  GLU A 238    14706  13822  13670    919    744   -360       C  
ATOM   3152  OE1 GLU A 238      -1.077  -7.554  77.545  1.00122.19           O  
ANISOU 3152  OE1 GLU A 238    16285  15167  14976    885    715   -426       O  
ATOM   3153  OE2 GLU A 238      -3.037  -7.786  76.571  1.00121.72           O  
ANISOU 3153  OE2 GLU A 238    15969  15258  15021   1070    854   -248       O  
ATOM   3154  N   GLN A 239       1.944  -9.205  73.025  1.00 56.90           N  
ANISOU 3154  N   GLN A 239     7516   6957   7147    348    326   -529       N  
ATOM   3155  CA  GLN A 239       2.749  -8.657  71.940  1.00 56.83           C  
ANISOU 3155  CA  GLN A 239     7510   6915   7167    265    265   -570       C  
ATOM   3156  C   GLN A 239       2.641  -9.523  70.691  1.00 59.35           C  
ANISOU 3156  C   GLN A 239     7655   7292   7604    246    239   -540       C  
ATOM   3157  O   GLN A 239       2.597  -9.008  69.563  1.00 55.60           O  
ANISOU 3157  O   GLN A 239     7164   6796   7167    238    234   -547       O  
ATOM   3158  CB  GLN A 239       4.206  -8.542  72.389  1.00 49.47           C  
ANISOU 3158  CB  GLN A 239     6638   5975   6182    138    173   -610       C  
ATOM   3159  CG  GLN A 239       4.406  -7.737  73.663  1.00 68.23           C  
ANISOU 3159  CG  GLN A 239     9221   8280   8424    128    173   -642       C  
ATOM   3160  CD  GLN A 239       5.740  -8.021  74.332  1.00 85.69           C  
ANISOU 3160  CD  GLN A 239    11445  10524  10589     -8     72   -648       C  
ATOM   3161  OE1 GLN A 239       6.329  -9.086  74.145  1.00 91.56           O  
ANISOU 3161  OE1 GLN A 239    12025  11363  11401    -48     30   -618       O  
ATOM   3162  NE2 GLN A 239       6.220  -7.067  75.121  1.00 92.03           N  
ANISOU 3162  NE2 GLN A 239    12457  11246  11265    -78     27   -678       N  
ATOM   3163  N   VAL A 240       2.558 -10.843  70.879  1.00 47.27           N  
ANISOU 3163  N   VAL A 240     6017   5823   6121    241    218   -504       N  
ATOM   3164  CA  VAL A 240       2.445 -11.756  69.748  1.00 48.97           C  
ANISOU 3164  CA  VAL A 240     6114   6069   6424    223    183   -477       C  
ATOM   3165  C   VAL A 240       1.148 -11.510  68.991  1.00 46.76           C  
ANISOU 3165  C   VAL A 240     5790   5790   6189    276    228   -426       C  
ATOM   3166  O   VAL A 240       1.123 -11.516  67.756  1.00 49.13           O  
ANISOU 3166  O   VAL A 240     6048   6081   6539    255    202   -425       O  
ATOM   3167  CB  VAL A 240       2.552 -13.214  70.235  1.00 52.92           C  
ANISOU 3167  CB  VAL A 240     6551   6611   6944    209    147   -445       C  
ATOM   3168  CG1 VAL A 240       2.000 -14.180  69.188  1.00 40.93           C  
ANISOU 3168  CG1 VAL A 240     4958   5099   5496    202    115   -401       C  
ATOM   3169  CG2 VAL A 240       3.999 -13.556  70.570  1.00 41.18           C  
ANISOU 3169  CG2 VAL A 240     5076   5143   5429    160     93   -481       C  
ATOM   3170  N   SER A 241       0.063 -11.231  69.718  1.00 42.48           N  
ANISOU 3170  N   SER A 241     5257   5266   5619    352    300   -371       N  
ATOM   3171  CA  SER A 241      -1.235 -11.029  69.080  1.00 55.91           C  
ANISOU 3171  CA  SER A 241     6888   7000   7357    408    346   -287       C  
ATOM   3172  C   SER A 241      -1.259  -9.745  68.253  1.00 55.71           C  
ANISOU 3172  C   SER A 241     6922   6923   7324    441    377   -321       C  
ATOM   3173  O   SER A 241      -1.728  -9.741  67.102  1.00 66.77           O  
ANISOU 3173  O   SER A 241     8251   8337   8783    430    362   -284       O  
ATOM   3174  CB  SER A 241      -2.327 -11.016  70.154  1.00 47.36           C  
ANISOU 3174  CB  SER A 241     5787   5976   6231    505    430   -197       C  
ATOM   3175  OG  SER A 241      -3.609 -10.784  69.601  1.00 80.75           O  
ANISOU 3175  OG  SER A 241     9925  10267  10489    569    481    -84       O  
ATOM   3176  N   ALA A 242      -0.729  -8.651  68.809  1.00 43.69           N  
ANISOU 3176  N   ALA A 242     5545   5333   5722    471    409   -388       N  
ATOM   3177  CA  ALA A 242      -0.694  -7.394  68.069  1.00 65.14           C  
ANISOU 3177  CA  ALA A 242     8347   7983   8420    494    430   -420       C  
ATOM   3178  C   ALA A 242       0.211  -7.500  66.844  1.00 46.15           C  
ANISOU 3178  C   ALA A 242     5896   5564   6074    386    346   -467       C  
ATOM   3179  O   ALA A 242      -0.128  -6.999  65.758  1.00 54.97           O  
ANISOU 3179  O   ALA A 242     6990   6668   7228    396    352   -454       O  
ATOM   3180  CB  ALA A 242      -0.232  -6.271  68.996  1.00 43.89           C  
ANISOU 3180  CB  ALA A 242     5865   5200   5611    525    458   -483       C  
ATOM   3181  N   ALA A 243       1.354  -8.181  66.993  1.00 41.74           N  
ANISOU 3181  N   ALA A 243     5318   5020   5522    293    273   -508       N  
ATOM   3182  CA  ALA A 243       2.230  -8.371  65.846  1.00 44.03           C  
ANISOU 3182  CA  ALA A 243     5554   5318   5857    217    208   -534       C  
ATOM   3183  C   ALA A 243       1.558  -9.229  64.784  1.00 49.82           C  
ANISOU 3183  C   ALA A 243     6175   6087   6669    229    195   -489       C  
ATOM   3184  O   ALA A 243       1.725  -8.979  63.584  1.00 57.26           O  
ANISOU 3184  O   ALA A 243     7094   7019   7642    208    174   -496       O  
ATOM   3185  CB  ALA A 243       3.553  -8.994  66.287  1.00 40.97           C  
ANISOU 3185  CB  ALA A 243     5154   4963   5449    144    145   -560       C  
ATOM   3186  N   ARG A 244       0.767 -10.222  65.206  1.00 49.00           N  
ANISOU 3186  N   ARG A 244     6011   6020   6588    251    200   -434       N  
ATOM   3187  CA  ARG A 244       0.053 -11.042  64.235  1.00 58.85           C  
ANISOU 3187  CA  ARG A 244     7178   7288   7893    236    166   -378       C  
ATOM   3188  C   ARG A 244      -0.972 -10.222  63.468  1.00 49.16           C  
ANISOU 3188  C   ARG A 244     5925   6063   6689    271    204   -328       C  
ATOM   3189  O   ARG A 244      -1.157 -10.433  62.265  1.00 48.56           O  
ANISOU 3189  O   ARG A 244     5814   5984   6653    238    163   -312       O  
ATOM   3190  CB  ARG A 244      -0.631 -12.224  64.929  1.00 40.75           C  
ANISOU 3190  CB  ARG A 244     4836   5036   5611    228    149   -310       C  
ATOM   3191  CG  ARG A 244       0.312 -13.335  65.367  1.00 41.73           C  
ANISOU 3191  CG  ARG A 244     4979   5153   5723    191     95   -346       C  
ATOM   3192  CD  ARG A 244      -0.160 -14.690  64.869  1.00 44.13           C  
ANISOU 3192  CD  ARG A 244     5261   5452   6054    145     24   -290       C  
ATOM   3193  NE  ARG A 244      -1.260 -15.243  65.647  1.00 58.57           N  
ANISOU 3193  NE  ARG A 244     7041   7325   7890    132     26   -193       N  
ATOM   3194  CZ  ARG A 244      -2.047 -16.228  65.226  1.00 57.48           C  
ANISOU 3194  CZ  ARG A 244     6878   7188   7771     66    -45   -108       C  
ATOM   3195  NH1 ARG A 244      -1.867 -16.756  64.023  1.00 49.11           N  
ANISOU 3195  NH1 ARG A 244     5868   6070   6720     17   -122   -123       N  
ATOM   3196  NH2 ARG A 244      -3.022 -16.681  66.003  1.00 67.36           N  
ANISOU 3196  NH2 ARG A 244     8067   8501   9025     43    -45      2       N  
ATOM   3197  N   LYS A 245      -1.617  -9.261  64.132  1.00 45.71           N  
ANISOU 3197  N   LYS A 245     5519   5631   6219    351    285   -302       N  
ATOM   3198  CA  LYS A 245      -2.562  -8.402  63.420  1.00 52.95           C  
ANISOU 3198  CA  LYS A 245     6413   6556   7150    409    332   -244       C  
ATOM   3199  C   LYS A 245      -1.852  -7.555  62.366  1.00 60.95           C  
ANISOU 3199  C   LYS A 245     7482   7507   8168    380    311   -315       C  
ATOM   3200  O   LYS A 245      -2.297  -7.475  61.207  1.00 57.75           O  
ANISOU 3200  O   LYS A 245     7023   7113   7806    366    292   -278       O  
ATOM   3201  CB  LYS A 245      -3.316  -7.505  64.403  1.00 55.12           C  
ANISOU 3201  CB  LYS A 245     6739   6840   7363    538    440   -201       C  
ATOM   3202  CG  LYS A 245      -4.326  -8.226  65.273  1.00 63.76           C  
ANISOU 3202  CG  LYS A 245     7743   8030   8454    589    479    -86       C  
ATOM   3203  CD  LYS A 245      -5.078  -7.234  66.145  1.00 75.36           C  
ANISOU 3203  CD  LYS A 245     9276   9513   9844    756    608    -34       C  
ATOM   3204  CE  LYS A 245      -4.114  -6.367  66.940  1.00 86.69           C  
ANISOU 3204  CE  LYS A 245    10919  10832  11189    787    634   -162       C  
ATOM   3205  NZ  LYS A 245      -4.826  -5.479  67.897  1.00 85.72           N  
ANISOU 3205  NZ  LYS A 245    10909  10701  10961    970    762   -119       N  
ATOM   3206  N   VAL A 246      -0.732  -6.931  62.744  1.00 50.99           N  
ANISOU 3206  N   VAL A 246     6327   6187   6860    356    305   -404       N  
ATOM   3207  CA  VAL A 246      -0.027  -6.082  61.780  1.00 51.39           C  
ANISOU 3207  CA  VAL A 246     6426   6190   6910    315    280   -454       C  
ATOM   3208  C   VAL A 246       0.469  -6.912  60.597  1.00 49.92           C  
ANISOU 3208  C   VAL A 246     6154   6034   6778    245    211   -460       C  
ATOM   3209  O   VAL A 246       0.357  -6.503  59.427  1.00 52.57           O  
ANISOU 3209  O   VAL A 246     6473   6360   7140    236    201   -453       O  
ATOM   3210  CB  VAL A 246       1.130  -5.332  62.468  1.00 53.87           C  
ANISOU 3210  CB  VAL A 246     6866   6448   7154    268    263   -524       C  
ATOM   3211  CG1 VAL A 246       1.846  -4.434  61.471  1.00 55.46           C  
ANISOU 3211  CG1 VAL A 246     7109   6611   7352    208    229   -554       C  
ATOM   3212  CG2 VAL A 246       0.618  -4.523  63.652  1.00 42.93           C  
ANISOU 3212  CG2 VAL A 246     5615   5007   5689    348    330   -526       C  
ATOM   3213  N   VAL A 247       1.003  -8.104  60.883  1.00 45.44           N  
ANISOU 3213  N   VAL A 247     5548   5498   6218    209    167   -469       N  
ATOM   3214  CA  VAL A 247       1.542  -8.952  59.828  1.00 40.22           C  
ANISOU 3214  CA  VAL A 247     4846   4853   5583    172    110   -477       C  
ATOM   3215  C   VAL A 247       0.429  -9.461  58.918  1.00 49.08           C  
ANISOU 3215  C   VAL A 247     5923   5979   6747    174     89   -420       C  
ATOM   3216  O   VAL A 247       0.614  -9.576  57.699  1.00 51.61           O  
ANISOU 3216  O   VAL A 247     6242   6289   7080    155     55   -425       O  
ATOM   3217  CB  VAL A 247       2.361 -10.099  60.447  1.00 40.18           C  
ANISOU 3217  CB  VAL A 247     4836   4872   5559    158     76   -495       C  
ATOM   3218  CG1 VAL A 247       2.712 -11.144  59.396  1.00 39.35           C  
ANISOU 3218  CG1 VAL A 247     4720   4768   5461    156     27   -494       C  
ATOM   3219  CG2 VAL A 247       3.626  -9.543  61.084  1.00 39.62           C  
ANISOU 3219  CG2 VAL A 247     4792   4817   5443    133     76   -534       C  
ATOM   3220  N   LYS A 248      -0.753  -9.739  59.479  1.00 40.02           N  
ANISOU 3220  N   LYS A 248     4736   4855   5614    191    106   -349       N  
ATOM   3221  CA  LYS A 248      -1.870 -10.155  58.639  1.00 47.33           C  
ANISOU 3221  CA  LYS A 248     5607   5800   6575    166     71   -265       C  
ATOM   3222  C   LYS A 248      -2.285  -9.039  57.689  1.00 50.63           C  
ANISOU 3222  C   LYS A 248     6013   6215   7010    189     99   -247       C  
ATOM   3223  O   LYS A 248      -2.575  -9.286  56.507  1.00 45.86           O  
ANISOU 3223  O   LYS A 248     5394   5606   6425    147     47   -220       O  
ATOM   3224  CB  LYS A 248      -3.052 -10.581  59.509  1.00 41.85           C  
ANISOU 3224  CB  LYS A 248     4847   5165   5890    176     87   -160       C  
ATOM   3225  CG  LYS A 248      -4.316 -10.872  58.717  1.00 58.35           C  
ANISOU 3225  CG  LYS A 248     6856   7302   8011    133     43    -35       C  
ATOM   3226  CD  LYS A 248      -5.520 -11.077  59.617  1.00 64.71           C  
ANISOU 3226  CD  LYS A 248     7564   8201   8820    154     75    103       C  
ATOM   3227  CE  LYS A 248      -6.794 -11.202  58.797  1.00 70.26           C  
ANISOU 3227  CE  LYS A 248     8164   8981   9553    101     28    259       C  
ATOM   3228  NZ  LYS A 248      -8.007 -11.219  59.658  1.00 76.06           N  
ANISOU 3228  NZ  LYS A 248     8768   9844  10285    141     78    429       N  
ATOM   3229  N   MET A 249      -2.279  -7.795  58.178  1.00 41.93           N  
ANISOU 3229  N   MET A 249     4942   5101   5888    256    176   -265       N  
ATOM   3230  CA  MET A 249      -2.631  -6.680  57.303  1.00 44.01           C  
ANISOU 3230  CA  MET A 249     5211   5349   6160    287    206   -250       C  
ATOM   3231  C   MET A 249      -1.635  -6.557  56.153  1.00 42.70           C  
ANISOU 3231  C   MET A 249     5079   5146   5999    231    157   -319       C  
ATOM   3232  O   MET A 249      -2.024  -6.413  54.981  1.00 40.57           O  
ANISOU 3232  O   MET A 249     4782   4879   5753    214    133   -288       O  
ATOM   3233  CB  MET A 249      -2.691  -5.379  58.104  1.00 44.72           C  
ANISOU 3233  CB  MET A 249     5381   5405   6206    375    294   -266       C  
ATOM   3234  CG  MET A 249      -3.091  -4.167  57.274  1.00 51.41           C  
ANISOU 3234  CG  MET A 249     6256   6224   7053    424    331   -246       C  
ATOM   3235  SD  MET A 249      -3.079  -2.629  58.212  1.00 53.07           S  
ANISOU 3235  SD  MET A 249     6630   6352   7181    536    426   -276       S  
ATOM   3236  CE  MET A 249      -1.319  -2.361  58.405  1.00 48.72           C  
ANISOU 3236  CE  MET A 249     6200   5721   6592    420    361   -405       C  
ATOM   3237  N   MET A 250      -0.338  -6.635  56.467  1.00 39.87           N  
ANISOU 3237  N   MET A 250     4770   4766   5612    202    142   -399       N  
ATOM   3238  CA  MET A 250       0.653  -6.499  55.402  1.00 39.56           C  
ANISOU 3238  CA  MET A 250     4745   4718   5568    163    107   -442       C  
ATOM   3239  C   MET A 250       0.600  -7.667  54.419  1.00 48.39           C  
ANISOU 3239  C   MET A 250     5839   5849   6699    140     49   -428       C  
ATOM   3240  O   MET A 250       0.864  -7.480  53.222  1.00 57.70           O  
ANISOU 3240  O   MET A 250     7024   7023   7877    130     30   -435       O  
ATOM   3241  CB  MET A 250       2.051  -6.346  55.993  1.00 39.48           C  
ANISOU 3241  CB  MET A 250     4770   4713   5519    135    102   -497       C  
ATOM   3242  CG  MET A 250       2.199  -5.107  56.870  1.00 47.69           C  
ANISOU 3242  CG  MET A 250     5883   5714   6523    133    136   -515       C  
ATOM   3243  SD  MET A 250       1.268  -3.682  56.252  1.00 53.81           S  
ANISOU 3243  SD  MET A 250     6710   6431   7303    174    180   -491       S  
ATOM   3244  CE  MET A 250       2.233  -3.212  54.821  1.00 56.26           C  
ANISOU 3244  CE  MET A 250     7008   6751   7618    107    138   -504       C  
ATOM   3245  N   ILE A 251       0.244  -8.866  54.888  1.00 47.87           N  
ANISOU 3245  N   ILE A 251     5764   5789   6634    132     17   -406       N  
ATOM   3246  CA  ILE A 251       0.098  -9.989  53.968  1.00 43.56           C  
ANISOU 3246  CA  ILE A 251     5244   5226   6079    104    -52   -391       C  
ATOM   3247  C   ILE A 251      -1.075  -9.755  53.026  1.00 43.94           C  
ANISOU 3247  C   ILE A 251     5269   5273   6155     72    -81   -323       C  
ATOM   3248  O   ILE A 251      -1.004 -10.076  51.831  1.00 40.82           O  
ANISOU 3248  O   ILE A 251     4918   4851   5742     49   -131   -326       O  
ATOM   3249  CB  ILE A 251      -0.062 -11.308  54.747  1.00 51.07           C  
ANISOU 3249  CB  ILE A 251     6218   6170   7018     88    -92   -375       C  
ATOM   3250  CG1 ILE A 251       1.247 -11.692  55.436  1.00 48.77           C  
ANISOU 3250  CG1 ILE A 251     5954   5885   6690    126    -72   -437       C  
ATOM   3251  CG2 ILE A 251      -0.533 -12.428  53.825  1.00 40.10           C  
ANISOU 3251  CG2 ILE A 251     4895   4736   5607     41   -181   -342       C  
ATOM   3252  CD1 ILE A 251       1.090 -12.790  56.462  1.00 41.71           C  
ANISOU 3252  CD1 ILE A 251     5076   4985   5786    118    -97   -421       C  
ATOM   3253  N   VAL A 252      -2.171  -9.188  53.539  1.00 40.12           N  
ANISOU 3253  N   VAL A 252     4715   4824   5703     79    -48   -251       N  
ATOM   3254  CA  VAL A 252      -3.296  -8.890  52.656  1.00 40.56           C  
ANISOU 3254  CA  VAL A 252     4723   4903   5783     52    -74   -161       C  
ATOM   3255  C   VAL A 252      -2.878  -7.868  51.605  1.00 54.92           C  
ANISOU 3255  C   VAL A 252     6562   6701   7603     73    -51   -200       C  
ATOM   3256  O   VAL A 252      -3.250  -7.974  50.427  1.00 46.88           O  
ANISOU 3256  O   VAL A 252     5550   5678   6586     32   -104   -167       O  
ATOM   3257  CB  VAL A 252      -4.510  -8.406  53.473  1.00 49.47           C  
ANISOU 3257  CB  VAL A 252     5757   6100   6938     89    -21    -53       C  
ATOM   3258  CG1 VAL A 252      -5.631  -7.945  52.547  1.00 44.27           C  
ANISOU 3258  CG1 VAL A 252     5026   5491   6304     75    -37     61       C  
ATOM   3259  CG2 VAL A 252      -5.003  -9.511  54.396  1.00 41.48           C  
ANISOU 3259  CG2 VAL A 252     4711   5124   5924     51    -56     10       C  
ATOM   3260  N   VAL A 253      -2.038  -6.905  51.999  1.00 47.82           N  
ANISOU 3260  N   VAL A 253     5689   5786   6695    123     16   -270       N  
ATOM   3261  CA  VAL A 253      -1.559  -5.905  51.043  1.00 41.59           C  
ANISOU 3261  CA  VAL A 253     4924   4977   5903    130     33   -301       C  
ATOM   3262  C   VAL A 253      -0.736  -6.567  49.938  1.00 59.61           C  
ANISOU 3262  C   VAL A 253     7245   7245   8158     97    -22   -343       C  
ATOM   3263  O   VAL A 253      -0.955  -6.328  48.737  1.00 40.70           O  
ANISOU 3263  O   VAL A 253     4856   4845   5763     82    -47   -324       O  
ATOM   3264  CB  VAL A 253      -0.748  -4.817  51.772  1.00 48.94           C  
ANISOU 3264  CB  VAL A 253     5897   5885   6814    160     92   -357       C  
ATOM   3265  CG1 VAL A 253       0.039  -3.979  50.777  1.00 39.71           C  
ANISOU 3265  CG1 VAL A 253     4757   4699   5633    141     89   -388       C  
ATOM   3266  CG2 VAL A 253      -1.661  -3.939  52.620  1.00 40.28           C  
ANISOU 3266  CG2 VAL A 253     4804   4779   5720    224    158   -314       C  
ATOM   3267  N   VAL A 254       0.220  -7.416  50.326  1.00 43.25           N  
ANISOU 3267  N   VAL A 254     5207   5173   6054    101    -36   -393       N  
ATOM   3268  CA  VAL A 254       1.103  -8.022  49.331  1.00 41.03           C  
ANISOU 3268  CA  VAL A 254     4977   4885   5727    110    -66   -426       C  
ATOM   3269  C   VAL A 254       0.327  -8.956  48.408  1.00 51.96           C  
ANISOU 3269  C   VAL A 254     6418   6232   7093     80   -139   -394       C  
ATOM   3270  O   VAL A 254       0.579  -9.005  47.195  1.00 48.76           O  
ANISOU 3270  O   VAL A 254     6064   5810   6651     87   -162   -402       O  
ATOM   3271  CB  VAL A 254       2.268  -8.754  50.021  1.00 45.44           C  
ANISOU 3271  CB  VAL A 254     5556   5463   6245    146    -54   -468       C  
ATOM   3272  CG1 VAL A 254       3.199  -9.362  48.986  1.00 50.54           C  
ANISOU 3272  CG1 VAL A 254     6260   6117   6828    196    -64   -486       C  
ATOM   3273  CG2 VAL A 254       3.028  -7.801  50.914  1.00 68.18           C  
ANISOU 3273  CG2 VAL A 254     8389   8382   9134    144     -5   -485       C  
ATOM   3274  N   CYS A 255      -0.638  -9.703  48.955  1.00 42.16           N  
ANISOU 3274  N   CYS A 255     5175   4976   5866     37   -186   -346       N  
ATOM   3275  CA  CYS A 255      -1.432 -10.593  48.114  1.00 48.30           C  
ANISOU 3275  CA  CYS A 255     6024   5712   6617    -28   -283   -298       C  
ATOM   3276  C   CYS A 255      -2.292  -9.806  47.137  1.00 47.57           C  
ANISOU 3276  C   CYS A 255     5886   5637   6550    -69   -302   -237       C  
ATOM   3277  O   CYS A 255      -2.451 -10.207  45.975  1.00 50.70           O  
ANISOU 3277  O   CYS A 255     6368   5993   6903   -109   -372   -226       O  
ATOM   3278  CB  CYS A 255      -2.308 -11.502  48.979  1.00 48.99           C  
ANISOU 3278  CB  CYS A 255     6103   5797   6716    -92   -340   -234       C  
ATOM   3279  SG  CYS A 255      -1.415 -12.792  49.887  1.00 55.46           S  
ANISOU 3279  SG  CYS A 255     7019   6570   7485    -58   -351   -296       S  
ATOM   3280  N   THR A 256      -2.848  -8.674  47.583  1.00 49.70           N  
ANISOU 3280  N   THR A 256     6040   5962   6881    -51   -239   -194       N  
ATOM   3281  CA  THR A 256      -3.631  -7.846  46.675  1.00 47.04           C  
ANISOU 3281  CA  THR A 256     5654   5650   6568    -70   -246   -127       C  
ATOM   3282  C   THR A 256      -2.766  -7.320  45.540  1.00 45.39           C  
ANISOU 3282  C   THR A 256     5503   5414   6331    -44   -232   -193       C  
ATOM   3283  O   THR A 256      -3.191  -7.305  44.378  1.00 41.19           O  
ANISOU 3283  O   THR A 256     4996   4872   5782    -85   -286   -156       O  
ATOM   3284  CB  THR A 256      -4.269  -6.691  47.446  1.00 44.54           C  
ANISOU 3284  CB  THR A 256     5229   5389   6305    -16   -160    -73       C  
ATOM   3285  OG1 THR A 256      -5.133  -7.213  48.463  1.00 45.00           O  
ANISOU 3285  OG1 THR A 256     5221   5493   6382    -29   -166      9       O  
ATOM   3286  CG2 THR A 256      -5.071  -5.803  46.512  1.00 41.49           C  
ANISOU 3286  CG2 THR A 256     4790   5034   5942    -16   -159      6       C  
ATOM   3287  N   PHE A 257      -1.523  -6.942  45.851  1.00 40.32           N  
ANISOU 3287  N   PHE A 257     4878   4767   5674     16   -167   -278       N  
ATOM   3288  CA  PHE A 257      -0.604  -6.482  44.813  1.00 40.22           C  
ANISOU 3288  CA  PHE A 257     4904   4751   5627     42   -150   -322       C  
ATOM   3289  C   PHE A 257      -0.303  -7.596  43.815  1.00 42.18           C  
ANISOU 3289  C   PHE A 257     5264   4961   5801     39   -214   -341       C  
ATOM   3290  O   PHE A 257      -0.334  -7.385  42.592  1.00 51.60           O  
ANISOU 3290  O   PHE A 257     6498   6145   6964     33   -237   -332       O  
ATOM   3291  CB  PHE A 257       0.681  -5.973  45.470  1.00 39.86           C  
ANISOU 3291  CB  PHE A 257     4840   4731   5573     86    -83   -379       C  
ATOM   3292  CG  PHE A 257       1.744  -5.525  44.503  1.00 39.92           C  
ANISOU 3292  CG  PHE A 257     4863   4764   5541    110    -62   -400       C  
ATOM   3293  CD1 PHE A 257       2.640  -6.437  43.961  1.00 40.16           C  
ANISOU 3293  CD1 PHE A 257     4951   4808   5500    159    -69   -424       C  
ATOM   3294  CD2 PHE A 257       1.876  -4.185  44.172  1.00 39.89           C  
ANISOU 3294  CD2 PHE A 257     4821   4775   5561     95    -30   -386       C  
ATOM   3295  CE1 PHE A 257       3.632  -6.025  43.086  1.00 44.56           C  
ANISOU 3295  CE1 PHE A 257     5503   5414   6012    196    -39   -422       C  
ATOM   3296  CE2 PHE A 257       2.871  -3.761  43.299  1.00 40.06           C  
ANISOU 3296  CE2 PHE A 257     4841   4836   5544    106    -14   -387       C  
ATOM   3297  CZ  PHE A 257       3.749  -4.683  42.754  1.00 43.40           C  
ANISOU 3297  CZ  PHE A 257     5296   5295   5897    159    -14   -400       C  
ATOM   3298  N   ALA A 258      -0.024  -8.799  44.324  1.00 42.11           N  
ANISOU 3298  N   ALA A 258     5327   4922   5751     50   -244   -366       N  
ATOM   3299  CA  ALA A 258       0.328  -9.909  43.443  1.00 44.42           C  
ANISOU 3299  CA  ALA A 258     5776   5155   5947     72   -299   -391       C  
ATOM   3300  C   ALA A 258      -0.826 -10.259  42.515  1.00 44.65           C  
ANISOU 3300  C   ALA A 258     5879   5130   5954    -21   -404   -335       C  
ATOM   3301  O   ALA A 258      -0.629 -10.458  41.306  1.00 49.78           O  
ANISOU 3301  O   ALA A 258     6645   5739   6529     -7   -437   -348       O  
ATOM   3302  CB  ALA A 258       0.730 -11.127  44.275  1.00 41.53           C  
ANISOU 3302  CB  ALA A 258     5489   4751   5537    104   -315   -420       C  
ATOM   3303  N   ILE A 259      -2.045 -10.291  43.058  1.00 46.68           N  
ANISOU 3303  N   ILE A 259     6064   5400   6271   -118   -457   -258       N  
ATOM   3304  CA  ILE A 259      -3.215 -10.601  42.245  1.00 42.93           C  
ANISOU 3304  CA  ILE A 259     5633   4898   5779   -235   -574   -172       C  
ATOM   3305  C   ILE A 259      -3.451  -9.514  41.205  1.00 42.89           C  
ANISOU 3305  C   ILE A 259     5570   4930   5795   -236   -555   -145       C  
ATOM   3306  O   ILE A 259      -3.702  -9.806  40.030  1.00 45.07           O  
ANISOU 3306  O   ILE A 259     5957   5160   6006   -287   -636   -127       O  
ATOM   3307  CB  ILE A 259      -4.448 -10.791  43.147  1.00 46.43           C  
ANISOU 3307  CB  ILE A 259     5966   5389   6286   -332   -623    -62       C  
ATOM   3308  CG1 ILE A 259      -4.284 -12.033  44.024  1.00 59.64           C  
ANISOU 3308  CG1 ILE A 259     7726   7011   7923   -355   -668    -80       C  
ATOM   3309  CG2 ILE A 259      -5.720 -10.869  42.313  1.00 44.19           C  
ANISOU 3309  CG2 ILE A 259     5672   5121   5996   -469   -742     66       C  
ATOM   3310  CD1 ILE A 259      -5.423 -12.245  44.995  1.00 64.78           C  
ANISOU 3310  CD1 ILE A 259     8253   7727   8633   -446   -708     41       C  
ATOM   3311  N   CYS A 260      -3.358  -8.243  41.609  1.00 44.22           N  
ANISOU 3311  N   CYS A 260     5588   5171   6043   -179   -452   -142       N  
ATOM   3312  CA  CYS A 260      -3.659  -7.159  40.683  1.00 48.74           C  
ANISOU 3312  CA  CYS A 260     6104   5775   6639   -180   -434   -107       C  
ATOM   3313  C   CYS A 260      -2.655  -7.082  39.546  1.00 55.71           C  
ANISOU 3313  C   CYS A 260     7092   6624   7451   -131   -421   -179       C  
ATOM   3314  O   CYS A 260      -3.022  -6.698  38.430  1.00 48.39           O  
ANISOU 3314  O   CYS A 260     6183   5696   6506   -162   -457   -143       O  
ATOM   3315  CB  CYS A 260      -3.711  -5.825  41.427  1.00 41.72           C  
ANISOU 3315  CB  CYS A 260     5075   4945   5832   -120   -327    -94       C  
ATOM   3316  SG  CYS A 260      -5.195  -5.594  42.405  1.00 55.48           S  
ANISOU 3316  SG  CYS A 260     6679   6756   7647   -145   -326     36       S  
ATOM   3317  N   TRP A 261      -1.394  -7.445  39.790  1.00 47.89           N  
ANISOU 3317  N   TRP A 261     6163   5620   6414    -48   -367   -265       N  
ATOM   3318  CA  TRP A 261      -0.403  -7.268  38.737  1.00 42.10           C  
ANISOU 3318  CA  TRP A 261     5500   4886   5609     21   -333   -310       C  
ATOM   3319  C   TRP A 261      -0.085  -8.529  37.941  1.00 43.06           C  
ANISOU 3319  C   TRP A 261     5824   4933   5603     50   -393   -342       C  
ATOM   3320  O   TRP A 261       0.519  -8.411  36.868  1.00 43.28           O  
ANISOU 3320  O   TRP A 261     5927   4960   5555    112   -373   -361       O  
ATOM   3321  CB  TRP A 261       0.889  -6.680  39.316  1.00 45.10           C  
ANISOU 3321  CB  TRP A 261     5804   5328   6003    106   -227   -355       C  
ATOM   3322  CG  TRP A 261       0.730  -5.233  39.642  1.00 52.82           C  
ANISOU 3322  CG  TRP A 261     6647   6353   7068     81   -175   -329       C  
ATOM   3323  CD1 TRP A 261       0.517  -4.688  40.874  1.00 43.94           C  
ANISOU 3323  CD1 TRP A 261     5436   5244   6016     67   -139   -324       C  
ATOM   3324  CD2 TRP A 261       0.730  -4.140  38.713  1.00 53.09           C  
ANISOU 3324  CD2 TRP A 261     6648   6411   7115     73   -157   -303       C  
ATOM   3325  NE1 TRP A 261       0.401  -3.322  40.773  1.00 53.12           N  
ANISOU 3325  NE1 TRP A 261     6536   6424   7225     56   -100   -300       N  
ATOM   3326  CE2 TRP A 261       0.528  -2.960  39.457  1.00 47.79           C  
ANISOU 3326  CE2 TRP A 261     5883   5755   6519     55   -112   -285       C  
ATOM   3327  CE3 TRP A 261       0.891  -4.045  37.326  1.00 52.38           C  
ANISOU 3327  CE3 TRP A 261     6612   6323   6968     83   -173   -292       C  
ATOM   3328  CZ2 TRP A 261       0.479  -1.699  38.863  1.00 47.26           C  
ANISOU 3328  CZ2 TRP A 261     5782   5699   6475     43    -88   -256       C  
ATOM   3329  CZ3 TRP A 261       0.845  -2.790  36.734  1.00 45.23           C  
ANISOU 3329  CZ3 TRP A 261     5647   5444   6095     66   -147   -260       C  
ATOM   3330  CH2 TRP A 261       0.638  -1.634  37.504  1.00 43.07           C  
ANISOU 3330  CH2 TRP A 261     5286   5179   5901     44   -107   -242       C  
ATOM   3331  N   LEU A 262      -0.484  -9.721  38.400  1.00 43.33           N  
ANISOU 3331  N   LEU A 262     5969   4897   5600     12   -469   -344       N  
ATOM   3332  CA  LEU A 262      -0.163 -10.918  37.621  1.00 49.31           C  
ANISOU 3332  CA  LEU A 262     6973   5553   6211     51   -530   -380       C  
ATOM   3333  C   LEU A 262      -0.716 -10.893  36.195  1.00 59.78           C  
ANISOU 3333  C   LEU A 262     8425   6826   7464     -7   -613   -352       C  
ATOM   3334  O   LEU A 262       0.061 -11.149  35.255  1.00 50.47           O  
ANISOU 3334  O   LEU A 262     7398   5613   6166    100   -585   -396       O  
ATOM   3335  CB  LEU A 262      -0.637 -12.167  38.374  1.00 48.56           C  
ANISOU 3335  CB  LEU A 262     6994   5372   6086     -9   -618   -375       C  
ATOM   3336  CG  LEU A 262      -0.359 -13.477  37.631  1.00 54.34           C  
ANISOU 3336  CG  LEU A 262     8038   5963   6645     31   -694   -414       C  
ATOM   3337  CD1 LEU A 262       1.141 -13.707  37.505  1.00 48.23           C  
ANISOU 3337  CD1 LEU A 262     7338   5205   5781    248   -570   -487       C  
ATOM   3338  CD2 LEU A 262      -1.036 -14.654  38.318  1.00 53.20           C  
ANISOU 3338  CD2 LEU A 262     8022   5719   6472    -74   -814   -391       C  
ATOM   3339  N   PRO A 263      -2.010 -10.619  35.951  1.00 50.42           N  
ANISOU 3339  N   PRO A 263     7186   5640   6331   -162   -714   -270       N  
ATOM   3340  CA  PRO A 263      -2.485 -10.615  34.555  1.00 46.27           C  
ANISOU 3340  CA  PRO A 263     6790   5065   5725   -226   -803   -239       C  
ATOM   3341  C   PRO A 263      -1.767  -9.619  33.661  1.00 57.42           C  
ANISOU 3341  C   PRO A 263     8151   6538   7130   -124   -705   -267       C  
ATOM   3342  O   PRO A 263      -1.577  -9.893  32.474  1.00 46.80           O  
ANISOU 3342  O   PRO A 263     6984   5134   5663    -99   -742   -284       O  
ATOM   3343  CB  PRO A 263      -3.977 -10.275  34.695  1.00 50.45           C  
ANISOU 3343  CB  PRO A 263     7186   5637   6346   -406   -906   -116       C  
ATOM   3344  CG  PRO A 263      -4.326 -10.682  36.086  1.00 46.10           C  
ANISOU 3344  CG  PRO A 263     6540   5109   5869   -444   -909    -89       C  
ATOM   3345  CD  PRO A 263      -3.111 -10.352  36.892  1.00 51.03           C  
ANISOU 3345  CD  PRO A 263     7089   5771   6529   -282   -753   -185       C  
ATOM   3346  N   PHE A 264      -1.349  -8.479  34.207  1.00 53.30           N  
ANISOU 3346  N   PHE A 264     7407   6124   6721    -68   -585   -268       N  
ATOM   3347  CA  PHE A 264      -0.682  -7.449  33.413  1.00 47.03           C  
ANISOU 3347  CA  PHE A 264     6549   5395   5927      6   -500   -278       C  
ATOM   3348  C   PHE A 264       0.667  -7.939  32.893  1.00 48.18           C  
ANISOU 3348  C   PHE A 264     6825   5534   5945    160   -428   -341       C  
ATOM   3349  O   PHE A 264       0.961  -7.865  31.687  1.00 48.67           O  
ANISOU 3349  O   PHE A 264     6992   5588   5914    209   -426   -343       O  
ATOM   3350  CB  PHE A 264      -0.529  -6.201  34.289  1.00 48.97           C  
ANISOU 3350  CB  PHE A 264     6561   5735   6310     14   -405   -261       C  
ATOM   3351  CG  PHE A 264       0.063  -5.009  33.598  1.00 43.36           C  
ANISOU 3351  CG  PHE A 264     5770   5091   5614     57   -331   -254       C  
ATOM   3352  CD1 PHE A 264       1.428  -4.777  33.640  1.00 43.23           C  
ANISOU 3352  CD1 PHE A 264     5728   5134   5564    160   -235   -288       C  
ATOM   3353  CD2 PHE A 264      -0.750  -4.085  32.960  1.00 43.39           C  
ANISOU 3353  CD2 PHE A 264     5709   5110   5669     -9   -358   -194       C  
ATOM   3354  CE1 PHE A 264       1.979  -3.660  33.035  1.00 46.04           C  
ANISOU 3354  CE1 PHE A 264     6003   5558   5932    178   -177   -263       C  
ATOM   3355  CE2 PHE A 264      -0.207  -2.964  32.352  1.00 44.21           C  
ANISOU 3355  CE2 PHE A 264     5746   5266   5785     22   -295   -183       C  
ATOM   3356  CZ  PHE A 264       1.161  -2.752  32.390  1.00 45.82           C  
ANISOU 3356  CZ  PHE A 264     5932   5525   5954    108   -208   -217       C  
ATOM   3357  N   HIS A 265       1.494  -8.472  33.794  1.00 47.64           N  
ANISOU 3357  N   HIS A 265     6755   5481   5866    251   -365   -382       N  
ATOM   3358  CA  HIS A 265       2.784  -9.006  33.382  1.00 55.22           C  
ANISOU 3358  CA  HIS A 265     7826   6458   6698    424   -285   -419       C  
ATOM   3359  C   HIS A 265       2.631 -10.241  32.506  1.00 57.21           C  
ANISOU 3359  C   HIS A 265     8383   6577   6777    472   -359   -448       C  
ATOM   3360  O   HIS A 265       3.440 -10.450  31.596  1.00 54.09           O  
ANISOU 3360  O   HIS A 265     8115   6190   6248    620   -300   -461       O  
ATOM   3361  CB  HIS A 265       3.633  -9.305  34.614  1.00 45.10           C  
ANISOU 3361  CB  HIS A 265     6459   5232   5445    504   -208   -438       C  
ATOM   3362  CG  HIS A 265       4.049  -8.078  35.363  1.00 49.40           C  
ANISOU 3362  CG  HIS A 265     6748   5902   6119    473   -132   -410       C  
ATOM   3363  ND1 HIS A 265       4.888  -7.128  34.821  1.00 48.14           N  
ANISOU 3363  ND1 HIS A 265     6480   5854   5958    522    -54   -376       N  
ATOM   3364  CD2 HIS A 265       3.734  -7.637  36.604  1.00 50.81           C  
ANISOU 3364  CD2 HIS A 265     6782   6102   6420    391   -131   -406       C  
ATOM   3365  CE1 HIS A 265       5.080  -6.160  35.699  1.00 53.96           C  
ANISOU 3365  CE1 HIS A 265     7032   6664   6807    457    -20   -354       C  
ATOM   3366  NE2 HIS A 265       4.390  -6.444  36.789  1.00 50.20           N  
ANISOU 3366  NE2 HIS A 265     6539   6131   6405    387    -61   -378       N  
ATOM   3367  N   ILE A 266       1.596 -11.055  32.733  1.00 53.26           N  
ANISOU 3367  N   ILE A 266     8020   5954   6265    348   -492   -449       N  
ATOM   3368  CA  ILE A 266       1.360 -12.176  31.826  1.00 61.07           C  
ANISOU 3368  CA  ILE A 266     9343   6787   7072    360   -591   -473       C  
ATOM   3369  C   ILE A 266       0.997 -11.665  30.438  1.00 55.08           C  
ANISOU 3369  C   ILE A 266     8655   6016   6256    320   -635   -449       C  
ATOM   3370  O   ILE A 266       1.450 -12.204  29.420  1.00 56.03           O  
ANISOU 3370  O   ILE A 266     9030   6062   6199    432   -633   -480       O  
ATOM   3371  CB  ILE A 266       0.268 -13.107  32.386  1.00 66.84           C  
ANISOU 3371  CB  ILE A 266    10198   7393   7805    191   -751   -456       C  
ATOM   3372  CG1 ILE A 266       0.807 -13.924  33.559  1.00 58.68           C  
ANISOU 3372  CG1 ILE A 266     9191   6335   6769    271   -710   -494       C  
ATOM   3373  CG2 ILE A 266      -0.279 -14.024  31.294  1.00 67.86           C  
ANISOU 3373  CG2 ILE A 266    10680   7348   7755    125   -902   -458       C  
ATOM   3374  CD1 ILE A 266      -0.181 -14.940  34.090  1.00 60.28           C  
ANISOU 3374  CD1 ILE A 266     9539   6410   6955    106   -871   -470       C  
ATOM   3375  N   PHE A 267       0.199 -10.597  30.376  1.00 58.50           N  
ANISOU 3375  N   PHE A 267     8871   6525   6829    176   -665   -389       N  
ATOM   3376  CA  PHE A 267      -0.207 -10.047  29.091  1.00 57.16           C  
ANISOU 3376  CA  PHE A 267     8747   6354   6617    126   -710   -356       C  
ATOM   3377  C   PHE A 267       0.983  -9.507  28.320  1.00 58.50           C  
ANISOU 3377  C   PHE A 267     8907   6604   6719    309   -571   -381       C  
ATOM   3378  O   PHE A 267       1.019  -9.599  27.088  1.00 50.12           O  
ANISOU 3378  O   PHE A 267     8020   5497   5527    343   -598   -383       O  
ATOM   3379  CB  PHE A 267      -1.243  -8.941  29.307  1.00 53.69           C  
ANISOU 3379  CB  PHE A 267     8050   5999   6350    -37   -749   -275       C  
ATOM   3380  CG  PHE A 267      -1.668  -8.245  28.042  1.00 57.14           C  
ANISOU 3380  CG  PHE A 267     8496   6453   6762    -90   -789   -230       C  
ATOM   3381  CD1 PHE A 267      -0.997  -7.118  27.589  1.00 49.88           C  
ANISOU 3381  CD1 PHE A 267     7434   5637   5883      1   -669   -229       C  
ATOM   3382  CD2 PHE A 267      -2.749  -8.710  27.313  1.00 51.37           C  
ANISOU 3382  CD2 PHE A 267     7917   5637   5964   -246   -957   -175       C  
ATOM   3383  CE1 PHE A 267      -1.388  -6.480  26.427  1.00 48.40           C  
ANISOU 3383  CE1 PHE A 267     7255   5463   5670    -47   -706   -185       C  
ATOM   3384  CE2 PHE A 267      -3.148  -8.073  26.153  1.00 58.50           C  
ANISOU 3384  CE2 PHE A 267     8826   6561   6842   -299   -998   -127       C  
ATOM   3385  CZ  PHE A 267      -2.466  -6.957  25.709  1.00 52.46           C  
ANISOU 3385  CZ  PHE A 267     7918   5895   6120   -191   -867   -137       C  
ATOM   3386  N   PHE A 268       1.962  -8.937  29.018  1.00 51.97           N  
ANISOU 3386  N   PHE A 268     7877   5902   5969    420   -428   -388       N  
ATOM   3387  CA  PHE A 268       3.118  -8.418  28.297  1.00 48.52           C  
ANISOU 3387  CA  PHE A 268     7404   5569   5464    582   -299   -382       C  
ATOM   3388  C   PHE A 268       4.232  -9.441  28.099  1.00 62.95           C  
ANISOU 3388  C   PHE A 268     9426   7379   7113    805   -218   -417       C  
ATOM   3389  O   PHE A 268       5.121  -9.204  27.273  1.00 56.13           O  
ANISOU 3389  O   PHE A 268     8581   6597   6149    960   -119   -395       O  
ATOM   3390  CB  PHE A 268       3.656  -7.166  28.990  1.00 47.31           C  
ANISOU 3390  CB  PHE A 268     6936   5573   5467    572   -198   -344       C  
ATOM   3391  CG  PHE A 268       2.899  -5.924  28.626  1.00 60.28           C  
ANISOU 3391  CG  PHE A 268     8428   7251   7226    433   -234   -298       C  
ATOM   3392  CD1 PHE A 268       3.118  -5.300  27.406  1.00 55.35           C  
ANISOU 3392  CD1 PHE A 268     7816   6669   6545    463   -210   -267       C  
ATOM   3393  CD2 PHE A 268       1.944  -5.399  29.481  1.00 50.87           C  
ANISOU 3393  CD2 PHE A 268     7094   6048   6187    289   -286   -279       C  
ATOM   3394  CE1 PHE A 268       2.413  -4.163  27.055  1.00 48.42           C  
ANISOU 3394  CE1 PHE A 268     6811   5817   5769    343   -242   -220       C  
ATOM   3395  CE2 PHE A 268       1.235  -4.259  29.138  1.00 51.05           C  
ANISOU 3395  CE2 PHE A 268     6993   6099   6304    189   -309   -228       C  
ATOM   3396  CZ  PHE A 268       1.469  -3.642  27.920  1.00 51.35           C  
ANISOU 3396  CZ  PHE A 268     7046   6173   6290    212   -291   -200       C  
ATOM   3397  N   LEU A 269       4.209 -10.570  28.810  1.00 59.42           N  
ANISOU 3397  N   LEU A 269     9128   6834   6615    839   -252   -459       N  
ATOM   3398  CA  LEU A 269       5.198 -11.617  28.587  1.00 59.08           C  
ANISOU 3398  CA  LEU A 269     9310   6757   6381   1075   -175   -488       C  
ATOM   3399  C   LEU A 269       4.726 -12.701  27.628  1.00 71.40           C  
ANISOU 3399  C   LEU A 269    11281   8114   7735   1104   -278   -532       C  
ATOM   3400  O   LEU A 269       5.560 -13.456  27.116  1.00 69.17           O  
ANISOU 3400  O   LEU A 269    11233   7794   7253   1339   -200   -552       O  
ATOM   3401  CB  LEU A 269       5.596 -12.264  29.914  1.00 61.49           C  
ANISOU 3401  CB  LEU A 269     9570   7067   6728   1125   -141   -507       C  
ATOM   3402  CG  LEU A 269       6.380 -11.369  30.873  1.00 60.60           C  
ANISOU 3402  CG  LEU A 269     9103   7154   6767   1143    -25   -461       C  
ATOM   3403  CD1 LEU A 269       6.500 -12.029  32.233  1.00 56.20           C  
ANISOU 3403  CD1 LEU A 269     8514   6577   6262   1145    -27   -483       C  
ATOM   3404  CD2 LEU A 269       7.750 -11.052  30.301  1.00 64.20           C  
ANISOU 3404  CD2 LEU A 269     9486   7777   7130   1361    131   -404       C  
ATOM   3405  N   LEU A 270       3.423 -12.785  27.364  1.00 81.26           N  
ANISOU 3405  N   LEU A 270    12629   9234   9012    876   -452   -536       N  
ATOM   3406  CA  LEU A 270       2.901 -13.799  26.451  1.00 77.73           C  
ANISOU 3406  CA  LEU A 270    12598   8578   8359    857   -584   -570       C  
ATOM   3407  C   LEU A 270       3.553 -13.795  25.073  1.00 80.86           C  
ANISOU 3407  C   LEU A 270    13203   8965   8556   1047   -512   -579       C  
ATOM   3408  O   LEU A 270       3.833 -14.891  24.559  1.00 92.46           O  
ANISOU 3408  O   LEU A 270    15066  10273   9791   1192   -531   -626       O  
ATOM   3409  CB  LEU A 270       1.377 -13.647  26.323  1.00 79.10           C  
ANISOU 3409  CB  LEU A 270    12772   8668   8616    547   -789   -533       C  
ATOM   3410  CG  LEU A 270       0.554 -14.481  27.306  1.00 82.46           C  
ANISOU 3410  CG  LEU A 270    13264   8982   9086    375   -931   -529       C  
ATOM   3411  CD1 LEU A 270      -0.928 -14.418  26.968  1.00 84.30           C  
ANISOU 3411  CD1 LEU A 270    13523   9148   9361     76  -1143   -459       C  
ATOM   3412  CD2 LEU A 270       1.047 -15.920  27.317  1.00 74.89           C  
ANISOU 3412  CD2 LEU A 270    12705   7839   7912    515   -954   -594       C  
ATOM   3413  N   PRO A 271       3.804 -12.654  24.419  1.00 73.95           N  
ANISOU 3413  N   PRO A 271    12113   8241   7742   1063   -432   -535       N  
ATOM   3414  CA  PRO A 271       4.408 -12.713  23.075  1.00 79.55           C  
ANISOU 3414  CA  PRO A 271    13038   8944   8245   1253   -363   -537       C  
ATOM   3415  C   PRO A 271       5.741 -13.443  23.028  1.00 92.21           C  
ANISOU 3415  C   PRO A 271    14800  10575   9662   1593   -195   -553       C  
ATOM   3416  O   PRO A 271       6.064 -14.046  21.997  1.00106.86           O  
ANISOU 3416  O   PRO A 271    16997  12332  11272   1773   -172   -575       O  
ATOM   3417  CB  PRO A 271       4.561 -11.233  22.699  1.00 64.57           C  
ANISOU 3417  CB  PRO A 271    10791   7247   6494   1204   -286   -471       C  
ATOM   3418  CG  PRO A 271       3.501 -10.544  23.470  1.00 67.66           C  
ANISOU 3418  CG  PRO A 271    10923   7659   7125    924   -395   -448       C  
ATOM   3419  CD  PRO A 271       3.441 -11.270  24.781  1.00 62.77           C  
ANISOU 3419  CD  PRO A 271    10292   6989   6568    901   -417   -479       C  
ATOM   3420  N   TYR A 272       6.532 -13.401  24.103  1.00 96.97           N  
ANISOU 3420  N   TYR A 272    15169  11313  10362   1698    -73   -531       N  
ATOM   3421  CA  TYR A 272       7.829 -14.071  24.089  1.00 93.56           C  
ANISOU 3421  CA  TYR A 272    14852  10941   9755   2038     99   -518       C  
ATOM   3422  C   TYR A 272       7.698 -15.587  23.967  1.00100.14           C  
ANISOU 3422  C   TYR A 272    16171  11523  10356   2164     36   -593       C  
ATOM   3423  O   TYR A 272       8.615 -16.241  23.457  1.00110.37           O  
ANISOU 3423  O   TYR A 272    17702  12811  11422   2484    165   -587       O  
ATOM   3424  CB  TYR A 272       8.624 -13.711  25.346  1.00 85.93           C  
ANISOU 3424  CB  TYR A 272    13521  10175   8952   2086    217   -466       C  
ATOM   3425  CG  TYR A 272       8.933 -12.236  25.482  1.00 87.26           C  
ANISOU 3425  CG  TYR A 272    13250  10586   9318   1984    286   -384       C  
ATOM   3426  CD1 TYR A 272       9.056 -11.423  24.361  1.00 86.98           C  
ANISOU 3426  CD1 TYR A 272    13162  10639   9248   1998    324   -336       C  
ATOM   3427  CD2 TYR A 272       9.096 -11.655  26.733  1.00 84.29           C  
ANISOU 3427  CD2 TYR A 272    12537  10338   9153   1867    304   -352       C  
ATOM   3428  CE1 TYR A 272       9.335 -10.074  24.485  1.00 87.93           C  
ANISOU 3428  CE1 TYR A 272    12907  10963   9541   1892    374   -257       C  
ATOM   3429  CE2 TYR A 272       9.376 -10.308  26.866  1.00 84.25           C  
ANISOU 3429  CE2 TYR A 272    12175  10526   9310   1762    351   -278       C  
ATOM   3430  CZ  TYR A 272       9.494  -9.522  25.741  1.00 83.93           C  
ANISOU 3430  CZ  TYR A 272    12093  10565   9233   1771    383   -229       C  
ATOM   3431  OH  TYR A 272       9.771  -8.179  25.869  1.00 82.35           O  
ANISOU 3431  OH  TYR A 272    11564  10541   9186   1655    417   -150       O  
ATOM   3432  N   ILE A 273       6.590 -16.167  24.428  1.00 94.38           N  
ANISOU 3432  N   ILE A 273    15605  10587   9668   1925   -159   -651       N  
ATOM   3433  CA  ILE A 273       6.399 -17.611  24.346  1.00 93.92           C  
ANISOU 3433  CA  ILE A 273    16037  10264   9386   2005   -249   -719       C  
ATOM   3434  C   ILE A 273       5.283 -18.015  23.388  1.00110.39           C  
ANISOU 3434  C   ILE A 273    18501  12104  11338   1809   -464   -760       C  
ATOM   3435  O   ILE A 273       5.223 -19.193  23.001  1.00114.96           O  
ANISOU 3435  O   ILE A 273    19576  12438  11667   1902   -539   -816       O  
ATOM   3436  CB  ILE A 273       6.150 -18.228  25.738  1.00 97.63           C  
ANISOU 3436  CB  ILE A 273    16455  10674   9967   1906   -310   -741       C  
ATOM   3437  CG1 ILE A 273       4.781 -17.811  26.282  1.00 97.99           C  
ANISOU 3437  CG1 ILE A 273    16319  10680  10230   1508   -508   -733       C  
ATOM   3438  CG2 ILE A 273       7.259 -17.834  26.702  1.00103.07           C  
ANISOU 3438  CG2 ILE A 273    16776  11606  10781   2085   -111   -693       C  
ATOM   3439  CD1 ILE A 273       4.380 -18.544  27.546  1.00 90.32           C  
ANISOU 3439  CD1 ILE A 273    15358   9621   9339   1391   -596   -750       C  
ATOM   3440  N   ASN A 274       4.402 -17.094  22.997  1.00114.84           N  
ANISOU 3440  N   ASN A 274    18867  12721  12048   1541   -571   -727       N  
ATOM   3441  CA  ASN A 274       3.329 -17.370  22.048  1.00112.81           C  
ANISOU 3441  CA  ASN A 274    18926  12264  11673   1330   -785   -741       C  
ATOM   3442  C   ASN A 274       2.759 -16.049  21.547  1.00105.37           C  
ANISOU 3442  C   ASN A 274    17652  11477  10905   1137   -813   -680       C  
ATOM   3443  O   ASN A 274       2.051 -15.363  22.295  1.00108.21           O  
ANISOU 3443  O   ASN A 274    17659  11940  11516    899   -875   -633       O  
ATOM   3444  CB  ASN A 274       2.231 -18.223  22.691  1.00116.28           C  
ANISOU 3444  CB  ASN A 274    19551  12501  12129   1053  -1020   -752       C  
ATOM   3445  CG  ASN A 274       1.152 -18.631  21.703  1.00117.61           C  
ANISOU 3445  CG  ASN A 274    20086  12455  12146    818  -1265   -747       C  
ATOM   3446  OD1 ASN A 274       1.350 -18.573  20.488  1.00108.37           O  
ANISOU 3446  OD1 ASN A 274    19158  11228  10790    920  -1255   -764       O  
ATOM   3447  ND2 ASN A 274       0.003 -19.048  22.221  1.00120.44           N  
ANISOU 3447  ND2 ASN A 274    20482  12703  12575    494  -1494   -711       N  
ATOM   3448  N   PRO A 275       3.043 -15.661  20.292  1.00116.34           N  
ANISOU 3448  N   PRO A 275    19156  12889  12161   1245   -763   -673       N  
ATOM   3449  CA  PRO A 275       2.642 -14.329  19.808  1.00132.71           C  
ANISOU 3449  CA  PRO A 275    20895  15128  14399   1096   -763   -610       C  
ATOM   3450  C   PRO A 275       1.164 -14.026  20.004  1.00161.05           C  
ANISOU 3450  C   PRO A 275    24374  18670  18148    718   -987   -565       C  
ATOM   3451  O   PRO A 275       0.814 -13.191  20.845  1.00170.57           O  
ANISOU 3451  O   PRO A 275    25168  20027  19612    579   -970   -516       O  
ATOM   3452  CB  PRO A 275       3.011 -14.379  18.320  1.00123.48           C  
ANISOU 3452  CB  PRO A 275    20025  13905  12986   1258   -728   -622       C  
ATOM   3453  CG  PRO A 275       4.131 -15.362  18.253  1.00120.04           C  
ANISOU 3453  CG  PRO A 275    19900  13399  12309   1611   -585   -673       C  
ATOM   3454  CD  PRO A 275       3.812 -16.410  19.283  1.00119.03           C  
ANISOU 3454  CD  PRO A 275    19936  13110  12181   1541   -685   -719       C  
ATOM   3455  N   ASP A 276       0.298 -14.695  19.245  1.00170.11           N  
ANISOU 3455  N   ASP A 276    25892  19612  19131    554  -1196   -569       N  
ATOM   3456  CA  ASP A 276      -1.162 -14.599  19.401  1.00171.09           C  
ANISOU 3456  CA  ASP A 276    25945  19688  19371    184  -1434   -497       C  
ATOM   3457  C   ASP A 276      -1.558 -13.127  19.280  1.00160.00           C  
ANISOU 3457  C   ASP A 276    24091  18504  18198     71  -1390   -415       C  
ATOM   3458  O   ASP A 276      -1.193 -12.490  18.278  1.00155.08           O  
ANISOU 3458  O   ASP A 276    23464  17943  17514    169  -1315   -412       O  
ATOM   3459  CB  ASP A 276      -1.555 -15.291  20.703  1.00175.08           C  
ANISOU 3459  CB  ASP A 276    26413  20138  19972     65  -1512   -494       C  
ATOM   3460  CG  ASP A 276      -3.054 -15.458  20.850  1.00176.05           C  
ANISOU 3460  CG  ASP A 276    26525  20199  20165   -310  -1774   -399       C  
ATOM   3461  OD1 ASP A 276      -3.660 -16.150  20.006  1.00180.08           O  
ANISOU 3461  OD1 ASP A 276    27420  20522  20478   -459  -1978   -384       O  
ATOM   3462  OD2 ASP A 276      -3.624 -14.900  21.811  1.00171.85           O  
ANISOU 3462  OD2 ASP A 276    25607  19811  19876   -456  -1779   -326       O  
ATOM   3463  N   LEU A 277      -2.280 -12.557  20.248  1.00150.90           N  
ANISOU 3463  N   LEU A 277    22573  17467  17295   -116  -1428   -345       N  
ATOM   3464  CA  LEU A 277      -2.691 -11.151  20.231  1.00139.97           C  
ANISOU 3464  CA  LEU A 277    20777  16278  16126   -207  -1382   -264       C  
ATOM   3465  C   LEU A 277      -3.442 -10.803  18.946  1.00142.34           C  
ANISOU 3465  C   LEU A 277    21183  16550  16349   -352  -1516   -201       C  
ATOM   3466  O   LEU A 277      -3.098  -9.862  18.225  1.00142.39           O  
ANISOU 3466  O   LEU A 277    21061  16663  16378   -269  -1417   -188       O  
ATOM   3467  CB  LEU A 277      -1.491 -10.224  20.442  1.00133.23           C  
ANISOU 3467  CB  LEU A 277    19659  15597  15367     32  -1132   -299       C  
ATOM   3468  CG  LEU A 277      -0.760 -10.352  21.783  1.00133.70           C  
ANISOU 3468  CG  LEU A 277    19543  15723  15534    154   -997   -339       C  
ATOM   3469  CD1 LEU A 277       0.210  -9.194  21.983  1.00135.76           C  
ANISOU 3469  CD1 LEU A 277    19486  16180  15918    308   -791   -332       C  
ATOM   3470  CD2 LEU A 277      -1.742 -10.441  22.945  1.00128.17           C  
ANISOU 3470  CD2 LEU A 277    18670  15025  15004    -51  -1102   -292       C  
ATOM   3471  N   TYR A 278      -4.472 -11.591  18.651  1.00137.66           N  
ANISOU 3471  N   TYR A 278    20835  15814  15656   -584  -1754   -151       N  
ATOM   3472  CA  TYR A 278      -5.329 -11.341  17.497  1.00117.92           C  
ANISOU 3472  CA  TYR A 278    18438  13286  13080   -770  -1920    -70       C  
ATOM   3473  C   TYR A 278      -6.776 -11.724  17.799  1.00109.15           C  
ANISOU 3473  C   TYR A 278    17308  12144  12021  -1110  -2175     63       C  
ATOM   3474  O   TYR A 278      -7.515 -10.962  18.424  1.00104.22           O  
ANISOU 3474  O   TYR A 278    16295  11685  11618  -1237  -2179    177       O  
ATOM   3475  CB  TYR A 278      -4.821 -12.102  16.282  1.00111.78           C  
ANISOU 3475  CB  TYR A 278    18153  12322  11998   -663  -1963   -151       C  
ATOM   3476  N   PHE A 282     -10.317  -9.352  19.839  1.00106.19           N  
ANISOU 3476  N   PHE A 282    15633  12350  12364  -1688  -2333    600       N  
ATOM   3477  CA  PHE A 282     -10.940  -9.042  21.120  1.00108.37           C  
ANISOU 3477  CA  PHE A 282    15561  12773  12843  -1739  -2298    706       C  
ATOM   3478  C   PHE A 282      -9.900  -8.611  22.150  1.00107.27           C  
ANISOU 3478  C   PHE A 282    15257  12675  12825  -1483  -2047    569       C  
ATOM   3479  O   PHE A 282     -10.188  -8.544  23.347  1.00 89.09           O  
ANISOU 3479  O   PHE A 282    12734  10456  10661  -1487  -1999    614       O  
ATOM   3480  CB  PHE A 282     -11.725 -10.241  21.631  1.00106.02           C  
ANISOU 3480  CB  PHE A 282    15398  12403  12484  -1972  -2513    800       C  
ATOM   3481  N   ILE A 283      -8.686  -8.326  21.675  1.00107.10           N  
ANISOU 3481  N   ILE A 283    15345  12605  12742  -1265  -1890    413       N  
ATOM   3482  CA  ILE A 283      -7.605  -7.957  22.583  1.00106.18           C  
ANISOU 3482  CA  ILE A 283    15092  12531  12720  -1038  -1668    294       C  
ATOM   3483  C   ILE A 283      -7.897  -6.635  23.287  1.00100.16           C  
ANISOU 3483  C   ILE A 283    13932  11946  12179   -997  -1540    365       C  
ATOM   3484  O   ILE A 283      -7.520  -6.454  24.453  1.00 92.67           O  
ANISOU 3484  O   ILE A 283    12826  11045  11342   -904  -1420    324       O  
ATOM   3485  CB  ILE A 283      -6.266  -7.920  21.815  1.00106.22           C  
ANISOU 3485  CB  ILE A 283    15286  12475  12599   -824  -1538    150       C  
ATOM   3486  CG1 ILE A 283      -5.499  -9.233  22.004  1.00114.15           C  
ANISOU 3486  CG1 ILE A 283    16611  13322  13438   -731  -1545     32       C  
ATOM   3487  CG2 ILE A 283      -5.405  -6.742  22.250  1.00102.74           C  
ANISOU 3487  CG2 ILE A 283    14572  12166  12299   -638  -1314    105       C  
ATOM   3488  CD1 ILE A 283      -6.219 -10.457  21.479  1.00121.27           C  
ANISOU 3488  CD1 ILE A 283    17866  14052  14159   -913  -1778     63       C  
ATOM   3489  N   GLN A 284      -8.588  -5.705  22.619  1.00 99.49           N  
ANISOU 3489  N   GLN A 284    13698  11955  12150  -1063  -1568    476       N  
ATOM   3490  CA  GLN A 284      -8.820  -4.398  23.228  1.00 90.11           C  
ANISOU 3490  CA  GLN A 284    12176  10914  11148   -994  -1436    539       C  
ATOM   3491  C   GLN A 284      -9.702  -4.504  24.466  1.00 86.84           C  
ANISOU 3491  C   GLN A 284    11563  10578  10857  -1068  -1461    646       C  
ATOM   3492  O   GLN A 284      -9.466  -3.809  25.463  1.00 76.09           O  
ANISOU 3492  O   GLN A 284    10003   9285   9623   -951  -1313    627       O  
ATOM   3493  CB  GLN A 284      -9.443  -3.441  22.210  1.00 80.42           C  
ANISOU 3493  CB  GLN A 284    10851   9765   9942  -1044  -1469    649       C  
ATOM   3494  CG  GLN A 284      -9.680  -2.034  22.750  1.00 89.00           C  
ANISOU 3494  CG  GLN A 284    11634  10982  11200   -952  -1330    715       C  
ATOM   3495  CD  GLN A 284     -10.266  -1.090  21.713  1.00104.06           C  
ANISOU 3495  CD  GLN A 284    13456  12961  13120   -987  -1358    826       C  
ATOM   3496  OE1 GLN A 284     -11.358  -0.552  21.895  1.00106.12           O  
ANISOU 3496  OE1 GLN A 284    13519  13334  13470  -1045  -1391    992       O  
ATOM   3497  NE2 GLN A 284      -9.537  -0.880  20.621  1.00108.65           N  
ANISOU 3497  NE2 GLN A 284    14183  13490  13609   -939  -1337    745       N  
ATOM   3498  N   GLN A 285     -10.710  -5.381  24.433  1.00 76.07           N  
ANISOU 3498  N   GLN A 285    10257   9203   9442  -1267  -1650    767       N  
ATOM   3499  CA  GLN A 285     -11.567  -5.548  25.603  1.00 75.65           C  
ANISOU 3499  CA  GLN A 285    10006   9244   9495  -1340  -1676    891       C  
ATOM   3500  C   GLN A 285     -10.822  -6.240  26.737  1.00 75.46           C  
ANISOU 3500  C   GLN A 285    10046   9148   9479  -1255  -1601    762       C  
ATOM   3501  O   GLN A 285     -11.009  -5.898  27.911  1.00 78.97           O  
ANISOU 3501  O   GLN A 285    10282   9679  10046  -1194  -1505    796       O  
ATOM   3502  CB  GLN A 285     -12.829  -6.327  25.233  1.00 81.65           C  
ANISOU 3502  CB  GLN A 285    10804  10029  10192  -1603  -1917   1082       C  
ATOM   3503  CG  GLN A 285     -13.745  -5.606  24.251  1.00 91.58           C  
ANISOU 3503  CG  GLN A 285    11941  11397  11458  -1703  -2000   1256       C  
ATOM   3504  CD  GLN A 285     -13.310  -5.776  22.807  1.00105.48           C  
ANISOU 3504  CD  GLN A 285    13972  13036  13067  -1743  -2084   1176       C  
ATOM   3505  OE1 GLN A 285     -13.007  -6.883  22.365  1.00114.88           O  
ANISOU 3505  OE1 GLN A 285    15481  14067  14099  -1837  -2215   1098       O  
ATOM   3506  NE2 GLN A 285     -13.274  -4.675  22.065  1.00113.02           N  
ANISOU 3506  NE2 GLN A 285    14821  14061  14062  -1661  -2005   1195       N  
ATOM   3507  N   VAL A 286      -9.981  -7.223  26.406  1.00 67.32           N  
ANISOU 3507  N   VAL A 286     9312   7959   8308  -1239  -1640    619       N  
ATOM   3508  CA  VAL A 286      -9.179  -7.885  27.428  1.00 59.60           C  
ANISOU 3508  CA  VAL A 286     8403   6912   7329  -1140  -1562    495       C  
ATOM   3509  C   VAL A 286      -8.155  -6.922  28.013  1.00 56.67           C  
ANISOU 3509  C   VAL A 286     7877   6596   7058   -918  -1333    383       C  
ATOM   3510  O   VAL A 286      -7.869  -6.953  29.216  1.00 56.88           O  
ANISOU 3510  O   VAL A 286     7798   6649   7165   -847  -1243    346       O  
ATOM   3511  CB  VAL A 286      -8.503  -9.140  26.848  1.00 63.06           C  
ANISOU 3511  CB  VAL A 286     9221   7165   7574  -1145  -1649    378       C  
ATOM   3512  CG1 VAL A 286      -7.740  -9.888  27.935  1.00 61.08           C  
ANISOU 3512  CG1 VAL A 286     9039   6849   7319  -1043  -1575    269       C  
ATOM   3513  CG2 VAL A 286      -9.536 -10.043  26.196  1.00 81.25           C  
ANISOU 3513  CG2 VAL A 286    11719   9394   9760  -1395  -1902    495       C  
ATOM   3514  N   TYR A 287      -7.590  -6.047  27.178  1.00 54.10           N  
ANISOU 3514  N   TYR A 287     7541   6290   6725   -819  -1246    337       N  
ATOM   3515  CA  TYR A 287      -6.581  -5.120  27.676  1.00 55.14           C  
ANISOU 3515  CA  TYR A 287     7542   6471   6938   -639  -1052    246       C  
ATOM   3516  C   TYR A 287      -7.183  -4.101  28.631  1.00 49.29           C  
ANISOU 3516  C   TYR A 287     6524   5843   6362   -623   -973    328       C  
ATOM   3517  O   TYR A 287      -6.552  -3.730  29.627  1.00 54.64           O  
ANISOU 3517  O   TYR A 287     7111   6541   7110   -517   -848    263       O  
ATOM   3518  CB  TYR A 287      -5.889  -4.409  26.516  1.00 56.17           C  
ANISOU 3518  CB  TYR A 287     7723   6603   7016   -556   -991    200       C  
ATOM   3519  CG  TYR A 287      -4.780  -3.501  26.984  1.00 65.45           C  
ANISOU 3519  CG  TYR A 287     8779   7829   8259   -400   -812    122       C  
ATOM   3520  CD1 TYR A 287      -4.927  -2.121  26.969  1.00 71.48           C  
ANISOU 3520  CD1 TYR A 287     9359   8673   9129   -372   -734    172       C  
ATOM   3521  CD2 TYR A 287      -3.592  -4.028  27.469  1.00 78.78           C  
ANISOU 3521  CD2 TYR A 287    10546   9487   9900   -286   -729     14       C  
ATOM   3522  CE1 TYR A 287      -3.911  -1.292  27.407  1.00 70.57           C  
ANISOU 3522  CE1 TYR A 287     9157   8593   9063   -261   -595    111       C  
ATOM   3523  CE2 TYR A 287      -2.574  -3.210  27.908  1.00 85.97           C  
ANISOU 3523  CE2 TYR A 287    11340  10458  10867   -173   -586    -33       C  
ATOM   3524  CZ  TYR A 287      -2.738  -1.845  27.875  1.00 81.70           C  
ANISOU 3524  CZ  TYR A 287    10632   9984  10425   -174   -528     15       C  
ATOM   3525  OH  TYR A 287      -1.717  -1.036  28.311  1.00 98.84           O  
ANISOU 3525  OH  TYR A 287    12711  12204  12640    -91   -409    -22       O  
ATOM   3526  N   LEU A 288      -8.406  -3.641  28.350  1.00 51.11           N  
ANISOU 3526  N   LEU A 288     6627   6150   6642   -722  -1045    481       N  
ATOM   3527  CA  LEU A 288      -9.052  -2.693  29.251  1.00 58.70           C  
ANISOU 3527  CA  LEU A 288     7344   7219   7739   -676   -961    575       C  
ATOM   3528  C   LEU A 288      -9.317  -3.324  30.608  1.00 63.33           C  
ANISOU 3528  C   LEU A 288     7870   7821   8372   -686   -956    591       C  
ATOM   3529  O   LEU A 288      -9.208  -2.657  31.645  1.00 55.32           O  
ANISOU 3529  O   LEU A 288     6722   6851   7446   -580   -831    580       O  
ATOM   3530  CB  LEU A 288     -10.356  -2.185  28.637  1.00 53.05           C  
ANISOU 3530  CB  LEU A 288     6501   6601   7053   -766  -1041    764       C  
ATOM   3531  CG  LEU A 288     -10.248  -1.025  27.649  1.00 48.90           C  
ANISOU 3531  CG  LEU A 288     5941   6101   6539   -709   -990    777       C  
ATOM   3532  CD1 LEU A 288     -11.609  -0.696  27.066  1.00 58.19           C  
ANISOU 3532  CD1 LEU A 288     6990   7386   7735   -808  -1086    985       C  
ATOM   3533  CD2 LEU A 288      -9.649   0.189  28.336  1.00 47.81           C  
ANISOU 3533  CD2 LEU A 288     5699   5977   6488   -539   -808    714       C  
ATOM   3534  N   ALA A 289      -9.637  -4.619  30.624  1.00 48.51           N  
ANISOU 3534  N   ALA A 289     6112   5895   6422   -816  -1095    613       N  
ATOM   3535  CA  ALA A 289      -9.872  -5.304  31.888  1.00 55.96           C  
ANISOU 3535  CA  ALA A 289     7009   6853   7402   -837  -1099    632       C  
ATOM   3536  C   ALA A 289      -8.568  -5.512  32.646  1.00 54.44           C  
ANISOU 3536  C   ALA A 289     6896   6583   7205   -703   -981    451       C  
ATOM   3537  O   ALA A 289      -8.485  -5.243  33.851  1.00 47.56           O  
ANISOU 3537  O   ALA A 289     5904   5755   6413   -628   -884    441       O  
ATOM   3538  CB  ALA A 289     -10.571  -6.640  31.635  1.00 51.31           C  
ANISOU 3538  CB  ALA A 289     6548   6221   6725  -1035  -1301    716       C  
ATOM   3539  N   ILE A 290      -7.530  -5.974  31.946  1.00 48.25           N  
ANISOU 3539  N   ILE A 290     6315   5696   6320   -662   -983    319       N  
ATOM   3540  CA  ILE A 290      -6.250  -6.227  32.596  1.00 46.20           C  
ANISOU 3540  CA  ILE A 290     6123   5386   6046   -533   -875    171       C  
ATOM   3541  C   ILE A 290      -5.631  -4.926  33.087  1.00 48.44           C  
ANISOU 3541  C   ILE A 290     6247   5734   6423   -404   -712    129       C  
ATOM   3542  O   ILE A 290      -5.064  -4.867  34.185  1.00 59.17           O  
ANISOU 3542  O   ILE A 290     7553   7103   7828   -330   -624     71       O  
ATOM   3543  CB  ILE A 290      -5.312  -6.973  31.630  1.00 46.63           C  
ANISOU 3543  CB  ILE A 290     6427   5336   5955   -493   -903     66       C  
ATOM   3544  CG1 ILE A 290      -5.817  -8.395  31.374  1.00 52.14           C  
ANISOU 3544  CG1 ILE A 290     7343   5929   6538   -617  -1070     89       C  
ATOM   3545  CG2 ILE A 290      -3.902  -6.998  32.169  1.00 49.02           C  
ANISOU 3545  CG2 ILE A 290     6753   5628   6245   -333   -768    -59       C  
ATOM   3546  CD1 ILE A 290      -4.944  -9.188  30.431  1.00 63.54           C  
ANISOU 3546  CD1 ILE A 290     9081   7251   7811   -551  -1095    -13       C  
ATOM   3547  N   MET A 291      -5.738  -3.860  32.293  1.00 51.98           N  
ANISOU 3547  N   MET A 291     6632   6222   6895   -385   -679    163       N  
ATOM   3548  CA  MET A 291      -5.200  -2.577  32.728  1.00 51.08           C  
ANISOU 3548  CA  MET A 291     6399   6151   6859   -282   -543    133       C  
ATOM   3549  C   MET A 291      -5.992  -2.013  33.899  1.00 50.09           C  
ANISOU 3549  C   MET A 291     6117   6080   6835   -267   -496    206       C  
ATOM   3550  O   MET A 291      -5.410  -1.430  34.823  1.00 47.85           O  
ANISOU 3550  O   MET A 291     5787   5798   6596   -186   -394    152       O  
ATOM   3551  CB  MET A 291      -5.180  -1.586  31.564  1.00 49.56           C  
ANISOU 3551  CB  MET A 291     6193   5978   6660   -271   -529    161       C  
ATOM   3552  CG  MET A 291      -4.977  -0.140  31.987  1.00 65.93           C  
ANISOU 3552  CG  MET A 291     8151   8086   8815   -196   -416    168       C  
ATOM   3553  SD  MET A 291      -4.386   0.909  30.649  1.00 76.65           S  
ANISOU 3553  SD  MET A 291     9534   9448  10142   -171   -384    160       S  
ATOM   3554  CE  MET A 291      -2.632   0.595  30.755  1.00 66.31           C  
ANISOU 3554  CE  MET A 291     8303   8122   8770   -108   -317     36       C  
ATOM   3555  N   TRP A 292      -7.317  -2.191  33.894  1.00 44.82           N  
ANISOU 3555  N   TRP A 292     5372   5465   6194   -342   -572    342       N  
ATOM   3556  CA  TRP A 292      -8.109  -1.693  35.012  1.00 46.80           C  
ANISOU 3556  CA  TRP A 292     5470   5785   6526   -298   -513    431       C  
ATOM   3557  C   TRP A 292      -7.732  -2.404  36.301  1.00 55.89           C  
ANISOU 3557  C   TRP A 292     6634   6916   7687   -277   -484    368       C  
ATOM   3558  O   TRP A 292      -7.623  -1.771  37.358  1.00 44.01           O  
ANISOU 3558  O   TRP A 292     5062   5427   6232   -184   -379    353       O  
ATOM   3559  CB  TRP A 292      -9.604  -1.863  34.739  1.00 46.05           C  
ANISOU 3559  CB  TRP A 292     5265   5783   6447   -386   -604    622       C  
ATOM   3560  CG  TRP A 292     -10.459  -1.269  35.829  1.00 58.22           C  
ANISOU 3560  CG  TRP A 292     6638   7421   8061   -304   -521    739       C  
ATOM   3561  CD1 TRP A 292     -11.062  -0.043  35.821  1.00 60.21           C  
ANISOU 3561  CD1 TRP A 292     6778   7741   8358   -199   -434    837       C  
ATOM   3562  CD2 TRP A 292     -10.785  -1.866  37.096  1.00 50.79           C  
ANISOU 3562  CD2 TRP A 292     5636   6518   7143   -297   -506    774       C  
ATOM   3563  NE1 TRP A 292     -11.748   0.156  36.996  1.00 52.22           N  
ANISOU 3563  NE1 TRP A 292     5646   6807   7386   -112   -359    933       N  
ATOM   3564  CE2 TRP A 292     -11.593  -0.947  37.794  1.00 47.48           C  
ANISOU 3564  CE2 TRP A 292     5067   6196   6776   -176   -402    897       C  
ATOM   3565  CE3 TRP A 292     -10.478  -3.091  37.702  1.00 49.10           C  
ANISOU 3565  CE3 TRP A 292     5490   6264   6903   -372   -566    719       C  
ATOM   3566  CZ2 TRP A 292     -12.093  -1.212  39.070  1.00 49.33           C  
ANISOU 3566  CZ2 TRP A 292     5209   6498   7035   -126   -353    968       C  
ATOM   3567  CZ3 TRP A 292     -10.973  -3.350  38.966  1.00 50.86           C  
ANISOU 3567  CZ3 TRP A 292     5615   6551   7160   -341   -527    786       C  
ATOM   3568  CH2 TRP A 292     -11.774  -2.416  39.636  1.00 49.97           C  
ANISOU 3568  CH2 TRP A 292     5343   6545   7097   -219   -420    912       C  
ATOM   3569  N   LEU A 293      -7.518  -3.719  36.233  1.00 46.28           N  
ANISOU 3569  N   LEU A 293     5524   5651   6410   -360   -577    330       N  
ATOM   3570  CA  LEU A 293      -7.175  -4.464  37.438  1.00 44.19           C  
ANISOU 3570  CA  LEU A 293     5275   5365   6151   -344   -557    277       C  
ATOM   3571  C   LEU A 293      -5.828  -4.019  37.984  1.00 54.53           C  
ANISOU 3571  C   LEU A 293     6620   6633   7465   -231   -440    133       C  
ATOM   3572  O   LEU A 293      -5.675  -3.800  39.192  1.00 48.94           O  
ANISOU 3572  O   LEU A 293     5855   5941   6800   -173   -365    112       O  
ATOM   3573  CB  LEU A 293      -7.169  -5.965  37.145  1.00 44.74           C  
ANISOU 3573  CB  LEU A 293     5489   5370   6138   -452   -689    263       C  
ATOM   3574  CG  LEU A 293      -6.687  -6.857  38.293  1.00 46.29           C  
ANISOU 3574  CG  LEU A 293     5731   5530   6328   -434   -675    197       C  
ATOM   3575  CD1 LEU A 293      -7.551  -6.648  39.531  1.00 44.45           C  
ANISOU 3575  CD1 LEU A 293     5331   5384   6175   -433   -639    298       C  
ATOM   3576  CD2 LEU A 293      -6.678  -8.324  37.882  1.00 45.14           C  
ANISOU 3576  CD2 LEU A 293     5775   5294   6082   -536   -813    183       C  
ATOM   3577  N   ALA A 294      -4.848  -3.841  37.096  1.00 45.92           N  
ANISOU 3577  N   ALA A 294     5621   5502   6324   -202   -424     49       N  
ATOM   3578  CA  ALA A 294      -3.512  -3.463  37.538  1.00 45.12           C  
ANISOU 3578  CA  ALA A 294     5539   5386   6218   -116   -329    -59       C  
ATOM   3579  C   ALA A 294      -3.520  -2.090  38.201  1.00 51.29           C  
ANISOU 3579  C   ALA A 294     6224   6196   7071    -61   -234    -46       C  
ATOM   3580  O   ALA A 294      -2.961  -1.906  39.288  1.00 49.57           O  
ANISOU 3580  O   ALA A 294     5990   5973   6872    -19   -172    -95       O  
ATOM   3581  CB  ALA A 294      -2.553  -3.484  36.349  1.00 42.27           C  
ANISOU 3581  CB  ALA A 294     5273   5004   5782    -92   -329   -115       C  
ATOM   3582  N   MET A 295      -4.158  -1.110  37.561  1.00 42.15           N  
ANISOU 3582  N   MET A 295     5018   5057   5940    -59   -225     21       N  
ATOM   3583  CA  MET A 295      -4.212   0.232  38.128  1.00 42.06           C  
ANISOU 3583  CA  MET A 295     4959   5047   5976      5   -138     35       C  
ATOM   3584  C   MET A 295      -5.142   0.320  39.330  1.00 44.09           C  
ANISOU 3584  C   MET A 295     5148   5328   6278     47   -102     98       C  
ATOM   3585  O   MET A 295      -4.976   1.222  40.159  1.00 42.25           O  
ANISOU 3585  O   MET A 295     4923   5071   6061    118    -22     80       O  
ATOM   3586  CB  MET A 295      -4.631   1.237  37.053  1.00 44.26           C  
ANISOU 3586  CB  MET A 295     5222   5334   6263     11   -136     95       C  
ATOM   3587  CG  MET A 295      -3.761   1.173  35.804  1.00 55.52           C  
ANISOU 3587  CG  MET A 295     6711   6748   7637    -24   -167     47       C  
ATOM   3588  SD  MET A 295      -3.719   2.719  34.881  1.00 74.58           S  
ANISOU 3588  SD  MET A 295     9121   9155  10062     -3   -130     83       S  
ATOM   3589  CE  MET A 295      -2.847   3.773  36.038  1.00 69.17           C  
ANISOU 3589  CE  MET A 295     8464   8423   9394     43    -43     26       C  
ATOM   3590  N   SER A 296      -6.095  -0.607  39.463  1.00 42.70           N  
ANISOU 3590  N   SER A 296     4919   5198   6109      3   -164    178       N  
ATOM   3591  CA  SER A 296      -6.953  -0.614  40.642  1.00 47.35           C  
ANISOU 3591  CA  SER A 296     5426   5833   6731     50   -123    255       C  
ATOM   3592  C   SER A 296      -6.155  -0.874  41.911  1.00 50.08           C  
ANISOU 3592  C   SER A 296     5815   6140   7072     86    -72    156       C  
ATOM   3593  O   SER A 296      -6.625  -0.549  43.006  1.00 48.02           O  
ANISOU 3593  O   SER A 296     5515   5900   6830    160     -5    195       O  
ATOM   3594  CB  SER A 296      -8.061  -1.661  40.503  1.00 45.00           C  
ANISOU 3594  CB  SER A 296     5053   5608   6436    -37   -220    380       C  
ATOM   3595  OG  SER A 296      -7.538  -2.971  40.610  1.00 50.97           O  
ANISOU 3595  OG  SER A 296     5885   6323   7157   -122   -297    310       O  
ATOM   3596  N   SER A 297      -4.952  -1.440  41.782  1.00 41.83           N  
ANISOU 3596  N   SER A 297     4852   5045   5995     48    -96     40       N  
ATOM   3597  CA  SER A 297      -4.107  -1.711  42.937  1.00 43.46           C  
ANISOU 3597  CA  SER A 297     5094   5225   6193     73    -56    -46       C  
ATOM   3598  C   SER A 297      -3.738  -0.441  43.692  1.00 46.41           C  
ANISOU 3598  C   SER A 297     5493   5567   6574    144     34    -77       C  
ATOM   3599  O   SER A 297      -3.391  -0.515  44.876  1.00 58.30           O  
ANISOU 3599  O   SER A 297     7020   7057   8075    171     71   -118       O  
ATOM   3600  CB  SER A 297      -2.836  -2.435  42.492  1.00 40.88           C  
ANISOU 3600  CB  SER A 297     4840   4871   5820     38    -90   -141       C  
ATOM   3601  OG  SER A 297      -1.957  -1.554  41.817  1.00 41.98           O  
ANISOU 3601  OG  SER A 297     5010   4998   5944     49    -60   -182       O  
ATOM   3602  N   THR A 298      -3.801   0.720  43.039  1.00 42.98           N  
ANISOU 3602  N   THR A 298     5077   5111   6141    170     62    -58       N  
ATOM   3603  CA  THR A 298      -3.463   1.973  43.701  1.00 46.42           C  
ANISOU 3603  CA  THR A 298     5583   5488   6565    228    132    -86       C  
ATOM   3604  C   THR A 298      -4.520   2.427  44.698  1.00 42.40           C  
ANISOU 3604  C   THR A 298     5067   4979   6062    333    201    -19       C  
ATOM   3605  O   THR A 298      -4.248   3.351  45.470  1.00 49.12           O  
ANISOU 3605  O   THR A 298     6020   5760   6883    392    259    -52       O  
ATOM   3606  CB  THR A 298      -3.234   3.085  42.668  1.00 57.67           C  
ANISOU 3606  CB  THR A 298     7051   6879   7982    222    136    -78       C  
ATOM   3607  OG1 THR A 298      -4.462   3.383  41.992  1.00 46.32           O  
ANISOU 3607  OG1 THR A 298     5554   5477   6569    269    142     25       O  
ATOM   3608  CG2 THR A 298      -2.188   2.666  41.647  1.00 41.53           C  
ANISOU 3608  CG2 THR A 298     5006   4853   5921    137     81   -127       C  
ATOM   3609  N   MET A 299      -5.719   1.836  44.691  1.00 42.78           N  
ANISOU 3609  N   MET A 299     5009   5109   6138    360    195     86       N  
ATOM   3610  CA  MET A 299      -6.786   2.266  45.587  1.00 46.04           C  
ANISOU 3610  CA  MET A 299     5391   5554   6549    487    276    180       C  
ATOM   3611  C   MET A 299      -7.068   1.320  46.753  1.00 50.29           C  
ANISOU 3611  C   MET A 299     5878   6142   7089    495    284    198       C  
ATOM   3612  O   MET A 299      -7.871   1.675  47.623  1.00 60.39           O  
ANISOU 3612  O   MET A 299     7137   7456   8354    619    366    277       O  
ATOM   3613  CB  MET A 299      -8.088   2.470  44.796  1.00 45.72           C  
ANISOU 3613  CB  MET A 299     5234   5605   6533    529    276    339       C  
ATOM   3614  CG  MET A 299      -8.813   1.176  44.438  1.00 59.15           C  
ANISOU 3614  CG  MET A 299     6792   7417   8263    429    186    436       C  
ATOM   3615  SD  MET A 299     -10.110   1.391  43.198  1.00 68.53           S  
ANISOU 3615  SD  MET A 299     7845   8719   9475    417    143    626       S  
ATOM   3616  CE  MET A 299     -11.565   1.599  44.219  1.00 82.22           C  
ANISOU 3616  CE  MET A 299     9434  10595  11212    568    237    831       C  
ATOM   3617  N   TYR A 300      -6.445   0.140  46.810  1.00 44.32           N  
ANISOU 3617  N   TYR A 300     5108   5390   6340    384    208    133       N  
ATOM   3618  CA  TYR A 300      -6.881  -0.848  47.797  1.00 42.98           C  
ANISOU 3618  CA  TYR A 300     4876   5277   6176    380    203    174       C  
ATOM   3619  C   TYR A 300      -6.238  -0.645  49.166  1.00 49.39           C  
ANISOU 3619  C   TYR A 300     5774   6034   6957    438    267     88       C  
ATOM   3620  O   TYR A 300      -6.891  -0.870  50.191  1.00 47.34           O  
ANISOU 3620  O   TYR A 300     5474   5823   6690    506    315    151       O  
ATOM   3621  CB  TYR A 300      -6.602  -2.263  47.293  1.00 42.48           C  
ANISOU 3621  CB  TYR A 300     4786   5232   6124    243     89    153       C  
ATOM   3622  CG  TYR A 300      -7.405  -2.632  46.070  1.00 51.32           C  
ANISOU 3622  CG  TYR A 300     5836   6406   7258    167      6    256       C  
ATOM   3623  CD1 TYR A 300      -8.794  -2.559  46.079  1.00 47.85           C  
ANISOU 3623  CD1 TYR A 300     5268   6072   6838    189      8    432       C  
ATOM   3624  CD2 TYR A 300      -6.776  -3.056  44.905  1.00 42.53           C  
ANISOU 3624  CD2 TYR A 300     4783   5246   6128     76    -76    193       C  
ATOM   3625  CE1 TYR A 300      -9.531  -2.894  44.959  1.00 49.61           C  
ANISOU 3625  CE1 TYR A 300     5427   6353   7070     95    -86    542       C  
ATOM   3626  CE2 TYR A 300      -7.503  -3.394  43.784  1.00 43.07           C  
ANISOU 3626  CE2 TYR A 300     4815   5352   6196     -4   -165    285       C  
ATOM   3627  CZ  TYR A 300      -8.879  -3.310  43.814  1.00 49.62           C  
ANISOU 3627  CZ  TYR A 300     5517   6285   7050     -8   -178    460       C  
ATOM   3628  OH  TYR A 300      -9.608  -3.647  42.699  1.00 54.64           O  
ANISOU 3628  OH  TYR A 300     6115   6965   7680   -112   -284    567       O  
ATOM   3629  N   ASN A 301      -4.967  -0.238  49.208  1.00 42.29           N  
ANISOU 3629  N   ASN A 301     4990   5047   6033    405    263    -40       N  
ATOM   3630  CA  ASN A 301      -4.260  -0.167  50.487  1.00 45.68           C  
ANISOU 3630  CA  ASN A 301     5506   5426   6425    425    298   -119       C  
ATOM   3631  C   ASN A 301      -4.951   0.723  51.514  1.00 51.11           C  
ANISOU 3631  C   ASN A 301     6258   6089   7072    566    398    -77       C  
ATOM   3632  O   ASN A 301      -5.113   0.278  52.664  1.00 51.80           O  
ANISOU 3632  O   ASN A 301     6346   6195   7140    605    430    -72       O  
ATOM   3633  CB  ASN A 301      -2.809   0.276  50.260  1.00 41.61           C  
ANISOU 3633  CB  ASN A 301     5090   4837   5883    350    267   -229       C  
ATOM   3634  CG  ASN A 301      -1.980  -0.785  49.574  1.00 50.02           C  
ANISOU 3634  CG  ASN A 301     6102   5939   6966    249    189   -272       C  
ATOM   3635  OD1 ASN A 301      -2.402  -1.934  49.449  1.00 62.76           O  
ANISOU 3635  OD1 ASN A 301     7641   7602   8601    227    152   -242       O  
ATOM   3636  ND2 ASN A 301      -0.784  -0.409  49.134  1.00 54.29           N  
ANISOU 3636  ND2 ASN A 301     6689   6453   7484    190    164   -331       N  
ATOM   3637  N   PRO A 302      -5.365   1.959  51.202  1.00 57.06           N  
ANISOU 3637  N   PRO A 302     7085   6796   7800    659    457    -43       N  
ATOM   3638  CA  PRO A 302      -6.097   2.738  52.216  1.00 54.77           C  
ANISOU 3638  CA  PRO A 302     6881   6479   7449    832    567      7       C  
ATOM   3639  C   PRO A 302      -7.364   2.057  52.688  1.00 50.93           C  
ANISOU 3639  C   PRO A 302     6239   6128   6982    924    617    146       C  
ATOM   3640  O   PRO A 302      -7.727   2.183  53.865  1.00 46.20           O  
ANISOU 3640  O   PRO A 302     5691   5532   6330   1046    699    171       O  
ATOM   3641  CB  PRO A 302      -6.400   4.060  51.500  1.00 54.79           C  
ANISOU 3641  CB  PRO A 302     6976   6416   7424    918    611     37       C  
ATOM   3642  CG  PRO A 302      -5.376   4.144  50.413  1.00 62.91           C  
ANISOU 3642  CG  PRO A 302     8021   7398   8484    759    517    -45       C  
ATOM   3643  CD  PRO A 302      -5.170   2.733  49.964  1.00 58.98           C  
ANISOU 3643  CD  PRO A 302     7356   7000   8053    630    433    -47       C  
ATOM   3644  N   ILE A 303      -8.052   1.337  51.801  1.00 49.26           N  
ANISOU 3644  N   ILE A 303     5844   6036   6839    863    563    249       N  
ATOM   3645  CA  ILE A 303      -9.203   0.549  52.226  1.00 51.59           C  
ANISOU 3645  CA  ILE A 303     5968   6480   7154    903    581    405       C  
ATOM   3646  C   ILE A 303      -8.760  -0.591  53.132  1.00 46.96           C  
ANISOU 3646  C   ILE A 303     5364   5907   6573    819    538    351       C  
ATOM   3647  O   ILE A 303      -9.444  -0.933  54.105  1.00 47.30           O  
ANISOU 3647  O   ILE A 303     5343   6033   6597    899    594    443       O  
ATOM   3648  CB  ILE A 303      -9.970   0.030  50.997  1.00 54.50           C  
ANISOU 3648  CB  ILE A 303     6164   6961   7583    813    500    533       C  
ATOM   3649  CG1 ILE A 303     -10.303   1.187  50.051  1.00 46.67           C  
ANISOU 3649  CG1 ILE A 303     5195   5951   6587    892    539    577       C  
ATOM   3650  CG2 ILE A 303     -11.233  -0.703  51.422  1.00 47.14           C  
ANISOU 3650  CG2 ILE A 303     5041   6204   6666    836    507    733       C  
ATOM   3651  CD1 ILE A 303     -11.071   0.760  48.813  1.00 46.94           C  
ANISOU 3651  CD1 ILE A 303     5068   6097   6672    798    453    712       C  
ATOM   3652  N   ILE A 304      -7.596  -1.180  52.845  1.00 46.12           N  
ANISOU 3652  N   ILE A 304     5315   5726   6484    671    446    212       N  
ATOM   3653  CA  ILE A 304      -7.104  -2.282  53.664  1.00 43.64           C  
ANISOU 3653  CA  ILE A 304     4993   5418   6172    596    403    159       C  
ATOM   3654  C   ILE A 304      -6.711  -1.786  55.050  1.00 56.01           C  
ANISOU 3654  C   ILE A 304     6679   6927   7677    694    487     95       C  
ATOM   3655  O   ILE A 304      -7.019  -2.430  56.063  1.00 49.01           O  
ANISOU 3655  O   ILE A 304     5751   6092   6778    719    509    133       O  
ATOM   3656  CB  ILE A 304      -5.934  -2.986  52.954  1.00 43.31           C  
ANISOU 3656  CB  ILE A 304     4988   5318   6150    447    298     41       C  
ATOM   3657  CG1 ILE A 304      -6.442  -3.744  51.726  1.00 44.99           C  
ANISOU 3657  CG1 ILE A 304     5106   5584   6403    348    204    113       C  
ATOM   3658  CG2 ILE A 304      -5.211  -3.927  53.907  1.00 42.02           C  
ANISOU 3658  CG2 ILE A 304     4852   5140   5974    397    270    -31       C  
ATOM   3659  CD1 ILE A 304      -5.342  -4.336  50.865  1.00 41.65           C  
ANISOU 3659  CD1 ILE A 304     4744   5101   5980    240    118      5       C  
ATOM   3660  N   TYR A 305      -6.051  -0.626  55.125  1.00 43.98           N  
ANISOU 3660  N   TYR A 305     5317   5289   6104    742    528      4       N  
ATOM   3661  CA  TYR A 305      -5.654  -0.092  56.424  1.00 46.87           C  
ANISOU 3661  CA  TYR A 305     5838   5578   6391    820    592    -60       C  
ATOM   3662  C   TYR A 305      -6.870   0.248  57.274  1.00 46.86           C  
ANISOU 3662  C   TYR A 305     5828   5635   6343   1011    712     57       C  
ATOM   3663  O   TYR A 305      -6.857   0.058  58.497  1.00 52.31           O  
ANISOU 3663  O   TYR A 305     6574   6320   6979   1071    759     45       O  
ATOM   3664  CB  TYR A 305      -4.788   1.156  56.248  1.00 44.58           C  
ANISOU 3664  CB  TYR A 305     5749   5144   6044    814    593   -161       C  
ATOM   3665  CG  TYR A 305      -3.550   0.971  55.404  1.00 55.09           C  
ANISOU 3665  CG  TYR A 305     7081   6440   7411    641    487   -252       C  
ATOM   3666  CD1 TYR A 305      -2.931  -0.269  55.295  1.00 42.59           C  
ANISOU 3666  CD1 TYR A 305     5389   4916   5876    521    411   -284       C  
ATOM   3667  CD2 TYR A 305      -2.995   2.047  54.719  1.00 47.89           C  
ANISOU 3667  CD2 TYR A 305     6285   5438   6475    609    469   -295       C  
ATOM   3668  CE1 TYR A 305      -1.796  -0.434  54.522  1.00 54.54           C  
ANISOU 3668  CE1 TYR A 305     6899   6416   7408    397    333   -349       C  
ATOM   3669  CE2 TYR A 305      -1.860   1.895  53.945  1.00 48.21           C  
ANISOU 3669  CE2 TYR A 305     6307   5472   6541    461    382   -354       C  
ATOM   3670  CZ  TYR A 305      -1.265   0.653  53.847  1.00 56.00           C  
ANISOU 3670  CZ  TYR A 305     7174   6534   7570    366    321   -378       C  
ATOM   3671  OH  TYR A 305      -0.135   0.496  53.075  1.00 45.82           O  
ANISOU 3671  OH  TYR A 305     5861   5257   6293    251    251   -419       O  
ATOM   3672  N   CYS A 306      -7.934   0.749  56.640  1.00 48.26           N  
ANISOU 3672  N   CYS A 306     5928   5877   6531   1120    769    184       N  
ATOM   3673  CA  CYS A 306      -9.121   1.155  57.385  1.00 48.17           C  
ANISOU 3673  CA  CYS A 306     5896   5945   6463   1338    903    325       C  
ATOM   3674  C   CYS A 306      -9.855  -0.039  57.982  1.00 56.36           C  
ANISOU 3674  C   CYS A 306     6734   7149   7533   1326    902    450       C  
ATOM   3675  O   CYS A 306     -10.547   0.104  58.996  1.00 58.84           O  
ANISOU 3675  O   CYS A 306     7047   7526   7782   1497   1014    542       O  
ATOM   3676  CB  CYS A 306     -10.050   1.959  56.478  1.00 49.02           C  
ANISOU 3676  CB  CYS A 306     5946   6104   6575   1458    960    452       C  
ATOM   3677  SG  CYS A 306     -11.463   2.709  57.317  1.00 59.78           S  
ANISOU 3677  SG  CYS A 306     7306   7566   7841   1787   1156    643       S  
ATOM   3678  N   CYS A 307      -9.728  -1.215  57.369  1.00 59.88           N  
ANISOU 3678  N   CYS A 307     7023   7662   8067   1131    776    462       N  
ATOM   3679  CA  CYS A 307     -10.421  -2.401  57.853  1.00 51.23           C  
ANISOU 3679  CA  CYS A 307     5747   6715   7002   1084    749    591       C  
ATOM   3680  C   CYS A 307      -9.620  -3.192  58.878  1.00 51.15           C  
ANISOU 3680  C   CYS A 307     5803   6655   6978   1011    715    480       C  
ATOM   3681  O   CYS A 307     -10.217  -3.839  59.746  1.00 51.41           O  
ANISOU 3681  O   CYS A 307     5742   6794   6999   1044    745    584       O  
ATOM   3682  CB  CYS A 307     -10.780  -3.319  56.680  1.00 64.95           C  
ANISOU 3682  CB  CYS A 307     7317   8537   8825    903    616    675       C  
ATOM   3683  SG  CYS A 307     -12.044  -2.661  55.564  1.00 79.66           S  
ANISOU 3683  SG  CYS A 307     9031  10527  10710    973    642    877       S  
ATOM   3684  N   LEU A 308      -8.289  -3.164  58.803  1.00 45.68           N  
ANISOU 3684  N   LEU A 308     5256   5818   6282    911    654    290       N  
ATOM   3685  CA  LEU A 308      -7.461  -4.055  59.608  1.00 48.70           C  
ANISOU 3685  CA  LEU A 308     5676   6167   6660    818    602    195       C  
ATOM   3686  C   LEU A 308      -6.576  -3.332  60.619  1.00 61.28           C  
ANISOU 3686  C   LEU A 308     7469   7642   8173    881    655     64       C  
ATOM   3687  O   LEU A 308      -5.741  -3.981  61.262  1.00 53.58           O  
ANISOU 3687  O   LEU A 308     6533   6633   7190    798    607    -22       O  
ATOM   3688  CB  LEU A 308      -6.598  -4.935  58.697  1.00 48.57           C  
ANISOU 3688  CB  LEU A 308     5637   6113   6705    631    467    111       C  
ATOM   3689  CG  LEU A 308      -7.387  -5.796  57.705  1.00 56.51           C  
ANISOU 3689  CG  LEU A 308     6490   7209   7773    536    383    229       C  
ATOM   3690  CD1 LEU A 308      -6.474  -6.747  56.949  1.00 48.43           C  
ANISOU 3690  CD1 LEU A 308     5496   6128   6780    380    259    135       C  
ATOM   3691  CD2 LEU A 308      -8.496  -6.564  58.418  1.00 53.49           C  
ANISOU 3691  CD2 LEU A 308     5971   6960   7395    548    393    394       C  
ATOM   3692  N   ASN A 309      -6.732  -2.019  60.791  1.00 54.06           N  
ANISOU 3692  N   ASN A 309     6697   6656   7187   1021    747     52       N  
ATOM   3693  CA  ASN A 309      -5.899  -1.270  61.726  1.00 46.44           C  
ANISOU 3693  CA  ASN A 309     5963   5556   6125   1059    778    -69       C  
ATOM   3694  C   ASN A 309      -6.754  -0.238  62.445  1.00 51.19           C  
ANISOU 3694  C   ASN A 309     6694   6135   6620   1292    921     -4       C  
ATOM   3695  O   ASN A 309      -7.328   0.647  61.804  1.00 53.80           O  
ANISOU 3695  O   ASN A 309     7056   6451   6935   1401    979     50       O  
ATOM   3696  CB  ASN A 309      -4.731  -0.594  61.003  1.00 48.32           C  
ANISOU 3696  CB  ASN A 309     6332   5666   6361    943    701   -196       C  
ATOM   3697  CG  ASN A 309      -3.746   0.045  61.960  1.00 50.36           C  
ANISOU 3697  CG  ASN A 309     6827   5790   6518    922    692   -311       C  
ATOM   3698  OD1 ASN A 309      -3.982   1.139  62.478  1.00 52.33           O  
ANISOU 3698  OD1 ASN A 309     7283   5939   6661   1048    765   -320       O  
ATOM   3699  ND2 ASN A 309      -2.630  -0.633  62.197  1.00 44.91           N  
ANISOU 3699  ND2 ASN A 309     6122   5095   5848    763    598   -389       N  
ATOM   3700  N   ASP A 310      -6.825  -0.348  63.776  1.00 51.60           N  
ANISOU 3700  N   ASP A 310     6834   6182   6590   1380    983     -8       N  
ATOM   3701  CA  ASP A 310      -7.677   0.548  64.552  1.00 58.62           C  
ANISOU 3701  CA  ASP A 310     7863   7055   7354   1638   1138     64       C  
ATOM   3702  C   ASP A 310      -7.232   2.001  64.431  1.00 57.42           C  
ANISOU 3702  C   ASP A 310     8014   6707   7097   1710   1164    -32       C  
ATOM   3703  O   ASP A 310      -8.068   2.912  64.407  1.00 56.50           O  
ANISOU 3703  O   ASP A 310     7993   6574   6901   1933   1287     47       O  
ATOM   3704  CB  ASP A 310      -7.685   0.126  66.023  1.00 60.63           C  
ANISOU 3704  CB  ASP A 310     8183   7326   7527   1706   1190     61       C  
ATOM   3705  CG  ASP A 310      -8.417  -1.177  66.256  1.00 68.33           C  
ANISOU 3705  CG  ASP A 310     8872   8506   8583   1683   1192    198       C  
ATOM   3706  OD1 ASP A 310      -9.322  -1.501  65.462  1.00 68.53           O  
ANISOU 3706  OD1 ASP A 310     8671   8677   8690   1698   1201    345       O  
ATOM   3707  OD2 ASP A 310      -8.089  -1.873  67.240  1.00 74.38           O  
ANISOU 3707  OD2 ASP A 310     9646   9289   9328   1640   1175    167       O  
ATOM   3708  N   ARG A 311      -5.921   2.242  64.344  1.00 52.57           N  
ANISOU 3708  N   ARG A 311     7556   5946   6470   1524   1047   -187       N  
ATOM   3709  CA  ARG A 311      -5.448   3.622  64.277  1.00 57.33           C  
ANISOU 3709  CA  ARG A 311     8474   6349   6960   1558   1049   -271       C  
ATOM   3710  C   ARG A 311      -5.806   4.266  62.943  1.00 56.06           C  
ANISOU 3710  C   ARG A 311     8265   6183   6855   1580   1053   -228       C  
ATOM   3711  O   ARG A 311      -6.273   5.411  62.904  1.00 55.39           O  
ANISOU 3711  O   ARG A 311     8385   5993   6668   1756   1139   -206       O  
ATOM   3712  CB  ARG A 311      -3.941   3.678  64.519  1.00 71.14           C  
ANISOU 3712  CB  ARG A 311    10374   7971   8684   1322    905   -415       C  
ATOM   3713  CG  ARG A 311      -3.535   3.367  65.953  1.00 82.50           C  
ANISOU 3713  CG  ARG A 311    11948   9371  10026   1316    903   -467       C  
ATOM   3714  CD  ARG A 311      -2.183   3.978  66.300  1.00 96.55           C  
ANISOU 3714  CD  ARG A 311    13989  10980  11717   1129    777   -588       C  
ATOM   3715  NE  ARG A 311      -1.762   3.636  67.656  1.00112.58           N  
ANISOU 3715  NE  ARG A 311    16141  12979  13654   1104    760   -632       N  
ATOM   3716  CZ  ARG A 311      -0.732   4.192  68.287  1.00120.36           C  
ANISOU 3716  CZ  ARG A 311    17394  13814  14521    963    659   -718       C  
ATOM   3717  NH1 ARG A 311      -0.010   5.130  67.689  1.00119.21           N  
ANISOU 3717  NH1 ARG A 311    17423  13535  14336    827    561   -763       N  
ATOM   3718  NH2 ARG A 311      -0.427   3.813  69.521  1.00124.84           N  
ANISOU 3718  NH2 ARG A 311    18059  14369  15007    945    645   -748       N  
ATOM   3719  N   PHE A 312      -5.609   3.545  61.838  1.00 51.08           N  
ANISOU 3719  N   PHE A 312     7380   5657   6372   1417    964   -211       N  
ATOM   3720  CA  PHE A 312      -6.013   4.079  60.543  1.00 52.57           C  
ANISOU 3720  CA  PHE A 312     7501   5857   6615   1437    967   -160       C  
ATOM   3721  C   PHE A 312      -7.527   4.217  60.449  1.00 52.67           C  
ANISOU 3721  C   PHE A 312     7396   5991   6624   1674   1104      8       C  
ATOM   3722  O   PHE A 312      -8.033   5.144  59.806  1.00 58.86           O  
ANISOU 3722  O   PHE A 312     8245   6738   7381   1796   1162     59       O  
ATOM   3723  CB  PHE A 312      -5.485   3.193  59.414  1.00 47.84           C  
ANISOU 3723  CB  PHE A 312     6671   5346   6161   1219    843   -176       C  
ATOM   3724  CG  PHE A 312      -4.031   3.404  59.112  1.00 63.00           C  
ANISOU 3724  CG  PHE A 312     8700   7157   8079   1015    723   -307       C  
ATOM   3725  CD1 PHE A 312      -3.616   4.512  58.388  1.00 60.58           C  
ANISOU 3725  CD1 PHE A 312     8544   6733   7741    982    694   -345       C  
ATOM   3726  CD2 PHE A 312      -3.078   2.499  59.555  1.00 59.51           C  
ANISOU 3726  CD2 PHE A 312     8203   6742   7664    857    637   -374       C  
ATOM   3727  CE1 PHE A 312      -2.276   4.714  58.109  1.00 53.49           C  
ANISOU 3727  CE1 PHE A 312     7724   5762   6838    783    579   -435       C  
ATOM   3728  CE2 PHE A 312      -1.734   2.693  59.278  1.00 56.20           C  
ANISOU 3728  CE2 PHE A 312     7856   6257   7239    676    530   -462       C  
ATOM   3729  CZ  PHE A 312      -1.332   3.802  58.554  1.00 57.94           C  
ANISOU 3729  CZ  PHE A 312     8211   6375   7428    633    499   -486       C  
ATOM   3730  N   ARG A 313      -8.271   3.315  61.094  1.00 52.11           N  
ANISOU 3730  N   ARG A 313     7144   6079   6575   1745   1159    112       N  
ATOM   3731  CA  ARG A 313      -9.725   3.442  61.095  1.00 64.36           C  
ANISOU 3731  CA  ARG A 313     8561   7781   8113   1976   1293    307       C  
ATOM   3732  C   ARG A 313     -10.163   4.697  61.842  1.00 59.31           C  
ANISOU 3732  C   ARG A 313     8199   7033   7305   2263   1449    325       C  
ATOM   3733  O   ARG A 313     -11.050   5.431  61.381  1.00 62.25           O  
ANISOU 3733  O   ARG A 313     8564   7443   7644   2463   1553    447       O  
ATOM   3734  CB  ARG A 313     -10.357   2.193  61.711  1.00 54.59           C  
ANISOU 3734  CB  ARG A 313     7076   6741   6924   1968   1307    427       C  
ATOM   3735  CG  ARG A 313     -11.874   2.182  61.671  1.00 65.19           C  
ANISOU 3735  CG  ARG A 313     8215   8291   8262   2176   1430    672       C  
ATOM   3736  CD  ARG A 313     -12.410   0.759  61.622  1.00 81.83           C  
ANISOU 3736  CD  ARG A 313    10001  10614  10476   2039   1362    808       C  
ATOM   3737  NE  ARG A 313     -13.749   0.698  61.040  1.00 98.89           N  
ANISOU 3737  NE  ARG A 313    11908  12993  12673   2137   1416   1061       N  
ATOM   3738  CZ  ARG A 313     -14.334  -0.422  60.625  1.00 96.64           C  
ANISOU 3738  CZ  ARG A 313    11335  12898  12487   1982   1325   1213       C  
ATOM   3739  NH1 ARG A 313     -13.696  -1.581  60.724  1.00 91.98           N  
ANISOU 3739  NH1 ARG A 313    10696  12288  11965   1740   1186   1124       N  
ATOM   3740  NH2 ARG A 313     -15.555  -0.382  60.108  1.00 91.42           N  
ANISOU 3740  NH2 ARG A 313    10444  12444  11848   2065   1367   1464       N  
ATOM   3741  N   LEU A 314      -9.525   4.980  62.982  1.00 61.40           N  
ANISOU 3741  N   LEU A 314     8730   7149   7449   2291   1464    206       N  
ATOM   3742  CA  LEU A 314      -9.815   6.213  63.705  1.00 67.36           C  
ANISOU 3742  CA  LEU A 314     9827   7753   8015   2558   1599    198       C  
ATOM   3743  C   LEU A 314      -9.411   7.436  62.896  1.00 63.18           C  
ANISOU 3743  C   LEU A 314     9538   7029   7440   2552   1568    121       C  
ATOM   3744  O   LEU A 314     -10.104   8.459  62.916  1.00 61.85           O  
ANISOU 3744  O   LEU A 314     9554   6794   7154   2819   1700    188       O  
ATOM   3745  CB  LEU A 314      -9.099   6.213  65.055  1.00 75.64           C  
ANISOU 3745  CB  LEU A 314    11139   8664   8937   2542   1589     73       C  
ATOM   3746  CG  LEU A 314      -9.672   5.330  66.161  1.00 79.05           C  
ANISOU 3746  CG  LEU A 314    11435   9255   9348   2649   1674    162       C  
ATOM   3747  CD1 LEU A 314      -8.813   5.437  67.409  1.00 85.24           C  
ANISOU 3747  CD1 LEU A 314    12518   9871   9999   2606   1642     16       C  
ATOM   3748  CD2 LEU A 314     -11.107   5.730  66.458  1.00 69.17           C  
ANISOU 3748  CD2 LEU A 314    10142   8132   8006   3014   1884    361       C  
ATOM   3749  N   GLY A 315      -8.315   7.339  62.142  1.00 63.52           N  
ANISOU 3749  N   GLY A 315     9574   6990   7572   2261   1400     -5       N  
ATOM   3750  CA  GLY A 315      -7.903   8.473  61.334  1.00 65.61           C  
ANISOU 3750  CA  GLY A 315    10052   7079   7798   2231   1358    -67       C  
ATOM   3751  C   GLY A 315      -8.860   8.741  60.190  1.00 66.05           C  
ANISOU 3751  C   GLY A 315     9921   7249   7927   2352   1423     71       C  
ATOM   3752  O   GLY A 315      -9.137   9.896  59.858  1.00 73.13           O  
ANISOU 3752  O   GLY A 315    11033   8019   8733   2505   1485     86       O  
ATOM   3753  N   PHE A 316      -9.398   7.678  59.586  1.00 57.97           N  
ANISOU 3753  N   PHE A 316     8508   6460   7058   2282   1403    180       N  
ATOM   3754  CA  PHE A 316     -10.398   7.857  58.539  1.00 60.06           C  
ANISOU 3754  CA  PHE A 316     8570   6860   7389   2390   1458    337       C  
ATOM   3755  C   PHE A 316     -11.701   8.407  59.102  1.00 65.77           C  
ANISOU 3755  C   PHE A 316     9326   7660   8002   2753   1657    509       C  
ATOM   3756  O   PHE A 316     -12.374   9.211  58.445  1.00 76.31           O  
ANISOU 3756  O   PHE A 316    10679   9003   9311   2925   1736    611       O  
ATOM   3757  CB  PHE A 316     -10.640   6.539  57.807  1.00 55.12           C  
ANISOU 3757  CB  PHE A 316     7550   6455   6936   2202   1366    418       C  
ATOM   3758  CG  PHE A 316      -9.742   6.335  56.624  1.00 55.40           C  
ANISOU 3758  CG  PHE A 316     7528   6443   7079   1932   1208    316       C  
ATOM   3759  CD1 PHE A 316     -10.082   6.854  55.384  1.00 56.74           C  
ANISOU 3759  CD1 PHE A 316     7633   6630   7295   1938   1196    376       C  
ATOM   3760  CD2 PHE A 316      -8.557   5.631  56.751  1.00 61.28           C  
ANISOU 3760  CD2 PHE A 316     8279   7135   7870   1688   1078    170       C  
ATOM   3761  CE1 PHE A 316      -9.257   6.670  54.289  1.00 58.98           C  
ANISOU 3761  CE1 PHE A 316     7868   6875   7665   1704   1060    288       C  
ATOM   3762  CE2 PHE A 316      -7.725   5.443  55.663  1.00 63.30           C  
ANISOU 3762  CE2 PHE A 316     8479   7362   8210   1469    949     91       C  
ATOM   3763  CZ  PHE A 316      -8.075   5.964  54.430  1.00 64.00           C  
ANISOU 3763  CZ  PHE A 316     8511   7464   8339   1476    941    148       C  
ATOM   3764  N   LYS A 317     -12.075   7.995  60.315  1.00 62.85           N  
ANISOU 3764  N   LYS A 317     8960   7358   7560   2890   1749    557       N  
ATOM   3765  CA  LYS A 317     -13.250   8.597  60.937  1.00 72.36           C  
ANISOU 3765  CA  LYS A 317    10228   8634   8632   3274   1959    726       C  
ATOM   3766  C   LYS A 317     -13.072  10.084  61.217  1.00 71.24           C  
ANISOU 3766  C   LYS A 317    10546   8220   8302   3482   2042    634       C  
ATOM   3767  O   LYS A 317     -14.008  10.874  61.045  1.00 67.99           O  
ANISOU 3767  O   LYS A 317    10204   7831   7799   3791   2197    772       O  
ATOM   3768  CB  LYS A 317     -13.616   7.854  62.222  1.00 76.32           C  
ANISOU 3768  CB  LYS A 317    10658   9258   9082   3374   2040    790       C  
ATOM   3769  CG  LYS A 317     -14.469   6.613  62.016  1.00 82.70           C  
ANISOU 3769  CG  LYS A 317    11004  10389  10028   3313   2032    993       C  
ATOM   3770  CD  LYS A 317     -14.897   6.019  63.351  1.00 92.67           C  
ANISOU 3770  CD  LYS A 317    12221  11771  11217   3449   2132   1076       C  
ATOM   3771  CE  LYS A 317     -15.929   4.917  63.170  1.00 97.15           C  
ANISOU 3771  CE  LYS A 317    12337  12677  11899   3419   2138   1329       C  
ATOM   3772  NZ  LYS A 317     -16.353   4.345  64.480  1.00 92.85           N  
ANISOU 3772  NZ  LYS A 317    11739  12260  11280   3551   2238   1424       N  
ATOM   3773  N   HIS A 318     -11.866  10.487  61.625  1.00 73.23           N  
ANISOU 3773  N   HIS A 318    11125   8212   8486   3311   1934    412       N  
ATOM   3774  CA  HIS A 318     -11.600  11.899  61.879  1.00 75.49           C  
ANISOU 3774  CA  HIS A 318    11897   8205   8581   3460   1977    315       C  
ATOM   3775  C   HIS A 318     -11.558  12.713  60.589  1.00 77.85           C  
ANISOU 3775  C   HIS A 318    12232   8429   8919   3441   1943    327       C  
ATOM   3776  O   HIS A 318     -11.997  13.870  60.557  1.00 81.20           O  
ANISOU 3776  O   HIS A 318    12940   8717   9195   3714   2061    369       O  
ATOM   3777  CB  HIS A 318     -10.267  12.045  62.616  1.00 88.37           C  
ANISOU 3777  CB  HIS A 318    13839   9598  10141   3219   1833     95       C  
ATOM   3778  CG  HIS A 318      -9.910  13.458  62.963  1.00109.39           C  
ANISOU 3778  CG  HIS A 318    17058  11944  12561   3378   1876      1       C  
ATOM   3779  ND1 HIS A 318      -8.633  13.845  63.309  1.00117.33           N  
ANISOU 3779  ND1 HIS A 318    18297  12852  13432   3700   2021     82       N  
ATOM   3780  CD2 HIS A 318     -10.668  14.579  63.011  1.00113.36           C  
ANISOU 3780  CD2 HIS A 318    17953  12198  12919   3256   1783   -161       C  
ATOM   3781  CE1 HIS A 318      -8.621  15.142  63.558  1.00118.18           C  
ANISOU 3781  CE1 HIS A 318    18943  12644  13315   3772   2016    -36       C  
ATOM   3782  NE2 HIS A 318      -9.843  15.612  63.385  1.00113.34           N  
ANISOU 3782  NE2 HIS A 318    18437  11937  12692   3493   1865   -183       N  
ATOM   3783  N   ALA A 319     -11.043  12.117  59.509  1.00 74.90           N  
ANISOU 3783  N   ALA A 319    11586   8138   8734   3135   1787    295       N  
ATOM   3784  CA  ALA A 319     -10.943  12.833  58.242  1.00 63.95           C  
ANISOU 3784  CA  ALA A 319    10220   6686   7391   3092   1743    303       C  
ATOM   3785  C   ALA A 319     -12.332  13.066  57.664  1.00 73.10           C  
ANISOU 3785  C   ALA A 319    11180   8029   8568   3376   1895    524       C  
ATOM   3786  O   ALA A 319     -12.551  14.060  56.961  1.00 81.72           O  
ANISOU 3786  O   ALA A 319    12418   9020   9613   3489   1930    553       O  
ATOM   3787  CB  ALA A 319     -10.068  12.090  57.234  1.00 59.14           C  
ANISOU 3787  CB  ALA A 319     9360   6140   6969   2711   1548    225       C  
ATOM   3788  N   PHE A 320     -13.278  12.175  57.947  1.00 78.55           N  
ANISOU 3788  N   PHE A 320    11532   8994   9319   3487   1982    695       N  
ATOM   3789  CA  PHE A 320     -14.627  12.245  57.396  1.00 82.27           C  
ANISOU 3789  CA  PHE A 320    11742   9698   9820   3727   2113    945       C  
ATOM   3790  C   PHE A 320     -15.664  12.520  58.482  1.00 96.39           C  
ANISOU 3790  C   PHE A 320    13597  11575  11451   4134   2338   1108       C  
ATOM   3791  O   PHE A 320     -16.769  11.974  58.460  1.00 98.93           O  
ANISOU 3791  O   PHE A 320    13575  12194  11821   4278   2435   1347       O  
ATOM   3792  CB  PHE A 320     -14.964  10.960  56.644  1.00 70.38           C  
ANISOU 3792  CB  PHE A 320     9745   8477   8519   3498   2010   1060       C  
ATOM   3793  CG  PHE A 320     -14.100  10.721  55.436  1.00 70.32           C  
ANISOU 3793  CG  PHE A 320     9660   8408   8653   3152   1815    935       C  
ATOM   3794  CD1 PHE A 320     -14.295  11.448  54.273  1.00 68.92           C  
ANISOU 3794  CD1 PHE A 320     9482   8202   8501   3171   1802    979       C  
ATOM   3795  CD2 PHE A 320     -13.097   9.766  55.460  1.00 58.25           C  
ANISOU 3795  CD2 PHE A 320     8056   6855   7220   2826   1651    782       C  
ATOM   3796  CE1 PHE A 320     -13.504  11.229  53.159  1.00 73.07           C  
ANISOU 3796  CE1 PHE A 320     9939   8680   9146   2868   1632    871       C  
ATOM   3797  CE2 PHE A 320     -12.303   9.544  54.350  1.00 65.36           C  
ANISOU 3797  CE2 PHE A 320     8888   7710   8234   2540   1488    679       C  
ATOM   3798  CZ  PHE A 320     -12.506  10.276  53.198  1.00 62.10           C  
ANISOU 3798  CZ  PHE A 320     8478   7272   7844   2559   1479    723       C  
ATOM   3799  N   ARG A 321     -15.317  13.373  59.442  1.00103.45           N  
ANISOU 3799  N   ARG A 321    14944  12217  12145   4321   2421    990       N  
ATOM   3800  CA  ARG A 321     -16.208  13.703  60.552  1.00111.01           C  
ANISOU 3800  CA  ARG A 321    16033  13227  12919   4738   2649   1126       C  
ATOM   3801  C   ARG A 321     -17.481  14.408  60.079  1.00129.02           C  
ANISOU 3801  C   ARG A 321    18231  15652  15137   5123   2842   1377       C  
ATOM   3802  O   ARG A 321     -18.525  14.310  60.723  1.00136.09           O  
ANISOU 3802  O   ARG A 321    19008  16754  15946   5458   3038   1593       O  
ATOM   3803  CB  ARG A 321     -15.477  14.573  61.580  1.00108.15           C  
ANISOU 3803  CB  ARG A 321    16248  12513  12332   4843   2676    926       C  
ATOM   3804  CG  ARG A 321     -14.937  15.884  61.026  1.00124.91           C  
ANISOU 3804  CG  ARG A 321    18799  14312  14351   4854   2632    795       C  
ATOM   3805  CD  ARG A 321     -14.288  16.728  62.113  1.00131.34           C  
ANISOU 3805  CD  ARG A 321    20216  14772  14916   4954   2649    617       C  
ATOM   3806  NE  ARG A 321     -13.859  18.028  61.604  1.00140.35           N  
ANISOU 3806  NE  ARG A 321    21795  15594  15937   4976   2606    516       N  
ATOM   3807  CZ  ARG A 321     -14.590  19.136  61.669  1.00148.58           C  
ANISOU 3807  CZ  ARG A 321    23127  16543  16783   5330   2761    612       C  
ATOM   3808  NH1 ARG A 321     -15.792  19.109  62.229  1.00149.76           N  
ANISOU 3808  NH1 ARG A 321    23131  16938  16831   5643   2952    827       N  
ATOM   3809  NH2 ARG A 321     -14.120  20.275  61.176  1.00149.74           N  
ANISOU 3809  NH2 ARG A 321    23655  16412  16828   5266   2678    516       N  
HETATM 3810  N   YCM A 322     -17.389  15.113  58.954  1.00135.42           N  
ANISOU 3810  N   YCM A 322    19095  16371  15989   5079   2789   1364       N  
HETATM 3811  CA  YCM A 322     -18.558  15.853  58.380  1.00151.50           C  
ANISOU 3811  CA  YCM A 322    21056  18540  17970   5439   2964   1607       C  
HETATM 3812  CB  YCM A 322     -18.118  16.654  57.158  1.00154.59           C  
ANISOU 3812  CB  YCM A 322    21581  18750  18405   5310   2859   1519       C  
HETATM 3813  SG  YCM A 322     -17.423  15.551  55.971  1.00152.12           S  
ANISOU 3813  SG  YCM A 322    20855  18562  18380   4760   2587   1438       S  
HETATM 3814  CD  YCM A 322     -16.220  16.663  55.326  1.00147.12           C  
ANISOU 3814  CD  YCM A 322    20667  17533  17700   4583   2451   1183       C  
HETATM 3815  CE  YCM A 322     -14.909  16.389  56.022  1.00141.45           C  
ANISOU 3815  CE  YCM A 322    20189  16594  16962   4299   2306    923       C  
HETATM 3816  OZ1 YCM A 322     -14.899  15.831  57.108  1.00143.55           O  
ANISOU 3816  OZ1 YCM A 322    20462  16900  17179   4340   2348    904       O  
HETATM 3817  NZ2 YCM A 322     -13.800  16.782  55.398  1.00133.77           N  
ANISOU 3817  NZ2 YCM A 322    19402  15402  16024   4010   2133    739       N  
HETATM 3818  C   YCM A 322     -19.704  14.960  58.000  1.00160.62           C  
ANISOU 3818  C   YCM A 322    21634  20128  19268   5465   3010   1901       C  
HETATM 3819  O   YCM A 322     -20.872  15.302  58.195  1.00166.98           O  
ANISOU 3819  O   YCM A 322    22315  21142  19988   5844   3213   2171       O  
ATOM   3820  N   CYS A 323     -19.368  13.800  57.444  1.00160.40           N  
ANISOU 3820  N   CYS A 323    21254  20239  19450   5054   2814   1862       N  
ATOM   3821  CA  CYS A 323     -20.355  12.807  57.028  1.00154.01           C  
ANISOU 3821  CA  CYS A 323    19901  19826  18790   4983   2800   2128       C  
ATOM   3822  C   CYS A 323     -20.972  12.146  58.261  1.00153.17           C  
ANISOU 3822  C   CYS A 323    19652  19933  18610   5187   2942   2295       C  
ATOM   3823  O   CYS A 323     -20.391  12.209  59.345  1.00150.37           O  
ANISOU 3823  O   CYS A 323    19595  19404  18134   5265   2993   2140       O  
ATOM   3824  CB  CYS A 323     -19.685  11.769  56.116  1.00139.43           C  
ANISOU 3824  CB  CYS A 323    17812  18008  17158   4480   2539   2001       C  
ATOM   3825  SG  CYS A 323     -20.757  10.480  55.436  1.00127.11           S  
ANISOU 3825  SG  CYS A 323    15697  16809  15789   4296   2437   2275       S  
ATOM   3826  N   PRO A 324     -22.162  11.537  58.115  1.00151.92           N  
ANISOU 3826  N   PRO A 324    19043  20163  18517   5272   3005   2627       N  
ATOM   3827  CA  PRO A 324     -22.714  10.725  59.206  1.00145.89           C  
ANISOU 3827  CA  PRO A 324    18077  19643  17713   5395   3107   2804       C  
ATOM   3828  C   PRO A 324     -21.824   9.594  59.721  1.00134.51           C  
ANISOU 3828  C   PRO A 324    16607  18134  16368   5023   2931   2600       C  
ATOM   3829  O   PRO A 324     -21.915   8.474  59.220  1.00126.69           O  
ANISOU 3829  O   PRO A 324    15254  17335  15547   4699   2767   2677       O  
ATOM   3830  CB  PRO A 324     -23.990  10.163  58.560  1.00148.16           C  
ANISOU 3830  CB  PRO A 324    17830  20363  18100   5411   3123   3194       C  
ATOM   3831  CG  PRO A 324     -23.841  10.410  57.078  1.00149.93           C  
ANISOU 3831  CG  PRO A 324    17972  20545  18450   5198   2975   3167       C  
ATOM   3832  CD  PRO A 324     -22.999  11.635  56.973  1.00152.85           C  
ANISOU 3832  CD  PRO A 324    18841  20520  18715   5314   3010   2888       C  
TER    3833      PRO A 324                                                      
HETATM 3834  C13 GBQ A1501       4.538  -1.327  35.159  1.00 48.71           C  
ANISOU 3834  C13 GBQ A1501     6004   6105   6399    178      7   -227       C  
HETATM 3835  C21 GBQ A1501       5.940  -1.423  26.965  1.00 46.54           C  
ANISOU 3835  C21 GBQ A1501     6094   6011   5579    514     79    -69       C  
HETATM 3836  C22 GBQ A1501       4.987  -0.275  27.202  1.00 46.00           C  
ANISOU 3836  C22 GBQ A1501     5930   5894   5653    355     21    -56       C  
HETATM 3837  C24 GBQ A1501       7.260  -3.132  27.839  1.00 59.09           C  
ANISOU 3837  C24 GBQ A1501     7757   7655   7038    729    167    -97       C  
HETATM 3838  C01 GBQ A1501       4.771   2.111  30.585  1.00 44.86           C  
ANISOU 3838  C01 GBQ A1501     5469   5730   5846    100     21    -39       C  
HETATM 3839  C02 GBQ A1501       3.928   0.809  30.515  1.00 45.12           C  
ANISOU 3839  C02 GBQ A1501     5606   5688   5848    147    -20    -96       C  
HETATM 3840  C03 GBQ A1501       3.372   0.471  31.950  1.00 42.98           C  
ANISOU 3840  C03 GBQ A1501     5319   5358   5654    115    -39   -137       C  
HETATM 3841  C04 GBQ A1501       4.139  -0.245  32.888  1.00 45.85           C  
ANISOU 3841  C04 GBQ A1501     5669   5752   5998    158     -9   -167       C  
HETATM 3842  C05 GBQ A1501       3.642  -0.536  34.174  1.00 48.28           C  
ANISOU 3842  C05 GBQ A1501     5963   6009   6370    130    -24   -201       C  
HETATM 3843  C06 GBQ A1501       2.358  -0.118  34.558  1.00 41.98           C  
ANISOU 3843  C06 GBQ A1501     5158   5139   5653     71    -62   -196       C  
HETATM 3844  C07 GBQ A1501       1.576   0.599  33.628  1.00 56.86           C  
ANISOU 3844  C07 GBQ A1501     7045   7002   7556     38    -87   -156       C  
HETATM 3845  C08 GBQ A1501       2.077   0.892  32.339  1.00 48.62           C  
ANISOU 3845  C08 GBQ A1501     6022   5998   6453     53    -80   -131       C  
HETATM 3846  C09 GBQ A1501       0.163   1.067  34.035  1.00 62.44           C  
ANISOU 3846  C09 GBQ A1501     7725   7658   8343     -1   -115   -122       C  
HETATM 3847  C18 GBQ A1501       4.213  -1.283  29.250  1.00 55.06           C  
ANISOU 3847  C18 GBQ A1501     7088   6931   6904    304    -31   -141       C  
HETATM 3848  C19 GBQ A1501       5.253  -2.499  29.110  1.00 49.19           C  
ANISOU 3848  C19 GBQ A1501     6442   6227   6022    458     22   -161       C  
HETATM 3849  C25 GBQ A1501       8.433  -2.646  26.985  1.00 52.89           C  
ANISOU 3849  C25 GBQ A1501     6892   7037   6166    833    264     -3       C  
HETATM 3850  C27 GBQ A1501      10.323  -1.521  26.386  1.00 52.40           C  
ANISOU 3850  C27 GBQ A1501     6572   7290   6048    910    402    188       C  
HETATM 3851  C31 GBQ A1501       5.874  -3.030  30.445  1.00 49.64           C  
ANISOU 3851  C31 GBQ A1501     6442   6314   6104    496     60   -182       C  
HETATM 3852  C32 GBQ A1501       5.375  -4.182  31.100  1.00 45.01           C  
ANISOU 3852  C32 GBQ A1501     5967   5630   5503    510     15   -242       C  
HETATM 3853  C33 GBQ A1501       5.926  -4.666  32.307  1.00 51.54           C  
ANISOU 3853  C33 GBQ A1501     6745   6486   6353    546     48   -258       C  
HETATM 3854  C34 GBQ A1501       7.001  -3.975  32.880  1.00 54.57           C  
ANISOU 3854  C34 GBQ A1501     6959   7003   6771    556    120   -207       C  
HETATM 3855  C35 GBQ A1501       7.537  -2.821  32.279  1.00 55.39           C  
ANISOU 3855  C35 GBQ A1501     6949   7208   6887    524    154   -137       C  
HETATM 3856  C36 GBQ A1501       6.964  -2.360  31.075  1.00 46.59           C  
ANISOU 3856  C36 GBQ A1501     5890   6057   5753    499    128   -129       C  
HETATM 3857  F10 GBQ A1501      -0.032   2.409  34.173  1.00 79.23           F  
ANISOU 3857  F10 GBQ A1501     9812   9772  10520    -15    -85    -88       F  
HETATM 3858  F11 GBQ A1501      -0.305   0.603  35.224  1.00 71.33           F  
ANISOU 3858  F11 GBQ A1501     8833   8761   9509      0   -117   -136       F  
HETATM 3859  F12 GBQ A1501      -0.846   0.731  33.200  1.00 73.78           F  
ANISOU 3859  F12 GBQ A1501     9188   9078   9769    -24   -175    -82       F  
HETATM 3860  F14 GBQ A1501       4.228  -2.638  35.342  1.00 56.30           F  
ANISOU 3860  F14 GBQ A1501     7052   7019   7320    227    -18   -268       F  
HETATM 3861  F15 GBQ A1501       5.858  -1.402  34.851  1.00 57.81           F  
ANISOU 3861  F15 GBQ A1501     7121   7363   7482    239     59   -196       F  
HETATM 3862  F16 GBQ A1501       4.597  -0.869  36.436  1.00 53.71           F  
ANISOU 3862  F16 GBQ A1501     6576   6732   7100    129     16   -235       F  
HETATM 3863  F37 GBQ A1501       7.542  -4.431  34.050  1.00 58.58           F  
ANISOU 3863  F37 GBQ A1501     7416   7546   7297    583    145   -214       F  
HETATM 3864  N20 GBQ A1501       6.403  -2.023  28.247  1.00 60.82           N  
ANISOU 3864  N20 GBQ A1501     7861   7833   7415    546    105    -95       N  
HETATM 3865  N26 GBQ A1501       9.396  -1.767  27.445  1.00 61.74           N  
ANISOU 3865  N26 GBQ A1501     7795   8320   7343    799    321     89       N  
HETATM 3866  N29 GBQ A1501       9.876  -2.282  25.249  1.00 59.88           N  
ANISOU 3866  N29 GBQ A1501     7742   8146   6862   1030    400    138       N  
HETATM 3867  N30 GBQ A1501       8.695  -2.974  25.643  1.00 53.35           N  
ANISOU 3867  N30 GBQ A1501     7082   7118   6072    965    303     19       N  
HETATM 3868  O17 GBQ A1501       4.782  -0.233  30.017  1.00 56.18           O  
ANISOU 3868  O17 GBQ A1501     7074   7141   7131    256     13   -107       O  
HETATM 3869  O23 GBQ A1501       3.900  -0.735  27.985  1.00 56.46           O  
ANISOU 3869  O23 GBQ A1501     7295   7108   7047    287    -50   -106       O  
HETATM 3870  O28 GBQ A1501      11.318  -0.811  26.381  1.00 51.37           O  
ANISOU 3870  O28 GBQ A1501     6261   7339   5920    903    458    307       O  
HETATM 3871  C1  CIT A1502       5.465  18.365  20.149  1.00 78.89           C  
ANISOU 3871  C1  CIT A1502     9883   9945  10148   -818   -218    984       C  
HETATM 3872  O1  CIT A1502       5.936  18.231  18.998  1.00 87.15           O  
ANISOU 3872  O1  CIT A1502    10844  11129  11140   -818   -202   1055       O  
HETATM 3873  O2  CIT A1502       4.872  17.442  20.745  1.00 66.18           O  
ANISOU 3873  O2  CIT A1502     8266   8310   8571   -715   -187    883       O  
HETATM 3874  C2  CIT A1502       5.620  19.697  20.838  1.00 72.51           C  
ANISOU 3874  C2  CIT A1502     9212   8987   9352   -950   -280   1026       C  
HETATM 3875  C3  CIT A1502       5.356  19.536  22.326  1.00 91.92           C  
ANISOU 3875  C3  CIT A1502    11756  11322  11847   -936   -285    937       C  
HETATM 3876  O7  CIT A1502       4.495  18.415  22.549  1.00 95.42           O  
ANISOU 3876  O7  CIT A1502    12148  11777  12331   -777   -228    834       O  
HETATM 3877  C4  CIT A1502       6.671  19.320  23.062  1.00109.31           C  
ANISOU 3877  C4  CIT A1502    13898  13620  14014  -1065   -316    976       C  
HETATM 3878  C5  CIT A1502       6.442  18.562  24.345  1.00104.30           C  
ANISOU 3878  C5  CIT A1502    13279  12938  13411  -1003   -295    869       C  
HETATM 3879  O3  CIT A1502       5.298  18.131  24.598  1.00107.49           O  
ANISOU 3879  O3  CIT A1502    13722  13255  13863   -859   -252    773       O  
HETATM 3880  O4  CIT A1502       7.418  18.391  25.105  1.00113.31           O  
ANISOU 3880  O4  CIT A1502    14383  14141  14527  -1105   -324    896       O  
HETATM 3881  C6  CIT A1502       4.660  20.758  22.861  1.00 82.29           C  
ANISOU 3881  C6  CIT A1502    10748   9874  10644   -955   -321    931       C  
HETATM 3882  O5  CIT A1502       5.317  21.816  22.947  1.00 79.09           O  
ANISOU 3882  O5  CIT A1502    10450   9402  10198  -1110   -390   1009       O  
HETATM 3883  O6  CIT A1502       3.459  20.668  23.199  1.00 61.92           O  
ANISOU 3883  O6  CIT A1502     8235   7184   8108   -812   -282    860       O  
HETATM 3884  C1  OLA A1503      16.599  13.120  24.413  1.00123.39           C  
ANISOU 3884  C1  OLA A1503    14189  17357  15338  -1046    -51   1767       C  
HETATM 3885  O1  OLA A1503      16.384  11.975  23.960  1.00127.81           O  
ANISOU 3885  O1  OLA A1503    14735  17966  15859   -792     66   1686       O  
HETATM 3886  O2  OLA A1503      17.125  14.031  23.735  1.00125.38           O  
ANISOU 3886  O2  OLA A1503    14370  17714  15555  -1186    -95   1937       O  
HETATM 3887  C2  OLA A1503      16.212  13.418  25.844  1.00109.79           C  
ANISOU 3887  C2  OLA A1503    12591  15431  13693  -1190   -149   1661       C  
HETATM 3888  C3  OLA A1503      15.426  12.250  26.429  1.00 86.18           C  
ANISOU 3888  C3  OLA A1503     9684  12317  10742   -989    -80   1452       C  
HETATM 3889  C4  OLA A1503      15.135  12.479  27.908  1.00 80.52           C  
ANISOU 3889  C4  OLA A1503     9076  11427  10090  -1116   -164   1361       C  
HETATM 3890  C5  OLA A1503      14.307  11.343  28.501  1.00 86.85           C  
ANISOU 3890  C5  OLA A1503     9956  12110  10934   -927   -100   1165       C  
HETATM 3891  C6  OLA A1503      13.888  11.675  29.929  1.00 78.79           C  
ANISOU 3891  C6  OLA A1503     9064  10899   9975  -1045   -179   1069       C  
HETATM 3892  C7  OLA A1503      12.843  10.699  30.462  1.00 69.40           C  
ANISOU 3892  C7  OLA A1503     7968   9564   8836   -872   -124    874       C  
HETATM 3893  C8  OLA A1503      12.138  11.295  31.677  1.00 74.40           C  
ANISOU 3893  C8  OLA A1503     8769   9971   9530   -973   -195    772       C  
HETATM 3894  C9  OLA A1503      10.704  11.620  31.330  1.00 72.19           C  
ANISOU 3894  C9  OLA A1503     8642   9482   9305   -896   -182    647       C  
HETATM 3895  C10 OLA A1503       9.819  11.915  32.282  1.00 77.71           C  
ANISOU 3895  C10 OLA A1503     9491   9983  10052   -902   -206    541       C  
HETATM 3896  C11 OLA A1503      10.227  11.953  33.737  1.00 78.74           C  
ANISOU 3896  C11 OLA A1503     9671  10069  10179   -994   -254    526       C  
HETATM 3897  C12 OLA A1503       9.612  13.175  34.411  1.00 76.11           C  
ANISOU 3897  C12 OLA A1503     9558   9507   9853  -1089   -317    488       C  
HETATM 3898  C13 OLA A1503      10.155  13.383  35.823  1.00 86.17           C  
ANISOU 3898  C13 OLA A1503    10915  10728  11098  -1216   -386    489       C  
HETATM 3899  C14 OLA A1503       9.427  12.534  36.862  1.00 79.09           C  
ANISOU 3899  C14 OLA A1503    10056   9756  10239  -1082   -333    360       C  
HETATM 3900  C15 OLA A1503       9.959  12.832  38.262  1.00 78.59           C  
ANISOU 3900  C15 OLA A1503    10100   9627  10135  -1215   -408    361       C  
HETATM 3901  C16 OLA A1503       9.126  12.159  39.349  1.00 85.82           C  
ANISOU 3901  C16 OLA A1503    11082  10443  11082  -1082   -355    234       C  
HETATM 3902  C17 OLA A1503       9.729  12.415  40.726  1.00 89.53           C  
ANISOU 3902  C17 OLA A1503    11663  10856  11500  -1218   -432    238       C  
HETATM 3903  C18 OLA A1503       8.898  11.781  41.820  1.00 85.87           C  
ANISOU 3903  C18 OLA A1503    11268  10297  11060  -1081   -376    118       C  
HETATM 3904  C1  OLA A1504       1.856 -17.667  56.991  1.00 83.12           C  
ANISOU 3904  C1  OLA A1504    10659  10052  10872    140   -289   -419       C  
HETATM 3905  O1  OLA A1504       1.857 -18.878  57.303  1.00 69.57           O  
ANISOU 3905  O1  OLA A1504     9050   8272   9111    137   -344   -407       O  
HETATM 3906  O2  OLA A1504       1.128 -16.815  57.551  1.00 84.08           O  
ANISOU 3906  O2  OLA A1504    10658  10232  11056     90   -260   -386       O  
HETATM 3907  C2  OLA A1504       2.778 -17.216  55.884  1.00 83.71           C  
ANISOU 3907  C2  OLA A1504    10762  10131  10911    220   -252   -466       C  
HETATM 3908  C3  OLA A1504       2.001 -16.951  54.599  1.00 71.15           C  
ANISOU 3908  C3  OLA A1504     9216   8495   9322    167   -299   -448       C  
HETATM 3909  C4  OLA A1504       2.290 -15.545  54.090  1.00 72.10           C  
ANISOU 3909  C4  OLA A1504     9228   8685   9482    186   -232   -467       C  
HETATM 3910  C5  OLA A1504       2.575 -15.515  52.593  1.00 84.46           C  
ANISOU 3910  C5  OLA A1504    10879  10214  10998    222   -247   -485       C  
HETATM 3911  C6  OLA A1504       2.895 -14.084  52.174  1.00 83.43           C  
ANISOU 3911  C6  OLA A1504    10634  10157  10908    232   -182   -496       C  
HETATM 3912  C7  OLA A1504       3.482 -14.017  50.772  1.00 86.78           C  
ANISOU 3912  C7  OLA A1504    11128  10571  11275    292   -176   -513       C  
HETATM 3913  C8  OLA A1504       2.427 -14.234  49.696  1.00 87.78           C  
ANISOU 3913  C8  OLA A1504    11345  10619  11390    227   -252   -491       C  
HETATM 3914  C9  OLA A1504       2.483 -13.071  48.734  1.00 77.23           C  
ANISOU 3914  C9  OLA A1504     9945   9324  10075    226   -218   -490       C  
HETATM 3915  C10 OLA A1504       2.957 -13.231  47.502  1.00 67.15           C  
ANISOU 3915  C10 OLA A1504     8763   8024   8727    284   -221   -506       C  
HETATM 3916  C11 OLA A1504       3.457 -14.579  47.040  1.00 66.15           C  
ANISOU 3916  C11 OLA A1504     8832   7819   8483    372   -251   -529       C  
HETATM 3917  C12 OLA A1504       2.774 -14.950  45.731  1.00 65.86           C  
ANISOU 3917  C12 OLA A1504     8958   7683   8381    334   -332   -522       C  
HETATM 3918  C1  OLA A1505       1.997 -21.838  55.304  1.00 99.15           C  
ANISOU 3918  C1  OLA A1505    13361  11689  12620    175   -549   -421       C  
HETATM 3919  O1  OLA A1505       1.501 -21.472  56.393  1.00 93.51           O  
ANISOU 3919  O1  OLA A1505    12483  11057  11989    102   -533   -382       O  
HETATM 3920  O2  OLA A1505       1.571 -21.447  54.196  1.00101.35           O  
ANISOU 3920  O2  OLA A1505    13677  11941  12891    132   -582   -417       O  
HETATM 3921  C2  OLA A1505       3.155 -22.807  55.326  1.00 95.67           C  
ANISOU 3921  C2  OLA A1505    13091  11185  12074    336   -523   -465       C  
HETATM 3922  C3  OLA A1505       4.024 -22.595  54.091  1.00 89.16           C  
ANISOU 3922  C3  OLA A1505    12355  10349  11172    482   -468   -511       C  
HETATM 3923  C4  OLA A1505       5.131 -23.641  54.016  1.00 91.87           C  
ANISOU 3923  C4  OLA A1505    12890  10630  11387    678   -432   -535       C  
HETATM 3924  C5  OLA A1505       6.282 -23.306  54.957  1.00 91.62           C  
ANISOU 3924  C5  OLA A1505    12672  10752  11387    802   -315   -531       C  
HETATM 3925  C6  OLA A1505       7.097 -24.546  55.308  1.00 82.85           C  
ANISOU 3925  C6  OLA A1505    11735   9580  10163    970   -296   -528       C  
HETATM 3926  C7  OLA A1505       8.324 -24.159  56.126  1.00 88.56           C  
ANISOU 3926  C7  OLA A1505    12253  10486  10911   1095   -182   -502       C  
HETATM 3927  C8  OLA A1505       8.746 -25.262  57.092  1.00 97.75           C  
ANISOU 3927  C8  OLA A1505    13506  11614  12021   1181   -183   -481       C  
HETATM 3928  C9  OLA A1505      10.042 -24.859  57.757  1.00108.14           C  
ANISOU 3928  C9  OLA A1505    14613  13129  13347   1308    -74   -436       C  
HETATM 3929  C10 OLA A1505      10.238 -24.983  59.070  1.00105.29           C  
ANISOU 3929  C10 OLA A1505    14136  12837  13033   1271    -71   -411       C  
HETATM 3930  C11 OLA A1505       9.182 -25.545  59.992  1.00 97.50           C  
ANISOU 3930  C11 OLA A1505    13215  11737  12093   1116   -164   -426       C  
HETATM 3931  C12 OLA A1505       9.816 -26.518  60.985  1.00 95.27           C  
ANISOU 3931  C12 OLA A1505    12978  11460  11759   1221   -149   -391       C  
HETATM 3932  C13 OLA A1505      10.394 -25.815  62.212  1.00 86.23           C  
ANISOU 3932  C13 OLA A1505    11570  10503  10691   1181   -100   -356       C  
HETATM 3933  C14 OLA A1505      11.874 -25.476  62.051  1.00 98.03           C  
ANISOU 3933  C14 OLA A1505    12930  12178  12138   1353      0   -298       C  
HETATM 3934  C15 OLA A1505      12.405 -24.722  63.266  1.00 97.49           C  
ANISOU 3934  C15 OLA A1505    12614  12288  12138   1271     21   -254       C  
HETATM 3935  C16 OLA A1505      13.829 -24.223  63.039  1.00 97.73           C  
ANISOU 3935  C16 OLA A1505    12477  12528  12129   1395    101   -167       C  
HETATM 3936  C17 OLA A1505      14.348 -23.487  64.270  1.00 95.99           C  
ANISOU 3936  C17 OLA A1505    12035  12473  11962   1280     95   -116       C  
HETATM 3937  C18 OLA A1505      15.768 -23.006  64.070  1.00 84.60           C  
ANISOU 3937  C18 OLA A1505    10408  11260  10475   1372    155      3       C  
HETATM 3938  C1  OLA A1506      -3.144 -19.683  56.543  1.00 84.48           C  
ANISOU 3938  C1  OLA A1506    10896  10126  11077   -360   -668    -43       C  
HETATM 3939  O1  OLA A1506      -3.937 -18.772  56.871  1.00 86.07           O  
ANISOU 3939  O1  OLA A1506    10914  10443  11346   -380   -617     32       O  
HETATM 3940  O2  OLA A1506      -3.274 -20.876  56.915  1.00 65.34           O  
ANISOU 3940  O2  OLA A1506     8588   7630   8606   -426   -758     -9       O  
HETATM 3941  C2  OLA A1506      -1.976 -19.321  55.658  1.00 72.67           C  
ANISOU 3941  C2  OLA A1506     9488   8578   9545   -240   -613   -168       C  
HETATM 3942  C3  OLA A1506      -2.228 -17.956  55.025  1.00 72.52           C  
ANISOU 3942  C3  OLA A1506     9340   8635   9581   -221   -549   -167       C  
HETATM 3943  C4  OLA A1506      -1.419 -17.782  53.744  1.00 78.06           C  
ANISOU 3943  C4  OLA A1506    10153   9275  10232   -154   -542   -249       C  
HETATM 3944  C5  OLA A1506      -1.600 -16.385  53.167  1.00 78.79           C  
ANISOU 3944  C5  OLA A1506    10118   9440  10379   -135   -476   -249       C  
HETATM 3945  C6  OLA A1506      -1.673 -16.424  51.643  1.00 79.42           C  
ANISOU 3945  C6  OLA A1506    10307   9456  10411   -158   -536   -257       C  
HETATM 3946  C7  OLA A1506      -0.460 -17.124  51.043  1.00 86.61           C  
ANISOU 3946  C7  OLA A1506    11398  10281  11227    -56   -532   -347       C  
HETATM 3947  C8  OLA A1506      -0.598 -17.242  49.528  1.00 88.38           C  
ANISOU 3947  C8  OLA A1506    11765  10431  11385    -74   -596   -352       C  
HETATM 3948  C11 OLA A1507      14.195 -21.005  56.334  1.00 66.06           C  
ANISOU 3948  C11 OLA A1507     8453   8614   8035   1558    260   -190       C  
HETATM 3949  C12 OLA A1507      13.911 -20.505  57.746  1.00 76.18           C  
ANISOU 3949  C12 OLA A1507     9592   9933   9421   1363    207   -199       C  
HETATM 3950  C13 OLA A1507      15.144 -19.834  58.337  1.00 73.89           C  
ANISOU 3950  C13 OLA A1507     9059   9881   9134   1358    245    -84       C  
HETATM 3951  C14 OLA A1507      14.852 -19.232  59.707  1.00 64.50           C  
ANISOU 3951  C14 OLA A1507     7762   8712   8033   1154    184   -101       C  
HETATM 3952  C15 OLA A1507      16.068 -18.478  60.232  1.00 71.25           C  
ANISOU 3952  C15 OLA A1507     8392   9798   8880   1107    194     23       C  
HETATM 3953  C16 OLA A1507      15.875 -18.058  61.684  1.00 78.48           C  
ANISOU 3953  C16 OLA A1507     9246  10721   9853    928    131      8       C  
HETATM 3954  C17 OLA A1507      17.219 -17.774  62.346  1.00 75.62           C  
ANISOU 3954  C17 OLA A1507     8692  10589   9452    910    128    156       C  
HETATM 3955  C18 OLA A1507      17.057 -17.519  63.829  1.00 83.53           C  
ANISOU 3955  C18 OLA A1507     9668  11582  10487    747     61    140       C  
HETATM 3956  C10 OLA A1508      12.959 -16.548  66.991  1.00 67.66           C  
ANISOU 3956  C10 OLA A1508     8002   9050   8656    312    -73   -235       C  
HETATM 3957  C11 OLA A1508      13.617 -17.287  65.849  1.00 68.40           C  
ANISOU 3957  C11 OLA A1508     8066   9201   8723    463    -34   -185       C  
HETATM 3958  C12 OLA A1508      12.717 -18.430  65.392  1.00 70.68           C  
ANISOU 3958  C12 OLA A1508     8483   9349   9023    571    -15   -244       C  
HETATM 3959  C13 OLA A1508      13.274 -19.092  64.136  1.00 77.97           C  
ANISOU 3959  C13 OLA A1508     9433  10295   9899    736     27   -209       C  
HETATM 3960  C14 OLA A1508      12.294 -20.112  63.570  1.00 72.29           C  
ANISOU 3960  C14 OLA A1508     8887   9403   9176    809     22   -273       C  
HETATM 3961  C15 OLA A1508      12.123 -19.915  62.069  1.00 77.49           C  
ANISOU 3961  C15 OLA A1508     9604  10018   9822    865     42   -294       C  
HETATM 3962  C16 OLA A1508      10.999 -20.782  61.512  1.00 84.18           C  
ANISOU 3962  C16 OLA A1508    10642  10679  10665    883      8   -356       C  
HETATM 3963  C17 OLA A1508      10.889 -20.604  60.003  1.00 84.35           C  
ANISOU 3963  C17 OLA A1508    10734  10655  10658    939     22   -374       C  
HETATM 3964  C18 OLA A1508       9.817 -21.496  59.418  1.00 84.75           C  
ANISOU 3964  C18 OLA A1508    10996  10518  10687    936    -33   -422       C  
HETATM 3965  C1  OLA A1509       3.184  17.830  60.008  1.00122.46           C  
ANISOU 3965  C1  OLA A1509    20350  12147  14031    -94   -240   -785       C  
HETATM 3966  O1  OLA A1509       4.231  17.200  59.742  1.00127.07           O  
ANISOU 3966  O1  OLA A1509    20650  12908  14722   -387   -375   -751       O  
HETATM 3967  O2  OLA A1509       2.816  18.078  61.176  1.00123.40           O  
ANISOU 3967  O2  OLA A1509    20806  12098  13981     52   -192   -839       O  
HETATM 3968  C2  OLA A1509       2.323  18.322  58.869  1.00111.95           C  
ANISOU 3968  C2  OLA A1509    18959  10811  12765    107   -124   -748       C  
HETATM 3969  C3  OLA A1509       2.271  17.280  57.758  1.00 91.12           C  
ANISOU 3969  C3  OLA A1509    15747   8494  10382     83    -78   -694       C  
HETATM 3970  C4  OLA A1509       1.115  17.595  56.818  1.00 86.38           C  
ANISOU 3970  C4  OLA A1509    15064   7913   9845    355     78   -654       C  
HETATM 3971  C5  OLA A1509       0.998  16.587  55.681  1.00 81.87           C  
ANISOU 3971  C5  OLA A1509    13963   7637   9507    331    116   -602       C  
HETATM 3972  C6  OLA A1509      -0.259  16.876  54.870  1.00 78.12           C  
ANISOU 3972  C6  OLA A1509    13413   7187   9082    613    271   -550       C  
HETATM 3973  C7  OLA A1509      -0.026  16.694  53.376  1.00 82.61           C  
ANISOU 3973  C7  OLA A1509    13674   7907   9806    488    226   -497       C  
HETATM 3974  C8  OLA A1509      -0.299  15.261  52.937  1.00 74.26           C  
ANISOU 3974  C8  OLA A1509    12137   7141   8937    509    281   -469       C  
HETATM 3975  C9  OLA A1509      -0.300  15.196  51.428  1.00 81.77           C  
ANISOU 3975  C9  OLA A1509    12841   8215  10014    447    262   -415       C  
HETATM 3976  C1  OLA A1510      -4.048 -12.804  29.409  1.00 99.97           C  
ANISOU 3976  C1  OLA A1510    14624  11425  11934   -527  -1335   -179       C  
HETATM 3977  O1  OLA A1510      -4.487 -12.728  28.239  1.00 96.12           O  
ANISOU 3977  O1  OLA A1510    14272  10891  11357   -609  -1434   -144       O  
HETATM 3978  O2  OLA A1510      -2.841 -12.649  29.696  1.00103.01           O  
ANISOU 3978  O2  OLA A1510    14980  11844  12315   -311  -1165   -272       O  
HETATM 3979  C2  OLA A1510      -5.017 -13.096  30.529  1.00 90.53           C  
ANISOU 3979  C2  OLA A1510    13286  10260  10852   -699  -1427    -90       C  
HETATM 3980  C3  OLA A1510      -4.270 -13.098  31.857  1.00 83.79           C  
ANISOU 3980  C3  OLA A1510    12284   9462  10091   -561  -1280   -153       C  
HETATM 3981  C4  OLA A1510      -5.208 -13.422  33.015  1.00 87.10           C  
ANISOU 3981  C4  OLA A1510    12563   9916  10613   -717  -1361    -61       C  
HETATM 3982  C5  OLA A1510      -5.148 -14.900  33.381  1.00 92.33           C  
ANISOU 3982  C5  OLA A1510    13508  10422  11153   -762  -1471    -91       C  
HETATM 3983  C6  OLA A1510      -4.075 -15.158  34.433  1.00 94.91           C  
ANISOU 3983  C6  OLA A1510    13801  10756  11506   -574  -1322   -192       C  
HETATM 3984  C7  OLA A1510      -3.889 -16.652  34.672  1.00 94.65           C  
ANISOU 3984  C7  OLA A1510    14093  10545  11326   -585  -1421   -232       C  
HETATM 3985  C8  OLA A1510      -2.794 -16.909  35.700  1.00 88.21           C  
ANISOU 3985  C8  OLA A1510    13234   9748  10532   -387  -1268   -322       C  
HETATM 3986  C9  OLA A1510      -2.404 -18.367  35.662  1.00 91.71           C  
ANISOU 3986  C9  OLA A1510    14060   9993  10792   -340  -1345   -379       C  
HETATM 3987  C1  OLA A1511     -17.677  -5.389  29.223  1.00114.22           C  
ANISOU 3987  C1  OLA A1511    13625  14990  14785  -1792  -1920   2054       C  
HETATM 3988  O1  OLA A1511     -17.882  -5.689  28.028  1.00117.78           O  
ANISOU 3988  O1  OLA A1511    14215  15393  15142  -1963  -2090   2095       O  
HETATM 3989  O2  OLA A1511     -17.208  -6.195  30.055  1.00120.72           O  
ANISOU 3989  O2  OLA A1511    14551  15722  15595  -1798  -1916   1946       O  
HETATM 3990  C2  OLA A1511     -18.023  -3.995  29.690  1.00106.15           C  
ANISOU 3990  C2  OLA A1511    12315  14131  13884  -1563  -1712   2143       C  
HETATM 3991  C3  OLA A1511     -17.210  -3.659  30.935  1.00 99.51           C  
ANISOU 3991  C3  OLA A1511    11460  13235  13114  -1332  -1497   1964       C  
HETATM 3992  C4  OLA A1511     -17.754  -2.403  31.603  1.00 97.23           C  
ANISOU 3992  C4  OLA A1511    10905  13111  12927  -1113  -1306   2090       C  
HETATM 3993  C5  OLA A1511     -17.260  -2.263  33.039  1.00 96.33           C  
ANISOU 3993  C5  OLA A1511    10762  12971  12869   -931  -1133   1978       C  
HETATM 3994  C6  OLA A1511     -18.351  -1.633  33.896  1.00107.41           C  
ANISOU 3994  C6  OLA A1511    11882  14592  14336   -802  -1026   2220       C  
HETATM 3995  C7  OLA A1511     -17.881  -1.338  35.315  1.00107.11           C  
ANISOU 3995  C7  OLA A1511    11831  14523  14342   -595   -839   2109       C  
HETATM 3996  C8  OLA A1511     -19.017  -0.717  36.121  1.00102.52           C  
ANISOU 3996  C8  OLA A1511    10984  14165  13803   -440   -724   2365       C  
HETATM 3997  C9  OLA A1511     -18.462  -0.034  37.347  1.00 99.92           C  
ANISOU 3997  C9  OLA A1511    10689  13774  13501   -181   -507   2228       C  
HETATM 3998  C10 OLA A1511     -18.755   1.240  37.597  1.00 95.74           C  
ANISOU 3998  C10 OLA A1511    10089  13298  12990     69   -330   2288       C  
HETATM 3999  C11 OLA A1511     -19.645   2.022  36.660  1.00 91.04           C  
ANISOU 3999  C11 OLA A1511     9352  12842  12398    113   -334   2500       C  
HETATM 4000  C6  OLA A1512      17.058  -1.854  54.989  1.00 77.85           C  
ANISOU 4000  C6  OLA A1512     8913  10793   9874   -865   -380    355       C  
HETATM 4001  C7  OLA A1512      15.883  -2.504  54.268  1.00 85.77           C  
ANISOU 4001  C7  OLA A1512     9982  11667  10941   -652   -268    206       C  
HETATM 4002  C8  OLA A1512      16.187  -2.667  52.785  1.00 87.04           C  
ANISOU 4002  C8  OLA A1512    10029  11941  11103   -546   -206    271       C  
HETATM 4003  C9  OLA A1512      15.090  -3.471  52.130  1.00 85.70           C  
ANISOU 4003  C9  OLA A1512     9933  11649  10980   -347   -113    137       C  
HETATM 4004  C10 OLA A1512      14.584  -3.089  50.960  1.00 83.33           C  
ANISOU 4004  C10 OLA A1512     9665  11296  10700   -308    -83    106       C  
HETATM 4005  C11 OLA A1512      15.101  -1.845  50.278  1.00 83.45           C  
ANISOU 4005  C11 OLA A1512     9644  11369  10696   -450   -132    201       C  
HETATM 4006  C12 OLA A1512      15.833  -2.242  49.003  1.00 86.57           C  
ANISOU 4006  C12 OLA A1512     9896  11942  11054   -335    -70    308       C  
HETATM 4007  C13 OLA A1512      16.585  -1.061  48.399  1.00 77.95           C  
ANISOU 4007  C13 OLA A1512     8726  10959   9932   -494   -126    446       C  
HETATM 4008  C14 OLA A1512      17.461  -1.522  47.241  1.00 80.80           C  
ANISOU 4008  C14 OLA A1512     8919  11540  10240   -362    -53    584       C  
HETATM 4009  C15 OLA A1512      16.639  -2.303  46.222  1.00 86.25           C  
ANISOU 4009  C15 OLA A1512     9689  12140  10943   -141     45    469       C  
HETATM 4010  C16 OLA A1512      17.533  -2.993  45.200  1.00 84.44           C  
ANISOU 4010  C16 OLA A1512     9326  12123  10635     45    138    597       C  
HETATM 4011  C17 OLA A1512      16.701  -3.845  44.250  1.00 74.22           C  
ANISOU 4011  C17 OLA A1512     8160  10709   9332    258    220    473       C  
HETATM 4012  C18 OLA A1512      17.576  -4.806  43.476  1.00 71.80           C  
ANISOU 4012  C18 OLA A1512     7771  10588   8921    497    327    581       C  
HETATM 4013  C10 OLA A1513      18.753 -11.030  57.205  1.00 74.97           C  
ANISOU 4013  C10 OLA A1513     8156  10919   9408    358     60    434       C  
HETATM 4014  C11 OLA A1513      18.001 -12.197  56.610  1.00 75.91           C  
ANISOU 4014  C11 OLA A1513     8418  10899   9527    582    142    319       C  
HETATM 4015  C12 OLA A1513      17.643 -11.897  55.158  1.00 72.93           C  
ANISOU 4015  C12 OLA A1513     8089  10473   9147    647    185    286       C  
HETATM 4016  C13 OLA A1513      17.056 -13.130  54.479  1.00 79.97           C  
ANISOU 4016  C13 OLA A1513     9140  11238  10008    869    254    198       C  
HETATM 4017  C14 OLA A1513      16.658 -12.844  53.034  1.00 84.70           C  
ANISOU 4017  C14 OLA A1513     9807  11779  10595    926    288    161       C  
HETATM 4018  C15 OLA A1513      16.174 -14.113  52.339  1.00 85.20           C  
ANISOU 4018  C15 OLA A1513    10061  11713  10600   1140    342     87       C  
HETATM 4019  C16 OLA A1513      15.659 -13.818  50.934  1.00 85.57           C  
ANISOU 4019  C16 OLA A1513    10201  11680  10632   1176    360     39       C  
HETATM 4020  C17 OLA A1513      15.048 -15.062  50.298  1.00 76.86           C  
ANISOU 4020  C17 OLA A1513     9336  10407   9460   1349    384    -47       C  
HETATM 4021  C18 OLA A1513      14.638 -14.798  48.866  1.00 71.49           C  
ANISOU 4021  C18 OLA A1513     8755   9661   8747   1389    399    -81       C  
HETATM 4022  C10 OLA A1514       6.338  19.713  34.195  1.00 73.68           C  
ANISOU 4022  C10 OLA A1514    10445   8115   9434  -1212   -489    465       C  
HETATM 4023  C11 OLA A1514       5.755  20.039  32.841  1.00 90.87           C  
ANISOU 4023  C11 OLA A1514    12565  10317  11646  -1130   -447    503       C  
HETATM 4024  C12 OLA A1514       6.841  19.924  31.776  1.00 93.83           C  
ANISOU 4024  C12 OLA A1514    12742  10893  12016  -1283   -495    615       C  
HETATM 4025  C13 OLA A1514       6.322  20.331  30.400  1.00 91.83           C  
ANISOU 4025  C13 OLA A1514    12449  10656  11785  -1220   -464    659       C  
HETATM 4026  C14 OLA A1514       7.457  20.381  29.382  1.00 93.05           C  
ANISOU 4026  C14 OLA A1514    12436  11003  11916  -1378   -513    786       C  
HETATM 4027  C15 OLA A1514       7.039  21.127  28.120  1.00 84.66           C  
ANISOU 4027  C15 OLA A1514    11401   9911  10853  -1360   -510    844       C  
HETATM 4028  C16 OLA A1514       8.249  21.452  27.251  1.00 86.33           C  
ANISOU 4028  C16 OLA A1514    11491  10289  11021  -1549   -575    995       C  
HETATM 4029  C17 OLA A1514       7.956  22.620  26.316  1.00 85.21           C  
ANISOU 4029  C17 OLA A1514    11472  10047  10858  -1598   -613   1066       C  
HETATM 4030  C18 OLA A1514       9.167  22.967  25.478  1.00 77.71           C  
ANISOU 4030  C18 OLA A1514    10393   9274   9859  -1796   -680   1235       C  
HETATM 4031  C1  OLA A1515     -11.153  -9.701  58.868  1.00119.01           C  
ANISOU 4031  C1  OLA A1515    13852  15614  15751    276    190    888       C  
HETATM 4032  O1  OLA A1515     -11.794  -8.644  58.679  1.00122.28           O  
ANISOU 4032  O1  OLA A1515    14203  16100  16158    411    290    973       O  
HETATM 4033  O2  OLA A1515     -11.036 -10.232  59.995  1.00121.49           O  
ANISOU 4033  O2  OLA A1515    14169  15946  16044    290    214    887       O  
HETATM 4034  C2  OLA A1515     -10.494 -10.368  57.683  1.00107.20           C  
ANISOU 4034  C2  OLA A1515    12448  14003  14281    104     41    786       C  
HETATM 4035  C3  OLA A1515     -10.319  -9.356  56.556  1.00 91.32           C  
ANISOU 4035  C3  OLA A1515    10472  11943  12281    148     64    730       C  
HETATM 4036  C4  OLA A1515      -9.596  -9.977  55.367  1.00 81.08           C  
ANISOU 4036  C4  OLA A1515     9284  10530  10993      3    -70    622       C  
HETATM 4037  C5  OLA A1515      -9.093  -8.905  54.407  1.00 81.77           C  
ANISOU 4037  C5  OLA A1515     9434  10550  11086     63    -29    523       C  
HETATM 4038  C6  OLA A1515     -10.243  -8.148  53.752  1.00 82.79           C  
ANISOU 4038  C6  OLA A1515     9436  10786  11233     99     -5    687       C  
HETATM 4039  C7  OLA A1515      -9.734  -6.886  53.064  1.00 80.39           C  
ANISOU 4039  C7  OLA A1515     9203  10412  10929    194     66    586       C  
HETATM 4040  C8  OLA A1515     -10.365  -6.698  51.687  1.00 91.08           C  
ANISOU 4040  C8  OLA A1515    10499  11806  12303    125     -4    682       C  
HETATM 4041  C9  OLA A1515      -9.974  -5.343  51.145  1.00 99.72           C  
ANISOU 4041  C9  OLA A1515    11652  12842  13395    238     81    603       C  
HETATM 4042  C10 OLA A1515      -9.505  -5.194  49.907  1.00 97.56           C  
ANISOU 4042  C10 OLA A1515    11441  12501  13127    170     18    534       C  
HETATM 4043  C11 OLA A1515      -9.343  -6.371  48.973  1.00 93.38           C  
ANISOU 4043  C11 OLA A1515    10949  11938  12592     -7   -137    524       C  
HETATM 4044  C12 OLA A1515     -10.053  -6.059  47.661  1.00 89.80           C  
ANISOU 4044  C12 OLA A1515    10443  11530  12148    -63   -199    629       C  
HETATM 4045  C13 OLA A1515      -9.850  -7.152  46.617  1.00100.57           C  
ANISOU 4045  C13 OLA A1515    11896  12833  13483   -236   -360    607       C  
HETATM 4046  C14 OLA A1515      -8.505  -7.018  45.911  1.00 99.26           C  
ANISOU 4046  C14 OLA A1515    11889  12535  13289   -219   -355    413       C  
HETATM 4047  C15 OLA A1515      -8.527  -7.735  44.565  1.00 80.30           C  
ANISOU 4047  C15 OLA A1515     9584  10082  10843   -350   -495    419       C  
HETATM 4048  C16 OLA A1515      -9.475  -7.034  43.598  1.00 70.55           C  
ANISOU 4048  C16 OLA A1515     8259   8922   9627   -380   -523    551       C  
HETATM 4049  C17 OLA A1515      -9.887  -7.961  42.461  1.00 79.22           C  
ANISOU 4049  C17 OLA A1515     9440   9989  10669   -553   -697    612       C  
HETATM 4050  C18 OLA A1515     -10.900  -7.293  41.557  1.00 89.65           C  
ANISOU 4050  C18 OLA A1515    10651  11403  12008   -596   -736    767       C  
HETATM 4051  C1  OLA A1516     -11.320   5.716  50.646  1.00 85.05           C  
ANISOU 4051  C1  OLA A1516    10483  10600  11234   1560    938    663       C  
HETATM 4052  O1  OLA A1516     -10.475   5.436  49.770  1.00 95.21           O  
ANISOU 4052  O1  OLA A1516    11771  11831  12574   1360    819    555       O  
HETATM 4053  O2  OLA A1516     -11.294   5.223  51.795  1.00 84.72           O  
ANISOU 4053  O2  OLA A1516    10454  10574  11161   1597    974    647       O  
HETATM 4054  C2  OLA A1516     -12.419   6.693  50.298  1.00 81.23           C  
ANISOU 4054  C2  OLA A1516     9980  10174  10712   1785   1050    828       C  
HETATM 4055  C3  OLA A1516     -12.274   7.116  48.840  1.00 87.84           C  
ANISOU 4055  C3  OLA A1516    10792  10985  11598   1688    976    825       C  
HETATM 4056  C4  OLA A1516     -13.308   8.171  48.460  1.00 94.12           C  
ANISOU 4056  C4  OLA A1516    11584  11828  12351   1921   1090    990       C  
HETATM 4057  C5  OLA A1516     -14.654   7.546  48.106  1.00 94.77           C  
ANISOU 4057  C5  OLA A1516    11351  12173  12484   1963   1100   1244       C  
HETATM 4058  C6  OLA A1516     -14.865   7.504  46.597  1.00 97.42           C  
ANISOU 4058  C6  OLA A1516    11549  12574  12892   1825    997   1311       C  
HETATM 4059  C7  OLA A1516     -16.261   6.993  46.256  1.00100.11           C  
ANISOU 4059  C7  OLA A1516    11583  13185  13270   1859    997   1594       C  
HETATM 4060  C8  OLA A1516     -16.554   7.119  44.764  1.00 94.92           C  
ANISOU 4060  C8  OLA A1516    10813  12586  12665   1746    902   1676       C  
HETATM 4061  C9  OLA A1516     -15.644   6.200  43.987  1.00 89.99           C  
ANISOU 4061  C9  OLA A1516    10197  11891  12105   1432    718   1517       C  
HETATM 4062  C1  OLA A1517       9.391  14.677  59.200  1.00145.59           C  
ANISOU 4062  C1  OLA A1517    21872  16072  17375  -1635   -984   -473       C  
HETATM 4063  O1  OLA A1517       8.474  15.485  59.461  1.00151.68           O  
ANISOU 4063  O1  OLA A1517    22997  16593  18040  -1456   -913   -548       O  
HETATM 4064  O2  OLA A1517      10.107  14.153  60.081  1.00149.13           O  
ANISOU 4064  O2  OLA A1517    22278  16598  17788  -1780  -1070   -453       O  
HETATM 4065  C2  OLA A1517       9.642  14.314  57.755  1.00127.80           C  
ANISOU 4065  C2  OLA A1517    19230  14039  15288  -1662   -958   -397       C  
HETATM 4066  C3  OLA A1517       9.034  12.949  57.451  1.00111.91           C  
ANISOU 4066  C3  OLA A1517    16819  12249  13451  -1422   -783   -431       C  
HETATM 4067  C4  OLA A1517       9.463  12.455  56.074  1.00 94.99           C  
ANISOU 4067  C4  OLA A1517    14296  10339  11456  -1468   -773   -350       C  
HETATM 4068  C5  OLA A1517       8.521  11.376  55.551  1.00 86.78           C  
ANISOU 4068  C5  OLA A1517    12967   9438  10568  -1196   -593   -399       C  
HETATM 4069  C6  OLA A1517       9.028  10.806  54.229  1.00 82.87           C  
ANISOU 4069  C6  OLA A1517    12121   9168  10196  -1240   -588   -322       C  
HETATM 4070  C7  OLA A1517       7.873  10.380  53.331  1.00 79.54           C  
ANISOU 4070  C7  OLA A1517    11553   8783   9887   -995   -437   -365       C  
HETATM 4071  C8  OLA A1517       8.365  10.082  51.919  1.00 87.48           C  
ANISOU 4071  C8  OLA A1517    12293   9965  10982  -1046   -444   -292       C  
HETATM 4072  C9  OLA A1517       7.241  10.249  50.922  1.00 83.61           C  
ANISOU 4072  C9  OLA A1517    11774   9436  10557   -864   -340   -319       C  
HETATM 4073  C10 OLA A1517       7.439  10.954  49.810  1.00 86.38           C  
ANISOU 4073  C10 OLA A1517    12121   9785  10916   -930   -372   -266       C  
HETATM 4074  C11 OLA A1517       8.787  11.587  49.553  1.00 94.46           C  
ANISOU 4074  C11 OLA A1517    13161  10852  11880  -1194   -514   -169       C  
HETATM 4075  C12 OLA A1517       9.339  11.152  48.200  1.00 85.09           C  
ANISOU 4075  C12 OLA A1517    11692   9870  10768  -1226   -508    -87       C  
HETATM 4076  C13 OLA A1517      10.770  11.657  48.042  1.00 81.03           C  
ANISOU 4076  C13 OLA A1517    11144   9451  10193  -1494   -648     44       C  
HETATM 4077  C14 OLA A1517      11.334  11.334  46.664  1.00 73.10           C  
ANISOU 4077  C14 OLA A1517     9875   8656   9246  -1508   -631    141       C  
HETATM 4078  C1  OLA A1518     -10.115  17.801  60.129  1.00119.88           C  
ANISOU 4078  C1  OLA A1518    19321  12598  13631   3691   1898      8       C  
HETATM 4079  O1  OLA A1518     -10.684  18.875  59.833  1.00121.63           O  
ANISOU 4079  O1  OLA A1518    19804  12684  13724   3957   2004     66       O  
HETATM 4080  O2  OLA A1518     -10.365  17.169  61.179  1.00122.54           O  
ANISOU 4080  O2  OLA A1518    19610  13026  13924   3795   1975     22       O  
HETATM 4081  C2  OLA A1518      -9.085  17.243  59.174  1.00109.70           C  
ANISOU 4081  C2  OLA A1518    17765  11369  12548   3243   1676    -75       C  
HETATM 4082  C3  OLA A1518      -9.752  16.975  57.830  1.00106.83           C  
ANISOU 4082  C3  OLA A1518    16990  11232  12368   3260   1705     59       C  
HETATM 4083  C4  OLA A1518      -8.744  16.923  56.687  1.00104.98           C  
ANISOU 4083  C4  OLA A1518    16639  10971  12276   2882   1503    -24       C  
HETATM 4084  C5  OLA A1518      -8.006  15.591  56.637  1.00 96.25           C  
ANISOU 4084  C5  OLA A1518    15179  10044  11345   2559   1368    -80       C  
HETATM 4085  C6  OLA A1518      -7.407  15.351  55.255  1.00 92.04           C  
ANISOU 4085  C6  OLA A1518    14402   9588  10981   2277   1226    -94       C  
HETATM 4086  C7  OLA A1518      -6.400  16.431  54.876  1.00 88.44           C  
ANISOU 4086  C7  OLA A1518    14286   8876  10443   2097   1097   -195       C  
HETATM 4087  C8  OLA A1518      -5.876  16.209  53.461  1.00 78.51           C  
ANISOU 4087  C8  OLA A1518    12769   7716   9345   1849    976   -189       C  
HETATM 4088  C9  OLA A1518      -4.725  17.150  53.192  1.00 82.21           C  
ANISOU 4088  C9  OLA A1518    13544   7957   9735   1619    826   -278       C  
HETATM 4089  C1  OLA A1519     -10.798  14.603  52.676  1.00114.95           C  
ANISOU 4089  C1  OLA A1519    16360  13132  14182   2729   1491    405       C  
HETATM 4090  O1  OLA A1519     -11.873  14.141  53.118  1.00119.70           O  
ANISOU 4090  O1  OLA A1519    16773  13922  14785   2944   1619    555       O  
HETATM 4091  O2  OLA A1519     -10.016  15.284  53.373  1.00122.16           O  
ANISOU 4091  O2  OLA A1519    17649  13800  14966   2703   1462    268       O  
HETATM 4092  C2  OLA A1519     -10.428  14.330  51.237  1.00 96.06           C  
ANISOU 4092  C2  OLA A1519    13742  10817  11940   2484   1361    401       C  
HETATM 4093  C3  OLA A1519      -9.031  14.878  50.968  1.00 76.21           C  
ANISOU 4093  C3  OLA A1519    11475   8080   9399   2232   1216    226       C  
HETATM 4094  C4  OLA A1519      -8.644  14.721  49.503  1.00 67.29           C  
ANISOU 4094  C4  OLA A1519    10147   7021   8400   2016   1101    228       C  
HETATM 4095  C5  OLA A1519      -9.563  15.537  48.602  1.00 80.82           C  
ANISOU 4095  C5  OLA A1519    11852   8750  10105   2203   1179    357       C  
HETATM 4096  C6  OLA A1519      -9.073  15.523  47.158  1.00 82.50           C  
ANISOU 4096  C6  OLA A1519    11924   8999  10424   1983   1059    344       C  
HETATM 4097  C7  OLA A1519      -7.656  16.075  47.058  1.00 86.26           C  
ANISOU 4097  C7  OLA A1519    12644   9271  10858   1747    930    192       C  
HETATM 4098  C8  OLA A1519      -7.263  16.334  45.607  1.00 93.76           C  
ANISOU 4098  C8  OLA A1519    13500  10240  11884   1583    838    201       C  
HETATM 4099  C8  OLC A1520      -6.272 -12.274  49.849  1.00 68.35           C  
ANISOU 4099  C8  OLC A1520     8319   8399   9251   -356   -512    165       C  
HETATM 4100  C24 OLC A1520       0.572 -14.520  61.230  1.00 70.24           C  
ANISOU 4100  C24 OLC A1520     8633   8666   9389    113    -66   -358       C  
HETATM 4101  C7  OLC A1520      -5.373 -13.186  50.677  1.00 58.60           C  
ANISOU 4101  C7  OLC A1520     7183   7100   7983   -330   -510     71       C  
HETATM 4102  C6  OLC A1520      -5.656 -13.036  52.167  1.00 60.38           C  
ANISOU 4102  C6  OLC A1520     7293   7401   8249   -288   -437    111       C  
HETATM 4103  C5  OLC A1520      -4.612 -13.779  52.996  1.00 70.62           C  
ANISOU 4103  C5  OLC A1520     8679   8639   9514   -245   -420      7       C  
HETATM 4104  C4  OLC A1520      -4.835 -13.600  54.495  1.00 68.63           C  
ANISOU 4104  C4  OLC A1520     8325   8458   9293   -201   -345     39       C  
HETATM 4105  C3  OLC A1520      -3.750 -14.318  55.294  1.00 74.22           C  
ANISOU 4105  C3  OLC A1520     9119   9112   9969   -161   -332    -60       C  
HETATM 4106  C2  OLC A1520      -3.832 -14.012  56.787  1.00 77.85           C  
ANISOU 4106  C2  OLC A1520     9492   9637  10450   -107   -249    -45       C  
HETATM 4107  C21 OLC A1520      -0.976 -14.247  59.312  1.00 77.89           C  
ANISOU 4107  C21 OLC A1520     9580   9615  10400     50   -122   -273       C  
HETATM 4108  C1  OLC A1520      -2.625 -14.599  57.487  1.00 86.90           C  
ANISOU 4108  C1  OLC A1520    10718  10737  11565    -64   -235   -147       C  
HETATM 4109  C22 OLC A1520      -0.830 -14.824  60.717  1.00 76.96           C  
ANISOU 4109  C22 OLC A1520     9455   9517  10268     59   -108   -267       C  
HETATM 4110  O19 OLC A1520      -1.856 -15.329  56.885  1.00 96.54           O  
ANISOU 4110  O19 OLC A1520    12049  11887  12746    -66   -285   -208       O  
HETATM 4111  O25 OLC A1520       0.999 -15.552  62.126  1.00 66.74           O  
ANISOU 4111  O25 OLC A1520     8217   8220   8921    115    -88   -361       O  
HETATM 4112  O23 OLC A1520      -1.800 -14.238  61.591  1.00 76.16           O  
ANISOU 4112  O23 OLC A1520     9274   9479  10186     73    -53   -197       O  
HETATM 4113  O20 OLC A1520      -2.336 -14.295  58.880  1.00 80.87           O  
ANISOU 4113  O20 OLC A1520     9907  10016  10805     -7   -158   -167       O  
HETATM 4114  C24 OLC A1521       1.191  17.143  31.217  1.00127.82           C  
ANISOU 4114  C24 OLC A1521    16770  15211  16585   -355    -93    353       C  
HETATM 4115  C3  OLC A1521       2.706  16.356  36.602  1.00 90.28           C  
ANISOU 4115  C3  OLC A1521    12341  10238  11724   -473   -134    138       C  
HETATM 4116  C2  OLC A1521       3.224  15.302  35.633  1.00 94.86           C  
ANISOU 4116  C2  OLC A1521    12654  11032  12355   -514   -137    160       C  
HETATM 4117  C21 OLC A1521       3.249  16.832  32.599  1.00126.11           C  
ANISOU 4117  C21 OLC A1521    16579  15029  16308   -593   -178    318       C  
HETATM 4118  C1  OLC A1521       2.399  15.315  34.366  1.00107.03           C  
ANISOU 4118  C1  OLC A1521    14112  12617  13938   -419    -98    194       C  
HETATM 4119  C22 OLC A1521       2.653  16.715  31.203  1.00128.83           C  
ANISOU 4119  C22 OLC A1521    16812  15450  16687   -520   -148    357       C  
HETATM 4120  O19 OLC A1521       1.858  14.299  33.965  1.00111.30           O  
ANISOU 4120  O19 OLC A1521    14498  13264  14528   -329    -58    178       O  
HETATM 4121  O25 OLC A1521       0.572  16.729  29.994  1.00130.10           O  
ANISOU 4121  O25 OLC A1521    16919  15602  16910   -290    -72    388       O  
HETATM 4122  O23 OLC A1521       3.397  17.554  30.315  1.00136.12           O  
ANISOU 4122  O23 OLC A1521    17759  16387  17574   -649   -202    436       O  
HETATM 4123  O20 OLC A1521       2.265  16.533  33.586  1.00118.35           O  
ANISOU 4123  O20 OLC A1521    15660  13963  15347   -447   -121    253       O  
HETATM 4124  C18 OLC A1522     -14.896  12.689  50.037  1.00 79.32           C  
ANISOU 4124  C18 OLC A1522    10494   9608  10036   2997   1646   1165       C  
HETATM 4125  C10 OLC A1522      -9.914  14.879  43.697  1.00110.32           C  
ANISOU 4125  C10 OLC A1522    14820  12880  14216   1786    940    555       C  
HETATM 4126  C9  OLC A1522      -8.929  14.345  42.980  1.00101.70           C  
ANISOU 4126  C9  OLC A1522    13643  11802  13197   1517    806    461       C  
HETATM 4127  C17 OLC A1522     -14.418  13.703  49.021  1.00 82.63           C  
ANISOU 4127  C17 OLC A1522    11098   9853  10446   2951   1597   1088       C  
HETATM 4128  C11 OLC A1522     -11.347  14.750  43.241  1.00117.75           C  
ANISOU 4128  C11 OLC A1522    15534  14011  15193   1972   1024    757       C  
HETATM 4129  C8  OLC A1522      -9.238  13.601  41.704  1.00 95.76           C  
ANISOU 4129  C8  OLC A1522    12604  11227  12552   1401    737    534       C  
HETATM 4130  C24 OLC A1522      -2.312  13.987  32.509  1.00133.36           C  
ANISOU 4130  C24 OLC A1522    17145  16087  17441     85     75    287       C  
HETATM 4131  C16 OLC A1522     -14.815  13.283  47.611  1.00 87.24           C  
ANISOU 4131  C16 OLC A1522    11371  10614  11163   2803   1506   1202       C  
HETATM 4132  C12 OLC A1522     -12.191  14.182  44.374  1.00117.77           C  
ANISOU 4132  C12 OLC A1522    15439  14135  15173   2149   1128    849       C  
HETATM 4133  C7  OLC A1522      -8.454  14.223  40.556  1.00 88.64           C  
ANISOU 4133  C7  OLC A1522    11778  10242  11659   1256    655    482       C  
HETATM 4134  C15 OLC A1522     -14.169  14.179  46.560  1.00 88.47           C  
ANISOU 4134  C15 OLC A1522    11699  10595  11319   2707   1435   1105       C  
HETATM 4135  C13 OLC A1522     -13.676  14.390  44.099  1.00112.18           C  
ANISOU 4135  C13 OLC A1522    14554  13606  14463   2394   1242   1088       C  
HETATM 4136  C6  OLC A1522      -6.956  14.151  40.824  1.00 85.79           C  
ANISOU 4136  C6  OLC A1522    11546   9770  11279   1050    566    325       C  
HETATM 4137  C14 OLC A1522     -14.529  13.701  45.158  1.00101.29           C  
ANISOU 4137  C14 OLC A1522    13024  12393  13069   2549   1338   1210       C  
HETATM 4138  C5  OLC A1522      -6.165  14.636  39.616  1.00 88.60           C  
ANISOU 4138  C5  OLC A1522    11929  10085  11648    892    481    297       C  
HETATM 4139  C4  OLC A1522      -6.641  13.949  38.342  1.00 86.67           C  
ANISOU 4139  C4  OLC A1522    11434  10009  11488    842    443    372       C  
HETATM 4140  C3  OLC A1522      -5.909  14.519  37.135  1.00100.37           C  
ANISOU 4140  C3  OLC A1522    13207  11705  13224    711    373    355       C  
HETATM 4141  C2  OLC A1522      -6.593  14.147  35.824  1.00111.80           C  
ANISOU 4141  C2  OLC A1522    14461  13290  14730    704    348    447       C  
HETATM 4142  C21 OLC A1522      -3.296  15.188  34.430  1.00128.25           C  
ANISOU 4142  C21 OLC A1522    16749  15229  16752    282    170    289       C  
HETATM 4143  C1  OLC A1522      -5.720  14.650  34.701  1.00122.58           C  
ANISOU 4143  C1  OLC A1522    15869  14619  16088    566    280    420       C  
HETATM 4144  C22 OLC A1522      -2.053  14.464  33.931  1.00129.56           C  
ANISOU 4144  C22 OLC A1522    16815  15486  16926    106     99    240       C  
HETATM 4145  O19 OLC A1522      -6.154  15.424  33.863  1.00126.07           O  
ANISOU 4145  O19 OLC A1522    16334  15042  16524    613    289    492       O  
HETATM 4146  O25 OLC A1522      -3.723  13.853  32.307  1.00137.33           O  
ANISOU 4146  O25 OLC A1522    17579  16622  17976    216    113    355       O  
HETATM 4147  O23 OLC A1522      -0.937  15.360  33.940  1.00132.00           O  
ANISOU 4147  O23 OLC A1522    17262  15709  17184    -19     52    227       O  
HETATM 4148  O20 OLC A1522      -4.330  14.229  34.639  1.00125.37           O  
ANISOU 4148  O20 OLC A1522    16230  14972  16435    385    209    322       O  
HETATM 4149  O   HOH A1601       4.848  23.798  22.253  1.00 73.80           O  
ANISOU 4149  O   HOH A1601    10036   8510   9496  -1184   -456   1105       O  
HETATM 4150  O   HOH A1602       4.608  15.519  19.731  1.00 50.18           O  
ANISOU 4150  O   HOH A1602     6123   6450   6494   -544   -126    820       O  
HETATM 4151  O   HOH A1603       7.523  16.648  18.645  1.00 64.88           O  
ANISOU 4151  O   HOH A1603     7815   8623   8215   -758   -128   1097       O  
HETATM 4152  O   HOH A1604      15.764 -15.473  79.051  1.00 58.74           O  
ANISOU 4152  O   HOH A1604     7050   8211   7056   -505   -523    -19       O  
HETATM 4153  O   HOH A1605      -2.594 -12.896  77.651  1.00 70.16           O  
ANISOU 4153  O   HOH A1605     8868   9036   8753    718    621    -82       O  
HETATM 4154  O   HOH A1606       5.868 -44.800  92.169  1.00 59.07           O  
ANISOU 4154  O   HOH A1606     8711   6831   6902     44  -1072   1110       O  
HETATM 4155  O   HOH A1607       1.704 -25.984  93.687  1.00 50.78           O  
ANISOU 4155  O   HOH A1607     6374   7125   5796    268    191    398       O  
HETATM 4156  O   HOH A1608      15.474 -36.584  74.603  1.00 62.17           O  
ANISOU 4156  O   HOH A1608     8957   7524   7140   2097   -123    277       O  
HETATM 4157  O   HOH A1609      -3.239   0.991  47.143  1.00 41.60           O  
ANISOU 4157  O   HOH A1609     5015   4861   5930    296    204   -156       O  
HETATM 4158  O   HOH A1610      -6.686  12.029  14.344  1.00 62.98           O  
ANISOU 4158  O   HOH A1610     7807   7986   8137   -333   -577   1033       O  
HETATM 4159  O   HOH A1611       3.870  19.201  17.917  1.00 74.63           O  
ANISOU 4159  O   HOH A1611     9398   9347   9610   -724   -220   1043       O  
HETATM 4160  O   HOH A1612      -1.177   2.944  49.083  1.00 60.84           O  
ANISOU 4160  O   HOH A1612     7759   7109   8250    277    253   -310       O  
HETATM 4161  O   HOH A1613      11.957 -36.992  75.432  1.00 53.19           O  
ANISOU 4161  O   HOH A1613     8067   5988   6154   1480   -396    135       O  
HETATM 4162  O   HOH A1614      -2.842  11.190  14.364  1.00 57.57           O  
ANISOU 4162  O   HOH A1614     7278   7318   7277   -270   -412    773       O  
HETATM 4163  O   HOH A1615      -9.058 -28.099  83.443  1.00 54.19           O  
ANISOU 4163  O   HOH A1615     5704   7943   6945   -414   -131   1676       O  
HETATM 4164  O   HOH A1616       8.758 -25.731  69.739  1.00 44.02           O  
ANISOU 4164  O   HOH A1616     5751   5373   5601    643   -205   -274       O  
HETATM 4165  O   HOH A1617       9.928  -6.545  23.870  1.00 90.98           O  
ANISOU 4165  O   HOH A1617    12540  11786  10242   1625    462    -43       O  
HETATM 4166  O   HOH A1618     -10.233 -26.792  89.641  1.00 61.75           O  
ANISOU 4166  O   HOH A1618     6418   9531   7512    221    498   1998       O  
HETATM 4167  O   HOH A1619      -2.051  -4.121  47.872  1.00 71.62           O  
ANISOU 4167  O   HOH A1619     8723   8766   9725    113     13   -249       O  
HETATM 4168  O   HOH A1620      19.884 -29.956  81.575  1.00 66.13           O  
ANISOU 4168  O   HOH A1620     7580   9659   7886   1166   -212    733       O  
HETATM 4169  O   HOH A1621      -6.193   9.099  22.443  1.00 50.91           O  
ANISOU 4169  O   HOH A1621     6146   6305   6891   -164   -368    675       O  
HETATM 4170  O   HOH A1622      -4.183 -17.795  84.099  1.00 64.56           O  
ANISOU 4170  O   HOH A1622     7899   8778   7851    758    698    373       O  
HETATM 4171  O   HOH A1623       6.626 -25.521  73.115  1.00 61.93           O  
ANISOU 4171  O   HOH A1623     7888   7689   7955    360   -243   -222       O  
HETATM 4172  O   HOH A1624      -3.515  10.378  32.484  1.00 46.87           O  
ANISOU 4172  O   HOH A1624     5830   5413   6566    120     45    267       O  
HETATM 4173  O   HOH A1625       0.646   2.902  51.777  1.00 44.54           O  
ANISOU 4173  O   HOH A1625     5887   4961   6076    182    226   -431       O  
HETATM 4174  O   HOH A1626      -4.423   6.758   8.041  1.00 67.25           O  
ANISOU 4174  O   HOH A1626     9353   8500   7698   -419   -892    787       O  
HETATM 4175  O   HOH A1627      -3.013   3.032  27.182  1.00 69.34           O  
ANISOU 4175  O   HOH A1627     8683   8555   9106   -142   -340    178       O  
HETATM 4176  O   HOH A1628       3.996 -43.754  93.545  1.00 76.89           O  
ANISOU 4176  O   HOH A1628    10620   9362   9231   -240  -1035   1232       O  
HETATM 4177  O   HOH A1629      11.900  -0.313  19.987  1.00 61.80           O  
ANISOU 4177  O   HOH A1629     7922   8874   6685   1345    650    518       O  
HETATM 4178  O   HOH A1630       5.357  -5.426  53.812  1.00 48.08           O  
ANISOU 4178  O   HOH A1630     5822   5904   6543     40     46   -512       O  
HETATM 4179  O   HOH A1631       4.005   1.578  62.975  1.00 58.28           O  
ANISOU 4179  O   HOH A1631     8402   6462   7280    -24    113   -689       O  
HETATM 4180  O   HOH A1632       5.786  -7.861  31.996  1.00 59.84           O  
ANISOU 4180  O   HOH A1632     8269   7330   7137    762     -7   -362       O  
HETATM 4181  O   HOH A1633      15.556 -24.783  70.060  1.00 62.97           O  
ANISOU 4181  O   HOH A1633     7592   8546   7786   1115      1     53       O  
HETATM 4182  O   HOH A1634      -1.080   5.271  10.411  1.00 53.99           O  
ANISOU 4182  O   HOH A1634     7699   6846   5968    -66   -553    521       O  
HETATM 4183  O   HOH A1635      10.687 -30.943  76.771  1.00 51.81           O  
ANISOU 4183  O   HOH A1635     6853   6444   6387    818   -295      3       O  
HETATM 4184  O   HOH A1636      -4.403 -20.645  95.530  1.00 62.51           O  
ANISOU 4184  O   HOH A1636     8040   8978   6735   1167   1054    734       O  
HETATM 4185  O   HOH A1637     -10.015 -32.102  75.427  1.00 65.18           O  
ANISOU 4185  O   HOH A1637     7782   8510   8474  -1555  -1250   1812       O  
HETATM 4186  O   HOH A1638       7.377 -30.770  79.972  1.00 53.81           O  
ANISOU 4186  O   HOH A1638     7008   6694   6744    381   -375     57       O  
HETATM 4187  O   HOH A1639     -13.294 -21.842  88.179  1.00 61.20           O  
ANISOU 4187  O   HOH A1639     6064   9915   7274   1019   1137   2280       O  
HETATM 4188  O   HOH A1640      22.551 -41.491  92.741  1.00 72.59           O  
ANISOU 4188  O   HOH A1640     8851  10549   8182   2063   -366   1626       O  
HETATM 4189  O   HOH A1641       4.358  -5.276  39.414  1.00 47.05           O  
ANISOU 4189  O   HOH A1641     5895   5783   6198    267    -26   -375       O  
HETATM 4190  O   HOH A1642      -1.327 -20.287  91.859  1.00 56.28           O  
ANISOU 4190  O   HOH A1642     7295   7787   6303    726    651    296       O  
HETATM 4191  O   HOH A1643      -3.406 -22.743  72.734  1.00 49.59           O  
ANISOU 4191  O   HOH A1643     5835   6368   6640   -150   -214    323       O  
HETATM 4192  O   HOH A1644      -0.137  14.729  18.207  1.00 59.85           O  
ANISOU 4192  O   HOH A1644     7449   7473   7817   -308   -188    751       O  
HETATM 4193  O   HOH A1645      15.929 -18.020  88.648  1.00 75.72           O  
ANISOU 4193  O   HOH A1645     9651  10412   8709   -743   -746     69       O  
HETATM 4194  O   HOH A1646      -3.760  -7.055  35.603  1.00 44.12           O  
ANISOU 4194  O   HOH A1646     5851   5087   5826   -273   -628    -82       O  
HETATM 4195  O   HOH A1647      17.300  -3.775  21.675  1.00 68.66           O  
ANISOU 4195  O   HOH A1647     8497  10570   7021   2408   1247    976       O  
HETATM 4196  O   HOH A1648      21.402 -24.268  76.580  1.00 63.71           O  
ANISOU 4196  O   HOH A1648     6790   9756   7660    829   -194    788       O  
HETATM 4197  O   HOH A1649      -4.890  10.111  35.509  1.00 66.74           O  
ANISOU 4197  O   HOH A1649     8378   7868   9111    322    159    269       O  
HETATM 4198  O   HOH A1650       1.895  14.253  20.403  1.00 48.63           O  
ANISOU 4198  O   HOH A1650     5999   6076   6400   -362   -134    659       O  
HETATM 4199  O   HOH A1651       7.908 -15.824  95.346  1.00 63.53           O  
ANISOU 4199  O   HOH A1651     9537   8146   6455    -90   -110   -373       O  
HETATM 4200  O   HOH A1652       0.577 -22.310  68.830  1.00 61.38           O  
ANISOU 4200  O   HOH A1652     7675   7531   8117      1   -280   -125       O  
HETATM 4201  O   HOH A1653       4.219 -29.622  99.530  1.00 75.53           O  
ANISOU 4201  O   HOH A1653     9629  10435   8634    148     -2    585       O  
HETATM 4202  O   HOH A1654      -7.803 -36.890  80.830  1.00 71.99           O  
ANISOU 4202  O   HOH A1654     9139   9082   9133  -1607  -1408   1831       O  
HETATM 4203  O   HOH A1655      -4.088   0.002  65.393  1.00 70.14           O  
ANISOU 4203  O   HOH A1655     9615   8245   8791   1147    840   -323       O  
HETATM 4204  O   HOH A1656      18.468 -15.112  58.929  1.00 65.75           O  
ANISOU 4204  O   HOH A1656     7185   9627   8172    858    186    336       O  
HETATM 4205  O   HOH A1657       5.215  -6.749  64.000  1.00 76.61           O  
ANISOU 4205  O   HOH A1657     9722   9437   9949      8     75   -597       O  
HETATM 4206  O   HOH A1658       5.569  -7.188  24.910  1.00 77.88           O  
ANISOU 4206  O   HOH A1658    11188   9541   8862    989    -29   -291       O  
HETATM 4207  O   HOH A1659      -1.248   2.157  28.386  1.00 87.45           O  
ANISOU 4207  O   HOH A1659    11015  10851  11360    -70   -259     48       O  
HETATM 4208  O   HOH A1660       3.289  -5.348  52.816  1.00 65.37           O  
ANISOU 4208  O   HOH A1660     8028   8015   8795     90     63   -499       O  
HETATM 4209  O   HOH A1661     -12.612 -33.450  79.319  1.00 84.34           O  
ANISOU 4209  O   HOH A1661     9635  11562  10849  -1806  -1237   2577       O  
HETATM 4210  O   HOH A1662      -0.818 -36.895  77.488  1.00 54.42           O  
ANISOU 4210  O   HOH A1662     7933   5974   6769   -663  -1205    691       O  
HETATM 4211  O   HOH A1663      12.456 -43.527  97.250  1.00 78.71           O  
ANISOU 4211  O   HOH A1663    10522  10180   9203    722   -741   1138       O  
HETATM 4212  O   HOH A1664     -13.969 -25.007  84.196  1.00 68.95           O  
ANISOU 4212  O   HOH A1664     6730  10780   8686     43    411   2547       O  
HETATM 4213  O   HOH A1665      -2.058   2.836  19.278  1.00 65.54           O  
ANISOU 4213  O   HOH A1665     8712   8121   8069   -152   -515    263       O  
HETATM 4214  O   HOH A1666      20.117   2.874  61.093  1.00 72.36           O  
ANISOU 4214  O   HOH A1666     8902   9898   8693  -2382  -1280    730       O  
HETATM 4215  O   HOH A1667      -1.070 -41.484 100.680  1.00 82.77           O  
ANISOU 4215  O   HOH A1667    10344  11251   9853   -614   -649   1904       O  
HETATM 4216  O   HOH A1668       5.673  13.913  15.429  1.00 53.87           O  
ANISOU 4216  O   HOH A1668     6484   7329   6654   -342    -30    953       O  
HETATM 4217  O   HOH A1669       3.391 -33.548  74.405  1.00 62.28           O  
ANISOU 4217  O   HOH A1669     8830   7045   7790     74   -771    131       O  
HETATM 4218  O   HOH A1670      -1.404  -2.513  24.327  1.00 82.67           O  
ANISOU 4218  O   HOH A1670    11166  10057  10189    -61   -561    -37       O  
HETATM 4219  O   HOH A1671      -1.276 -19.147  94.056  1.00 74.08           O  
ANISOU 4219  O   HOH A1671     9876  10024   8247    907    785    251       O  
HETATM 4220  O   HOH A1672      22.001  -0.028  22.235  1.00 88.93           O  
ANISOU 4220  O   HOH A1672     9561  14522   9707   2057   1410   2054       O  
HETATM 4221  O   HOH A1673       7.069 -11.624  69.544  1.00 67.59           O  
ANISOU 4221  O   HOH A1673     8457   8523   8700      4     -6   -539       O  
HETATM 4222  O   HOH A1674      -3.634  -4.089  22.792  1.00 78.54           O  
ANISOU 4222  O   HOH A1674    11001   9357   9483   -326   -907     49       O  
CONECT  630 1225                                                                
CONECT 1225  630                                                                
CONECT 1623 1629                                                                
CONECT 1629 1623 1630                                                           
CONECT 1630 1629 1631 1637                                                      
CONECT 1631 1630 1632                                                           
CONECT 1632 1631 1633                                                           
CONECT 1633 1632 1634                                                           
CONECT 1634 1633 1635 1636                                                      
CONECT 1635 1634                                                                
CONECT 1636 1634                                                                
CONECT 1637 1630 1638 1639                                                      
CONECT 1638 1637                                                                
CONECT 1639 1637                                                                
CONECT 3801 3810                                                                
CONECT 3810 3801 3811                                                           
CONECT 3811 3810 3812 3818                                                      
CONECT 3812 3811 3813                                                           
CONECT 3813 3812 3814                                                           
CONECT 3814 3813 3815                                                           
CONECT 3815 3814 3816 3817                                                      
CONECT 3816 3815                                                                
CONECT 3817 3815                                                                
CONECT 3818 3811 3819 3820                                                      
CONECT 3819 3818                                                                
CONECT 3820 3818                                                                
CONECT 3834 3842 3860 3861 3862                                                 
CONECT 3835 3836 3864                                                           
CONECT 3836 3835 3869                                                           
CONECT 3837 3849 3864                                                           
CONECT 3838 3839                                                                
CONECT 3839 3838 3840 3868                                                      
CONECT 3840 3839 3841 3845                                                      
CONECT 3841 3840 3842                                                           
CONECT 3842 3834 3841 3843                                                      
CONECT 3843 3842 3844                                                           
CONECT 3844 3843 3845 3846                                                      
CONECT 3845 3840 3844                                                           
CONECT 3846 3844 3857 3858 3859                                                 
CONECT 3847 3848 3868 3869                                                      
CONECT 3848 3847 3851 3864                                                      
CONECT 3849 3837 3865 3867                                                      
CONECT 3850 3865 3866 3870                                                      
CONECT 3851 3848 3852 3856                                                      
CONECT 3852 3851 3853                                                           
CONECT 3853 3852 3854                                                           
CONECT 3854 3853 3855 3863                                                      
CONECT 3855 3854 3856                                                           
CONECT 3856 3851 3855                                                           
CONECT 3857 3846                                                                
CONECT 3858 3846                                                                
CONECT 3859 3846                                                                
CONECT 3860 3834                                                                
CONECT 3861 3834                                                                
CONECT 3862 3834                                                                
CONECT 3863 3854                                                                
CONECT 3864 3835 3837 3848                                                      
CONECT 3865 3849 3850                                                           
CONECT 3866 3850 3867                                                           
CONECT 3867 3849 3866                                                           
CONECT 3868 3839 3847                                                           
CONECT 3869 3836 3847                                                           
CONECT 3870 3850                                                                
CONECT 3871 3872 3873 3874                                                      
CONECT 3872 3871                                                                
CONECT 3873 3871                                                                
CONECT 3874 3871 3875                                                           
CONECT 3875 3874 3876 3877 3881                                                 
CONECT 3876 3875                                                                
CONECT 3877 3875 3878                                                           
CONECT 3878 3877 3879 3880                                                      
CONECT 3879 3878                                                                
CONECT 3880 3878                                                                
CONECT 3881 3875 3882 3883                                                      
CONECT 3882 3881                                                                
CONECT 3883 3881                                                                
CONECT 3884 3885 3886 3887                                                      
CONECT 3885 3884                                                                
CONECT 3886 3884                                                                
CONECT 3887 3884 3888                                                           
CONECT 3888 3887 3889                                                           
CONECT 3889 3888 3890                                                           
CONECT 3890 3889 3891                                                           
CONECT 3891 3890 3892                                                           
CONECT 3892 3891 3893                                                           
CONECT 3893 3892 3894                                                           
CONECT 3894 3893 3895                                                           
CONECT 3895 3894 3896                                                           
CONECT 3896 3895 3897                                                           
CONECT 3897 3896 3898                                                           
CONECT 3898 3897 3899                                                           
CONECT 3899 3898 3900                                                           
CONECT 3900 3899 3901                                                           
CONECT 3901 3900 3902                                                           
CONECT 3902 3901 3903                                                           
CONECT 3903 3902                                                                
CONECT 3904 3905 3906 3907                                                      
CONECT 3905 3904                                                                
CONECT 3906 3904                                                                
CONECT 3907 3904 3908                                                           
CONECT 3908 3907 3909                                                           
CONECT 3909 3908 3910                                                           
CONECT 3910 3909 3911                                                           
CONECT 3911 3910 3912                                                           
CONECT 3912 3911 3913                                                           
CONECT 3913 3912 3914                                                           
CONECT 3914 3913 3915                                                           
CONECT 3915 3914 3916                                                           
CONECT 3916 3915 3917                                                           
CONECT 3917 3916                                                                
CONECT 3918 3919 3920 3921                                                      
CONECT 3919 3918                                                                
CONECT 3920 3918                                                                
CONECT 3921 3918 3922                                                           
CONECT 3922 3921 3923                                                           
CONECT 3923 3922 3924                                                           
CONECT 3924 3923 3925                                                           
CONECT 3925 3924 3926                                                           
CONECT 3926 3925 3927                                                           
CONECT 3927 3926 3928                                                           
CONECT 3928 3927 3929                                                           
CONECT 3929 3928 3930                                                           
CONECT 3930 3929 3931                                                           
CONECT 3931 3930 3932                                                           
CONECT 3932 3931 3933                                                           
CONECT 3933 3932 3934                                                           
CONECT 3934 3933 3935                                                           
CONECT 3935 3934 3936                                                           
CONECT 3936 3935 3937                                                           
CONECT 3937 3936                                                                
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                                                                
CONECT 3948 3949                                                                
CONECT 3949 3948 3950                                                           
CONECT 3950 3949 3951                                                           
CONECT 3951 3950 3952                                                           
CONECT 3952 3951 3953                                                           
CONECT 3953 3952 3954                                                           
CONECT 3954 3953 3955                                                           
CONECT 3955 3954                                                                
CONECT 3956 3957                                                                
CONECT 3957 3956 3958                                                           
CONECT 3958 3957 3959                                                           
CONECT 3959 3958 3960                                                           
CONECT 3960 3959 3961                                                           
CONECT 3961 3960 3962                                                           
CONECT 3962 3961 3963                                                           
CONECT 3963 3962 3964                                                           
CONECT 3964 3963                                                                
CONECT 3965 3966 3967 3968                                                      
CONECT 3966 3965                                                                
CONECT 3967 3965                                                                
CONECT 3968 3965 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                                                                
CONECT 3976 3977 3978 3979                                                      
CONECT 3977 3976                                                                
CONECT 3978 3976                                                                
CONECT 3979 3976 3980                                                           
CONECT 3980 3979 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 3989 3990                                                      
CONECT 3988 3987                                                                
CONECT 3989 3987                                                                
CONECT 3990 3987 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 3998                                                           
CONECT 3998 3997 3999                                                           
CONECT 3999 3998                                                                
CONECT 4000 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 4008                                                           
CONECT 4008 4007 4009                                                           
CONECT 4009 4008 4010                                                           
CONECT 4010 4009 4011                                                           
CONECT 4011 4010 4012                                                           
CONECT 4012 4011                                                                
CONECT 4013 4014                                                                
CONECT 4014 4013 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                                                                
CONECT 4022 4023                                                                
CONECT 4023 4022 4024                                                           
CONECT 4024 4023 4025                                                           
CONECT 4025 4024 4026                                                           
CONECT 4026 4025 4027                                                           
CONECT 4027 4026 4028                                                           
CONECT 4028 4027 4029                                                           
CONECT 4029 4028 4030                                                           
CONECT 4030 4029                                                                
CONECT 4031 4032 4033 4034                                                      
CONECT 4032 4031                                                                
CONECT 4033 4031                                                                
CONECT 4034 4031 4035                                                           
CONECT 4035 4034 4036                                                           
CONECT 4036 4035 4037                                                           
CONECT 4037 4036 4038                                                           
CONECT 4038 4037 4039                                                           
CONECT 4039 4038 4040                                                           
CONECT 4040 4039 4041                                                           
CONECT 4041 4040 4042                                                           
CONECT 4042 4041 4043                                                           
CONECT 4043 4042 4044                                                           
CONECT 4044 4043 4045                                                           
CONECT 4045 4044 4046                                                           
CONECT 4046 4045 4047                                                           
CONECT 4047 4046 4048                                                           
CONECT 4048 4047 4049                                                           
CONECT 4049 4048 4050                                                           
CONECT 4050 4049                                                                
CONECT 4051 4052 4053 4054                                                      
CONECT 4052 4051                                                                
CONECT 4053 4051                                                                
CONECT 4054 4051 4055                                                           
CONECT 4055 4054 4056                                                           
CONECT 4056 4055 4057                                                           
CONECT 4057 4056 4058                                                           
CONECT 4058 4057 4059                                                           
CONECT 4059 4058 4060                                                           
CONECT 4060 4059 4061                                                           
CONECT 4061 4060                                                                
CONECT 4062 4063 4064 4065                                                      
CONECT 4063 4062                                                                
CONECT 4064 4062                                                                
CONECT 4065 4062 4066                                                           
CONECT 4066 4065 4067                                                           
CONECT 4067 4066 4068                                                           
CONECT 4068 4067 4069                                                           
CONECT 4069 4068 4070                                                           
CONECT 4070 4069 4071                                                           
CONECT 4071 4070 4072                                                           
CONECT 4072 4071 4073                                                           
CONECT 4073 4072 4074                                                           
CONECT 4074 4073 4075                                                           
CONECT 4075 4074 4076                                                           
CONECT 4076 4075 4077                                                           
CONECT 4077 4076                                                                
CONECT 4078 4079 4080 4081                                                      
CONECT 4079 4078                                                                
CONECT 4080 4078                                                                
CONECT 4081 4078 4082                                                           
CONECT 4082 4081 4083                                                           
CONECT 4083 4082 4084                                                           
CONECT 4084 4083 4085                                                           
CONECT 4085 4084 4086                                                           
CONECT 4086 4085 4087                                                           
CONECT 4087 4086 4088                                                           
CONECT 4088 4087                                                                
CONECT 4089 4090 4091 4092                                                      
CONECT 4090 4089                                                                
CONECT 4091 4089                                                                
CONECT 4092 4089 4093                                                           
CONECT 4093 4092 4094                                                           
CONECT 4094 4093 4095                                                           
CONECT 4095 4094 4096                                                           
CONECT 4096 4095 4097                                                           
CONECT 4097 4096 4098                                                           
CONECT 4098 4097                                                                
CONECT 4099 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 4119 4121                                                           
CONECT 4115 4116                                                                
CONECT 4116 4115 4118                                                           
CONECT 4117 4119 4123                                                           
CONECT 4118 4116 4120 4123                                                      
CONECT 4119 4114 4117 4122                                                      
CONECT 4120 4118                                                                
CONECT 4121 4114                                                                
CONECT 4122 4119                                                                
CONECT 4123 4117 4118                                                           
CONECT 4124 4127                                                                
CONECT 4125 4126 4128                                                           
CONECT 4126 4125 4129                                                           
CONECT 4127 4124 4131                                                           
CONECT 4128 4125 4132                                                           
CONECT 4129 4126 4133                                                           
CONECT 4130 4144 4146                                                           
CONECT 4131 4127 4134                                                           
CONECT 4132 4128 4135                                                           
CONECT 4133 4129 4136                                                           
CONECT 4134 4131 4137                                                           
CONECT 4135 4132 4137                                                           
CONECT 4136 4133 4138                                                           
CONECT 4137 4134 4135                                                           
CONECT 4138 4136 4139                                                           
CONECT 4139 4138 4140                                                           
CONECT 4140 4139 4141                                                           
CONECT 4141 4140 4143                                                           
CONECT 4142 4144 4148                                                           
CONECT 4143 4141 4145 4148                                                      
CONECT 4144 4130 4142 4147                                                      
CONECT 4145 4143                                                                
CONECT 4146 4130                                                                
CONECT 4147 4144                                                                
CONECT 4148 4142 4143                                                           
MASTER      456    0   24   20    8    0   35    6 4221    1  341   40          
END