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***  SIGNALING PROTEIN/ANTAGONIST 15-JUN-15 5C1M  ***

elNémo ID: 200210053412127408

Job options:

ID        	=	 200210053412127408
JOBID     	=	 SIGNALING PROTEIN/ANTAGONIST 15-JUN-15 5C1M
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 1
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    SIGNALING PROTEIN/ANTAGONIST            15-JUN-15   5C1M              
TITLE     CRYSTAL STRUCTURE OF ACTIVE MU-OPIOID RECEPTOR BOUND TO THE AGONIST   
TITLE    2 BU72                                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MU-TYPE OPIOID RECEPTOR;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MOR-1;                                                      
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: NANOBODY 39;                                               
COMPND   8 CHAIN: B;                                                            
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: OPRM1, MOR, OPRM;                                              
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: LAMA GLAMA;                                     
SOURCE  10 ORGANISM_TAXID: 9844;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    LIGANDS, MICE, AGONISTS, MORPHINANS, ACTIVATION, RECEPTORS, OPIOID,   
KEYWDS   2 MU, NANOBODY, SIGNALING PROTEIN-ANTAGONIST COMPLEX                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.J.HUANG,A.MANGLIK,A.J.VENKATAKRISHNAN,T.LAEREMANS,E.N.FEINBERG,     
AUTHOR   2 A.L.SANBORN,H.E.KATO,K.E.LIVINGSTON,T.S.THORSEN,R.KLING,S.GRANIER,   
AUTHOR   3 P.GMEINER,S.M.HUSBANDS,J.R.TRAYNOR,W.I.WEIS,J.STEYAERT,R.O.DROR,     
AUTHOR   4 B.K.KOBILKA                                                          
REVDAT   6   11-DEC-19 5C1M    1       REMARK                                   
REVDAT   5   06-SEP-17 5C1M    1       JRNL   REMARK                            
REVDAT   4   02-SEP-15 5C1M    1       JRNL                                     
REVDAT   3   26-AUG-15 5C1M    1       REMARK                                   
REVDAT   2   19-AUG-15 5C1M    1       JRNL                                     
REVDAT   1   05-AUG-15 5C1M    0                                                
JRNL        AUTH   W.HUANG,A.MANGLIK,A.J.VENKATAKRISHNAN,T.LAEREMANS,           
JRNL        AUTH 2 E.N.FEINBERG,A.L.SANBORN,H.E.KATO,K.E.LIVINGSTON,            
JRNL        AUTH 3 T.S.THORSEN,R.C.KLING,S.GRANIER,P.GMEINER,S.M.HUSBANDS,      
JRNL        AUTH 4 J.R.TRAYNOR,W.I.WEIS,J.STEYAERT,R.O.DROR,B.K.KOBILKA         
JRNL        TITL   STRUCTURAL INSIGHTS INTO MU-OPIOID RECEPTOR ACTIVATION.      
JRNL        REF    NATURE                        V. 524   315 2015              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   26245379                                                     
JRNL        DOI    10.1038/NATURE14886                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.46                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 39948                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1998                            
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 42.4638 -  5.0587    0.99     2882   152  0.1842 0.2098        
REMARK   3     2  5.0587 -  4.0162    0.99     2731   144  0.1694 0.2056        
REMARK   3     3  4.0162 -  3.5088    1.00     2759   145  0.1815 0.1963        
REMARK   3     4  3.5088 -  3.1881    1.00     2700   143  0.1892 0.2338        
REMARK   3     5  3.1881 -  2.9597    1.00     2706   142  0.1887 0.2527        
REMARK   3     6  2.9597 -  2.7852    1.00     2719   143  0.1791 0.2279        
REMARK   3     7  2.7852 -  2.6458    1.00     2686   142  0.1702 0.2116        
REMARK   3     8  2.6458 -  2.5306    1.00     2706   142  0.1808 0.2172        
REMARK   3     9  2.5306 -  2.4332    1.00     2687   141  0.1863 0.2492        
REMARK   3    10  2.4332 -  2.3492    1.00     2654   140  0.2036 0.2630        
REMARK   3    11  2.3492 -  2.2758    1.00     2709   143  0.2051 0.2420        
REMARK   3    12  2.2758 -  2.2107    1.00     2650   139  0.2219 0.2872        
REMARK   3    13  2.2107 -  2.1525    1.00     2676   141  0.2459 0.2583        
REMARK   3    14  2.1525 -  2.1000    1.00     2685   141  0.2583 0.2871        
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)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.760           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 43.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.62                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           3515                                  
REMARK   3   ANGLE     :  1.193           4790                                  
REMARK   3   CHIRALITY :  0.089            560                                  
REMARK   3   PLANARITY :  0.005            572                                  
REMARK   3   DIHEDRAL  : 14.848           1335                                  
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):  -2.4100  13.6674 -38.6891              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2443 T22:   0.2096                                     
REMARK   3      T33:   0.3193 T12:   0.0044                                     
REMARK   3      T13:  -0.0101 T23:  -0.0334                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1470 L22:   0.9213                                     
REMARK   3      L33:   3.1499 L12:   0.1458                                     
REMARK   3      L13:  -0.0856 L23:  -0.0317                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0820 S12:  -0.1589 S13:   0.0916                       
REMARK   3      S21:  -0.0369 S22:  -0.0081 S23:   0.0099                       
REMARK   3      S31:  -0.3262 S32:  -0.0490 S33:   0.0703                       
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 5C1M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000210873.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-NOV-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
REMARK 200  PH                             : 7.0-7.5                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0332                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63134                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.455                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.14200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 7.5100                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.84                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 14.45100                           
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 0.270                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: CUBIC                                                        
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: RECONSTITUTED IN 10:1                    
REMARK 280  MONOOLEIN:CHOLESTEROL MIX. PRECIPITANT SOLUTION:15-25% PEG300,      
REMARK 280  100 MM HEPES PH 7.0-7.5, 1% 1,2,3-HEPTANETRIOL, 0.5-1.0%            
REMARK 280  POLYPROPYLENE GLYCOL P 400, 100-300 MM (NH4)2HPO4, PH 7.5,          
REMARK 280  LIPIDIC CUBIC PHASE, TEMPERATURE 293K                               
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 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       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X,-Y+1/2,Z                                             
REMARK 290       7555   -X+1/2,Y,-Z                                             
REMARK 290       8555   X,-Y,-Z+1/2                                             
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       22.21500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      104.95000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      104.95000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.21500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       72.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       22.21500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       72.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      104.95000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       72.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       22.21500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      104.95000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2430 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19530 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     GLY B   103                                                      
REMARK 465     GLN B   104                                                      
REMARK 465     SER B   105                                                      
REMARK 465     SER B   106                                                      
REMARK 465     SER B   107                                                      
REMARK 465     PRO B   108                                                      
REMARK 465     TYR B   109                                                      
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     LYS A 269    CG   CD   CE   NZ                                   
REMARK 470     GLU A 270    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 273    CG   CD   NE   CZ   NH1  NH2                        
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   OD1  ASP A   164     O    HOH A   501              2.14            
REMARK 500   N    GLN B     3     O    HOH B   201              2.17            
REMARK 500   NH1  ARG B    99     O    ASP B   110              2.19            
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    HIS A  54      -94.65   -138.90                                   
REMARK 500    THR A 132      147.65   -170.59                                   
REMARK 500    ARG A 179       46.16    -95.48                                   
REMARK 500    PHE A 241      -61.42   -129.52                                   
REMARK 500    SER A 266      -76.71    -96.63                                   
REMARK 500    SER A 268      -27.95   -146.12                                   
REMARK 500    ARG B  29       18.68     55.32                                   
REMARK 500    MET B  34       -9.87   -141.91                                   
REMARK 500    ALA B 125       24.91    -78.75                                   
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     OLC A  402                                                       
REMARK 610     OLC A  403                                                       
REMARK 610     P6G A  407                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 4VO A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue P6G A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue P6G A 407                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4DKL   RELATED DB: PDB                                   
REMARK 900 4DKL CONTAINS THE SAME PROTEIN BOUND TO A MORPHINAN ANTAGONIST       
DBREF  5C1M A   52   347  UNP    P42866   OPRM_MOUSE      52    347             
DBREF  5C1M B    3   127  PDB    5C1M     5C1M             3    127             
SEQRES   1 A  296  GLY SER HIS SER LEU YCM PRO GLN THR GLY SER PRO SER          
SEQRES   2 A  296  MET VAL THR ALA ILE THR ILE MET ALA LEU TYR SER ILE          
SEQRES   3 A  296  VAL CYS VAL VAL GLY LEU PHE GLY ASN PHE LEU VAL MET          
SEQRES   4 A  296  TYR VAL ILE VAL ARG TYR THR LYS MET LYS THR ALA THR          
SEQRES   5 A  296  ASN ILE TYR ILE PHE ASN LEU ALA LEU ALA ASP ALA LEU          
SEQRES   6 A  296  ALA THR SER THR LEU PRO PHE GLN SER VAL ASN TYR LEU          
SEQRES   7 A  296  MET GLY THR TRP PRO PHE GLY ASN ILE LEU CYS LYS ILE          
SEQRES   8 A  296  VAL ILE SER ILE ASP TYR TYR ASN MET PHE THR SER ILE          
SEQRES   9 A  296  PHE THR LEU CYS THR MET SER VAL ASP ARG TYR ILE ALA          
SEQRES  10 A  296  VAL CYS HIS PRO VAL LYS ALA LEU ASP PHE ARG THR PRO          
SEQRES  11 A  296  ARG ASN ALA LYS ILE VAL ASN VAL CYS ASN TRP ILE LEU          
SEQRES  12 A  296  SER SER ALA ILE GLY LEU PRO VAL MET PHE MET ALA THR          
SEQRES  13 A  296  THR LYS TYR ARG GLN GLY SER ILE ASP CYS THR LEU THR          
SEQRES  14 A  296  PHE SER HIS PRO THR TRP TYR TRP GLU ASN LEU LEU LYS          
SEQRES  15 A  296  ILE CYS VAL PHE ILE PHE ALA PHE ILE MET PRO VAL LEU          
SEQRES  16 A  296  ILE ILE THR VAL CYS TYR GLY LEU MET ILE LEU ARG LEU          
SEQRES  17 A  296  LYS SER VAL ARG MET LEU SER GLY SER LYS GLU LYS ASP          
SEQRES  18 A  296  ARG ASN LEU ARG ARG ILE THR ARG MET VAL LEU VAL VAL          
SEQRES  19 A  296  VAL ALA VAL PHE ILE VAL CYS TRP THR PRO ILE HIS ILE          
SEQRES  20 A  296  TYR VAL ILE ILE LYS ALA LEU ILE THR ILE PRO GLU THR          
SEQRES  21 A  296  THR PHE GLN THR VAL SER TRP HIS PHE CYS ILE ALA LEU          
SEQRES  22 A  296  GLY TYR THR ASN SER CYS LEU ASN PRO VAL LEU TYR ALA          
SEQRES  23 A  296  PHE LEU ASP GLU ASN PHE LYS ARG CYS PHE                      
SEQRES   1 B  125  GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL ARG          
SEQRES   2 B  125  PRO GLY GLY SER LEU ARG LEU SER CYS VAL ASP SER GLU          
SEQRES   3 B  125  ARG THR SER TYR PRO MET GLY TRP PHE ARG ARG ALA PRO          
SEQRES   4 B  125  GLY LYS GLU ARG GLU PHE VAL ALA SER ILE THR TRP SER          
SEQRES   5 B  125  GLY ILE ASP PRO THR TYR ALA ASP SER VAL ALA ASP ARG          
SEQRES   6 B  125  PHE THR THR SER ARG ASP VAL ALA ASN ASN THR LEU TYR          
SEQRES   7 B  125  LEU GLN MET ASN SER LEU LYS HIS GLU ASP THR ALA VAL          
SEQRES   8 B  125  TYR TYR CYS ALA ALA ARG ALA PRO VAL GLY GLN SER SER          
SEQRES   9 B  125  SER PRO TYR ASP TYR ASP TYR TRP GLY GLN GLY THR GLN          
SEQRES  10 B  125  VAL THR VAL SER SER ALA ALA ALA                              
MODRES 5C1M YCM A   57  CYS  MODIFIED RESIDUE                                   
HET    YCM  A  57      10                                                       
HET    4VO  A 401      32                                                       
HET    OLC  A 402      16                                                       
HET    OLC  A 403      18                                                       
HET    CLR  A 404      28                                                       
HET    PO4  A 405       5                                                       
HET    P6G  A 406      19                                                       
HET    P6G  A 407      13                                                       
HETNAM     YCM S-(2-AMINO-2-OXOETHYL)-L-CYSTEINE                                
HETNAM     4VO (2S,3S,3AR,5AR,6R,11BR,11CS)-3A-METHOXY-3,14-DIMETHYL-           
HETNAM   2 4VO  2-PHENYL-2,3,3A,6,7,11C-HEXAHYDRO-1H-6,11B-                     
HETNAM   3 4VO  (EPIMINOETHANO)-3,5A-METHANONAPHTHO[2,1-G]INDOL-10-OL           
HETNAM     OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE                   
HETNAM     CLR CHOLESTEROL                                                      
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETSYN     YCM CYSTEINE-S-ACETAMIDE                                             
HETSYN     4VO BU72                                                             
HETSYN     OLC 1-OLEOYL-R-GLYCEROL                                              
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
FORMUL   1  YCM    C5 H10 N2 O3 S                                               
FORMUL   3  4VO    C28 H32 N2 O2                                                
FORMUL   4  OLC    2(C21 H40 O4)                                                
FORMUL   6  CLR    C27 H46 O                                                    
FORMUL   7  PO4    O4 P 3-                                                      
FORMUL   8  P6G    2(C12 H26 O7)                                                
FORMUL  10  HOH   *94(H2 O)                                                     
HELIX    1 AA1 SER A   64  TYR A   96  1                                  33    
HELIX    2 AA2 THR A  101  SER A  119  1                                  19    
HELIX    3 AA3 THR A  120  GLY A  131  1                                  12    
HELIX    4 AA4 PHE A  135  HIS A  171  1                                  37    
HELIX    5 AA5 HIS A  171  ARG A  179  1                                   9    
HELIX    6 AA6 THR A  180  MET A  205  1                                  26    
HELIX    7 AA7 PRO A  224  PHE A  241  1                                  18    
HELIX    8 AA8 PHE A  241  VAL A  262  1                                  22    
HELIX    9 AA9 SER A  268  ILE A  306  1                                  39    
HELIX   10 AB1 THR A  311  ALA A  337  1                                  27    
HELIX   11 AB2 ASP A  340  ARG A  345  1                                   6    
HELIX   12 AB3 LYS B   87  THR B   91  5                                   5    
SHEET    1 AA1 2 ALA A 206  ARG A 211  0                                        
SHEET    2 AA1 2 SER A 214  LEU A 219 -1  O  SER A 214   N  ARG A 211           
SHEET    1 AA2 4 VAL B   7  SER B   9  0                                        
SHEET    2 AA2 4 LEU B  20  VAL B  25 -1  O  SER B  23   N  SER B   9           
SHEET    3 AA2 4 THR B  78  MET B  83 -1  O  MET B  83   N  LEU B  20           
SHEET    4 AA2 4 PHE B  68  ASP B  73 -1  N  THR B  69   O  GLN B  82           
SHEET    1 AA3 6 GLY B  12  VAL B  14  0                                        
SHEET    2 AA3 6 THR B 118  VAL B 122  1  O  THR B 121   N  GLY B  12           
SHEET    3 AA3 6 ALA B  92  ARG B  99 -1  N  TYR B  94   O  THR B 118           
SHEET    4 AA3 6 TYR B  32  ARG B  39 -1  N  TYR B  32   O  ARG B  99           
SHEET    5 AA3 6 GLU B  46  ILE B  51 -1  O  GLU B  46   N  ARG B  38           
SHEET    6 AA3 6 PRO B  58  TYR B  60 -1  O  THR B  59   N  SER B  50           
SHEET    1 AA4 4 GLY B  12  VAL B  14  0                                        
SHEET    2 AA4 4 THR B 118  VAL B 122  1  O  THR B 121   N  GLY B  12           
SHEET    3 AA4 4 ALA B  92  ARG B  99 -1  N  TYR B  94   O  THR B 118           
SHEET    4 AA4 4 TYR B 113  TRP B 114 -1  O  TYR B 113   N  ALA B  98           
SSBOND   1 CYS A  140    CYS A  217                          1555   1555  2.05  
SSBOND   2 CYS B   24    CYS B   96                          1555   1555  2.05  
LINK         C   LEU A  56                 N   YCM A  57     1555   1555  1.33  
LINK         C   YCM A  57                 N   PRO A  58     1555   1555  1.34  
CISPEP   1 THR A   60    GLY A   61          0         1.07                     
CISPEP   2 HIS A  223    PRO A  224          0        -9.29                     
CISPEP   3 GLY A  267    SER A  268          0        -3.44                     
CISPEP   4 CYS A  346    PHE A  347          0         9.00                     
SITE     1 AC1  9 HIS A  54  SER A  55  GLN A 124  ASP A 147                    
SITE     2 AC1  9 VAL A 236  VAL A 300  TYR A 326  HOH A 526                    
SITE     3 AC1  9 HOH A 553                                                     
SITE     1 AC2  2 OLC A 403  CLR A 404                                          
SITE     1 AC3  3 LEU A 254  ILE A 306  OLC A 402                               
SITE     1 AC4  5 PRO A 295  TYR A 299  ILE A 302  SER A 317                    
SITE     2 AC4  5 OLC A 402                                                     
SITE     1 AC5  3 HIS A 223  PRO A 224  THR A 225                               
SITE     1 AC6  5 THR A 160  PHE A 178  ASN A 191  TRP A 226                    
SITE     2 AC6  5 MET A 243                                                     
SITE     1 AC7  1 PHE A  84                                                     
CRYST1   44.430  144.000  209.900  90.00  90.00  90.00 I 21 21 21    8          
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      0.022507  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006944  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004764        0.00000                         
ATOM      1  N   GLY A  52       5.542  11.620 -72.078  1.00 90.61           N  
ANISOU    1  N   GLY A  52    12764  11414  10250  -1188    732     47       N  
ATOM      2  CA  GLY A  52       4.534  11.789 -71.046  1.00 88.30           C  
ANISOU    2  CA  GLY A  52    12451  11007  10090  -1118    603     51       C  
ATOM      3  C   GLY A  52       4.419  13.218 -70.548  1.00 92.48           C  
ANISOU    3  C   GLY A  52    13023  11460  10657  -1163    518    164       C  
ATOM      4  O   GLY A  52       5.412  13.835 -70.155  1.00 86.64           O  
ANISOU    4  O   GLY A  52    12244  10734   9941  -1233    578    214       O  
ATOM      5  N   SER A  53       3.201  13.747 -70.566  1.00102.12           N  
ANISOU    5  N   SER A  53    14325  12602  11875  -1123    378    202       N  
ATOM      6  CA  SER A  53       2.941  15.079 -70.038  1.00108.64           C  
ANISOU    6  CA  SER A  53    15214  13324  12739  -1134    287    301       C  
ATOM      7  C   SER A  53       2.877  15.035 -68.515  1.00105.08           C  
ANISOU    7  C   SER A  53    14654  12810  12462  -1068    264    269       C  
ATOM      8  O   SER A  53       2.524  14.009 -67.934  1.00112.07           O  
ANISOU    8  O   SER A  53    15436  13714  13432   -990    270    182       O  
ATOM      9  CB  SER A  53       1.637  15.642 -70.611  1.00112.72           C  
ANISOU    9  CB  SER A  53    15851  13794  13183  -1081    145    354       C  
ATOM     10  OG  SER A  53       1.365  16.936 -70.101  1.00116.32           O  
ANISOU   10  OG  SER A  53    16392  14133  13672  -1066     59    447       O  
ATOM     11  N   HIS A  54       3.227  16.146 -67.874  1.00 96.07           N  
ANISOU   11  N   HIS A  54    13549  11589  11364  -1109    240    340       N  
ATOM     12  CA  HIS A  54       3.147  16.249 -66.418  1.00 78.47           C  
ANISOU   12  CA  HIS A  54    11233   9297   9285  -1053    210    314       C  
ATOM     13  C   HIS A  54       2.606  17.615 -66.001  1.00 73.27           C  
ANISOU   13  C   HIS A  54    10697   8502   8640  -1040    104    393       C  
ATOM     14  O   HIS A  54       1.395  17.816 -65.941  1.00 74.99           O  
ANISOU   14  O   HIS A  54    10960   8666   8866   -930     -5    398       O  
ATOM     15  CB  HIS A  54       4.519  16.003 -65.780  1.00 62.71           C  
ANISOU   15  CB  HIS A  54     9119   7363   7345  -1126    325    292       C  
ATOM     16  CG  HIS A  54       4.451  15.579 -64.343  1.00 56.06           C  
ANISOU   16  CG  HIS A  54     8149   6500   6649  -1049    313    235       C  
ATOM     17  ND1 HIS A  54       3.971  14.349 -63.955  1.00 48.70           N  
ANISOU   17  ND1 HIS A  54     7117   5601   5784   -944    320    152       N  
ATOM     18  CD2 HIS A  54       4.787  16.224 -63.201  1.00 44.74           C  
ANISOU   18  CD2 HIS A  54     6684   5015   5300  -1070    293    252       C  
ATOM     19  CE1 HIS A  54       4.022  14.245 -62.641  1.00 45.56           C  
ANISOU   19  CE1 HIS A  54     6629   5179   5505   -898    307    126       C  
ATOM     20  NE2 HIS A  54       4.531  15.365 -62.160  1.00 52.20           N  
ANISOU   20  NE2 HIS A  54     7503   5976   6357   -971    291    182       N  
ATOM     21  N   SER A  55       3.509  18.548 -65.716  1.00 73.51           N  
ANISOU   21  N   SER A  55    10781   8482   8666  -1151    137    450       N  
ATOM     22  CA  SER A  55       3.120  19.890 -65.294  1.00 82.21           C  
ANISOU   22  CA  SER A  55    12032   9427   9776  -1148     47    521       C  
ATOM     23  C   SER A  55       2.621  20.694 -66.488  1.00 88.04           C  
ANISOU   23  C   SER A  55    12970  10102  10377  -1158    -13    616       C  
ATOM     24  O   SER A  55       1.633  21.429 -66.394  1.00 85.37           O  
ANISOU   24  O   SER A  55    12753   9649  10035  -1052   -125    658       O  
ATOM     25  CB  SER A  55       4.295  20.611 -64.624  1.00 83.00           C  
ANISOU   25  CB  SER A  55    12141   9491   9903  -1294    104    548       C  
ATOM     26  OG  SER A  55       5.314  20.930 -65.560  1.00 86.53           O  
ANISOU   26  OG  SER A  55    12646   9995  10236  -1468    188    608       O  
ATOM     27  N   LEU A  56       3.318  20.544 -67.609  1.00 87.05           N  
ANISOU   27  N   LEU A  56    12879  10063  10134  -1278     64    650       N  
ATOM     28  CA  LEU A  56       2.947  21.223 -68.840  1.00 85.76           C  
ANISOU   28  CA  LEU A  56    12906   9859   9820  -1302     17    747       C  
ATOM     29  C   LEU A  56       1.650  20.647 -69.393  1.00 85.52           C  
ANISOU   29  C   LEU A  56    12866   9872   9755  -1146    -74    721       C  
ATOM     30  O   LEU A  56       1.601  19.501 -69.849  1.00 83.48           O  
ANISOU   30  O   LEU A  56    12493   9749   9477  -1132    -28    647       O  
ATOM     31  CB  LEU A  56       4.061  21.113 -69.882  1.00 79.06           C  
ANISOU   31  CB  LEU A  56    12077   9118   8844  -1477    136    783       C  
ATOM     32  CG  LEU A  56       3.808  21.847 -71.201  1.00 78.63           C  
ANISOU   32  CG  LEU A  56    12233   9028   8614  -1528     98    896       C  
ATOM     33  CD1 LEU A  56       3.815  23.355 -70.994  1.00 73.30           C  
ANISOU   33  CD1 LEU A  56    11779   8159   7913  -1585     36   1013       C  
ATOM     34  CD2 LEU A  56       4.829  21.442 -72.250  1.00 74.98           C  
ANISOU   34  CD2 LEU A  56    11748   8719   8022  -1683    230    906       C  
HETATM   35  N   YCM A  57       0.600  21.456 -69.336  1.00 83.99           N  
ANISOU   35  N   YCM A  57    12797   9566   9550  -1027   -203    780       N  
HETATM   36  CA  YCM A  57      -0.686  21.082 -69.851  1.00 84.37           C  
ANISOU   36  CA  YCM A  57    12835   9670   9552   -881   -306    769       C  
HETATM   37  CB  YCM A  57      -1.796  21.729 -69.036  1.00 84.66           C  
ANISOU   37  CB  YCM A  57    12902   9603   9662   -704   -432    784       C  
HETATM   38  SG  YCM A  57      -2.761  20.697 -67.977  1.00159.53           S  
ANISOU   38  SG  YCM A  57    22155  19173  19287   -558   -473    658       S  
HETATM   39  CD  YCM A  57      -1.733  19.310 -67.630  1.00 88.88           C  
ANISOU   39  CD  YCM A  57    13018  10335  10416   -683   -326    545       C  
HETATM   40  CE  YCM A  57      -2.391  18.023 -68.061  1.00 93.82           C  
ANISOU   40  CE  YCM A  57    13520  11104  11023   -649   -333    462       C  
HETATM   41  OZ1 YCM A  57      -1.726  16.968 -68.178  1.00 96.99           O  
ANISOU   41  OZ1 YCM A  57    13829  11585  11438   -727   -231    389       O  
HETATM   42  NZ2 YCM A  57      -3.737  18.054 -68.325  1.00 92.49           N  
ANISOU   42  NZ2 YCM A  57    13347  10979  10814   -529   -456    469       N  
HETATM   43  C   YCM A  57      -0.859  21.484 -71.311  1.00 97.54           C  
ANISOU   43  C   YCM A  57    14664  11362  11035   -916   -339    863       C  
HETATM   44  O   YCM A  57      -0.646  22.637 -71.703  1.00 88.34           O  
ANISOU   44  O   YCM A  57    13699  10079   9786   -958   -366    981       O  
ATOM     45  N   PRO A  58      -1.239  20.508 -72.149  1.00115.92           N  
ANISOU   45  N   PRO A  58    16916  13841  13285   -906   -338    812       N  
ATOM     46  CA  PRO A  58      -1.590  20.766 -73.551  1.00132.06           C  
ANISOU   46  CA  PRO A  58    19098  15938  15142   -920   -387    891       C  
ATOM     47  C   PRO A  58      -2.829  21.652 -73.605  1.00144.89           C  
ANISOU   47  C   PRO A  58    20834  17488  16730   -752   -553    977       C  
ATOM     48  O   PRO A  58      -3.916  21.184 -73.267  1.00150.55           O  
ANISOU   48  O   PRO A  58    21433  18272  17495   -611   -643    919       O  
ATOM     49  CB  PRO A  58      -1.871  19.367 -74.112  1.00129.31           C  
ANISOU   49  CB  PRO A  58    18611  15767  14754   -927   -359    780       C  
ATOM     50  CG  PRO A  58      -1.229  18.414 -73.137  1.00122.33           C  
ANISOU   50  CG  PRO A  58    17548  14909  14025   -961   -249    658       C  
ATOM     51  CD  PRO A  58      -1.344  19.080 -71.807  1.00119.95           C  
ANISOU   51  CD  PRO A  58    17223  14478  13876   -890   -288    673       C  
ATOM     52  N   GLN A  59      -2.675  22.908 -74.015  1.00148.23           N  
ANISOU   52  N   GLN A  59    21480  17778  17062   -764   -591   1116       N  
ATOM     53  CA  GLN A  59      -3.706  23.900 -73.722  1.00148.03           C  
ANISOU   53  CA  GLN A  59    21570  17634  17039   -575   -736   1197       C  
ATOM     54  C   GLN A  59      -4.362  24.609 -74.901  1.00142.47           C  
ANISOU   54  C   GLN A  59    21058  16926  16149   -499   -847   1330       C  
ATOM     55  O   GLN A  59      -5.405  25.239 -74.722  1.00143.92           O  
ANISOU   55  O   GLN A  59    21301  17056  16326   -297   -981   1385       O  
ATOM     56  CB  GLN A  59      -3.129  24.964 -72.783  1.00152.54           C  
ANISOU   56  CB  GLN A  59    22271  17986  17702   -598   -710   1245       C  
ATOM     57  CG  GLN A  59      -3.096  24.533 -71.329  1.00153.85           C  
ANISOU   57  CG  GLN A  59    22255  18136  18065   -556   -678   1126       C  
ATOM     58  CD  GLN A  59      -4.451  24.067 -70.844  1.00155.09           C  
ANISOU   58  CD  GLN A  59    22260  18379  18286   -340   -785   1060       C  
ATOM     59  OE1 GLN A  59      -5.485  24.518 -71.336  1.00160.22           O  
ANISOU   59  OE1 GLN A  59    22985  19038  18852   -180   -909   1127       O  
ATOM     60  NE2 GLN A  59      -4.457  23.152 -69.881  1.00150.78           N  
ANISOU   60  NE2 GLN A  59    21497  17909  17883   -335   -739    934       N  
ATOM     61  N   THR A  60      -3.763  24.523 -76.085  1.00136.48           N  
ANISOU   61  N   THR A  60    20393  16231  15231   -647   -791   1385       N  
ATOM     62  CA  THR A  60      -4.285  25.226 -77.256  1.00137.72           C  
ANISOU   62  CA  THR A  60    20753  16384  15192   -591   -892   1526       C  
ATOM     63  C   THR A  60      -5.784  24.970 -77.452  1.00133.36           C  
ANISOU   63  C   THR A  60    20112  15956  14604   -367  -1055   1515       C  
ATOM     64  O   THR A  60      -6.247  23.840 -77.294  1.00131.26           O  
ANISOU   64  O   THR A  60    19618  15866  14390   -348  -1058   1385       O  
ATOM     65  CB  THR A  60      -3.521  24.822 -78.533  1.00144.86           C  
ANISOU   65  CB  THR A  60    21710  17407  15924   -786   -801   1551       C  
ATOM     66  OG1 THR A  60      -3.420  23.395 -78.600  1.00147.32           O  
ANISOU   66  OG1 THR A  60    21789  17917  16271   -846   -729   1395       O  
ATOM     67  CG2 THR A  60      -2.121  25.419 -78.526  1.00144.97           C  
ANISOU   67  CG2 THR A  60    21860  17299  15925  -1000   -662   1612       C  
ATOM     68  N   GLY A  61      -6.544  26.020 -77.765  1.00132.47           N  
ANISOU   68  N   GLY A  61    20179  15753  14399   -197  -1190   1651       N  
ATOM     69  CA  GLY A  61      -6.010  27.361 -77.945  1.00130.79           C  
ANISOU   69  CA  GLY A  61    20270  15304  14121   -225  -1186   1808       C  
ATOM     70  C   GLY A  61      -5.921  28.174 -76.665  1.00128.94           C  
ANISOU   70  C   GLY A  61    20106  14838  14047   -143  -1185   1810       C  
ATOM     71  O   GLY A  61      -6.441  27.766 -75.627  1.00127.48           O  
ANISOU   71  O   GLY A  61    19730  14687  14019    -21  -1207   1699       O  
ATOM     72  N   SER A  62      -5.263  29.330 -76.756  1.00127.83           N  
ANISOU   72  N   SER A  62    20253  14463  13855   -220  -1158   1936       N  
ATOM     73  CA  SER A  62      -4.988  30.207 -75.614  1.00122.46           C  
ANISOU   73  CA  SER A  62    19696  13530  13304   -190  -1142   1942       C  
ATOM     74  C   SER A  62      -6.217  30.508 -74.754  1.00121.23           C  
ANISOU   74  C   SER A  62    19491  13327  13245    122  -1269   1912       C  
ATOM     75  O   SER A  62      -7.325  30.639 -75.276  1.00124.81           O  
ANISOU   75  O   SER A  62    19934  13868  13618    346  -1397   1960       O  
ATOM     76  CB  SER A  62      -4.375  31.517 -76.115  1.00123.53           C  
ANISOU   76  CB  SER A  62    20058  13485  13393   -285  -1096   2032       C  
ATOM     77  OG  SER A  62      -5.080  32.007 -77.241  1.00128.82           O  
ANISOU   77  OG  SER A  62    20836  14192  13918   -155  -1189   2138       O  
ATOM     78  N   PRO A  63      -6.018  30.629 -73.427  1.00114.92           N  
ANISOU   78  N   PRO A  63    18631  12414  12621    139  -1227   1821       N  
ATOM     79  CA  PRO A  63      -7.136  30.747 -72.481  1.00106.76           C  
ANISOU   79  CA  PRO A  63    17498  11372  11692    426  -1324   1763       C  
ATOM     80  C   PRO A  63      -7.921  32.050 -72.611  1.00 97.95           C  
ANISOU   80  C   PRO A  63    16558  10117  10544    665  -1415   1841       C  
ATOM     81  O   PRO A  63      -7.445  33.020 -73.202  1.00102.14           O  
ANISOU   81  O   PRO A  63    17293  10505  11010    582  -1382   1920       O  
ATOM     82  CB  PRO A  63      -6.445  30.673 -71.113  1.00103.87           C  
ANISOU   82  CB  PRO A  63    17055  10904  11508    324  -1225   1648       C  
ATOM     83  CG  PRO A  63      -5.074  31.190 -71.363  1.00107.32           C  
ANISOU   83  CG  PRO A  63    17690  11183  11906     39  -1114   1706       C  
ATOM     84  CD  PRO A  63      -4.713  30.704 -72.741  1.00111.24           C  
ANISOU   84  CD  PRO A  63    18188  11830  12250   -113  -1086   1771       C  
ATOM     85  N   SER A  64      -9.128  32.057 -72.056  1.00 85.52           N  
ANISOU   85  N   SER A  64    14868   8607   9019    957  -1518   1804       N  
ATOM     86  CA  SER A  64      -9.914  33.275 -71.975  1.00 84.29           C  
ANISOU   86  CA  SER A  64    14828   8335   8862   1205  -1583   1845       C  
ATOM     87  C   SER A  64      -9.516  34.082 -70.744  1.00 90.88           C  
ANISOU   87  C   SER A  64    15759   8939   9833   1204  -1515   1774       C  
ATOM     88  O   SER A  64      -8.770  33.602 -69.877  1.00 91.63           O  
ANISOU   88  O   SER A  64    15787   8996  10032   1040  -1432   1687       O  
ATOM     89  CB  SER A  64     -11.408  32.953 -71.927  1.00 79.60           C  
ANISOU   89  CB  SER A  64    14039   7949   8255   1523  -1715   1829       C  
ATOM     90  OG  SER A  64     -11.720  32.181 -70.783  1.00 76.75           O  
ANISOU   90  OG  SER A  64    13464   7679   8018   1590  -1715   1710       O  
ATOM     91  N   MET A  65     -10.028  35.305 -70.677  1.00 87.54           N  
ANISOU   91  N   MET A  65    15494   8369   9398   1389  -1553   1810       N  
ATOM     92  CA  MET A  65      -9.786  36.191 -69.552  1.00 81.82           C  
ANISOU   92  CA  MET A  65    14885   7428   8776   1414  -1501   1740       C  
ATOM     93  C   MET A  65     -10.252  35.574 -68.242  1.00 83.40           C  
ANISOU   93  C   MET A  65    14867   7710   9109   1538  -1502   1609       C  
ATOM     94  O   MET A  65      -9.440  35.268 -67.372  1.00 86.71           O  
ANISOU   94  O   MET A  65    15252   8068   9626   1358  -1418   1525       O  
ATOM     95  CB  MET A  65     -10.491  37.530 -69.770  1.00 78.88           C  
ANISOU   95  CB  MET A  65    14710   6913   8349   1644  -1559   1801       C  
ATOM     96  CG  MET A  65     -10.429  38.468 -68.566  1.00 80.70           C  
ANISOU   96  CG  MET A  65    15062   6932   8668   1712  -1519   1718       C  
ATOM     97  SD  MET A  65      -8.763  39.076 -68.253  1.00124.60           S  
ANISOU   97  SD  MET A  65    20848  12247  14248   1332  -1393   1698       S  
ATOM     98  CE  MET A  65      -8.474  40.015 -69.750  1.00 68.64           C  
ANISOU   98  CE  MET A  65    14044   5037   6999   1255  -1412   1860       C  
ATOM     99  N   VAL A  66     -11.565  35.392 -68.122  1.00 87.52           N  
ANISOU   99  N   VAL A  66    15230   8391   9631   1840  -1596   1595       N  
ATOM    100  CA  VAL A  66     -12.196  34.925 -66.890  1.00 91.97           C  
ANISOU  100  CA  VAL A  66    15581   9051  10311   2000  -1603   1474       C  
ATOM    101  C   VAL A  66     -11.567  33.642 -66.335  1.00 90.33           C  
ANISOU  101  C   VAL A  66    15190   8944  10187   1805  -1550   1395       C  
ATOM    102  O   VAL A  66     -11.460  33.468 -65.120  1.00 84.27           O  
ANISOU  102  O   VAL A  66    14337   8145   9537   1810  -1504   1288       O  
ATOM    103  CB  VAL A  66     -13.705  34.685 -67.111  1.00 94.19           C  
ANISOU  103  CB  VAL A  66    15661   9572  10553   2319  -1717   1483       C  
ATOM    104  CG1 VAL A  66     -14.417  34.467 -65.783  1.00 91.97           C  
ANISOU  104  CG1 VAL A  66    15182   9375  10385   2504  -1714   1359       C  
ATOM    105  CG2 VAL A  66     -14.319  35.860 -67.859  1.00 99.65           C  
ANISOU  105  CG2 VAL A  66    16531  10185  11146   2509  -1777   1582       C  
ATOM    106  N   THR A  67     -11.140  32.755 -67.228  1.00 92.63           N  
ANISOU  106  N   THR A  67    15430   9354  10411   1631  -1555   1447       N  
ATOM    107  CA  THR A  67     -10.612  31.458 -66.817  1.00 90.29           C  
ANISOU  107  CA  THR A  67    14956   9171  10180   1458  -1511   1378       C  
ATOM    108  C   THR A  67      -9.201  31.565 -66.241  1.00 86.77           C  
ANISOU  108  C   THR A  67    14612   8544   9813   1168  -1380   1336       C  
ATOM    109  O   THR A  67      -8.910  30.978 -65.200  1.00 88.85           O  
ANISOU  109  O   THR A  67    14688   8861  10209   1091  -1308   1212       O  
ATOM    110  CB  THR A  67     -10.612  30.452 -67.994  1.00 84.66           C  
ANISOU  110  CB  THR A  67    14077   8710   9382   1321  -1516   1397       C  
ATOM    111  OG1 THR A  67      -9.989  31.050 -69.138  1.00 95.13           O  
ANISOU  111  OG1 THR A  67    15671   9906  10568   1200  -1517   1533       O  
ATOM    112  CG2 THR A  67     -12.041  30.059 -68.352  1.00 70.99           C  
ANISOU  112  CG2 THR A  67    12148   7232   7594   1573  -1640   1397       C  
ATOM    113  N   ALA A  68      -8.330  32.314 -66.912  1.00 78.56           N  
ANISOU  113  N   ALA A  68    13798   7348   8703    985  -1328   1414       N  
ATOM    114  CA  ALA A  68      -6.952  32.463 -66.455  1.00 72.66           C  
ANISOU  114  CA  ALA A  68    13128   6466   8014    690  -1205   1378       C  
ATOM    115  C   ALA A  68      -6.895  33.175 -65.094  1.00 67.52           C  
ANISOU  115  C   ALA A  68    12510   5667   7477    746  -1172   1282       C  
ATOM    116  O   ALA A  68      -6.162  32.760 -64.194  1.00 65.22           O  
ANISOU  116  O   ALA A  68    12135   5363   7284    589  -1096   1199       O  
ATOM    117  CB  ALA A  68      -6.131  33.209 -67.483  1.00 71.14           C  
ANISOU  117  CB  ALA A  68    13146   6172   7712    493  -1159   1474       C  
ATOM    118  N   ILE A  69      -7.685  34.234 -64.950  1.00 67.36           N  
ANISOU  118  N   ILE A  69    12609   5548   7435    974  -1228   1293       N  
ATOM    119  CA  ILE A  69      -7.787  34.943 -63.681  1.00 71.80           C  
ANISOU  119  CA  ILE A  69    13214   5984   8085   1059  -1205   1200       C  
ATOM    120  C   ILE A  69      -8.257  33.973 -62.613  1.00 74.91           C  
ANISOU  120  C   ILE A  69    13356   6515   8592   1164  -1209   1091       C  
ATOM    121  O   ILE A  69      -7.693  33.921 -61.520  1.00 79.41           O  
ANISOU  121  O   ILE A  69    13888   7031   9254   1059  -1144    998       O  
ATOM    122  CB  ILE A  69      -8.760  36.152 -63.754  1.00 63.54           C  
ANISOU  122  CB  ILE A  69    12323   4834   6986   1335  -1272   1230       C  
ATOM    123  CG1 ILE A  69      -8.243  37.212 -64.716  1.00 69.04           C  
ANISOU  123  CG1 ILE A  69    13299   5361   7573   1224  -1265   1335       C  
ATOM    124  CG2 ILE A  69      -8.942  36.787 -62.382  1.00 60.56           C  
ANISOU  124  CG2 ILE A  69    11975   4347   6689   1437  -1247   1121       C  
ATOM    125  CD1 ILE A  69      -9.140  38.441 -64.788  1.00 72.90           C  
ANISOU  125  CD1 ILE A  69    13967   5724   8006   1492  -1326   1368       C  
ATOM    126  N   THR A  70      -9.275  33.185 -62.947  1.00 66.57           N  
ANISOU  126  N   THR A  70    12120   5654   7522   1362  -1288   1104       N  
ATOM    127  CA  THR A  70      -9.827  32.214 -62.005  1.00 62.25           C  
ANISOU  127  CA  THR A  70    11319   5262   7071   1475  -1302   1006       C  
ATOM    128  C   THR A  70      -8.755  31.239 -61.518  1.00 53.35           C  
ANISOU  128  C   THR A  70    10051   4187   6034   1190  -1203    934       C  
ATOM    129  O   THR A  70      -8.632  30.970 -60.326  1.00 52.06           O  
ANISOU  129  O   THR A  70     9765   4039   5978   1177  -1155    825       O  
ATOM    130  CB  THR A  70     -10.996  31.428 -62.641  1.00 68.99           C  
ANISOU  130  CB  THR A  70    11966   6371   7874   1676  -1401   1034       C  
ATOM    131  OG1 THR A  70     -12.032  32.344 -63.023  1.00 76.01           O  
ANISOU  131  OG1 THR A  70    12928   7262   8689   1943  -1479   1084       O  
ATOM    132  CG2 THR A  70     -11.565  30.409 -61.661  1.00 65.81           C  
ANISOU  132  CG2 THR A  70    11213   6208   7583   1729  -1376    898       C  
ATOM    133  N   ILE A  71      -7.964  30.722 -62.447  1.00 52.10           N  
ANISOU  133  N   ILE A  71     9872   4095   5830    951  -1156    980       N  
ATOM    134  CA  ILE A  71      -6.977  29.716 -62.111  1.00 55.98           C  
ANISOU  134  CA  ILE A  71    10166   4703   6402    687  -1047    899       C  
ATOM    135  C   ILE A  71      -5.840  30.326 -61.288  1.00 58.20           C  
ANISOU  135  C   ILE A  71    10597   4782   6735    503   -970    873       C  
ATOM    136  O   ILE A  71      -5.425  29.761 -60.269  1.00 55.91           O  
ANISOU  136  O   ILE A  71    10137   4557   6551    418   -906    769       O  
ATOM    137  CB  ILE A  71      -6.436  29.047 -63.378  1.00 53.24           C  
ANISOU  137  CB  ILE A  71     9769   4482   5976    499  -1012    954       C  
ATOM    138  CG1 ILE A  71      -7.573  28.283 -64.066  1.00 52.36           C  
ANISOU  138  CG1 ILE A  71     9471   4603   5819    658  -1087    955       C  
ATOM    139  CG2 ILE A  71      -5.294  28.100 -63.027  1.00 47.66           C  
ANISOU  139  CG2 ILE A  71     8886   3875   5347    239   -891    876       C  
ATOM    140  CD1 ILE A  71      -7.190  27.655 -65.402  1.00 52.16           C  
ANISOU  140  CD1 ILE A  71     9417   4705   5694    501  -1066   1005       C  
ATOM    141  N   MET A  72      -5.357  31.491 -61.708  1.00 54.53           N  
ANISOU  141  N   MET A  72    10459   4073   6188    437   -981    968       N  
ATOM    142  CA  MET A  72      -4.315  32.172 -60.949  1.00 57.13           C  
ANISOU  142  CA  MET A  72    10880   4270   6557    239   -901    919       C  
ATOM    143  C   MET A  72      -4.818  32.497 -59.542  1.00 55.61           C  
ANISOU  143  C   MET A  72    10645   4031   6455    399   -912    811       C  
ATOM    144  O   MET A  72      -4.088  32.339 -58.567  1.00 50.45           O  
ANISOU  144  O   MET A  72     9924   3370   5876    253   -849    729       O  
ATOM    145  CB  MET A  72      -3.862  33.452 -61.657  1.00 59.55           C  
ANISOU  145  CB  MET A  72    11438   4428   6762    145   -891    996       C  
ATOM    146  CG  MET A  72      -2.383  33.808 -61.441  1.00 73.19           C  
ANISOU  146  CG  MET A  72    13221   6101   8488   -184   -793    980       C  
ATOM    147  SD  MET A  72      -1.808  34.056 -59.735  1.00205.70           S  
ANISOU  147  SD  MET A  72    29945  22832  25378   -269   -742    846       S  
ATOM    148  CE  MET A  72      -2.127  35.800 -59.454  1.00 84.35           C  
ANISOU  148  CE  MET A  72    14868   7231   9948   -166   -780    851       C  
ATOM    149  N   ALA A  73      -6.064  32.954 -59.452  1.00 55.96           N  
ANISOU  149  N   ALA A  73    10718   4063   6483    701   -991    810       N  
ATOM    150  CA  ALA A  73      -6.669  33.309 -58.177  1.00 51.34           C  
ANISOU  150  CA  ALA A  73    10093   3450   5965    881  -1000    710       C  
ATOM    151  C   ALA A  73      -6.840  32.070 -57.319  1.00 56.94           C  
ANISOU  151  C   ALA A  73    10545   4309   6779    905   -986    621       C  
ATOM    152  O   ALA A  73      -6.685  32.124 -56.104  1.00 57.61           O  
ANISOU  152  O   ALA A  73    10578   4376   6936    898   -949    522       O  
ATOM    153  CB  ALA A  73      -7.998  33.998 -58.393  1.00 57.22           C  
ANISOU  153  CB  ALA A  73    10897   4187   6658   1206  -1082    735       C  
ATOM    154  N   LEU A  74      -7.156  30.949 -57.962  1.00 55.80           N  
ANISOU  154  N   LEU A  74    10198   4365   6638    914  -1004    642       N  
ATOM    155  CA  LEU A  74      -7.218  29.672 -57.274  1.00 60.51           C  
ANISOU  155  CA  LEU A  74    10456   5204   7332    869   -954    538       C  
ATOM    156  C   LEU A  74      -5.895  29.343 -56.597  1.00 49.26           C  
ANISOU  156  C   LEU A  74     8986   3756   5972    595   -856    482       C  
ATOM    157  O   LEU A  74      -5.854  29.056 -55.404  1.00 47.59           O  
ANISOU  157  O   LEU A  74     8655   3585   5843    602   -824    387       O  
ATOM    158  CB  LEU A  74      -7.574  28.551 -58.247  1.00 62.56           C  
ANISOU  158  CB  LEU A  74    10495   5707   7567    847   -963    562       C  
ATOM    159  CG  LEU A  74      -8.956  27.906 -58.208  1.00 64.34           C  
ANISOU  159  CG  LEU A  74    10494   6152   7801   1072  -1025    528       C  
ATOM    160  CD1 LEU A  74      -9.016  26.791 -59.246  1.00 58.68           C  
ANISOU  160  CD1 LEU A  74     9600   5646   7049    969  -1022    548       C  
ATOM    161  CD2 LEU A  74      -9.250  27.372 -56.824  1.00 57.94           C  
ANISOU  161  CD2 LEU A  74     9482   5438   7095   1123   -989    411       C  
ATOM    162  N   TYR A  75      -4.819  29.360 -57.379  1.00 49.82           N  
ANISOU  162  N   TYR A  75     9143   3786   6000    354   -810    544       N  
ATOM    163  CA  TYR A  75      -3.499  29.009 -56.869  1.00 49.02           C  
ANISOU  163  CA  TYR A  75     8976   3702   5948     87   -717    501       C  
ATOM    164  C   TYR A  75      -3.044  29.989 -55.782  1.00 40.95           C  
ANISOU  164  C   TYR A  75     8133   2479   4948     41   -709    458       C  
ATOM    165  O   TYR A  75      -2.436  29.587 -54.797  1.00 45.60           O  
ANISOU  165  O   TYR A  75     8592   3128   5607    -70   -657    378       O  
ATOM    166  CB  TYR A  75      -2.469  28.961 -58.010  1.00 49.12           C  
ANISOU  166  CB  TYR A  75     9056   3718   5889   -151   -668    583       C  
ATOM    167  CG  TYR A  75      -2.494  27.670 -58.814  1.00 51.55           C  
ANISOU  167  CG  TYR A  75     9127   4264   6195   -186   -636    584       C  
ATOM    168  CD1 TYR A  75      -2.057  26.478 -58.260  1.00 48.86           C  
ANISOU  168  CD1 TYR A  75     8521   4107   5938   -266   -568    502       C  
ATOM    169  CD2 TYR A  75      -2.935  27.652 -60.134  1.00 60.82           C  
ANISOU  169  CD2 TYR A  75    10362   5472   7275   -139   -675    667       C  
ATOM    170  CE1 TYR A  75      -2.077  25.298 -58.983  1.00 56.29           C  
ANISOU  170  CE1 TYR A  75     9276   5240   6873   -295   -535    495       C  
ATOM    171  CE2 TYR A  75      -2.949  26.468 -60.875  1.00 55.80           C  
ANISOU  171  CE2 TYR A  75     9528   5047   6628   -181   -644    656       C  
ATOM    172  CZ  TYR A  75      -2.521  25.298 -60.289  1.00 54.42           C  
ANISOU  172  CZ  TYR A  75     9104   5031   6540   -258   -572    566       C  
ATOM    173  OH  TYR A  75      -2.532  24.116 -60.995  1.00 45.41           O  
ANISOU  173  OH  TYR A  75     7794   4076   5386   -295   -537    547       O  
ATOM    174  N   SER A  76      -3.359  31.266 -55.957  1.00 40.77           N  
ANISOU  174  N   SER A  76     8389   2243   4859    130   -759    506       N  
ATOM    175  CA  SER A  76      -2.919  32.277 -55.013  1.00 43.97           C  
ANISOU  175  CA  SER A  76     8907   2533   5267     69   -732    447       C  
ATOM    176  C   SER A  76      -3.613  32.116 -53.667  1.00 50.80           C  
ANISOU  176  C   SER A  76     9671   3424   6208    251   -747    338       C  
ATOM    177  O   SER A  76      -2.969  32.122 -52.621  1.00 50.74           O  
ANISOU  177  O   SER A  76     9618   3417   6245    128   -703    259       O  
ATOM    178  CB  SER A  76      -3.176  33.674 -55.567  1.00 47.05           C  
ANISOU  178  CB  SER A  76     9558   2759   5561    136   -766    509       C  
ATOM    179  OG  SER A  76      -2.490  33.845 -56.787  1.00 71.49           O  
ANISOU  179  OG  SER A  76    12750   5835   8578    -45   -747    609       O  
ATOM    180  N   ILE A  77      -4.931  31.967 -53.703  1.00 50.71           N  
ANISOU  180  N   ILE A  77     9611   3454   6202    545   -809    333       N  
ATOM    181  CA  ILE A  77      -5.720  31.853 -52.486  1.00 49.02           C  
ANISOU  181  CA  ILE A  77     9293   3287   6046    744   -821    232       C  
ATOM    182  C   ILE A  77      -5.347  30.604 -51.696  1.00 48.69           C  
ANISOU  182  C   ILE A  77     9004   3399   6097    645   -777    155       C  
ATOM    183  O   ILE A  77      -5.135  30.665 -50.485  1.00 47.49           O  
ANISOU  183  O   ILE A  77     8824   3232   5988    625   -750     64       O  
ATOM    184  CB  ILE A  77      -7.218  31.852 -52.819  1.00 59.24           C  
ANISOU  184  CB  ILE A  77    10539   4652   7317   1076   -894    250       C  
ATOM    185  CG1 ILE A  77      -7.619  33.245 -53.322  1.00 65.01           C  
ANISOU  185  CG1 ILE A  77    11507   5237   7957   1194   -928    306       C  
ATOM    186  CG2 ILE A  77      -8.048  31.463 -51.611  1.00 54.60           C  
ANISOU  186  CG2 ILE A  77     9780   4174   6790   1272   -896    144       C  
ATOM    187  CD1 ILE A  77      -8.961  33.290 -54.007  1.00 68.35           C  
ANISOU  187  CD1 ILE A  77    11891   5747   8333   1491  -1005    356       C  
ATOM    188  N   VAL A  78      -5.241  29.474 -52.382  1.00 43.85           N  
ANISOU  188  N   VAL A  78     8160   2997   5504    563   -754    184       N  
ATOM    189  CA  VAL A  78      -4.903  28.234 -51.708  1.00 42.50           C  
ANISOU  189  CA  VAL A  78     7697   3038   5412    462   -694    115       C  
ATOM    190  C   VAL A  78      -3.505  28.313 -51.094  1.00 46.40           C  
ANISOU  190  C   VAL A  78     8222   3480   5930    204   -631     85       C  
ATOM    191  O   VAL A  78      -3.264  27.832 -49.984  1.00 40.88           O  
ANISOU  191  O   VAL A  78     7378   2867   5288    169   -597      6       O  
ATOM    192  CB  VAL A  78      -5.004  27.042 -52.663  1.00 41.13           C  
ANISOU  192  CB  VAL A  78     7314   3070   5244    418   -679    153       C  
ATOM    193  CG1 VAL A  78      -4.391  25.808 -52.046  1.00 35.13           C  
ANISOU  193  CG1 VAL A  78     6304   2486   4559    280   -608     94       C  
ATOM    194  CG2 VAL A  78      -6.460  26.771 -52.988  1.00 43.06           C  
ANISOU  194  CG2 VAL A  78     7459   3429   5475    664   -742    158       C  
ATOM    195  N   CYS A  79      -2.588  28.950 -51.809  1.00 49.14           N  
ANISOU  195  N   CYS A  79     8757   3694   6221     18   -619    152       N  
ATOM    196  CA  CYS A  79      -1.232  29.119 -51.315  1.00 46.13           C  
ANISOU  196  CA  CYS A  79     8405   3277   5845   -247   -564    130       C  
ATOM    197  C   CYS A  79      -1.218  29.977 -50.051  1.00 49.11           C  
ANISOU  197  C   CYS A  79     8926   3504   6228   -225   -580     53       C  
ATOM    198  O   CYS A  79      -0.667  29.576 -49.028  1.00 47.34           O  
ANISOU  198  O   CYS A  79     8568   3370   6048   -321   -545    -20       O  
ATOM    199  CB  CYS A  79      -0.347  29.752 -52.388  1.00 43.83           C  
ANISOU  199  CB  CYS A  79     8306   2871   5476   -454   -550    224       C  
ATOM    200  SG  CYS A  79       1.329  30.091 -51.834  1.00 53.33           S  
ANISOU  200  SG  CYS A  79     9522   4076   6666   -795   -483    201       S  
ATOM    201  N   VAL A  80      -1.825  31.161 -50.136  1.00 44.34           N  
ANISOU  201  N   VAL A  80     8539   2738   5568    -88   -621     67       N  
ATOM    202  CA  VAL A  80      -1.831  32.103 -49.025  1.00 49.52           C  
ANISOU  202  CA  VAL A  80     9304   3299   6211    -61   -621     -9       C  
ATOM    203  C   VAL A  80      -2.521  31.521 -47.788  1.00 49.18           C  
ANISOU  203  C   VAL A  80     9116   3335   6233    107   -627   -113       C  
ATOM    204  O   VAL A  80      -2.000  31.601 -46.686  1.00 47.13           O  
ANISOU  204  O   VAL A  80     8834   3085   5990     10   -602   -191       O  
ATOM    205  CB  VAL A  80      -2.509  33.423 -49.426  1.00 41.99           C  
ANISOU  205  CB  VAL A  80     8591   2181   5182     95   -660     28       C  
ATOM    206  CG1 VAL A  80      -2.688  34.320 -48.220  1.00 51.33           C  
ANISOU  206  CG1 VAL A  80     9886   3265   6350    162   -660    -61       C  
ATOM    207  CG2 VAL A  80      -1.685  34.130 -50.503  1.00 50.05           C  
ANISOU  207  CG2 VAL A  80     9782   3109   6125   -104   -648    123       C  
ATOM    208  N   VAL A  81      -3.692  30.932 -47.975  1.00 47.70           N  
ANISOU  208  N   VAL A  81     8827   3220   6074    356   -662   -113       N  
ATOM    209  CA  VAL A  81      -4.409  30.318 -46.870  1.00 49.07           C  
ANISOU  209  CA  VAL A  81     8826   3517   6303    519   -660   -207       C  
ATOM    210  C   VAL A  81      -3.610  29.152 -46.287  1.00 51.46           C  
ANISOU  210  C   VAL A  81     8857   4029   6665    330   -601   -242       C  
ATOM    211  O   VAL A  81      -3.533  28.991 -45.078  1.00 45.19           O  
ANISOU  211  O   VAL A  81     7987   3287   5895    329   -581   -326       O  
ATOM    212  CB  VAL A  81      -5.799  29.832 -47.314  1.00 44.83           C  
ANISOU  212  CB  VAL A  81     8141   3118   5773    790   -694   -187       C  
ATOM    213  CG1 VAL A  81      -6.415  28.917 -46.255  1.00 50.64           C  
ANISOU  213  CG1 VAL A  81     8604   4072   6565    893   -668   -270       C  
ATOM    214  CG2 VAL A  81      -6.702  31.035 -47.596  1.00 43.79           C  
ANISOU  214  CG2 VAL A  81     8235   2826   5577   1027   -748   -166       C  
ATOM    215  N   GLY A  82      -3.006  28.354 -47.161  1.00 44.44           N  
ANISOU  215  N   GLY A  82     7835   3257   5792    179   -574   -176       N  
ATOM    216  CA  GLY A  82      -2.184  27.234 -46.738  1.00 43.82           C  
ANISOU  216  CA  GLY A  82     7516   3369   5765     14   -517   -197       C  
ATOM    217  C   GLY A  82      -0.975  27.653 -45.920  1.00 45.31           C  
ANISOU  217  C   GLY A  82     7769   3503   5943   -199   -492   -238       C  
ATOM    218  O   GLY A  82      -0.717  27.093 -44.855  1.00 45.42           O  
ANISOU  218  O   GLY A  82     7629   3637   5992   -229   -467   -299       O  
ATOM    219  N   LEU A  83      -0.239  28.644 -46.417  1.00 38.99           N  
ANISOU  219  N   LEU A  83     7199   2528   5086   -358   -500   -199       N  
ATOM    220  CA  LEU A  83       0.942  29.130 -45.721  1.00 43.51           C  
ANISOU  220  CA  LEU A  83     7844   3054   5635   -593   -482   -236       C  
ATOM    221  C   LEU A  83       0.547  29.764 -44.397  1.00 49.90           C  
ANISOU  221  C   LEU A  83     8759   3767   6435   -505   -506   -336       C  
ATOM    222  O   LEU A  83       1.131  29.462 -43.359  1.00 50.21           O  
ANISOU  222  O   LEU A  83     8685   3906   6486   -608   -488   -399       O  
ATOM    223  CB  LEU A  83       1.716  30.134 -46.582  1.00 43.67           C  
ANISOU  223  CB  LEU A  83     8093   2917   5584   -787   -482   -168       C  
ATOM    224  CG  LEU A  83       2.354  29.436 -47.792  1.00 51.64           C  
ANISOU  224  CG  LEU A  83     8991   4038   6591   -925   -445    -79       C  
ATOM    225  CD1 LEU A  83       3.169  30.400 -48.648  1.00 49.17           C  
ANISOU  225  CD1 LEU A  83     8841   3646   6197  -1117   -428     -6       C  
ATOM    226  CD2 LEU A  83       3.217  28.261 -47.339  1.00 51.07           C  
ANISOU  226  CD2 LEU A  83     8611   4226   6567  -1046   -391   -102       C  
ATOM    227  N   PHE A  84      -0.468  30.616 -44.426  1.00 44.91           N  
ANISOU  227  N   PHE A  84     8316   2972   5774   -297   -544   -349       N  
ATOM    228  CA  PHE A  84      -0.850  31.330 -43.224  1.00 47.72           C  
ANISOU  228  CA  PHE A  84     8761   3262   6107   -199   -553   -443       C  
ATOM    229  C   PHE A  84      -1.341  30.394 -42.115  1.00 47.87           C  
ANISOU  229  C   PHE A  84     8586   3425   6177    -79   -547   -530       C  
ATOM    230  O   PHE A  84      -0.941  30.535 -40.960  1.00 50.82           O  
ANISOU  230  O   PHE A  84     8961   3812   6537   -154   -539   -614       O  
ATOM    231  CB  PHE A  84      -1.925  32.368 -43.511  1.00 50.62           C  
ANISOU  231  CB  PHE A  84     9311   3492   6432     39   -581   -431       C  
ATOM    232  CG  PHE A  84      -2.489  32.975 -42.267  1.00 62.67           C  
ANISOU  232  CG  PHE A  84    10908   4969   7935    183   -583   -534       C  
ATOM    233  CD1 PHE A  84      -1.777  33.936 -41.573  1.00 70.54           C  
ANISOU  233  CD1 PHE A  84    12062   5860   8878     31   -574   -583       C  
ATOM    234  CD2 PHE A  84      -3.704  32.551 -41.758  1.00 61.94           C  
ANISOU  234  CD2 PHE A  84    10711   4953   7869    460   -592   -588       C  
ATOM    235  CE1 PHE A  84      -2.275  34.479 -40.409  1.00 70.40           C  
ANISOU  235  CE1 PHE A  84    12117   5798   8833    157   -572   -683       C  
ATOM    236  CE2 PHE A  84      -4.208  33.097 -40.597  1.00 67.25           C  
ANISOU  236  CE2 PHE A  84    11441   5597   8513    591   -585   -686       C  
ATOM    237  CZ  PHE A  84      -3.495  34.067 -39.926  1.00 65.15           C  
ANISOU  237  CZ  PHE A  84    11352   5210   8194    442   -575   -735       C  
ATOM    238  N   GLY A  85      -2.211  29.455 -42.463  1.00 44.74           N  
ANISOU  238  N   GLY A  85     7973   3196   5829     99   -541   -501       N  
ATOM    239  CA  GLY A  85      -2.783  28.560 -41.476  1.00 43.71           C  
ANISOU  239  CA  GLY A  85     7604   3264   5739    218   -519   -562       C  
ATOM    240  C   GLY A  85      -1.749  27.646 -40.846  1.00 49.00           C  
ANISOU  240  C   GLY A  85     8070   4110   6439     16   -480   -573       C  
ATOM    241  O   GLY A  85      -1.765  27.393 -39.634  1.00 46.36           O  
ANISOU  241  O   GLY A  85     7649   3862   6105     31   -467   -645       O  
ATOM    242  N   ASN A  86      -0.829  27.141 -41.657  1.00 37.25           N  
ANISOU  242  N   ASN A  86     6502   2684   4969   -166   -461   -500       N  
ATOM    243  CA  ASN A  86       0.124  26.182 -41.125  1.00 38.06           C  
ANISOU  243  CA  ASN A  86     6389   2973   5098   -323   -424   -502       C  
ATOM    244  C   ASN A  86       1.281  26.849 -40.390  1.00 39.65           C  
ANISOU  244  C   ASN A  86     6686   3126   5254   -537   -428   -544       C  
ATOM    245  O   ASN A  86       1.809  26.289 -39.437  1.00 40.93           O  
ANISOU  245  O   ASN A  86     6697   3432   5421   -606   -414   -580       O  
ATOM    246  CB  ASN A  86       0.623  25.272 -42.240  1.00 34.53           C  
ANISOU  246  CB  ASN A  86     5795   2639   4684   -406   -393   -416       C  
ATOM    247  CG  ASN A  86      -0.432  24.273 -42.664  1.00 39.24           C  
ANISOU  247  CG  ASN A  86     6235   3347   5328   -225   -384   -392       C  
ATOM    248  OD1 ASN A  86      -0.768  23.348 -41.905  1.00 40.78           O  
ANISOU  248  OD1 ASN A  86     6249   3689   5558   -156   -363   -420       O  
ATOM    249  ND2 ASN A  86      -0.987  24.462 -43.862  1.00 37.49           N  
ANISOU  249  ND2 ASN A  86     6087   3059   5098   -155   -401   -338       N  
ATOM    250  N   PHE A  87       1.664  28.048 -40.813  1.00 39.90           N  
ANISOU  250  N   PHE A  87     6975   2955   5232   -647   -452   -539       N  
ATOM    251  CA  PHE A  87       2.664  28.801 -40.078  1.00 41.69           C  
ANISOU  251  CA  PHE A  87     7320   3119   5401   -864   -463   -591       C  
ATOM    252  C   PHE A  87       2.113  29.262 -38.733  1.00 46.89           C  
ANISOU  252  C   PHE A  87     8063   3722   6031   -757   -484   -702       C  
ATOM    253  O   PHE A  87       2.853  29.362 -37.747  1.00 46.77           O  
ANISOU  253  O   PHE A  87     8024   3766   5979   -906   -489   -762       O  
ATOM    254  CB  PHE A  87       3.152  29.996 -40.891  1.00 51.34           C  
ANISOU  254  CB  PHE A  87     8826   4117   6565  -1024   -481   -556       C  
ATOM    255  CG  PHE A  87       4.366  29.698 -41.727  1.00 59.59           C  
ANISOU  255  CG  PHE A  87     9778   5262   7602  -1275   -452   -476       C  
ATOM    256  CD1 PHE A  87       4.251  29.010 -42.911  1.00 56.76           C  
ANISOU  256  CD1 PHE A  87     9303   4983   7280  -1227   -425   -386       C  
ATOM    257  CD2 PHE A  87       5.625  30.108 -41.320  1.00 76.29           C  
ANISOU  257  CD2 PHE A  87    11890   7435   9664  -1545   -445   -491       C  
ATOM    258  CE1 PHE A  87       5.359  28.733 -43.686  1.00 60.25           C  
ANISOU  258  CE1 PHE A  87     9656   5531   7706  -1444   -389   -317       C  
ATOM    259  CE2 PHE A  87       6.741  29.835 -42.091  1.00 79.01           C  
ANISOU  259  CE2 PHE A  87    12120   7908   9994  -1761   -411   -417       C  
ATOM    260  CZ  PHE A  87       6.604  29.144 -43.278  1.00 69.39           C  
ANISOU  260  CZ  PHE A  87    10822   6733   8812  -1721   -383   -334       C  
ATOM    261  N   LEU A  88       0.815  29.547 -38.696  1.00 40.42           N  
ANISOU  261  N   LEU A  88     7335   2804   5219   -495   -497   -731       N  
ATOM    262  CA  LEU A  88       0.173  29.957 -37.461  1.00 46.96           C  
ANISOU  262  CA  LEU A  88     8237   3592   6015   -357   -507   -840       C  
ATOM    263  C   LEU A  88       0.200  28.798 -36.453  1.00 45.03           C  
ANISOU  263  C   LEU A  88     7702   3608   5800   -336   -481   -870       C  
ATOM    264  O   LEU A  88       0.508  28.991 -35.279  1.00 48.37           O  
ANISOU  264  O   LEU A  88     8139   4061   6177   -395   -485   -952       O  
ATOM    265  CB  LEU A  88      -1.258  30.415 -37.725  1.00 44.14           C  
ANISOU  265  CB  LEU A  88     8001   3112   5658    -55   -520   -855       C  
ATOM    266  CG  LEU A  88      -2.053  30.738 -36.459  1.00 48.30           C  
ANISOU  266  CG  LEU A  88     8574   3630   6149    128   -518   -971       C  
ATOM    267  CD1 LEU A  88      -1.359  31.854 -35.652  1.00 50.12           C  
ANISOU  267  CD1 LEU A  88     9037   3705   6300    -23   -529  -1054       C  
ATOM    268  CD2 LEU A  88      -3.488  31.117 -36.797  1.00 50.06           C  
ANISOU  268  CD2 LEU A  88     8876   3774   6371    450   -528   -978       C  
ATOM    269  N   VAL A  89      -0.132  27.601 -36.931  1.00 41.17           N  
ANISOU  269  N   VAL A  89     6965   3299   5378   -256   -455   -801       N  
ATOM    270  CA  VAL A  89      -0.045  26.392 -36.123  1.00 42.38           C  
ANISOU  270  CA  VAL A  89     6851   3691   5561   -249   -427   -806       C  
ATOM    271  C   VAL A  89       1.376  26.179 -35.595  1.00 48.82           C  
ANISOU  271  C   VAL A  89     7591   4607   6353   -494   -427   -806       C  
ATOM    272  O   VAL A  89       1.585  25.921 -34.403  1.00 45.79           O  
ANISOU  272  O   VAL A  89     7127   4333   5939   -516   -427   -861       O  
ATOM    273  CB  VAL A  89      -0.467  25.136 -36.927  1.00 38.59           C  
ANISOU  273  CB  VAL A  89     6151   3359   5154   -166   -399   -721       C  
ATOM    274  CG1 VAL A  89      -0.172  23.889 -36.138  1.00 34.12           C  
ANISOU  274  CG1 VAL A  89     5340   3013   4611   -192   -369   -714       C  
ATOM    275  CG2 VAL A  89      -1.945  25.202 -37.280  1.00 36.54           C  
ANISOU  275  CG2 VAL A  89     5911   3062   4909     78   -403   -726       C  
ATOM    276  N   MET A  90       2.353  26.279 -36.492  1.00 44.45           N  
ANISOU  276  N   MET A  90     7052   4033   5803   -677   -427   -743       N  
ATOM    277  CA  MET A  90       3.732  26.049 -36.109  1.00 48.60           C  
ANISOU  277  CA  MET A  90     7476   4687   6302   -909   -427   -734       C  
ATOM    278  C   MET A  90       4.185  27.096 -35.117  1.00 49.85           C  
ANISOU  278  C   MET A  90     7805   4759   6377  -1040   -463   -826       C  
ATOM    279  O   MET A  90       4.931  26.785 -34.199  1.00 48.18           O  
ANISOU  279  O   MET A  90     7475   4701   6132  -1155   -471   -854       O  
ATOM    280  CB  MET A  90       4.656  26.034 -37.327  1.00 40.91           C  
ANISOU  280  CB  MET A  90     6487   3718   5339  -1079   -413   -650       C  
ATOM    281  CG  MET A  90       4.555  24.744 -38.119  1.00 43.91           C  
ANISOU  281  CG  MET A  90     6646   4247   5790   -992   -372   -566       C  
ATOM    282  SD  MET A  90       5.757  24.654 -39.463  1.00 49.74           S  
ANISOU  282  SD  MET A  90     7342   5031   6525  -1195   -344   -476       S  
ATOM    283  CE  MET A  90       4.956  25.660 -40.710  1.00 50.34           C  
ANISOU  283  CE  MET A  90     7685   4849   6592  -1140   -358   -447       C  
ATOM    284  N   TYR A  91       3.724  28.332 -35.293  1.00 48.28           N  
ANISOU  284  N   TYR A  91     7895   4312   6139  -1019   -486   -874       N  
ATOM    285  CA  TYR A  91       4.060  29.400 -34.366  1.00 45.86           C  
ANISOU  285  CA  TYR A  91     7797   3884   5744  -1139   -519   -976       C  
ATOM    286  C   TYR A  91       3.487  29.116 -32.984  1.00 50.86           C  
ANISOU  286  C   TYR A  91     8362   4611   6352  -1000   -520  -1066       C  
ATOM    287  O   TYR A  91       4.180  29.253 -31.984  1.00 46.67           O  
ANISOU  287  O   TYR A  91     7816   4160   5756  -1148   -540  -1128       O  
ATOM    288  CB  TYR A  91       3.551  30.751 -34.871  1.00 44.94           C  
ANISOU  288  CB  TYR A  91     8035   3451   5590  -1102   -538  -1007       C  
ATOM    289  CG  TYR A  91       3.573  31.853 -33.823  1.00 51.45           C  
ANISOU  289  CG  TYR A  91     9071   4150   6328  -1140   -558  -1119       C  
ATOM    290  CD1 TYR A  91       4.742  32.540 -33.529  1.00 57.20           C  
ANISOU  290  CD1 TYR A  91     9848   4895   6991  -1408   -569  -1127       C  
ATOM    291  CD2 TYR A  91       2.418  32.206 -33.131  1.00 54.68           C  
ANISOU  291  CD2 TYR A  91     9589   4468   6720   -886   -555  -1203       C  
ATOM    292  CE1 TYR A  91       4.763  33.544 -32.570  1.00 60.35           C  
ANISOU  292  CE1 TYR A  91    10416   5202   7311  -1434   -581  -1220       C  
ATOM    293  CE2 TYR A  91       2.429  33.201 -32.175  1.00 52.36           C  
ANISOU  293  CE2 TYR A  91     9458   4089   6349   -900   -560  -1297       C  
ATOM    294  CZ  TYR A  91       3.600  33.868 -31.897  1.00 59.54           C  
ANISOU  294  CZ  TYR A  91    10431   4995   7196  -1178   -576  -1306       C  
ATOM    295  OH  TYR A  91       3.608  34.864 -30.943  1.00 67.97           O  
ANISOU  295  OH  TYR A  91    11674   5969   8183  -1199   -583  -1403       O  
ATOM    296  N   VAL A  92       2.212  28.748 -32.932  1.00 49.59           N  
ANISOU  296  N   VAL A  92     8159   4451   6233   -724   -498  -1072       N  
ATOM    297  CA  VAL A  92       1.540  28.518 -31.656  1.00 51.45           C  
ANISOU  297  CA  VAL A  92     8338   4774   6436   -577   -490  -1157       C  
ATOM    298  C   VAL A  92       2.202  27.365 -30.904  1.00 54.31           C  
ANISOU  298  C   VAL A  92     8422   5411   6803   -665   -480  -1130       C  
ATOM    299  O   VAL A  92       2.333  27.403 -29.677  1.00 52.49           O  
ANISOU  299  O   VAL A  92     8177   5261   6505   -689   -490  -1206       O  
ATOM    300  CB  VAL A  92       0.034  28.212 -31.850  1.00 49.51           C  
ANISOU  300  CB  VAL A  92     8052   4523   6235   -271   -462  -1153       C  
ATOM    301  CG1 VAL A  92      -0.557  27.584 -30.594  1.00 54.12           C  
ANISOU  301  CG1 VAL A  92     8487   5282   6795   -145   -438  -1211       C  
ATOM    302  CG2 VAL A  92      -0.717  29.482 -32.213  1.00 48.10           C  
ANISOU  302  CG2 VAL A  92     8172   4080   6026   -137   -477  -1206       C  
ATOM    303  N   ILE A  93       2.625  26.347 -31.647  1.00 51.67           N  
ANISOU  303  N   ILE A  93     7877   5217   6539   -704   -462  -1022       N  
ATOM    304  CA  ILE A  93       3.302  25.206 -31.050  1.00 49.41           C  
ANISOU  304  CA  ILE A  93     7335   5180   6259   -769   -453   -980       C  
ATOM    305  C   ILE A  93       4.673  25.596 -30.510  1.00 59.07           C  
ANISOU  305  C   ILE A  93     8564   6470   7410  -1023   -490  -1006       C  
ATOM    306  O   ILE A  93       5.036  25.254 -29.385  1.00 65.58           O  
ANISOU  306  O   ILE A  93     9289   7449   8180  -1061   -505  -1039       O  
ATOM    307  CB  ILE A  93       3.456  24.062 -32.055  1.00 49.96           C  
ANISOU  307  CB  ILE A  93     7206   5359   6417   -741   -421   -864       C  
ATOM    308  CG1 ILE A  93       2.136  23.308 -32.171  1.00 46.98           C  
ANISOU  308  CG1 ILE A  93     6747   5008   6096   -506   -386   -843       C  
ATOM    309  CG2 ILE A  93       4.557  23.108 -31.619  1.00 55.80           C  
ANISOU  309  CG2 ILE A  93     7726   6325   7151   -856   -420   -813       C  
ATOM    310  CD1 ILE A  93       2.118  22.317 -33.287  1.00 59.82           C  
ANISOU  310  CD1 ILE A  93     8232   6694   7803   -473   -355   -743       C  
ATOM    311  N   VAL A  94       5.424  26.329 -31.319  1.00 50.99           N  
ANISOU  311  N   VAL A  94     7659   5340   6376  -1204   -507   -989       N  
ATOM    312  CA  VAL A  94       6.778  26.710 -30.963  1.00 55.48           C  
ANISOU  312  CA  VAL A  94     8217   5992   6873  -1477   -542  -1005       C  
ATOM    313  C   VAL A  94       6.780  27.725 -29.814  1.00 61.76           C  
ANISOU  313  C   VAL A  94     9208   6696   7561  -1559   -584  -1133       C  
ATOM    314  O   VAL A  94       7.635  27.671 -28.929  1.00 62.76           O  
ANISOU  314  O   VAL A  94     9251   6981   7613  -1719   -618  -1167       O  
ATOM    315  CB  VAL A  94       7.525  27.266 -32.199  1.00 60.08           C  
ANISOU  315  CB  VAL A  94     8884   6480   7464  -1665   -541   -950       C  
ATOM    316  CG1 VAL A  94       8.767  28.028 -31.800  1.00 63.20           C  
ANISOU  316  CG1 VAL A  94     9340   6911   7762  -1975   -583   -992       C  
ATOM    317  CG2 VAL A  94       7.877  26.130 -33.148  1.00 53.27           C  
ANISOU  317  CG2 VAL A  94     7779   5778   6681  -1630   -501   -831       C  
ATOM    318  N   ARG A  95       5.796  28.619 -29.804  1.00 61.81           N  
ANISOU  318  N   ARG A  95     9473   6458   7554  -1434   -582  -1207       N  
ATOM    319  CA  ARG A  95       5.743  29.685 -28.804  1.00 66.35           C  
ANISOU  319  CA  ARG A  95    10284   6904   8023  -1501   -615  -1341       C  
ATOM    320  C   ARG A  95       5.053  29.269 -27.506  1.00 64.88           C  
ANISOU  320  C   ARG A  95    10023   6831   7798  -1329   -607  -1415       C  
ATOM    321  O   ARG A  95       5.484  29.657 -26.430  1.00 72.96           O  
ANISOU  321  O   ARG A  95    11104   7900   8719  -1448   -640  -1506       O  
ATOM    322  CB  ARG A  95       5.036  30.919 -29.385  1.00 71.72           C  
ANISOU  322  CB  ARG A  95    11309   7247   8693  -1431   -614  -1391       C  
ATOM    323  CG  ARG A  95       4.885  32.100 -28.423  1.00 80.31           C  
ANISOU  323  CG  ARG A  95    12667   8172   9676  -1459   -635  -1529       C  
ATOM    324  CD  ARG A  95       6.213  32.802 -28.181  1.00 84.06           C  
ANISOU  324  CD  ARG A  95    13164   8693  10084  -1763   -662  -1526       C  
ATOM    325  NE  ARG A  95       6.074  33.991 -27.342  1.00 92.36           N  
ANISOU  325  NE  ARG A  95    14439   9604  11051  -1764   -668  -1628       N  
ATOM    326  CZ  ARG A  95       6.244  34.000 -26.022  1.00 95.93           C  
ANISOU  326  CZ  ARG A  95    14875  10161  11414  -1811   -691  -1733       C  
ATOM    327  NH1 ARG A  95       6.556  32.878 -25.386  1.00 93.88           N  
ANISOU  327  NH1 ARG A  95    14383  10156  11134  -1858   -714  -1741       N  
ATOM    328  NH2 ARG A  95       6.104  35.130 -25.336  1.00 95.10           N  
ANISOU  328  NH2 ARG A  95    14990   9910  11234  -1811   -693  -1826       N  
ATOM    329  N   TYR A  96       3.982  28.490 -27.599  1.00 65.18           N  
ANISOU  329  N   TYR A  96     9936   6923   7906  -1063   -564  -1376       N  
ATOM    330  CA  TYR A  96       3.164  28.216 -26.417  1.00 62.66           C  
ANISOU  330  CA  TYR A  96     9577   6688   7541   -888   -547  -1449       C  
ATOM    331  C   TYR A  96       3.162  26.751 -25.953  1.00 67.32           C  
ANISOU  331  C   TYR A  96     9852   7561   8166   -818   -524  -1371       C  
ATOM    332  O   TYR A  96       3.570  26.461 -24.833  1.00 65.07           O  
ANISOU  332  O   TYR A  96     9482   7436   7804   -881   -542  -1406       O  
ATOM    333  CB  TYR A  96       1.728  28.683 -26.673  1.00 57.35           C  
ANISOU  333  CB  TYR A  96     9055   5840   6894   -620   -512  -1494       C  
ATOM    334  CG  TYR A  96       1.634  30.174 -26.905  1.00 73.66           C  
ANISOU  334  CG  TYR A  96    11473   7608   8907   -650   -534  -1585       C  
ATOM    335  CD1 TYR A  96       1.772  31.071 -25.847  1.00 78.43           C  
ANISOU  335  CD1 TYR A  96    12286   8123   9393   -714   -555  -1724       C  
ATOM    336  CD2 TYR A  96       1.422  30.691 -28.181  1.00 77.09           C  
ANISOU  336  CD2 TYR A  96    12050   7840   9399   -618   -534  -1531       C  
ATOM    337  CE1 TYR A  96       1.696  32.442 -26.052  1.00 81.19           C  
ANISOU  337  CE1 TYR A  96    12991   8170   9687   -743   -573  -1810       C  
ATOM    338  CE2 TYR A  96       1.344  32.061 -28.398  1.00 79.84           C  
ANISOU  338  CE2 TYR A  96    12749   7892   9693   -642   -555  -1605       C  
ATOM    339  CZ  TYR A  96       1.482  32.931 -27.329  1.00 87.19           C  
ANISOU  339  CZ  TYR A  96    13849   8756  10523   -693   -564  -1724       C  
ATOM    340  OH  TYR A  96       1.406  34.289 -27.539  1.00 90.94           O  
ANISOU  340  OH  TYR A  96    14556   9022  10976   -687   -556  -1736       O  
ATOM    341  N   THR A  97       2.719  25.828 -26.806  1.00 67.87           N  
ANISOU  341  N   THR A  97     9760   7686   8342   -695   -488  -1264       N  
ATOM    342  CA  THR A  97       2.515  24.441 -26.378  1.00 65.34           C  
ANISOU  342  CA  THR A  97     9181   7593   8052   -602   -458  -1193       C  
ATOM    343  C   THR A  97       3.821  23.662 -26.186  1.00 69.79           C  
ANISOU  343  C   THR A  97     9554   8355   8607   -771   -483  -1118       C  
ATOM    344  O   THR A  97       3.884  22.755 -25.352  1.00 74.15           O  
ANISOU  344  O   THR A  97     9943   9095   9133   -732   -477  -1088       O  
ATOM    345  CB  THR A  97       1.615  23.678 -27.370  1.00 64.36           C  
ANISOU  345  CB  THR A  97     8957   7459   8037   -430   -412  -1108       C  
ATOM    346  OG1 THR A  97       2.301  23.497 -28.616  1.00 65.47           O  
ANISOU  346  OG1 THR A  97     9062   7564   8249   -529   -417  -1021       O  
ATOM    347  CG2 THR A  97       0.310  24.437 -27.601  1.00 61.85           C  
ANISOU  347  CG2 THR A  97     8803   6975   7723   -245   -392  -1174       C  
ATOM    348  N   LYS A  98       4.831  24.000 -26.989  1.00 72.08           N  
ANISOU  348  N   LYS A  98     9864   8609   8915   -947   -508  -1082       N  
ATOM    349  CA  LYS A  98       6.225  23.560 -26.814  1.00 77.91           C  
ANISOU  349  CA  LYS A  98    10443   9537   9624  -1132   -541  -1030       C  
ATOM    350  C   LYS A  98       6.602  22.136 -27.271  1.00 82.13           C  
ANISOU  350  C   LYS A  98    10722  10252  10233  -1074   -513   -901       C  
ATOM    351  O   LYS A  98       7.761  21.737 -27.113  1.00 95.84           O  
ANISOU  351  O   LYS A  98    12310  12165  11940  -1199   -538   -854       O  
ATOM    352  CB  LYS A  98       6.635  23.717 -25.346  1.00 71.83           C  
ANISOU  352  CB  LYS A  98     9659   8900   8734  -1210   -584  -1101       C  
ATOM    353  CG  LYS A  98       6.745  25.162 -24.897  1.00 74.00           C  
ANISOU  353  CG  LYS A  98    10186   9018   8912  -1348   -624  -1233       C  
ATOM    354  CD  LYS A  98       7.765  25.912 -25.735  1.00 80.10           C  
ANISOU  354  CD  LYS A  98    11038   9716   9681  -1587   -654  -1224       C  
ATOM    355  CE  LYS A  98       8.191  27.205 -25.057  1.00 88.10           C  
ANISOU  355  CE  LYS A  98    12278  10627  10571  -1789   -706  -1352       C  
ATOM    356  NZ  LYS A  98       7.025  28.071 -24.739  1.00 91.88           N  
ANISOU  356  NZ  LYS A  98    13028  10859  11024  -1645   -688  -1465       N  
ATOM    357  N   MET A  99       5.657  21.382 -27.829  1.00 59.93           N  
ANISOU  357  N   MET A  99     7861   7403   7508   -889   -462   -847       N  
ATOM    358  CA  MET A  99       5.948  20.043 -28.358  1.00 61.98           C  
ANISOU  358  CA  MET A  99     7917   7793   7838   -828   -429   -731       C  
ATOM    359  C   MET A  99       6.472  19.019 -27.339  1.00 58.29           C  
ANISOU  359  C   MET A  99     7270   7548   7328   -808   -438   -683       C  
ATOM    360  O   MET A  99       7.365  18.233 -27.649  1.00 53.05           O  
ANISOU  360  O   MET A  99     6452   7019   6686   -836   -436   -600       O  
ATOM    361  CB  MET A  99       6.954  20.135 -29.517  1.00 61.72           C  
ANISOU  361  CB  MET A  99     7847   7761   7843   -957   -429   -676       C  
ATOM    362  CG  MET A  99       6.305  20.044 -30.898  1.00 59.92           C  
ANISOU  362  CG  MET A  99     7673   7389   7707   -876   -387   -636       C  
ATOM    363  SD  MET A  99       7.487  19.747 -32.224  1.00 69.15           S  
ANISOU  363  SD  MET A  99     8743   8616   8915   -996   -367   -551       S  
ATOM    364  CE  MET A  99       8.410  21.279 -32.175  1.00 58.92           C  
ANISOU  364  CE  MET A  99     7590   7260   7537  -1251   -418   -615       C  
ATOM    365  N   LYS A 100       5.904  19.006 -26.140  1.00 52.12           N  
ANISOU  365  N   LYS A 100     6511   6810   6482   -745   -446   -732       N  
ATOM    366  CA  LYS A 100       6.301  18.028 -25.132  1.00 55.22           C  
ANISOU  366  CA  LYS A 100     6750   7406   6824   -712   -457   -679       C  
ATOM    367  C   LYS A 100       5.501  16.743 -25.279  1.00 46.57           C  
ANISOU  367  C   LYS A 100     5568   6332   5795   -541   -399   -595       C  
ATOM    368  O   LYS A 100       5.853  15.713 -24.712  1.00 52.57           O  
ANISOU  368  O   LYS A 100     6202   7239   6533   -496   -397   -519       O  
ATOM    369  CB  LYS A 100       6.116  18.593 -23.721  1.00 60.00           C  
ANISOU  369  CB  LYS A 100     7424   8064   7310   -740   -492   -768       C  
ATOM    370  CG  LYS A 100       6.994  19.796 -23.405  1.00 63.46           C  
ANISOU  370  CG  LYS A 100     7953   8497   7660   -936   -556   -857       C  
ATOM    371  CD  LYS A 100       6.392  20.618 -22.280  1.00 69.00           C  
ANISOU  371  CD  LYS A 100     8805   9155   8257   -936   -573   -981       C  
ATOM    372  CE  LYS A 100       7.256  21.827 -21.962  1.00 79.62           C  
ANISOU  372  CE  LYS A 100    10268  10477   9507  -1152   -639  -1078       C  
ATOM    373  NZ  LYS A 100       8.618  21.413 -21.522  1.00 90.22           N  
ANISOU  373  NZ  LYS A 100    11437  12059  10783  -1299   -698  -1025       N  
ATOM    374  N   THR A 101       4.417  16.808 -26.039  1.00 40.72           N  
ANISOU  374  N   THR A 101     4901   5443   5128   -450   -354   -608       N  
ATOM    375  CA  THR A 101       3.496  15.681 -26.126  1.00 35.96           C  
ANISOU  375  CA  THR A 101     4234   4853   4576   -310   -299   -544       C  
ATOM    376  C   THR A 101       3.487  15.075 -27.510  1.00 41.44           C  
ANISOU  376  C   THR A 101     4892   5479   5375   -281   -265   -475       C  
ATOM    377  O   THR A 101       3.773  15.751 -28.497  1.00 36.18           O  
ANISOU  377  O   THR A 101     4284   4715   4747   -340   -274   -494       O  
ATOM    378  CB  THR A 101       2.057  16.099 -25.772  1.00 50.48           C  
ANISOU  378  CB  THR A 101     6162   6618   6400   -214   -271   -616       C  
ATOM    379  OG1 THR A 101       1.600  17.077 -26.719  1.00 46.57           O  
ANISOU  379  OG1 THR A 101     5786   5958   5950   -210   -272   -674       O  
ATOM    380  CG2 THR A 101       1.998  16.686 -24.347  1.00 49.06           C  
ANISOU  380  CG2 THR A 101     6029   6508   6103   -232   -296   -696       C  
ATOM    381  N   ALA A 102       3.140  13.796 -27.565  1.00 39.01           N  
ANISOU  381  N   ALA A 102     4502   5217   5104   -195   -223   -395       N  
ATOM    382  CA  ALA A 102       2.987  13.073 -28.814  1.00 43.09           C  
ANISOU  382  CA  ALA A 102     4993   5668   5710   -157   -183   -335       C  
ATOM    383  C   ALA A 102       2.051  13.801 -29.778  1.00 42.56           C  
ANISOU  383  C   ALA A 102     5021   5457   5692   -138   -172   -388       C  
ATOM    384  O   ALA A 102       2.336  13.919 -30.973  1.00 40.75           O  
ANISOU  384  O   ALA A 102     4810   5155   5517   -166   -167   -371       O  
ATOM    385  CB  ALA A 102       2.472  11.654 -28.541  1.00 34.77           C  
ANISOU  385  CB  ALA A 102     3878   4660   4673    -71   -138   -258       C  
ATOM    386  N   THR A 103       0.934  14.288 -29.256  1.00 39.10           N  
ANISOU  386  N   THR A 103     4640   4990   5226    -83   -168   -450       N  
ATOM    387  CA  THR A 103      -0.068  14.924 -30.099  1.00 42.54           C  
ANISOU  387  CA  THR A 103     5155   5308   5699    -33   -161   -495       C  
ATOM    388  C   THR A 103       0.471  16.206 -30.741  1.00 42.79           C  
ANISOU  388  C   THR A 103     5301   5227   5732   -101   -200   -543       C  
ATOM    389  O   THR A 103       0.251  16.448 -31.924  1.00 39.95           O  
ANISOU  389  O   THR A 103     4987   4771   5422    -94   -197   -532       O  
ATOM    390  CB  THR A 103      -1.348  15.242 -29.305  1.00 50.80           C  
ANISOU  390  CB  THR A 103     6227   6374   6702     59   -147   -557       C  
ATOM    391  OG1 THR A 103      -1.943  14.019 -28.867  1.00 54.80           O  
ANISOU  391  OG1 THR A 103     6634   6978   7208    102   -103   -503       O  
ATOM    392  CG2 THR A 103      -2.357  15.995 -30.180  1.00 49.94           C  
ANISOU  392  CG2 THR A 103     6194   6157   6623    133   -147   -602       C  
ATOM    393  N   ASN A 104       1.200  17.017 -29.979  1.00 37.98           N  
ANISOU  393  N   ASN A 104     4743   4628   5058   -180   -237   -594       N  
ATOM    394  CA  ASN A 104       1.765  18.237 -30.543  1.00 40.19           C  
ANISOU  394  CA  ASN A 104     5150   4791   5328   -274   -273   -637       C  
ATOM    395  C   ASN A 104       2.885  17.948 -31.521  1.00 40.98           C  
ANISOU  395  C   ASN A 104     5198   4905   5469   -380   -274   -570       C  
ATOM    396  O   ASN A 104       3.091  18.693 -32.479  1.00 38.35           O  
ANISOU  396  O   ASN A 104     4961   4457   5152   -439   -284   -576       O  
ATOM    397  CB  ASN A 104       2.245  19.165 -29.432  1.00 38.78           C  
ANISOU  397  CB  ASN A 104     5053   4622   5059   -355   -314   -718       C  
ATOM    398  CG  ASN A 104       1.101  19.889 -28.797  1.00 45.84           C  
ANISOU  398  CG  ASN A 104     6063   5444   5912   -247   -311   -808       C  
ATOM    399  OD1 ASN A 104       0.022  19.952 -29.388  1.00 45.08           O  
ANISOU  399  OD1 ASN A 104     6001   5270   5856   -123   -287   -813       O  
ATOM    400  ND2 ASN A 104       1.305  20.427 -27.603  1.00 48.88           N  
ANISOU  400  ND2 ASN A 104     6502   5865   6207   -285   -334   -883       N  
ATOM    401  N   ILE A 105       3.589  16.847 -31.287  1.00 35.37           N  
ANISOU  401  N   ILE A 105     4337   4335   4765   -392   -259   -501       N  
ATOM    402  CA  ILE A 105       4.636  16.405 -32.191  1.00 31.65           C  
ANISOU  402  CA  ILE A 105     3789   3907   4329   -462   -248   -435       C  
ATOM    403  C   ILE A 105       4.057  16.021 -33.569  1.00 36.28           C  
ANISOU  403  C   ILE A 105     4395   4400   4990   -401   -209   -397       C  
ATOM    404  O   ILE A 105       4.658  16.357 -34.595  1.00 38.73           O  
ANISOU  404  O   ILE A 105     4730   4669   5318   -478   -206   -378       O  
ATOM    405  CB  ILE A 105       5.423  15.233 -31.570  1.00 34.05           C  
ANISOU  405  CB  ILE A 105     3931   4385   4620   -445   -238   -368       C  
ATOM    406  CG1 ILE A 105       6.312  15.760 -30.446  1.00 38.10           C  
ANISOU  406  CG1 ILE A 105     4416   5013   5047   -544   -289   -400       C  
ATOM    407  CG2 ILE A 105       6.285  14.522 -32.620  1.00 31.37           C  
ANISOU  407  CG2 ILE A 105     3501   4092   4326   -459   -207   -295       C  
ATOM    408  CD1 ILE A 105       6.936  14.694 -29.601  1.00 39.93           C  
ANISOU  408  CD1 ILE A 105     4501   5425   5248   -501   -291   -336       C  
ATOM    409  N   TYR A 106       2.913  15.324 -33.584  1.00 33.75           N  
ANISOU  409  N   TYR A 106     4061   4059   4703   -280   -181   -387       N  
ATOM    410  CA  TYR A 106       2.205  14.969 -34.820  1.00 35.69           C  
ANISOU  410  CA  TYR A 106     4328   4224   5007   -224   -152   -362       C  
ATOM    411  C   TYR A 106       1.633  16.200 -35.524  1.00 40.63           C  
ANISOU  411  C   TYR A 106     5093   4712   5631   -229   -178   -409       C  
ATOM    412  O   TYR A 106       1.732  16.340 -36.740  1.00 37.21           O  
ANISOU  412  O   TYR A 106     4700   4212   5225   -253   -171   -384       O  
ATOM    413  CB  TYR A 106       1.062  13.984 -34.545  1.00 31.90           C  
ANISOU  413  CB  TYR A 106     3800   3773   4549   -117   -121   -346       C  
ATOM    414  CG  TYR A 106       1.518  12.577 -34.153  1.00 37.43           C  
ANISOU  414  CG  TYR A 106     4391   4572   5259    -98    -87   -281       C  
ATOM    415  CD1 TYR A 106       2.589  11.973 -34.803  1.00 37.68           C  
ANISOU  415  CD1 TYR A 106     4372   4632   5313   -130    -67   -227       C  
ATOM    416  CD2 TYR A 106       0.880  11.864 -33.133  1.00 31.21           C  
ANISOU  416  CD2 TYR A 106     3560   3847   4450    -42    -71   -270       C  
ATOM    417  CE1 TYR A 106       3.014  10.701 -34.466  1.00 41.51           C  
ANISOU  417  CE1 TYR A 106     4779   5190   5804    -88    -36   -165       C  
ATOM    418  CE2 TYR A 106       1.312  10.565 -32.766  1.00 30.23           C  
ANISOU  418  CE2 TYR A 106     3366   3792   4329    -20    -40   -200       C  
ATOM    419  CZ  TYR A 106       2.373  10.000 -33.449  1.00 31.08           C  
ANISOU  419  CZ  TYR A 106     3437   3910   4463    -33    -25   -149       C  
ATOM    420  OH  TYR A 106       2.831   8.746 -33.155  1.00 38.16           O  
ANISOU  420  OH  TYR A 106     4282   4856   5360     14      5    -78       O  
ATOM    421  N   ILE A 107       1.009  17.076 -34.748  1.00 34.31           N  
ANISOU  421  N   ILE A 107     4377   3868   4792   -194   -205   -475       N  
ATOM    422  CA  ILE A 107       0.431  18.305 -35.271  1.00 40.01           C  
ANISOU  422  CA  ILE A 107     5254   4445   5503   -170   -232   -522       C  
ATOM    423  C   ILE A 107       1.494  19.167 -35.940  1.00 40.45           C  
ANISOU  423  C   ILE A 107     5407   4418   5543   -310   -254   -515       C  
ATOM    424  O   ILE A 107       1.286  19.679 -37.047  1.00 37.74           O  
ANISOU  424  O   ILE A 107     5160   3964   5215   -311   -261   -500       O  
ATOM    425  CB  ILE A 107      -0.267  19.124 -34.169  1.00 42.22           C  
ANISOU  425  CB  ILE A 107     5617   4694   5730   -101   -253   -605       C  
ATOM    426  CG1 ILE A 107      -1.521  18.390 -33.662  1.00 44.06           C  
ANISOU  426  CG1 ILE A 107     5760   5011   5972     41   -225   -612       C  
ATOM    427  CG2 ILE A 107      -0.653  20.519 -34.697  1.00 39.05           C  
ANISOU  427  CG2 ILE A 107     5413   4116   5309    -76   -286   -653       C  
ATOM    428  CD1 ILE A 107      -2.216  19.113 -32.462  1.00 41.35           C  
ANISOU  428  CD1 ILE A 107     5478   4669   5565    124   -234   -699       C  
ATOM    429  N   PHE A 108       2.643  19.306 -35.288  1.00 33.38           N  
ANISOU  429  N   PHE A 108     4481   3590   4612   -436   -267   -522       N  
ATOM    430  CA  PHE A 108       3.704  20.106 -35.861  1.00 36.85           C  
ANISOU  430  CA  PHE A 108     4997   3977   5026   -600   -284   -515       C  
ATOM    431  C   PHE A 108       4.191  19.486 -37.168  1.00 41.23           C  
ANISOU  431  C   PHE A 108     5481   4560   5625   -635   -250   -438       C  
ATOM    432  O   PHE A 108       4.441  20.199 -38.129  1.00 37.48           O  
ANISOU  432  O   PHE A 108     5114   3986   5143   -713   -255   -425       O  
ATOM    433  CB  PHE A 108       4.882  20.278 -34.900  1.00 36.72           C  
ANISOU  433  CB  PHE A 108     4927   4072   4954   -743   -306   -535       C  
ATOM    434  CG  PHE A 108       5.958  21.168 -35.452  1.00 37.96           C  
ANISOU  434  CG  PHE A 108     5162   4187   5074   -942   -324   -532       C  
ATOM    435  CD1 PHE A 108       6.933  20.663 -36.300  1.00 43.18           C  
ANISOU  435  CD1 PHE A 108     5707   4947   5752  -1033   -296   -463       C  
ATOM    436  CD2 PHE A 108       5.958  22.526 -35.173  1.00 42.66           C  
ANISOU  436  CD2 PHE A 108     5959   4637   5612  -1038   -363   -600       C  
ATOM    437  CE1 PHE A 108       7.903  21.488 -36.845  1.00 41.01           C  
ANISOU  437  CE1 PHE A 108     5496   4651   5436  -1233   -306   -456       C  
ATOM    438  CE2 PHE A 108       6.936  23.367 -35.696  1.00 44.76           C  
ANISOU  438  CE2 PHE A 108     6314   4857   5836  -1250   -377   -594       C  
ATOM    439  CZ  PHE A 108       7.907  22.850 -36.538  1.00 46.30           C  
ANISOU  439  CZ  PHE A 108     6373   5173   6046  -1355   -348   -519       C  
ATOM    440  N   ASN A 109       4.340  18.167 -37.193  1.00 36.43           N  
ANISOU  440  N   ASN A 109     4706   4082   5054   -577   -214   -389       N  
ATOM    441  CA  ASN A 109       4.810  17.466 -38.388  1.00 38.76           C  
ANISOU  441  CA  ASN A 109     4932   4412   5384   -594   -173   -325       C  
ATOM    442  C   ASN A 109       3.831  17.647 -39.537  1.00 42.22           C  
ANISOU  442  C   ASN A 109     5469   4724   5850   -525   -167   -317       C  
ATOM    443  O   ASN A 109       4.224  17.754 -40.693  1.00 39.86           O  
ANISOU  443  O   ASN A 109     5198   4394   5553   -583   -150   -281       O  
ATOM    444  CB  ASN A 109       4.996  15.971 -38.092  1.00 41.15           C  
ANISOU  444  CB  ASN A 109     5068   4850   5717   -514   -134   -282       C  
ATOM    445  CG  ASN A 109       5.921  15.278 -39.096  1.00 40.60           C  
ANISOU  445  CG  ASN A 109     4912   4850   5663   -549    -88   -225       C  
ATOM    446  OD1 ASN A 109       7.125  15.485 -39.076  1.00 43.64           O  
ANISOU  446  OD1 ASN A 109     5235   5330   6018   -654    -86   -209       O  
ATOM    447  ND2 ASN A 109       5.356  14.435 -39.950  1.00 38.51           N  
ANISOU  447  ND2 ASN A 109     4638   4554   5439   -464    -50   -198       N  
ATOM    448  N   LEU A 110       2.543  17.649 -39.208  1.00 39.65           N  
ANISOU  448  N   LEU A 110     5183   4345   5538   -399   -182   -348       N  
ATOM    449  CA  LEU A 110       1.506  17.830 -40.204  1.00 38.09           C  
ANISOU  449  CA  LEU A 110     5064   4052   5358   -318   -187   -341       C  
ATOM    450  C   LEU A 110       1.547  19.265 -40.750  1.00 37.73           C  
ANISOU  450  C   LEU A 110     5201   3858   5276   -370   -224   -356       C  
ATOM    451  O   LEU A 110       1.492  19.478 -41.965  1.00 35.09           O  
ANISOU  451  O   LEU A 110     4933   3459   4942   -386   -223   -319       O  
ATOM    452  CB  LEU A 110       0.126  17.504 -39.618  1.00 34.85           C  
ANISOU  452  CB  LEU A 110     4626   3655   4959   -172   -194   -372       C  
ATOM    453  CG  LEU A 110      -1.076  17.575 -40.570  1.00 42.19           C  
ANISOU  453  CG  LEU A 110     5600   4530   5901    -72   -206   -366       C  
ATOM    454  CD1 LEU A 110      -0.957  16.543 -41.704  1.00 34.99           C  
ANISOU  454  CD1 LEU A 110     4619   3660   5018    -94   -174   -313       C  
ATOM    455  CD2 LEU A 110      -2.390  17.405 -39.817  1.00 36.53           C  
ANISOU  455  CD2 LEU A 110     4841   3858   5182     61   -214   -404       C  
ATOM    456  N   ALA A 111       1.663  20.247 -39.863  1.00 35.33           N  
ANISOU  456  N   ALA A 111     4996   3493   4935   -401   -256   -408       N  
ATOM    457  CA  ALA A 111       1.681  21.637 -40.290  1.00 38.17           C  
ANISOU  457  CA  ALA A 111     5566   3684   5255   -451   -291   -424       C  
ATOM    458  C   ALA A 111       2.898  21.933 -41.167  1.00 42.80           C  
ANISOU  458  C   ALA A 111     6187   4255   5821   -636   -279   -375       C  
ATOM    459  O   ALA A 111       2.794  22.651 -42.155  1.00 39.61           O  
ANISOU  459  O   ALA A 111     5930   3724   5396   -664   -291   -347       O  
ATOM    460  CB  ALA A 111       1.657  22.580 -39.088  1.00 32.64           C  
ANISOU  460  CB  ALA A 111     4978   2915   4509   -463   -324   -501       C  
ATOM    461  N   LEU A 112       4.052  21.391 -40.802  1.00 36.64           N  
ANISOU  461  N   LEU A 112     5269   3615   5037   -760   -254   -361       N  
ATOM    462  CA  LEU A 112       5.254  21.599 -41.598  1.00 43.48           C  
ANISOU  462  CA  LEU A 112     6133   4511   5878   -940   -233   -315       C  
ATOM    463  C   LEU A 112       5.090  21.011 -43.017  1.00 39.92           C  
ANISOU  463  C   LEU A 112     5650   4067   5451   -901   -196   -252       C  
ATOM    464  O   LEU A 112       5.425  21.649 -44.012  1.00 35.45           O  
ANISOU  464  O   LEU A 112     5193   3423   4851   -999   -191   -216       O  
ATOM    465  CB  LEU A 112       6.458  20.974 -40.895  1.00 38.21           C  
ANISOU  465  CB  LEU A 112     5280   4037   5200  -1044   -212   -311       C  
ATOM    466  CG  LEU A 112       7.794  21.041 -41.628  1.00 39.14           C  
ANISOU  466  CG  LEU A 112     5339   4248   5286  -1229   -181   -263       C  
ATOM    467  CD1 LEU A 112       8.207  22.504 -41.884  1.00 39.83           C  
ANISOU  467  CD1 LEU A 112     5626   4199   5308  -1420   -210   -276       C  
ATOM    468  CD2 LEU A 112       8.875  20.294 -40.841  1.00 44.56           C  
ANISOU  468  CD2 LEU A 112     5808   5160   5962  -1283   -166   -258       C  
ATOM    469  N   ALA A 113       4.575  19.791 -43.103  1.00 33.52           N  
ANISOU  469  N   ALA A 113     4700   3346   4689   -767   -168   -239       N  
ATOM    470  CA  ALA A 113       4.360  19.165 -44.411  1.00 36.49           C  
ANISOU  470  CA  ALA A 113     5053   3731   5081   -727   -134   -191       C  
ATOM    471  C   ALA A 113       3.355  19.961 -45.245  1.00 40.49           C  
ANISOU  471  C   ALA A 113     5734   4080   5572   -667   -170   -183       C  
ATOM    472  O   ALA A 113       3.537  20.156 -46.453  1.00 39.52           O  
ANISOU  472  O   ALA A 113     5675   3919   5423   -718   -157   -139       O  
ATOM    473  CB  ALA A 113       3.890  17.761 -44.240  1.00 27.38           C  
ANISOU  473  CB  ALA A 113     3750   2676   3976   -603   -104   -189       C  
ATOM    474  N   ASP A 114       2.286  20.413 -44.602  1.00 36.47           N  
ANISOU  474  N   ASP A 114     5298   3490   5069   -548   -215   -225       N  
ATOM    475  CA  ASP A 114       1.262  21.184 -45.291  1.00 41.96           C  
ANISOU  475  CA  ASP A 114     6150   4047   5743   -454   -257   -217       C  
ATOM    476  C   ASP A 114       1.774  22.545 -45.757  1.00 43.91           C  
ANISOU  476  C   ASP A 114     6609   4139   5934   -568   -281   -197       C  
ATOM    477  O   ASP A 114       1.411  22.992 -46.839  1.00 41.27           O  
ANISOU  477  O   ASP A 114     6395   3714   5571   -547   -298   -153       O  
ATOM    478  CB  ASP A 114       0.030  21.350 -44.399  1.00 38.00           C  
ANISOU  478  CB  ASP A 114     5661   3521   5257   -284   -293   -271       C  
ATOM    479  CG  ASP A 114      -0.780  20.063 -44.294  1.00 55.26           C  
ANISOU  479  CG  ASP A 114     7669   5840   7486   -170   -273   -275       C  
ATOM    480  OD1 ASP A 114      -0.659  19.204 -45.197  1.00 61.15           O1-
ANISOU  480  OD1 ASP A 114     8337   6650   8246   -193   -245   -235       O1-
ATOM    481  OD2 ASP A 114      -1.539  19.907 -43.320  1.00 60.56           O  
ANISOU  481  OD2 ASP A 114     8288   6551   8170    -65   -283   -320       O  
ATOM    482  N   ALA A 115       2.620  23.197 -44.959  1.00 38.82           N  
ANISOU  482  N   ALA A 115     6019   3466   5267   -700   -285   -227       N  
ATOM    483  CA  ALA A 115       3.222  24.460 -45.383  1.00 42.35           C  
ANISOU  483  CA  ALA A 115     6678   3760   5652   -851   -303   -206       C  
ATOM    484  C   ALA A 115       4.130  24.239 -46.605  1.00 45.28           C  
ANISOU  484  C   ALA A 115     7020   4186   5997  -1004   -260   -133       C  
ATOM    485  O   ALA A 115       4.114  25.020 -47.553  1.00 45.37           O  
ANISOU  485  O   ALA A 115     7210   4068   5960  -1058   -272    -84       O  
ATOM    486  CB  ALA A 115       4.000  25.087 -44.248  1.00 36.95           C  
ANISOU  486  CB  ALA A 115     6040   3060   4941   -991   -314   -261       C  
ATOM    487  N   LEU A 116       4.921  23.173 -46.574  1.00 41.28           N  
ANISOU  487  N   LEU A 116     6294   3876   5517  -1064   -208   -122       N  
ATOM    488  CA  LEU A 116       5.829  22.875 -47.683  1.00 46.95           C  
ANISOU  488  CA  LEU A 116     6957   4677   6204  -1197   -155    -61       C  
ATOM    489  C   LEU A 116       5.064  22.529 -48.948  1.00 43.02           C  
ANISOU  489  C   LEU A 116     6496   4144   5704  -1089   -149    -16       C  
ATOM    490  O   LEU A 116       5.454  22.949 -50.037  1.00 40.38           O  
ANISOU  490  O   LEU A 116     6256   3771   5315  -1192   -130     41       O  
ATOM    491  CB  LEU A 116       6.789  21.733 -47.319  1.00 38.77           C  
ANISOU  491  CB  LEU A 116     5669   3867   5195  -1241    -98    -65       C  
ATOM    492  CG  LEU A 116       7.917  22.197 -46.377  1.00 42.21           C  
ANISOU  492  CG  LEU A 116     6061   4377   5602  -1416   -100    -89       C  
ATOM    493  CD1 LEU A 116       8.603  21.013 -45.675  1.00 37.01           C  
ANISOU  493  CD1 LEU A 116     5143   3943   4976  -1387    -64   -101       C  
ATOM    494  CD2 LEU A 116       8.930  23.049 -47.121  1.00 43.85           C  
ANISOU  494  CD2 LEU A 116     6355   4572   5734  -1652    -79    -46       C  
ATOM    495  N   ALA A 117       3.971  21.782 -48.802  1.00 38.62           N  
ANISOU  495  N   ALA A 117     5868   3608   5197   -895   -165    -39       N  
ATOM    496  CA  ALA A 117       3.137  21.418 -49.945  1.00 40.30           C  
ANISOU  496  CA  ALA A 117     6107   3803   5401   -790   -170     -5       C  
ATOM    497  C   ALA A 117       2.636  22.661 -50.670  1.00 43.25           C  
ANISOU  497  C   ALA A 117     6718   3998   5716   -786   -221     35       C  
ATOM    498  O   ALA A 117       2.778  22.790 -51.904  1.00 39.48           O  
ANISOU  498  O   ALA A 117     6312   3501   5186   -837   -209     95       O  
ATOM    499  CB  ALA A 117       1.948  20.538 -49.500  1.00 31.93           C  
ANISOU  499  CB  ALA A 117     4939   2795   4397   -600   -190    -44       C  
ATOM    500  N   THR A 118       2.087  23.605 -49.911  1.00 41.07           N  
ANISOU  500  N   THR A 118     6580   3586   5440   -722   -277      5       N  
ATOM    501  CA  THR A 118       1.513  24.786 -50.542  1.00 45.00           C  
ANISOU  501  CA  THR A 118     7324   3893   5879   -679   -331     45       C  
ATOM    502  C   THR A 118       2.599  25.760 -50.997  1.00 40.33           C  
ANISOU  502  C   THR A 118     6908   3195   5221   -900   -315     93       C  
ATOM    503  O   THR A 118       2.340  26.609 -51.836  1.00 46.17           O  
ANISOU  503  O   THR A 118     7858   3786   5897   -901   -345    152       O  
ATOM    504  CB  THR A 118       0.499  25.493 -49.611  1.00 49.77           C  
ANISOU  504  CB  THR A 118     8037   4377   6498   -507   -392     -8       C  
ATOM    505  OG1 THR A 118       1.127  25.837 -48.373  1.00 50.77           O  
ANISOU  505  OG1 THR A 118     8169   4483   6639   -598   -383    -69       O  
ATOM    506  CG2 THR A 118      -0.689  24.562 -49.331  1.00 44.84           C  
ANISOU  506  CG2 THR A 118     7238   3874   5925   -296   -407    -44       C  
ATOM    507  N   SER A 119       3.820  25.605 -50.483  1.00 39.38           N  
ANISOU  507  N   SER A 119     6694   3164   5103  -1092   -267     74       N  
ATOM    508  CA  SER A 119       4.942  26.434 -50.927  1.00 41.43           C  
ANISOU  508  CA  SER A 119     7086   3364   5292  -1341   -242    121       C  
ATOM    509  C   SER A 119       5.350  26.124 -52.374  1.00 37.78           C  
ANISOU  509  C   SER A 119     6608   2970   4779  -1423   -196    202       C  
ATOM    510  O   SER A 119       6.077  26.896 -52.992  1.00 43.05           O  
ANISOU  510  O   SER A 119     7419   3569   5370  -1617   -178    259       O  
ATOM    511  CB  SER A 119       6.158  26.262 -50.012  1.00 44.93           C  
ANISOU  511  CB  SER A 119     7391   3936   5744  -1527   -205     79       C  
ATOM    512  OG  SER A 119       6.819  25.038 -50.292  1.00 43.52           O  
ANISOU  512  OG  SER A 119     6950   3996   5592  -1555   -138     89       O  
ATOM    513  N   THR A 120       4.872  25.013 -52.925  1.00 45.15           N  
ANISOU  513  N   THR A 120     7379   4032   5744  -1287   -175    206       N  
ATOM    514  CA  THR A 120       5.190  24.711 -54.316  1.00 46.45           C  
ANISOU  514  CA  THR A 120     7539   4260   5849  -1353   -131    274       C  
ATOM    515  C   THR A 120       4.259  25.437 -55.287  1.00 53.47           C  
ANISOU  515  C   THR A 120     8653   4985   6678  -1263   -189    337       C  
ATOM    516  O   THR A 120       4.558  25.547 -56.478  1.00 58.44           O  
ANISOU  516  O   THR A 120     9351   5622   7230  -1348   -162    407       O  
ATOM    517  CB  THR A 120       5.115  23.211 -54.616  1.00 40.62           C  
ANISOU  517  CB  THR A 120     6560   3720   5155  -1258    -82    250       C  
ATOM    518  OG1 THR A 120       3.742  22.789 -54.656  1.00 38.18           O  
ANISOU  518  OG1 THR A 120     6244   3379   4882  -1038   -136    228       O  
ATOM    519  CG2 THR A 120       5.919  22.397 -53.587  1.00 38.74           C  
ANISOU  519  CG2 THR A 120     6097   3643   4979  -1298    -33    192       C  
ATOM    520  N   LEU A 121       3.131  25.925 -54.777  1.00 52.30           N  
ANISOU  520  N   LEU A 121     8614   4700   6556  -1080   -267    313       N  
ATOM    521  CA  LEU A 121       2.097  26.510 -55.635  1.00 45.81           C  
ANISOU  521  CA  LEU A 121     7980   3747   5680   -940   -333    372       C  
ATOM    522  C   LEU A 121       2.497  27.770 -56.405  1.00 42.78           C  
ANISOU  522  C   LEU A 121     7883   3177   5194  -1073   -346    461       C  
ATOM    523  O   LEU A 121       2.006  27.966 -57.511  1.00 46.79           O  
ANISOU  523  O   LEU A 121     8503   3643   5634  -1013   -374    535       O  
ATOM    524  CB  LEU A 121       0.842  26.809 -54.809  1.00 44.78           C  
ANISOU  524  CB  LEU A 121     7891   3527   5597   -701   -409    322       C  
ATOM    525  CG  LEU A 121       0.091  25.574 -54.317  1.00 48.26           C  
ANISOU  525  CG  LEU A 121     8075   4144   6117   -540   -409    255       C  
ATOM    526  CD1 LEU A 121      -1.107  25.968 -53.462  1.00 46.30           C  
ANISOU  526  CD1 LEU A 121     7865   3825   5904   -317   -477    206       C  
ATOM    527  CD2 LEU A 121      -0.347  24.729 -55.486  1.00 49.48           C  
ANISOU  527  CD2 LEU A 121     8134   4422   6244   -488   -405    292       C  
ATOM    528  N   PRO A 122       3.352  28.648 -55.828  1.00 43.50           N  
ANISOU  528  N   PRO A 122     8110   3152   5265  -1259   -331    458       N  
ATOM    529  CA  PRO A 122       3.686  29.803 -56.664  1.00 47.82           C  
ANISOU  529  CA  PRO A 122     8908   3555   5706  -1376   -337    544       C  
ATOM    530  C   PRO A 122       4.435  29.363 -57.925  1.00 49.18           C  
ANISOU  530  C   PRO A 122     9034   3845   5806  -1549   -271    622       C  
ATOM    531  O   PRO A 122       4.288  29.993 -58.963  1.00 48.69           O  
ANISOU  531  O   PRO A 122     9139   3712   5651  -1555   -287    705       O  
ATOM    532  CB  PRO A 122       4.569  30.659 -55.754  1.00 44.78           C  
ANISOU  532  CB  PRO A 122     8560   3139   5314  -1536   -316    496       C  
ATOM    533  CG  PRO A 122       4.153  30.243 -54.328  1.00 39.16           C  
ANISOU  533  CG  PRO A 122     7735   2439   4704  -1417   -341    391       C  
ATOM    534  CD  PRO A 122       3.855  28.792 -54.443  1.00 43.62           C  
ANISOU  534  CD  PRO A 122     8070   3164   5338  -1334   -321    374       C  
ATOM    535  N   PHE A 123       5.204  28.283 -57.822  1.00 47.23           N  
ANISOU  535  N   PHE A 123     8530   3817   5598  -1654   -195    586       N  
ATOM    536  CA  PHE A 123       5.896  27.727 -58.971  1.00 49.45           C  
ANISOU  536  CA  PHE A 123     8718   4258   5812  -1782   -119    641       C  
ATOM    537  C   PHE A 123       4.877  27.214 -59.969  1.00 50.51           C  
ANISOU  537  C   PHE A 123     8852   4419   5921  -1587   -153    674       C  
ATOM    538  O   PHE A 123       4.999  27.437 -61.168  1.00 45.72           O  
ANISOU  538  O   PHE A 123     8354   3805   5211  -1656   -137    757       O  
ATOM    539  CB  PHE A 123       6.844  26.602 -58.553  1.00 47.20           C  
ANISOU  539  CB  PHE A 123     8123   4229   5582  -1867    -31    577       C  
ATOM    540  CG  PHE A 123       7.971  27.062 -57.681  1.00 52.90           C  
ANISOU  540  CG  PHE A 123     8815   4974   6310  -2086      4    552       C  
ATOM    541  CD1 PHE A 123       9.146  27.527 -58.244  1.00 48.68           C  
ANISOU  541  CD1 PHE A 123     8309   4505   5684  -2349     70    607       C  
ATOM    542  CD2 PHE A 123       7.844  27.046 -56.286  1.00 52.61           C  
ANISOU  542  CD2 PHE A 123     8710   4917   6361  -2027    -33    469       C  
ATOM    543  CE1 PHE A 123      10.186  27.968 -57.446  1.00 54.63           C  
ANISOU  543  CE1 PHE A 123     8981   5340   6434  -2515     93    568       C  
ATOM    544  CE2 PHE A 123       8.880  27.481 -55.473  1.00 53.99           C  
ANISOU  544  CE2 PHE A 123     8856   5127   6529  -2239     -9    443       C  
ATOM    545  CZ  PHE A 123      10.056  27.944 -56.050  1.00 56.09           C  
ANISOU  545  CZ  PHE A 123     9105   5501   6705  -2462     50    486       C  
ATOM    546  N   GLN A 124       3.857  26.535 -59.462  1.00 45.14           N  
ANISOU  546  N   GLN A 124     8049   3778   5326  -1354   -202    608       N  
ATOM    547  CA  GLN A 124       2.838  25.966 -60.324  1.00 44.59           C  
ANISOU  547  CA  GLN A 124     7950   3761   5231  -1175   -241    626       C  
ATOM    548  C   GLN A 124       1.976  27.046 -61.004  1.00 43.50           C  
ANISOU  548  C   GLN A 124     8087   3433   5010  -1076   -331    713       C  
ATOM    549  O   GLN A 124       1.553  26.888 -62.158  1.00 44.51           O  
ANISOU  549  O   GLN A 124     8259   3598   5056  -1028   -350    774       O  
ATOM    550  CB  GLN A 124       1.976  24.988 -59.517  1.00 39.69           C  
ANISOU  550  CB  GLN A 124     7122   3239   4718   -976   -269    533       C  
ATOM    551  CG  GLN A 124       2.739  23.731 -59.096  1.00 38.35           C  
ANISOU  551  CG  GLN A 124     6688   3266   4616  -1044   -181    462       C  
ATOM    552  CD  GLN A 124       1.842  22.639 -58.528  1.00 39.87           C  
ANISOU  552  CD  GLN A 124     6695   3560   4896   -863   -203    384       C  
ATOM    553  OE1 GLN A 124       0.845  22.252 -59.141  1.00 43.98           O  
ANISOU  553  OE1 GLN A 124     7206   4109   5394   -733   -249    389       O  
ATOM    554  NE2 GLN A 124       2.190  22.145 -57.334  1.00 39.78           N  
ANISOU  554  NE2 GLN A 124     6534   3606   4975   -865   -173    314       N  
ATOM    555  N   SER A 125       1.728  28.156 -60.320  1.00 43.64           N  
ANISOU  555  N   SER A 125     8303   3243   5035  -1039   -387    723       N  
ATOM    556  CA  SER A 125       0.916  29.190 -60.950  1.00 48.45           C  
ANISOU  556  CA  SER A 125     9188   3659   5561   -918   -473    811       C  
ATOM    557  C   SER A 125       1.688  29.888 -62.074  1.00 53.29           C  
ANISOU  557  C   SER A 125    10016   4189   6044  -1124   -440    928       C  
ATOM    558  O   SER A 125       1.117  30.187 -63.124  1.00 54.37           O  
ANISOU  558  O   SER A 125    10293   4280   6085  -1041   -489   1017       O  
ATOM    559  CB  SER A 125       0.425  30.202 -59.928  1.00 52.54           C  
ANISOU  559  CB  SER A 125     9888   3958   6116   -802   -537    785       C  
ATOM    560  OG  SER A 125       1.504  30.904 -59.357  1.00 75.41           O  
ANISOU  560  OG  SER A 125    12832   6808   9012  -1010   -481    756       O  
ATOM    561  N   VAL A 126       2.978  30.143 -61.864  1.00 53.95           N  
ANISOU  561  N   VAL A 126    10076   4306   6118  -1381   -356    916       N  
ATOM    562  CA  VAL A 126       3.801  30.719 -62.928  1.00 55.50           C  
ANISOU  562  CA  VAL A 126    10377   4517   6192  -1577   -306    997       C  
ATOM    563  C   VAL A 126       3.877  29.749 -64.096  1.00 58.00           C  
ANISOU  563  C   VAL A 126    10612   4983   6443  -1623   -263   1055       C  
ATOM    564  O   VAL A 126       3.685  30.138 -65.242  1.00 54.86           O  
ANISOU  564  O   VAL A 126    10356   4559   5930  -1622   -280   1145       O  
ATOM    565  CB  VAL A 126       5.228  31.044 -62.464  1.00 49.55           C  
ANISOU  565  CB  VAL A 126     9555   3832   5439  -1846   -220    961       C  
ATOM    566  CG1 VAL A 126       6.082  31.518 -63.659  1.00 49.00           C  
ANISOU  566  CG1 VAL A 126     9571   3810   5237  -2053   -162   1046       C  
ATOM    567  CG2 VAL A 126       5.199  32.103 -61.378  1.00 55.65           C  
ANISOU  567  CG2 VAL A 126    10443   4452   6251  -1824   -263    908       C  
ATOM    568  N   ASN A 127       4.158  28.483 -63.792  1.00 52.00           N  
ANISOU  568  N   ASN A 127     9568   4433   5758  -1627   -203    975       N  
ATOM    569  CA  ASN A 127       4.202  27.440 -64.816  1.00 53.22           C  
ANISOU  569  CA  ASN A 127     9561   4795   5863  -1618   -152    977       C  
ATOM    570  C   ASN A 127       2.934  27.445 -65.669  1.00 56.52           C  
ANISOU  570  C   ASN A 127    10078   5176   6220  -1409   -246   1026       C  
ATOM    571  O   ASN A 127       2.989  27.360 -66.902  1.00 60.11           O  
ANISOU  571  O   ASN A 127    10594   5690   6554  -1457   -229   1096       O  
ATOM    572  CB  ASN A 127       4.411  26.073 -64.165  1.00 48.58           C  
ANISOU  572  CB  ASN A 127     8650   4419   5389  -1567    -95    856       C  
ATOM    573  CG  ASN A 127       4.553  24.951 -65.178  1.00 54.89           C  
ANISOU  573  CG  ASN A 127     9296   5423   6136  -1567    -31    843       C  
ATOM    574  OD1 ASN A 127       5.583  24.816 -65.832  1.00 56.64           O  
ANISOU  574  OD1 ASN A 127     9488   5752   6281  -1748     66    872       O  
ATOM    575  ND2 ASN A 127       3.519  24.125 -65.293  1.00 58.04           N  
ANISOU  575  ND2 ASN A 127     9596   5885   6571  -1368    -82    793       N  
ATOM    576  N   TYR A 128       1.789  27.565 -65.008  1.00 54.39           N  
ANISOU  576  N   TYR A 128     9819   4824   6024  -1177   -345    989       N  
ATOM    577  CA  TYR A 128       0.535  27.673 -65.726  1.00 52.46           C  
ANISOU  577  CA  TYR A 128     9659   4555   5717   -966   -448   1039       C  
ATOM    578  C   TYR A 128       0.483  28.980 -66.515  1.00 60.78           C  
ANISOU  578  C   TYR A 128    11048   5409   6639   -998   -498   1179       C  
ATOM    579  O   TYR A 128       0.172  28.975 -67.698  1.00 63.85           O  
ANISOU  579  O   TYR A 128    11514   5839   6907   -976   -525   1259       O  
ATOM    580  CB  TYR A 128      -0.669  27.590 -64.787  1.00 48.08           C  
ANISOU  580  CB  TYR A 128     9033   3971   5264   -708   -540    971       C  
ATOM    581  CG  TYR A 128      -1.916  28.121 -65.446  1.00 55.86           C  
ANISOU  581  CG  TYR A 128    10163   4891   6169   -490   -660   1045       C  
ATOM    582  CD1 TYR A 128      -2.587  27.369 -66.403  1.00 66.48           C  
ANISOU  582  CD1 TYR A 128    11403   6408   7450   -405   -696   1056       C  
ATOM    583  CD2 TYR A 128      -2.394  29.394 -65.156  1.00 60.53           C  
ANISOU  583  CD2 TYR A 128    11009   5251   6737   -368   -739   1108       C  
ATOM    584  CE1 TYR A 128      -3.714  27.869 -67.044  1.00 73.95           C  
ANISOU  584  CE1 TYR A 128    12469   7320   8308   -204   -814   1132       C  
ATOM    585  CE2 TYR A 128      -3.520  29.899 -65.786  1.00 69.35           C  
ANISOU  585  CE2 TYR A 128    12259   6320   7772   -145   -853   1185       C  
ATOM    586  CZ  TYR A 128      -4.176  29.131 -66.728  1.00 72.55           C  
ANISOU  586  CZ  TYR A 128    12531   6923   8112    -63   -893   1200       C  
ATOM    587  OH  TYR A 128      -5.296  29.623 -67.356  1.00 78.41           O  
ANISOU  587  OH  TYR A 128    13384   7645   8763    164  -1014   1280       O  
ATOM    588  N   LEU A 129       0.787  30.091 -65.849  1.00 56.37           N  
ANISOU  588  N   LEU A 129    10697   4627   6094  -1054   -511   1207       N  
ATOM    589  CA  LEU A 129       0.630  31.422 -66.427  1.00 69.09           C  
ANISOU  589  CA  LEU A 129    12571   6071   7607  -1032   -558   1295       C  
ATOM    590  C   LEU A 129       1.487  31.634 -67.671  1.00 70.23           C  
ANISOU  590  C   LEU A 129    12792   6274   7619  -1250   -491   1380       C  
ATOM    591  O   LEU A 129       1.072  32.307 -68.609  1.00 69.72           O  
ANISOU  591  O   LEU A 129    12902   6143   7445  -1186   -542   1470       O  
ATOM    592  CB  LEU A 129       0.972  32.485 -65.383  1.00 78.99           C  
ANISOU  592  CB  LEU A 129    13914   7172   8924  -1063   -553   1238       C  
ATOM    593  CG  LEU A 129      -0.103  33.468 -64.921  1.00 83.11           C  
ANISOU  593  CG  LEU A 129    14599   7518   9463   -804   -654   1234       C  
ATOM    594  CD1 LEU A 129      -1.434  32.776 -64.687  1.00 84.41           C  
ANISOU  594  CD1 LEU A 129    14661   7732   9678   -509   -742   1212       C  
ATOM    595  CD2 LEU A 129       0.368  34.146 -63.647  1.00 77.92           C  
ANISOU  595  CD2 LEU A 129    13968   6756   8883   -867   -627   1146       C  
ATOM    596  N   MET A 130       2.687  31.061 -67.661  1.00 64.72           N  
ANISOU  596  N   MET A 130    11949   5713   6928  -1499   -374   1348       N  
ATOM    597  CA  MET A 130       3.645  31.248 -68.744  1.00 65.26           C  
ANISOU  597  CA  MET A 130    12057   5864   6873  -1725   -292   1414       C  
ATOM    598  C   MET A 130       3.489  30.154 -69.778  1.00 62.59           C  
ANISOU  598  C   MET A 130    11627   5704   6452  -1725   -263   1451       C  
ATOM    599  O   MET A 130       3.985  30.269 -70.901  1.00 62.15           O  
ANISOU  599  O   MET A 130    11624   5723   6266  -1856   -213   1518       O  
ATOM    600  CB  MET A 130       5.082  31.258 -68.205  1.00 66.92           C  
ANISOU  600  CB  MET A 130    12143   6162   7120  -1991   -178   1357       C  
ATOM    601  CG  MET A 130       5.365  32.363 -67.198  1.00 64.58           C  
ANISOU  601  CG  MET A 130    11947   5708   6883  -2029   -202   1315       C  
ATOM    602  SD  MET A 130       4.795  33.968 -67.788  1.00110.82           S  
ANISOU  602  SD  MET A 130    18149  11317  12639  -1950   -289   1406       S  
ATOM    603  CE  MET A 130       4.995  34.953 -66.308  1.00 97.02           C  
ANISOU  603  CE  MET A 130    16480   9402  10981  -1962   -313   1322       C  
ATOM    604  N   GLY A 131       2.792  29.091 -69.385  1.00 56.38           N  
ANISOU  604  N   GLY A 131    10668   5011   5742  -1565   -293   1384       N  
ATOM    605  CA  GLY A 131       2.644  27.912 -70.218  1.00 58.99           C  
ANISOU  605  CA  GLY A 131    10804   5579   6031  -1528   -258   1344       C  
ATOM    606  C   GLY A 131       3.966  27.182 -70.383  1.00 64.64           C  
ANISOU  606  C   GLY A 131    11339   6484   6739  -1754   -105   1296       C  
ATOM    607  O   GLY A 131       4.190  26.512 -71.388  1.00 64.99           O  
ANISOU  607  O   GLY A 131    11312   6693   6687  -1801    -48   1300       O  
ATOM    608  N   THR A 132       4.838  27.300 -69.386  1.00 69.77           N  
ANISOU  608  N   THR A 132    11907   7119   7482  -1884    -40   1246       N  
ATOM    609  CA  THR A 132       6.196  26.765 -69.469  1.00 67.42           C  
ANISOU  609  CA  THR A 132    11439   7006   7171  -2102    105   1212       C  
ATOM    610  C   THR A 132       6.889  26.838 -68.112  1.00 65.58           C  
ANISOU  610  C   THR A 132    11087   6763   7069  -2184    141   1140       C  
ATOM    611  O   THR A 132       6.616  27.742 -67.328  1.00 71.86           O  
ANISOU  611  O   THR A 132    12032   7359   7913  -2172     70   1157       O  
ATOM    612  CB  THR A 132       7.016  27.535 -70.526  1.00 72.21           C  
ANISOU  612  CB  THR A 132    12232   7602   7605  -2345    171   1336       C  
ATOM    613  OG1 THR A 132       6.514  27.203 -71.818  1.00 86.38           O  
ANISOU  613  OG1 THR A 132    14082   9470   9271  -2276    158   1385       O  
ATOM    614  CG2 THR A 132       8.489  27.190 -70.485  1.00 62.52           C  
ANISOU  614  CG2 THR A 132    10814   6575   6366  -2574    319   1298       C  
ATOM    615  N   TRP A 133       7.766  25.874 -67.838  1.00 66.53           N  
ANISOU  615  N   TRP A 133    10941   7100   7237  -2254    248   1057       N  
ATOM    616  CA  TRP A 133       8.600  25.887 -66.642  1.00 61.84           C  
ANISOU  616  CA  TRP A 133    10208   6544   6743  -2358    292    997       C  
ATOM    617  C   TRP A 133       9.847  26.736 -66.852  1.00 59.29           C  
ANISOU  617  C   TRP A 133     9965   6238   6326  -2662    370   1068       C  
ATOM    618  O   TRP A 133      10.739  26.349 -67.602  1.00 60.46           O  
ANISOU  618  O   TRP A 133     9998   6586   6388  -2795    479   1081       O  
ATOM    619  CB  TRP A 133       9.006  24.462 -66.249  1.00 58.39           C  
ANISOU  619  CB  TRP A 133     9450   6343   6393  -2281    369    884       C  
ATOM    620  CG  TRP A 133       9.804  24.409 -64.980  1.00 50.86           C  
ANISOU  620  CG  TRP A 133     8337   5448   5540  -2359    402    823       C  
ATOM    621  CD1 TRP A 133      11.165  24.432 -64.861  1.00 46.65           C  
ANISOU  621  CD1 TRP A 133     7675   5077   4972  -2573    505    825       C  
ATOM    622  CD2 TRP A 133       9.283  24.344 -63.648  1.00 47.28           C  
ANISOU  622  CD2 TRP A 133     7831   4909   5226  -2229    328    752       C  
ATOM    623  NE1 TRP A 133      11.524  24.376 -63.530  1.00 48.85           N  
ANISOU  623  NE1 TRP A 133     7823   5378   5361  -2581    492    761       N  
ATOM    624  CE2 TRP A 133      10.386  24.324 -62.767  1.00 45.41           C  
ANISOU  624  CE2 TRP A 133     7440   4784   5032  -2373    386    715       C  
ATOM    625  CE3 TRP A 133       7.990  24.300 -63.112  1.00 49.31           C  
ANISOU  625  CE3 TRP A 133     8147   5023   5568  -2006    220    716       C  
ATOM    626  CZ2 TRP A 133      10.236  24.259 -61.386  1.00 42.74           C  
ANISOU  626  CZ2 TRP A 133     7019   4407   4812  -2301    337    645       C  
ATOM    627  CZ3 TRP A 133       7.845  24.234 -61.740  1.00 49.26           C  
ANISOU  627  CZ3 TRP A 133     8054   4980   5681  -1936    181    646       C  
ATOM    628  CH2 TRP A 133       8.960  24.214 -60.893  1.00 43.25           C  
ANISOU  628  CH2 TRP A 133     7155   4321   4956  -2083    238    611       C  
ATOM    629  N   PRO A 134       9.925  27.892 -66.174  1.00 58.76           N  
ANISOU  629  N   PRO A 134    10021   6016   6291  -2699    302   1067       N  
ATOM    630  CA  PRO A 134      11.037  28.823 -66.401  1.00 62.74           C  
ANISOU  630  CA  PRO A 134    10561   6561   6716  -2919    345   1094       C  
ATOM    631  C   PRO A 134      12.160  28.717 -65.371  1.00 50.81           C  
ANISOU  631  C   PRO A 134     8841   5197   5269  -3061    400   1021       C  
ATOM    632  O   PRO A 134      13.137  29.462 -65.473  1.00 59.07           O  
ANISOU  632  O   PRO A 134     9900   6297   6249  -3257    433   1037       O  
ATOM    633  CB  PRO A 134      10.353  30.183 -66.284  1.00 69.76           C  
ANISOU  633  CB  PRO A 134    11743   7175   7589  -2864    233   1135       C  
ATOM    634  CG  PRO A 134       9.345  29.939 -65.151  1.00 57.66           C  
ANISOU  634  CG  PRO A 134    10208   5510   6191  -2651    147   1072       C  
ATOM    635  CD  PRO A 134       8.886  28.489 -65.312  1.00 56.68           C  
ANISOU  635  CD  PRO A 134     9907   5515   6113  -2530    179   1047       C  
ATOM    636  N   PHE A 135      12.015  27.827 -64.388  1.00 55.00           N  
ANISOU  636  N   PHE A 135     9185   5793   5919  -2966    403    945       N  
ATOM    637  CA  PHE A 135      12.877  27.880 -63.210  1.00 57.77           C  
ANISOU  637  CA  PHE A 135     9371   6242   6338  -3065    421    876       C  
ATOM    638  C   PHE A 135      14.142  27.021 -63.313  1.00 56.13           C  
ANISOU  638  C   PHE A 135     8864   6353   6108  -3192    544    849       C  
ATOM    639  O   PHE A 135      14.960  26.998 -62.392  1.00 59.02           O  
ANISOU  639  O   PHE A 135     9064   6845   6518  -3278    561    797       O  
ATOM    640  CB  PHE A 135      12.077  27.478 -61.965  1.00 55.28           C  
ANISOU  640  CB  PHE A 135     9017   5825   6162  -2894    351    805       C  
ATOM    641  CG  PHE A 135      10.883  28.362 -61.698  1.00 56.90           C  
ANISOU  641  CG  PHE A 135     9489   5738   6392  -2748    231    818       C  
ATOM    642  CD1 PHE A 135      11.052  29.639 -61.176  1.00 56.92           C  
ANISOU  642  CD1 PHE A 135     9657   5595   6375  -2820    176    814       C  
ATOM    643  CD2 PHE A 135       9.592  27.912 -61.960  1.00 50.55           C  
ANISOU  643  CD2 PHE A 135     8769   4815   5624  -2531    174    831       C  
ATOM    644  CE1 PHE A 135       9.961  30.457 -60.931  1.00 56.48           C  
ANISOU  644  CE1 PHE A 135     9842   5281   6336  -2662     75    822       C  
ATOM    645  CE2 PHE A 135       8.497  28.720 -61.711  1.00 55.57           C  
ANISOU  645  CE2 PHE A 135     9629   5208   6279  -2370     65    841       C  
ATOM    646  CZ  PHE A 135       8.680  29.997 -61.199  1.00 57.52           C  
ANISOU  646  CZ  PHE A 135    10036   5313   6507  -2428     19    836       C  
ATOM    647  N   GLY A 136      14.294  26.302 -64.418  1.00 59.18           N  
ANISOU  647  N   GLY A 136     9178   6885   6423  -3189    630    881       N  
ATOM    648  CA  GLY A 136      15.487  25.502 -64.628  1.00 59.81           C  
ANISOU  648  CA  GLY A 136     8975   7280   6468  -3279    756    855       C  
ATOM    649  C   GLY A 136      15.430  24.093 -64.057  1.00 59.64           C  
ANISOU  649  C   GLY A 136     8709   7414   6540  -3144    812    787       C  
ATOM    650  O   GLY A 136      14.470  23.704 -63.371  1.00 56.97           O  
ANISOU  650  O   GLY A 136     8390   6941   6315  -2940    732    736       O  
ATOM    651  N   ASN A 137      16.486  23.333 -64.325  1.00 58.55           N  
ANISOU  651  N   ASN A 137     8313   7572   6361  -3188    933    762       N  
ATOM    652  CA  ASN A 137      16.523  21.916 -64.001  1.00 58.79           C  
ANISOU  652  CA  ASN A 137     8094   7772   6472  -2972    984    677       C  
ATOM    653  C   ASN A 137      16.663  21.632 -62.505  1.00 62.87           C  
ANISOU  653  C   ASN A 137     8451   8315   7121  -2897    933    610       C  
ATOM    654  O   ASN A 137      16.030  20.706 -61.985  1.00 62.36           O  
ANISOU  654  O   ASN A 137     8308   8220   7164  -2648    898    541       O  
ATOM    655  CB  ASN A 137      17.663  21.243 -64.766  1.00 62.85           C  
ANISOU  655  CB  ASN A 137     8389   8602   6889  -3029   1136    674       C  
ATOM    656  CG  ASN A 137      17.526  19.730 -64.805  1.00 72.74           C  
ANISOU  656  CG  ASN A 137     9455   9981   8204  -2747   1188    586       C  
ATOM    657  OD1 ASN A 137      16.460  19.196 -65.122  1.00 75.71           O  
ANISOU  657  OD1 ASN A 137     9940  10206   8620  -2549   1141    555       O  
ATOM    658  ND2 ASN A 137      18.606  19.030 -64.470  1.00 72.75           N  
ANISOU  658  ND2 ASN A 137     9175  10259   8207  -2727   1284    546       N  
ATOM    659  N   ILE A 138      17.488  22.419 -61.817  1.00 66.07           N  
ANISOU  659  N   ILE A 138     8815   8781   7509  -3123    928    630       N  
ATOM    660  CA  ILE A 138      17.712  22.220 -60.386  1.00 60.37           C  
ANISOU  660  CA  ILE A 138     7940   8107   6893  -3078    879    570       C  
ATOM    661  C   ILE A 138      16.435  22.450 -59.577  1.00 58.79           C  
ANISOU  661  C   ILE A 138     7917   7618   6804  -2919    747    537       C  
ATOM    662  O   ILE A 138      16.079  21.639 -58.722  1.00 55.22           O  
ANISOU  662  O   ILE A 138     7338   7182   6459  -2713    714    471       O  
ATOM    663  CB  ILE A 138      18.816  23.147 -59.845  1.00 61.52           C  
ANISOU  663  CB  ILE A 138     8026   8353   6993  -3285    857    574       C  
ATOM    664  CG1 ILE A 138      20.168  22.798 -60.475  1.00 65.07           C  
ANISOU  664  CG1 ILE A 138     8240   9132   7351  -3366    969    583       C  
ATOM    665  CG2 ILE A 138      18.886  23.057 -58.327  1.00 63.48           C  
ANISOU  665  CG2 ILE A 138     8163   8616   7339  -3250    789    517       C  
ATOM    666  CD1 ILE A 138      21.264  23.809 -60.171  1.00 69.94           C  
ANISOU  666  CD1 ILE A 138     8828   9847   7899  -3582    942    591       C  
ATOM    667  N   LEU A 139      15.747  23.549 -59.868  1.00 58.19           N  
ANISOU  667  N   LEU A 139     8136   7281   6693  -3007    676    588       N  
ATOM    668  CA  LEU A 139      14.503  23.885 -59.186  1.00 53.44           C  
ANISOU  668  CA  LEU A 139     7716   6408   6182  -2852    555    561       C  
ATOM    669  C   LEU A 139      13.396  22.906 -59.530  1.00 50.73           C  
ANISOU  669  C   LEU A 139     7362   6011   5902  -2557    534    527       C  
ATOM    670  O   LEU A 139      12.506  22.660 -58.719  1.00 50.16           O  
ANISOU  670  O   LEU A 139     7305   5824   5930  -2376    456    476       O  
ATOM    671  CB  LEU A 139      14.062  25.304 -59.536  1.00 54.08           C  
ANISOU  671  CB  LEU A 139     8123   6229   6198  -2976    487    625       C  
ATOM    672  CG  LEU A 139      14.422  26.373 -58.507  1.00 59.98           C  
ANISOU  672  CG  LEU A 139     8939   6895   6956  -3074    417    595       C  
ATOM    673  CD1 LEU A 139      15.803  26.115 -57.947  1.00 74.88           C  
ANISOU  673  CD1 LEU A 139    10563   9060   8830  -3219    476    561       C  
ATOM    674  CD2 LEU A 139      14.361  27.753 -59.138  1.00 58.92           C  
ANISOU  674  CD2 LEU A 139     9080   6580   6725  -3175    376    652       C  
ATOM    675  N   CYS A 140      13.454  22.361 -60.743  1.00 46.39           N  
ANISOU  675  N   CYS A 140     6790   5553   5284  -2524    604    553       N  
ATOM    676  CA  CYS A 140      12.507  21.342 -61.158  1.00 39.87           C  
ANISOU  676  CA  CYS A 140     5941   4705   4502  -2274    593    514       C  
ATOM    677  C   CYS A 140      12.593  20.135 -60.226  1.00 44.30           C  
ANISOU  677  C   CYS A 140     6268   5391   5175  -2102    610    428       C  
ATOM    678  O   CYS A 140      11.585  19.684 -59.706  1.00 42.75           O  
ANISOU  678  O   CYS A 140     6089   5088   5067  -1915    542    384       O  
ATOM    679  CB  CYS A 140      12.759  20.910 -62.608  1.00 45.66           C  
ANISOU  679  CB  CYS A 140     6673   5549   5125  -2294    681    546       C  
ATOM    680  SG  CYS A 140      11.682  19.560 -63.098  1.00 56.47           S  
ANISOU  680  SG  CYS A 140     8007   6910   6539  -2013    672    482       S  
ATOM    681  N   LYS A 141      13.807  19.636 -60.010  1.00 45.14           N  
ANISOU  681  N   LYS A 141     6153   5730   5268  -2167    700    411       N  
ATOM    682  CA  LYS A 141      14.040  18.523 -59.090  1.00 48.95           C  
ANISOU  682  CA  LYS A 141     6414   6340   5843  -2007    719    342       C  
ATOM    683  C   LYS A 141      13.612  18.852 -57.666  1.00 47.04           C  
ANISOU  683  C   LYS A 141     6183   5988   5700  -1970    622    313       C  
ATOM    684  O   LYS A 141      12.983  18.048 -56.995  1.00 42.01           O  
ANISOU  684  O   LYS A 141     5490   5318   5156  -1778    588    262       O  
ATOM    685  CB  LYS A 141      15.522  18.127 -59.111  1.00 43.96           C  
ANISOU  685  CB  LYS A 141     5545   5996   5162  -2095    829    342       C  
ATOM    686  CG  LYS A 141      15.966  17.554 -60.462  1.00 48.98           C  
ANISOU  686  CG  LYS A 141     6135   6772   5702  -2084    945    354       C  
ATOM    687  CD  LYS A 141      17.441  17.214 -60.478  1.00 55.45           C  
ANISOU  687  CD  LYS A 141     6704   7901   6464  -2161   1058    354       C  
ATOM    688  CE  LYS A 141      17.788  16.346 -61.676  1.00 58.04           C  
ANISOU  688  CE  LYS A 141     6966   8376   6713  -2072   1181    340       C  
ATOM    689  NZ  LYS A 141      17.157  14.992 -61.558  1.00 54.62           N1+
ANISOU  689  NZ  LYS A 141     6501   7894   6359  -1783   1185    268       N1+
ATOM    690  N   ILE A 142      13.953  20.048 -57.209  1.00 45.46           N  
ANISOU  690  N   ILE A 142     6070   5730   5473  -2165    579    343       N  
ATOM    691  CA  ILE A 142      13.680  20.426 -55.837  1.00 45.66           C  
ANISOU  691  CA  ILE A 142     6106   5668   5575  -2152    494    308       C  
ATOM    692  C   ILE A 142      12.186  20.534 -55.577  1.00 40.96           C  
ANISOU  692  C   ILE A 142     5684   4833   5047  -1980    400    286       C  
ATOM    693  O   ILE A 142      11.686  19.987 -54.599  1.00 44.05           O  
ANISOU  693  O   ILE A 142     6003   5208   5526  -1828    358    235       O  
ATOM    694  CB  ILE A 142      14.375  21.748 -55.490  1.00 47.78           C  
ANISOU  694  CB  ILE A 142     6462   5910   5782  -2423    470    340       C  
ATOM    695  CG1 ILE A 142      15.881  21.514 -55.387  1.00 52.98           C  
ANISOU  695  CG1 ILE A 142     6879   6862   6388  -2582    553    346       C  
ATOM    696  CG2 ILE A 142      13.862  22.299 -54.179  1.00 43.29           C  
ANISOU  696  CG2 ILE A 142     5976   5194   5280  -2403    371    298       C  
ATOM    697  CD1 ILE A 142      16.686  22.771 -55.154  1.00 58.67           C  
ANISOU  697  CD1 ILE A 142     7671   7591   7030  -2896    540    378       C  
ATOM    698  N   VAL A 143      11.466  21.225 -56.455  1.00 40.34           N  
ANISOU  698  N   VAL A 143     5826   4581   4920  -1998    367    330       N  
ATOM    699  CA  VAL A 143      10.042  21.440 -56.232  1.00 39.15           C  
ANISOU  699  CA  VAL A 143     5834   4222   4822  -1833    274    314       C  
ATOM    700  C   VAL A 143       9.249  20.143 -56.394  1.00 41.39           C  
ANISOU  700  C   VAL A 143     6012   4550   5165  -1606    280    272       C  
ATOM    701  O   VAL A 143       8.360  19.847 -55.595  1.00 43.75           O  
ANISOU  701  O   VAL A 143     6301   4779   5542  -1455    221    228       O  
ATOM    702  CB  VAL A 143       9.490  22.517 -57.177  1.00 43.03           C  
ANISOU  702  CB  VAL A 143     6589   4526   5234  -1894    232    381       C  
ATOM    703  CG1 VAL A 143       7.972  22.628 -57.034  1.00 43.09           C  
ANISOU  703  CG1 VAL A 143     6727   4356   5289  -1688    138    365       C  
ATOM    704  CG2 VAL A 143      10.161  23.856 -56.872  1.00 40.73           C  
ANISOU  704  CG2 VAL A 143     6444   4144   4887  -2124    216    418       C  
ATOM    705  N   ILE A 144       9.578  19.351 -57.413  1.00 36.81           N  
ANISOU  705  N   ILE A 144     5356   4090   4541  -1591    357    282       N  
ATOM    706  CA  ILE A 144       8.901  18.070 -57.573  1.00 35.39           C  
ANISOU  706  CA  ILE A 144     5090   3949   4409  -1399    369    235       C  
ATOM    707  C   ILE A 144       9.128  17.162 -56.345  1.00 35.24           C  
ANISOU  707  C   ILE A 144     4887   4018   4484  -1300    381    177       C  
ATOM    708  O   ILE A 144       8.195  16.553 -55.816  1.00 36.51           O  
ANISOU  708  O   ILE A 144     5035   4123   4715  -1149    337    137       O  
ATOM    709  CB  ILE A 144       9.359  17.360 -58.855  1.00 45.40           C  
ANISOU  709  CB  ILE A 144     6314   5335   5602  -1409    461    245       C  
ATOM    710  CG1 ILE A 144       8.659  17.987 -60.060  1.00 54.87           C  
ANISOU  710  CG1 ILE A 144     7709   6425   6716  -1439    426    295       C  
ATOM    711  CG2 ILE A 144       9.047  15.882 -58.796  1.00 40.93           C  
ANISOU  711  CG2 ILE A 144     5628   4837   5088  -1237    496    182       C  
ATOM    712  CD1 ILE A 144       8.883  17.228 -61.337  1.00 67.47           C  
ANISOU  712  CD1 ILE A 144     9280   8124   8230  -1428    506    293       C  
ATOM    713  N   SER A 145      10.362  17.104 -55.872  1.00 38.88           N  
ANISOU  713  N   SER A 145     5207   4627   4940  -1391    436    178       N  
ATOM    714  CA  SER A 145      10.682  16.246 -54.748  1.00 37.58           C  
ANISOU  714  CA  SER A 145     4867   4561   4849  -1293    448    135       C  
ATOM    715  C   SER A 145       9.981  16.721 -53.470  1.00 36.36           C  
ANISOU  715  C   SER A 145     4760   4290   4763  -1256    354    112       C  
ATOM    716  O   SER A 145       9.409  15.918 -52.722  1.00 38.14           O  
ANISOU  716  O   SER A 145     4925   4507   5061  -1109    333     74       O  
ATOM    717  CB  SER A 145      12.198  16.188 -54.554  1.00 46.33           C  
ANISOU  717  CB  SER A 145     5802   5880   5920  -1403    520    148       C  
ATOM    718  OG  SER A 145      12.542  15.271 -53.528  1.00 53.31           O  
ANISOU  718  OG  SER A 145     6513   6874   6867  -1285    531    115       O  
ATOM    719  N   ILE A 146      10.014  18.025 -53.224  1.00 37.14           N  
ANISOU  719  N   ILE A 146     4983   4296   4834  -1392    301    133       N  
ATOM    720  CA  ILE A 146       9.296  18.604 -52.082  1.00 37.52           C  
ANISOU  720  CA  ILE A 146     5106   4216   4933  -1354    214    104       C  
ATOM    721  C   ILE A 146       7.813  18.295 -52.186  1.00 37.80           C  
ANISOU  721  C   ILE A 146     5229   4121   5013  -1177    162     84       C  
ATOM    722  O   ILE A 146       7.168  17.906 -51.194  1.00 37.09           O  
ANISOU  722  O   ILE A 146     5095   4010   4987  -1059    125     43       O  
ATOM    723  CB  ILE A 146       9.525  20.141 -51.986  1.00 40.65           C  
ANISOU  723  CB  ILE A 146     5673   4496   5277  -1533    168    128       C  
ATOM    724  CG1 ILE A 146      10.887  20.422 -51.358  1.00 40.23           C  
ANISOU  724  CG1 ILE A 146     5502   4590   5194  -1713    197    127       C  
ATOM    725  CG2 ILE A 146       8.441  20.829 -51.161  1.00 39.50           C  
ANISOU  725  CG2 ILE A 146     5675   4165   5170  -1451     78     96       C  
ATOM    726  CD1 ILE A 146      11.340  21.873 -51.523  1.00 44.81           C  
ANISOU  726  CD1 ILE A 146     6255   5071   5699  -1945    173    158       C  
ATOM    727  N   ASP A 147       7.282  18.426 -53.399  1.00 38.92           N  
ANISOU  727  N   ASP A 147     5482   4194   5111  -1163    163    114       N  
ATOM    728  CA  ASP A 147       5.873  18.175 -53.626  1.00 35.70           C  
ANISOU  728  CA  ASP A 147     5146   3688   4729  -1009    110     99       C  
ATOM    729  C   ASP A 147       5.462  16.722 -53.336  1.00 37.71           C  
ANISOU  729  C   ASP A 147     5256   4027   5043   -870    136     56       C  
ATOM    730  O   ASP A 147       4.469  16.499 -52.634  1.00 36.17           O  
ANISOU  730  O   ASP A 147     5057   3785   4901   -757     85     24       O  
ATOM    731  CB  ASP A 147       5.493  18.534 -55.053  1.00 36.01           C  
ANISOU  731  CB  ASP A 147     5319   3668   4693  -1030    105    145       C  
ATOM    732  CG  ASP A 147       4.014  18.725 -55.205  1.00 39.01           C  
ANISOU  732  CG  ASP A 147     5801   3938   5084   -892     24    141       C  
ATOM    733  OD1 ASP A 147       3.411  19.465 -54.391  1.00 42.81           O1-
ANISOU  733  OD1 ASP A 147     6355   4317   5594   -841    -44    128       O1-
ATOM    734  OD2 ASP A 147       3.439  18.115 -56.115  1.00 43.66           O  
ANISOU  734  OD2 ASP A 147     6389   4554   5646   -830     27    144       O  
ATOM    735  N   TYR A 148       6.192  15.735 -53.863  1.00 30.86           N  
ANISOU  735  N   TYR A 148     4282   3281   4164   -875    217     53       N  
ATOM    736  CA  TYR A 148       5.867  14.346 -53.505  1.00 30.63           C  
ANISOU  736  CA  TYR A 148     4144   3307   4189   -749    245     12       C  
ATOM    737  C   TYR A 148       6.170  14.050 -52.026  1.00 42.01           C  
ANISOU  737  C   TYR A 148     5473   4793   5695   -711    238    -11       C  
ATOM    738  O   TYR A 148       5.379  13.368 -51.366  1.00 40.24           O  
ANISOU  738  O   TYR A 148     5219   4546   5524   -605    215    -40       O  
ATOM    739  CB  TYR A 148       6.599  13.328 -54.389  1.00 32.39           C  
ANISOU  739  CB  TYR A 148     4296   3633   4378   -742    339      8       C  
ATOM    740  CG  TYR A 148       5.971  13.132 -55.767  1.00 33.25           C  
ANISOU  740  CG  TYR A 148     4503   3702   4428   -733    345     10       C  
ATOM    741  CD1 TYR A 148       6.344  13.931 -56.838  1.00 35.79           C  
ANISOU  741  CD1 TYR A 148     4911   4023   4665   -838    359     52       C  
ATOM    742  CD2 TYR A 148       5.023  12.132 -55.992  1.00 34.30           C  
ANISOU  742  CD2 TYR A 148     4646   3806   4580   -633    337    -29       C  
ATOM    743  CE1 TYR A 148       5.783  13.753 -58.113  1.00 40.18           C  
ANISOU  743  CE1 TYR A 148     5558   4555   5153   -830    361     56       C  
ATOM    744  CE2 TYR A 148       4.458  11.949 -57.247  1.00 44.62           C  
ANISOU  744  CE2 TYR A 148     6040   5092   5821   -636    336    -32       C  
ATOM    745  CZ  TYR A 148       4.836  12.771 -58.305  1.00 40.44           C  
ANISOU  745  CZ  TYR A 148     5594   4568   5205   -728    346     11       C  
ATOM    746  OH  TYR A 148       4.272  12.586 -59.551  1.00 36.25           O  
ANISOU  746  OH  TYR A 148     5151   4026   4597   -731    340     10       O  
ATOM    747  N   TYR A 149       7.305  14.526 -51.509  1.00 36.82           N  
ANISOU  747  N   TYR A 149     4751   4212   5026   -805    257      4       N  
ATOM    748  CA  TYR A 149       7.638  14.244 -50.107  1.00 37.07           C  
ANISOU  748  CA  TYR A 149     4673   4305   5106   -771    245    -15       C  
ATOM    749  C   TYR A 149       6.533  14.680 -49.169  1.00 37.46           C  
ANISOU  749  C   TYR A 149     4791   4246   5197   -715    165    -40       C  
ATOM    750  O   TYR A 149       6.170  13.965 -48.258  1.00 35.04           O  
ANISOU  750  O   TYR A 149     4416   3961   4937   -621    157    -62       O  
ATOM    751  CB  TYR A 149       8.916  14.940 -49.682  1.00 32.92           C  
ANISOU  751  CB  TYR A 149     4081   3880   4547   -908    256      3       C  
ATOM    752  CG  TYR A 149      10.074  14.014 -49.509  1.00 43.53           C  
ANISOU  752  CG  TYR A 149     5243   5408   5887   -882    327     11       C  
ATOM    753  CD1 TYR A 149      10.098  13.080 -48.475  1.00 37.88           C  
ANISOU  753  CD1 TYR A 149     4418   4754   5221   -760    327     -4       C  
ATOM    754  CD2 TYR A 149      11.163  14.084 -50.364  1.00 44.24           C  
ANISOU  754  CD2 TYR A 149     5269   5622   5917   -973    395     37       C  
ATOM    755  CE1 TYR A 149      11.190  12.227 -48.314  1.00 38.59           C  
ANISOU  755  CE1 TYR A 149     4344   5018   5302   -710    389     10       C  
ATOM    756  CE2 TYR A 149      12.246  13.250 -50.211  1.00 45.22           C  
ANISOU  756  CE2 TYR A 149     5212   5936   6031   -927    462     44       C  
ATOM    757  CZ  TYR A 149      12.259  12.326 -49.181  1.00 43.82           C  
ANISOU  757  CZ  TYR A 149     4933   5811   5906   -786    456     31       C  
ATOM    758  OH  TYR A 149      13.351  11.492 -49.046  1.00 44.83           O  
ANISOU  758  OH  TYR A 149     4885   6131   6019   -714    520     44       O  
ATOM    759  N   ASN A 150       5.990  15.864 -49.407  1.00 34.86           N  
ANISOU  759  N   ASN A 150     4604   3798   4842   -766    110    -35       N  
ATOM    760  CA  ASN A 150       5.079  16.435 -48.445  1.00 33.87           C  
ANISOU  760  CA  ASN A 150     4543   3583   4745   -711     40    -64       C  
ATOM    761  C   ASN A 150       3.635  16.078 -48.671  1.00 39.64           C  
ANISOU  761  C   ASN A 150     5317   4246   5500   -580      7    -80       C  
ATOM    762  O   ASN A 150       2.840  16.146 -47.741  1.00 38.06           O  
ANISOU  762  O   ASN A 150     5114   4017   5329   -501    -34   -111       O  
ATOM    763  CB  ASN A 150       5.296  17.945 -48.401  1.00 32.81           C  
ANISOU  763  CB  ASN A 150     4550   3349   4568   -823     -4    -56       C  
ATOM    764  CG  ASN A 150       6.602  18.265 -47.751  1.00 40.97           C  
ANISOU  764  CG  ASN A 150     5516   4470   5582   -961     15    -55       C  
ATOM    765  OD1 ASN A 150       6.719  18.173 -46.534  1.00 38.94           O  
ANISOU  765  OD1 ASN A 150     5191   4255   5348   -944     -5    -88       O  
ATOM    766  ND2 ASN A 150       7.617  18.548 -48.549  1.00 34.85           N  
ANISOU  766  ND2 ASN A 150     4737   3749   4756  -1102     57    -18       N  
ATOM    767  N   MET A 151       3.290  15.666 -49.881  1.00 34.21           N  
ANISOU  767  N   MET A 151     4657   3551   4790   -560     25    -62       N  
ATOM    768  CA  MET A 151       2.025  14.980 -50.056  1.00 33.16           C  
ANISOU  768  CA  MET A 151     4516   3404   4677   -448      3    -82       C  
ATOM    769  C   MET A 151       1.994  13.738 -49.152  1.00 37.42           C  
ANISOU  769  C   MET A 151     4928   4019   5269   -388     36   -109       C  
ATOM    770  O   MET A 151       1.023  13.479 -48.453  1.00 31.85           O  
ANISOU  770  O   MET A 151     4199   3308   4593   -312      4   -133       O  
ATOM    771  CB  MET A 151       1.818  14.571 -51.521  1.00 30.95           C  
ANISOU  771  CB  MET A 151     4277   3128   4355   -456     23    -64       C  
ATOM    772  CG  MET A 151       0.639  13.637 -51.728  1.00 29.22           C  
ANISOU  772  CG  MET A 151     4026   2925   4150   -368      8    -90       C  
ATOM    773  SD  MET A 151       0.388  13.217 -53.497  1.00 36.55           S  
ANISOU  773  SD  MET A 151     5016   3861   5008   -393     24    -77       S  
ATOM    774  CE  MET A 151      -1.268  12.587 -53.478  1.00 98.81           C  
ANISOU  774  CE  MET A 151    12877  11762  12902   -308    -32   -111       C  
ATOM    775  N   PHE A 152       3.058  12.954 -49.185  1.00 32.15           N  
ANISOU  775  N   PHE A 152     4179   3429   4607   -416    102   -100       N  
ATOM    776  CA  PHE A 152       3.034  11.705 -48.457  1.00 33.36           C  
ANISOU  776  CA  PHE A 152     4238   3635   4802   -348    135   -115       C  
ATOM    777  C   PHE A 152       3.193  11.943 -46.946  1.00 32.14           C  
ANISOU  777  C   PHE A 152     4026   3508   4677   -333    110   -123       C  
ATOM    778  O   PHE A 152       2.552  11.278 -46.153  1.00 32.92           O  
ANISOU  778  O   PHE A 152     4088   3615   4806   -267    104   -136       O  
ATOM    779  CB  PHE A 152       4.117  10.771 -48.984  1.00 29.45           C  
ANISOU  779  CB  PHE A 152     3682   3210   4296   -352    216   -102       C  
ATOM    780  CG  PHE A 152       3.754  10.118 -50.289  1.00 35.38           C  
ANISOU  780  CG  PHE A 152     4487   3936   5021   -340    249   -110       C  
ATOM    781  CD1 PHE A 152       2.698   9.211 -50.350  1.00 33.62           C  
ANISOU  781  CD1 PHE A 152     4287   3675   4815   -285    243   -136       C  
ATOM    782  CD2 PHE A 152       4.447  10.407 -51.445  1.00 42.08           C  
ANISOU  782  CD2 PHE A 152     5365   4807   5816   -398    287    -96       C  
ATOM    783  CE1 PHE A 152       2.347   8.592 -51.562  1.00 43.27           C  
ANISOU  783  CE1 PHE A 152     5566   4874   5999   -289    269   -153       C  
ATOM    784  CE2 PHE A 152       4.100   9.799 -52.666  1.00 40.07           C  
ANISOU  784  CE2 PHE A 152     5167   4533   5523   -390    318   -110       C  
ATOM    785  CZ  PHE A 152       3.048   8.885 -52.712  1.00 36.91           C  
ANISOU  785  CZ  PHE A 152     4794   4089   5139   -335    306   -142       C  
ATOM    786  N   THR A 153       4.039  12.898 -46.570  1.00 30.70           N  
ANISOU  786  N   THR A 153     3844   3344   4476   -408     96   -114       N  
ATOM    787  CA  THR A 153       4.250  13.222 -45.154  1.00 36.46           C  
ANISOU  787  CA  THR A 153     4530   4107   5218   -409     66   -128       C  
ATOM    788  C   THR A 153       2.959  13.733 -44.518  1.00 41.32           C  
ANISOU  788  C   THR A 153     5209   4647   5845   -351      9   -160       C  
ATOM    789  O   THR A 153       2.589  13.330 -43.422  1.00 37.96           O  
ANISOU  789  O   THR A 153     4730   4254   5438   -296      0   -176       O  
ATOM    790  CB  THR A 153       5.377  14.258 -44.990  1.00 32.18           C  
ANISOU  790  CB  THR A 153     3992   3595   4639   -531     56   -120       C  
ATOM    791  OG1 THR A 153       6.602  13.659 -45.401  1.00 43.11           O  
ANISOU  791  OG1 THR A 153     5275   5095   6010   -569    115    -91       O  
ATOM    792  CG2 THR A 153       5.523  14.695 -43.512  1.00 39.37           C  
ANISOU  792  CG2 THR A 153     4875   4536   5550   -544     15   -145       C  
ATOM    793  N   SER A 154       2.269  14.621 -45.223  1.00 35.75           N  
ANISOU  793  N   SER A 154     4614   3848   5120   -355    -28   -166       N  
ATOM    794  CA  SER A 154       0.986  15.123 -44.772  1.00 30.13           C  
ANISOU  794  CA  SER A 154     3959   3078   4413   -274    -80   -197       C  
ATOM    795  C   SER A 154      -0.022  13.990 -44.577  1.00 33.30           C  
ANISOU  795  C   SER A 154     4284   3527   4841   -186    -67   -207       C  
ATOM    796  O   SER A 154      -0.618  13.828 -43.503  1.00 30.75           O  
ANISOU  796  O   SER A 154     3918   3234   4530   -130    -79   -231       O  
ATOM    797  CB  SER A 154       0.442  16.138 -45.774  1.00 32.55           C  
ANISOU  797  CB  SER A 154     4398   3283   4687   -272   -120   -189       C  
ATOM    798  OG  SER A 154      -0.897  16.481 -45.466  1.00 41.91           O  
ANISOU  798  OG  SER A 154     5616   4436   5873   -160   -166   -216       O  
ATOM    799  N   ILE A 155      -0.188  13.188 -45.616  1.00 29.27           N  
ANISOU  799  N   ILE A 155     3762   3027   4332   -186    -40   -189       N  
ATOM    800  CA  ILE A 155      -1.147  12.108 -45.590  1.00 29.74           C  
ANISOU  800  CA  ILE A 155     3768   3123   4408   -134    -28   -199       C  
ATOM    801  C   ILE A 155      -0.789  11.010 -44.551  1.00 29.10           C  
ANISOU  801  C   ILE A 155     3601   3100   4356   -123     15   -196       C  
ATOM    802  O   ILE A 155      -1.665  10.515 -43.848  1.00 30.63           O  
ANISOU  802  O   ILE A 155     3755   3324   4560    -85     10   -209       O  
ATOM    803  CB  ILE A 155      -1.263  11.492 -46.971  1.00 33.32           C  
ANISOU  803  CB  ILE A 155     4247   3567   4846   -157     -7   -188       C  
ATOM    804  CG1 ILE A 155      -1.951  12.489 -47.920  1.00 34.60           C  
ANISOU  804  CG1 ILE A 155     4493   3684   4971   -146    -62   -185       C  
ATOM    805  CG2 ILE A 155      -2.029  10.191 -46.912  1.00 28.56           C  
ANISOU  805  CG2 ILE A 155     3596   3001   4256   -137     16   -200       C  
ATOM    806  CD1 ILE A 155      -1.954  12.022 -49.362  1.00 40.00           C  
ANISOU  806  CD1 ILE A 155     5213   4365   5621   -181    -45   -173       C  
ATOM    807  N   PHE A 156       0.484  10.624 -44.477  1.00 27.15           N  
ANISOU  807  N   PHE A 156     3322   2878   4114   -154     57   -173       N  
ATOM    808  CA  PHE A 156       0.881   9.595 -43.521  1.00 35.64           C  
ANISOU  808  CA  PHE A 156     4327   4006   5209   -125     93   -158       C  
ATOM    809  C   PHE A 156       0.715  10.115 -42.082  1.00 37.32           C  
ANISOU  809  C   PHE A 156     4507   4251   5419   -108     59   -170       C  
ATOM    810  O   PHE A 156       0.398   9.350 -41.182  1.00 33.95           O  
ANISOU  810  O   PHE A 156     4040   3861   5001    -73     73   -163       O  
ATOM    811  CB  PHE A 156       2.321   9.131 -43.759  1.00 36.23           C  
ANISOU  811  CB  PHE A 156     4362   4122   5282   -138    142   -129       C  
ATOM    812  CG  PHE A 156       2.529   8.420 -45.080  1.00 39.18           C  
ANISOU  812  CG  PHE A 156     4766   4470   5649   -139    190   -123       C  
ATOM    813  CD1 PHE A 156       1.447   7.961 -45.825  1.00 37.97           C  
ANISOU  813  CD1 PHE A 156     4670   4262   5494   -135    188   -143       C  
ATOM    814  CD2 PHE A 156       3.806   8.213 -45.570  1.00 34.65           C  
ANISOU  814  CD2 PHE A 156     4158   3944   5062   -146    238   -103       C  
ATOM    815  CE1 PHE A 156       1.642   7.311 -47.022  1.00 37.19           C  
ANISOU  815  CE1 PHE A 156     4612   4139   5379   -142    233   -146       C  
ATOM    816  CE2 PHE A 156       4.009   7.566 -46.775  1.00 39.49           C  
ANISOU  816  CE2 PHE A 156     4807   4538   5661   -138    290   -106       C  
ATOM    817  CZ  PHE A 156       2.928   7.115 -47.494  1.00 36.30           C  
ANISOU  817  CZ  PHE A 156     4478   4063   5253   -138    287   -130       C  
ATOM    818  N   THR A 157       0.909  11.412 -41.869  1.00 35.45           N  
ANISOU  818  N   THR A 157     4306   3998   5165   -138     17   -190       N  
ATOM    819  CA  THR A 157       0.761  11.966 -40.520  1.00 29.11           C  
ANISOU  819  CA  THR A 157     3489   3223   4349   -124    -14   -214       C  
ATOM    820  C   THR A 157      -0.703  11.986 -40.099  1.00 40.64           C  
ANISOU  820  C   THR A 157     4957   4675   5808    -59    -34   -244       C  
ATOM    821  O   THR A 157      -1.026  11.726 -38.940  1.00 36.65           O  
ANISOU  821  O   THR A 157     4409   4223   5295    -28    -32   -253       O  
ATOM    822  CB  THR A 157       1.339  13.370 -40.418  1.00 29.18           C  
ANISOU  822  CB  THR A 157     3560   3197   4331   -184    -53   -237       C  
ATOM    823  OG1 THR A 157       2.698  13.317 -40.836  1.00 32.54           O  
ANISOU  823  OG1 THR A 157     3955   3659   4749   -261    -30   -207       O  
ATOM    824  CG2 THR A 157       1.295  13.877 -38.937  1.00 31.67           C  
ANISOU  824  CG2 THR A 157     3867   3546   4621   -175    -82   -271       C  
ATOM    825  N   LEU A 158      -1.606  12.272 -41.032  1.00 32.92           N  
ANISOU  825  N   LEU A 158     4025   3652   4831    -36    -51   -256       N  
ATOM    826  CA  LEU A 158      -2.998  12.316 -40.629  1.00 39.65           C  
ANISOU  826  CA  LEU A 158     4859   4531   5675     31    -70   -284       C  
ATOM    827  C   LEU A 158      -3.554  10.887 -40.479  1.00 35.60           C  
ANISOU  827  C   LEU A 158     4272   4079   5174     29    -30   -265       C  
ATOM    828  O   LEU A 158      -4.462  10.664 -39.677  1.00 38.91           O  
ANISOU  828  O   LEU A 158     4643   4560   5582     62    -29   -280       O  
ATOM    829  CB  LEU A 158      -3.816  13.181 -41.597  1.00 44.19           C  
ANISOU  829  CB  LEU A 158     5499   5056   6236     72   -112   -301       C  
ATOM    830  CG  LEU A 158      -4.108  12.758 -43.020  1.00 40.84           C  
ANISOU  830  CG  LEU A 158     5090   4615   5813     53   -111   -279       C  
ATOM    831  CD1 LEU A 158      -5.311  11.837 -43.013  1.00 34.57           C  
ANISOU  831  CD1 LEU A 158     4219   3900   5018     76   -104   -286       C  
ATOM    832  CD2 LEU A 158      -4.356  13.986 -43.910  1.00 38.98           C  
ANISOU  832  CD2 LEU A 158     4953   4305   5551     84   -162   -282       C  
ATOM    833  N   CYS A 159      -3.004   9.917 -41.212  1.00 31.95           N  
ANISOU  833  N   CYS A 159     3811   3599   4731    -13      7   -232       N  
ATOM    834  CA  CYS A 159      -3.305   8.508 -40.905  1.00 36.22           C  
ANISOU  834  CA  CYS A 159     4312   4171   5279    -27     50   -211       C  
ATOM    835  C   CYS A 159      -2.812   8.126 -39.514  1.00 32.67           C  
ANISOU  835  C   CYS A 159     3823   3763   4826    -14     70   -190       C  
ATOM    836  O   CYS A 159      -3.486   7.389 -38.806  1.00 32.07           O  
ANISOU  836  O   CYS A 159     3718   3728   4741    -14     90   -180       O  
ATOM    837  CB  CYS A 159      -2.672   7.556 -41.919  1.00 36.82           C  
ANISOU  837  CB  CYS A 159     4421   4199   5369    -60     91   -186       C  
ATOM    838  SG  CYS A 159      -3.361   7.672 -43.586  1.00 50.44           S  
ANISOU  838  SG  CYS A 159     6194   5888   7081    -89     73   -207       S  
ATOM    839  N   THR A 160      -1.611   8.586 -39.168  1.00 34.07           N  
ANISOU  839  N   THR A 160     4000   3943   5004    -12     65   -179       N  
ATOM    840  CA  THR A 160      -1.007   8.297 -37.875  1.00 40.74           C  
ANISOU  840  CA  THR A 160     4803   4842   5833      2     74   -156       C  
ATOM    841  C   THR A 160      -1.886   8.819 -36.740  1.00 33.74           C  
ANISOU  841  C   THR A 160     3895   4006   4917     23     50   -187       C  
ATOM    842  O   THR A 160      -2.076   8.145 -35.731  1.00 38.71           O  
ANISOU  842  O   THR A 160     4492   4688   5526     34     70   -164       O  
ATOM    843  CB  THR A 160       0.401   8.903 -37.762  1.00 37.63           C  
ANISOU  843  CB  THR A 160     4397   4468   5433    -15     59   -147       C  
ATOM    844  OG1 THR A 160       1.258   8.276 -38.721  1.00 34.59           O  
ANISOU  844  OG1 THR A 160     4012   4063   5069    -21     94   -115       O  
ATOM    845  CG2 THR A 160       0.981   8.658 -36.364  1.00 34.34           C  
ANISOU  845  CG2 THR A 160     3928   4131   4988      2     56   -124       C  
ATOM    846  N   MET A 161      -2.437  10.016 -36.916  1.00 35.12           N  
ANISOU  846  N   MET A 161     4098   4163   5081     37     12   -239       N  
ATOM    847  CA  MET A 161      -3.374  10.573 -35.949  1.00 32.99           C  
ANISOU  847  CA  MET A 161     3814   3944   4778     79     -4   -280       C  
ATOM    848  C   MET A 161      -4.648   9.735 -35.826  1.00 37.13           C  
ANISOU  848  C   MET A 161     4288   4526   5296     91     23   -274       C  
ATOM    849  O   MET A 161      -5.212   9.611 -34.746  1.00 35.82           O  
ANISOU  849  O   MET A 161     4080   4437   5094    109     36   -284       O  
ATOM    850  CB  MET A 161      -3.721  12.018 -36.317  1.00 37.52           C  
ANISOU  850  CB  MET A 161     4449   4467   5341    114    -49   -336       C  
ATOM    851  CG  MET A 161      -2.503  12.948 -36.203  1.00 44.29           C  
ANISOU  851  CG  MET A 161     5368   5273   6189     73    -76   -349       C  
ATOM    852  SD  MET A 161      -2.834  14.681 -36.607  1.00 52.69           S  
ANISOU  852  SD  MET A 161     6554   6235   7232    106   -127   -410       S  
ATOM    853  CE  MET A 161      -3.566  15.243 -35.070  1.00112.37           C  
ANISOU  853  CE  MET A 161    14113  13848  14737    181   -135   -476       C  
ATOM    854  N   SER A 162      -5.104   9.144 -36.919  1.00 29.72           N  
ANISOU  854  N   SER A 162     3352   3561   4382     66     34   -259       N  
ATOM    855  CA  SER A 162      -6.254   8.246 -36.836  1.00 31.27           C  
ANISOU  855  CA  SER A 162     3497   3819   4564     43     61   -251       C  
ATOM    856  C   SER A 162      -5.908   6.970 -36.060  1.00 31.21           C  
ANISOU  856  C   SER A 162     3481   3826   4550     -2    109   -197       C  
ATOM    857  O   SER A 162      -6.664   6.523 -35.194  1.00 36.00           O  
ANISOU  857  O   SER A 162     4044   4511   5122    -18    133   -190       O  
ATOM    858  CB  SER A 162      -6.751   7.876 -38.229  1.00 37.07           C  
ANISOU  858  CB  SER A 162     4245   4522   5317      8     56   -251       C  
ATOM    859  OG  SER A 162      -7.943   7.135 -38.117  1.00 49.11           O  
ANISOU  859  OG  SER A 162     5713   6127   6818    -35     75   -251       O  
ATOM    860  N   VAL A 163      -4.774   6.370 -36.398  1.00 31.62           N  
ANISOU  860  N   VAL A 163     3579   3806   4628    -17    127   -156       N  
ATOM    861  CA  VAL A 163      -4.331   5.148 -35.729  1.00 29.67           C  
ANISOU  861  CA  VAL A 163     3347   3552   4373    -35    169    -96       C  
ATOM    862  C   VAL A 163      -4.082   5.410 -34.222  1.00 32.52           C  
ANISOU  862  C   VAL A 163     3673   3989   4693     -4    165    -83       C  
ATOM    863  O   VAL A 163      -4.400   4.591 -33.362  1.00 35.68           O  
ANISOU  863  O   VAL A 163     4071   4426   5062    -23    196    -41       O  
ATOM    864  CB  VAL A 163      -3.057   4.620 -36.369  1.00 31.59           C  
ANISOU  864  CB  VAL A 163     3639   3716   4647    -19    186    -60       C  
ATOM    865  CG1 VAL A 163      -2.446   3.523 -35.511  1.00 35.01           C  
ANISOU  865  CG1 VAL A 163     4094   4145   5065      1    222      9       C  
ATOM    866  CG2 VAL A 163      -3.354   4.123 -37.796  1.00 32.05           C  
ANISOU  866  CG2 VAL A 163     3747   3700   4732    -56    202    -72       C  
ATOM    867  N   ASP A 164      -3.499   6.561 -33.929  1.00 33.81           N  
ANISOU  867  N   ASP A 164     3822   4174   4851     32    125   -117       N  
ATOM    868  CA  ASP A 164      -3.268   6.993 -32.553  1.00 32.40           C  
ANISOU  868  CA  ASP A 164     3616   4073   4622     55    112   -122       C  
ATOM    869  C   ASP A 164      -4.557   7.019 -31.726  1.00 37.29           C  
ANISOU  869  C   ASP A 164     4200   4776   5195     55    128   -146       C  
ATOM    870  O   ASP A 164      -4.592   6.524 -30.605  1.00 36.67           O  
ANISOU  870  O   ASP A 164     4104   4762   5067     50    149   -112       O  
ATOM    871  CB  ASP A 164      -2.615   8.373 -32.565  1.00 35.11           C  
ANISOU  871  CB  ASP A 164     3969   4409   4961     71     63   -176       C  
ATOM    872  CG  ASP A 164      -2.373   8.921 -31.165  1.00 43.15           C  
ANISOU  872  CG  ASP A 164     4971   5507   5918     85     44   -197       C  
ATOM    873  OD1 ASP A 164      -1.586   8.307 -30.418  1.00 46.90           O1-
ANISOU  873  OD1 ASP A 164     5425   6029   6365     81     48   -144       O1-
ATOM    874  OD2 ASP A 164      -2.956   9.979 -30.833  1.00 42.78           O  
ANISOU  874  OD2 ASP A 164     4938   5475   5842    107     22   -268       O  
ATOM    875  N   ARG A 165      -5.615   7.594 -32.293  1.00 32.59           N  
ANISOU  875  N   ARG A 165     3586   4191   4606     65    120   -200       N  
ATOM    876  CA  ARG A 165      -6.903   7.671 -31.623  1.00 35.41           C  
ANISOU  876  CA  ARG A 165     3885   4654   4914     74    139   -229       C  
ATOM    877  C   ARG A 165      -7.592   6.308 -31.540  1.00 38.62           C  
ANISOU  877  C   ARG A 165     4267   5098   5307     -3    190   -173       C  
ATOM    878  O   ARG A 165      -8.240   5.992 -30.542  1.00 34.29           O  
ANISOU  878  O   ARG A 165     3675   4652   4701    -22    222   -162       O  
ATOM    879  CB  ARG A 165      -7.792   8.684 -32.336  1.00 34.91           C  
ANISOU  879  CB  ARG A 165     3802   4603   4859    126    111   -298       C  
ATOM    880  CG  ARG A 165      -7.213  10.095 -32.270  1.00 38.50           C  
ANISOU  880  CG  ARG A 165     4310   5006   5313    196     64   -355       C  
ATOM    881  CD  ARG A 165      -7.704  10.953 -33.447  1.00 47.58           C  
ANISOU  881  CD  ARG A 165     5486   6102   6491    247     27   -397       C  
ATOM    882  NE  ARG A 165      -7.413  12.366 -33.243  1.00 50.70           N  
ANISOU  882  NE  ARG A 165     5952   6442   6869    317    -12   -457       N  
ATOM    883  CZ  ARG A 165      -7.765  13.339 -34.076  1.00 53.25           C  
ANISOU  883  CZ  ARG A 165     6328   6701   7202    382    -49   -493       C  
ATOM    884  NH1 ARG A 165      -8.417  13.064 -35.203  1.00 47.53           N1+
ANISOU  884  NH1 ARG A 165     5577   5979   6504    389    -58   -475       N1+
ATOM    885  NH2 ARG A 165      -7.452  14.590 -33.782  1.00 56.64           N  
ANISOU  885  NH2 ARG A 165     6852   7059   7609    438    -81   -547       N  
ATOM    886  N   TYR A 166      -7.446   5.502 -32.582  1.00 33.88           N  
ANISOU  886  N   TYR A 166     3706   4414   4753    -55    200   -139       N  
ATOM    887  CA  TYR A 166      -7.951   4.143 -32.544  1.00 33.40           C  
ANISOU  887  CA  TYR A 166     3658   4353   4678   -147    248    -84       C  
ATOM    888  C   TYR A 166      -7.284   3.351 -31.394  1.00 28.97           C  
ANISOU  888  C   TYR A 166     3139   3787   4082   -155    279    -11       C  
ATOM    889  O   TYR A 166      -7.957   2.652 -30.644  1.00 37.06           O  
ANISOU  889  O   TYR A 166     4153   4873   5055   -218    319     25       O  
ATOM    890  CB  TYR A 166      -7.728   3.462 -33.904  1.00 31.80           C  
ANISOU  890  CB  TYR A 166     3520   4036   4527   -194    251    -70       C  
ATOM    891  CG  TYR A 166      -7.775   1.967 -33.826  1.00 30.13           C  
ANISOU  891  CG  TYR A 166     3380   3765   4304   -283    302     -5       C  
ATOM    892  CD1 TYR A 166      -8.982   1.315 -33.704  1.00 29.74           C  
ANISOU  892  CD1 TYR A 166     3306   3780   4214   -393    333      0       C  
ATOM    893  CD2 TYR A 166      -6.601   1.204 -33.856  1.00 30.97           C  
ANISOU  893  CD2 TYR A 166     3584   3752   4432   -255    320     52       C  
ATOM    894  CE1 TYR A 166      -9.046  -0.060 -33.611  1.00 33.27           C  
ANISOU  894  CE1 TYR A 166     3847   4151   4644   -494    381     61       C  
ATOM    895  CE2 TYR A 166      -6.658  -0.172 -33.772  1.00 30.46           C  
ANISOU  895  CE2 TYR A 166     3615   3606   4351   -324    368    114       C  
ATOM    896  CZ  TYR A 166      -7.886  -0.796 -33.657  1.00 34.17           C  
ANISOU  896  CZ  TYR A 166     4084   4118   4782   -452    399    117       C  
ATOM    897  OH  TYR A 166      -7.981  -2.169 -33.565  1.00 42.80           O  
ANISOU  897  OH  TYR A 166     5299   5110   5852   -542    448    179       O  
ATOM    898  N   ILE A 167      -5.969   3.491 -31.259  1.00 31.10           N  
ANISOU  898  N   ILE A 167     3449   3995   4372    -94    259     13       N  
ATOM    899  CA  ILE A 167      -5.222   2.782 -30.224  1.00 37.51           C  
ANISOU  899  CA  ILE A 167     4297   4809   5146    -79    276     89       C  
ATOM    900  C   ILE A 167      -5.656   3.258 -28.819  1.00 36.30           C  
ANISOU  900  C   ILE A 167     4090   4789   4915    -70    277     78       C  
ATOM    901  O   ILE A 167      -5.898   2.432 -27.928  1.00 33.18           O  
ANISOU  901  O   ILE A 167     3714   4429   4462   -106    313    143       O  
ATOM    902  CB  ILE A 167      -3.717   2.955 -30.447  1.00 39.73           C  
ANISOU  902  CB  ILE A 167     4603   5033   5459     -7    246    109       C  
ATOM    903  CG1 ILE A 167      -3.278   2.046 -31.603  1.00 39.95           C  
ANISOU  903  CG1 ILE A 167     4702   4935   5542    -11    269    143       C  
ATOM    904  CG2 ILE A 167      -2.883   2.646 -29.171  1.00 33.07           C  
ANISOU  904  CG2 ILE A 167     3762   4244   4559     38    240    175       C  
ATOM    905  CD1 ILE A 167      -1.842   2.261 -32.013  1.00 36.44           C  
ANISOU  905  CD1 ILE A 167     4259   4458   5130     63    247    155       C  
ATOM    906  N   ALA A 168      -5.819   4.571 -28.656  1.00 34.55           N  
ANISOU  906  N   ALA A 168     3813   4631   4684    -25    241     -4       N  
ATOM    907  CA  ALA A 168      -6.288   5.157 -27.394  1.00 36.90           C  
ANISOU  907  CA  ALA A 168     4064   5056   4901     -6    245    -35       C  
ATOM    908  C   ALA A 168      -7.588   4.521 -26.911  1.00 38.35           C  
ANISOU  908  C   ALA A 168     4207   5333   5030    -69    301    -18       C  
ATOM    909  O   ALA A 168      -7.748   4.225 -25.724  1.00 40.84           O  
ANISOU  909  O   ALA A 168     4513   5739   5265    -85    329     16       O  
ATOM    910  CB  ALA A 168      -6.474   6.661 -27.538  1.00 31.75           C  
ANISOU  910  CB  ALA A 168     3383   4429   4252     56    205   -140       C  
ATOM    911  N   VAL A 169      -8.511   4.291 -27.833  1.00 33.31           N  
ANISOU  911  N   VAL A 169     3542   4688   4427   -117    318    -37       N  
ATOM    912  CA  VAL A 169      -9.833   3.826 -27.461  1.00 29.41           C  
ANISOU  912  CA  VAL A 169     2984   4315   3877   -192    369    -32       C  
ATOM    913  C   VAL A 169      -9.927   2.300 -27.446  1.00 40.30           C  
ANISOU  913  C   VAL A 169     4428   5641   5244   -314    417     65       C  
ATOM    914  O   VAL A 169     -10.518   1.723 -26.525  1.00 37.99           O  
ANISOU  914  O   VAL A 169     4119   5442   4873   -387    467    109       O  
ATOM    915  CB  VAL A 169     -10.908   4.399 -28.399  1.00 39.26           C  
ANISOU  915  CB  VAL A 169     4149   5619   5150   -188    358   -106       C  
ATOM    916  CG1 VAL A 169     -12.259   3.759 -28.140  1.00 38.32           C  
ANISOU  916  CG1 VAL A 169     3945   5646   4971   -292    413    -93       C  
ATOM    917  CG2 VAL A 169     -11.000   5.897 -28.232  1.00 36.23           C  
ANISOU  917  CG2 VAL A 169     3718   5290   4757    -57    320   -199       C  
ATOM    918  N   CYS A 170      -9.336   1.646 -28.441  1.00 30.12           N  
ANISOU  918  N   CYS A 170     3225   4197   4023   -338    407     99       N  
ATOM    919  CA  CYS A 170      -9.536   0.211 -28.611  1.00 36.88           C  
ANISOU  919  CA  CYS A 170     4170   4973   4870   -458    454    178       C  
ATOM    920  C   CYS A 170      -8.434  -0.616 -27.971  1.00 33.82           C  
ANISOU  920  C   CYS A 170     3901   4481   4468   -427    466    275       C  
ATOM    921  O   CYS A 170      -8.639  -1.794 -27.697  1.00 41.41           O  
ANISOU  921  O   CYS A 170     4955   5384   5393   -518    512    355       O  
ATOM    922  CB  CYS A 170      -9.658  -0.147 -30.110  1.00 37.38           C  
ANISOU  922  CB  CYS A 170     4275   4924   5002   -507    444    153       C  
ATOM    923  SG  CYS A 170     -11.156   0.552 -30.885  1.00 38.13           S  
ANISOU  923  SG  CYS A 170     4228   5166   5095   -564    430     60       S  
ATOM    924  N   HIS A 171      -7.267  -0.010 -27.744  1.00 31.77           N  
ANISOU  924  N   HIS A 171     3643   4198   4229   -301    422    272       N  
ATOM    925  CA  HIS A 171      -6.183  -0.688 -27.009  1.00 34.71           C  
ANISOU  925  CA  HIS A 171     4101   4513   4574   -245    424    367       C  
ATOM    926  C   HIS A 171      -5.564   0.210 -25.934  1.00 34.15           C  
ANISOU  926  C   HIS A 171     3964   4556   4453   -157    385    353       C  
ATOM    927  O   HIS A 171      -4.379   0.540 -25.998  1.00 35.81           O  
ANISOU  927  O   HIS A 171     4177   4738   4689    -66    341    358       O  
ATOM    928  CB  HIS A 171      -5.098  -1.159 -27.978  1.00 35.90           C  
ANISOU  928  CB  HIS A 171     4334   4507   4798   -180    409    393       C  
ATOM    929  CG  HIS A 171      -5.630  -2.004 -29.097  1.00 48.50           C  
ANISOU  929  CG  HIS A 171     6012   5978   6437   -265    445    392       C  
ATOM    930  ND1 HIS A 171      -5.894  -3.350 -28.949  1.00 48.34           N  
ANISOU  930  ND1 HIS A 171     6125   5857   6386   -342    496    473       N  
ATOM    931  CD2 HIS A 171      -5.973  -1.689 -30.367  1.00 45.89           C  
ANISOU  931  CD2 HIS A 171     5661   5607   6166   -296    434    318       C  
ATOM    932  CE1 HIS A 171      -6.364  -3.828 -30.088  1.00 48.51           C  
ANISOU  932  CE1 HIS A 171     6204   5779   6447   -423    516    440       C  
ATOM    933  NE2 HIS A 171      -6.420  -2.842 -30.966  1.00 43.94           N  
ANISOU  933  NE2 HIS A 171     5528   5245   5924   -394    477    348       N  
ATOM    934  N   PRO A 172      -6.371   0.611 -24.941  1.00 37.19           N  
ANISOU  934  N   PRO A 172     4287   5084   4759   -192    402    332       N  
ATOM    935  CA  PRO A 172      -5.920   1.593 -23.942  1.00 31.68           C  
ANISOU  935  CA  PRO A 172     3531   4502   4004   -121    365    294       C  
ATOM    936  C   PRO A 172      -4.674   1.183 -23.169  1.00 38.72           C  
ANISOU  936  C   PRO A 172     4474   5385   4854    -57    337    380       C  
ATOM    937  O   PRO A 172      -3.889   2.050 -22.769  1.00 40.15           O  
ANISOU  937  O   PRO A 172     4613   5625   5016      8    283    340       O  
ATOM    938  CB  PRO A 172      -7.136   1.721 -23.004  1.00 33.63           C  
ANISOU  938  CB  PRO A 172     3722   4899   4156   -181    411    275       C  
ATOM    939  CG  PRO A 172      -7.960   0.479 -23.221  1.00 33.21           C  
ANISOU  939  CG  PRO A 172     3717   4809   4094   -300    475    348       C  
ATOM    940  CD  PRO A 172      -7.753   0.163 -24.698  1.00 36.75           C  
ANISOU  940  CD  PRO A 172     4209   5102   4654   -309    461    336       C  
ATOM    941  N   VAL A 173      -4.462  -0.112 -22.970  1.00 34.01           N  
ANISOU  941  N   VAL A 173     3972   4716   4236    -75    368    497       N  
ATOM    942  CA  VAL A 173      -3.245  -0.539 -22.287  1.00 37.23           C  
ANISOU  942  CA  VAL A 173     4423   5121   4601     11    335    589       C  
ATOM    943  C   VAL A 173      -2.012  -0.367 -23.166  1.00 40.71           C  
ANISOU  943  C   VAL A 173     4858   5485   5125    105    288    580       C  
ATOM    944  O   VAL A 173      -1.003   0.184 -22.729  1.00 39.62           O  
ANISOU  944  O   VAL A 173     4668   5425   4963    178    231    576       O  
ATOM    945  CB  VAL A 173      -3.342  -2.000 -21.824  1.00 43.52           C  
ANISOU  945  CB  VAL A 173     5347   5843   5345    -15    382    728       C  
ATOM    946  CG1 VAL A 173      -1.987  -2.478 -21.298  1.00 42.98           C  
ANISOU  946  CG1 VAL A 173     5325   5763   5241    110    340    829       C  
ATOM    947  CG2 VAL A 173      -4.409  -2.118 -20.744  1.00 43.39           C  
ANISOU  947  CG2 VAL A 173     5326   5941   5220   -114    428    749       C  
ATOM    948  N   LYS A 174      -2.090  -0.827 -24.411  1.00 39.70           N  
ANISOU  948  N   LYS A 174     4778   5218   5088     94    311    572       N  
ATOM    949  CA  LYS A 174      -1.005  -0.600 -25.363  1.00 39.26           C  
ANISOU  949  CA  LYS A 174     4705   5103   5110    176    277    551       C  
ATOM    950  C   LYS A 174      -0.799   0.896 -25.622  1.00 37.48           C  
ANISOU  950  C   LYS A 174     4368   4960   4910    175    227    437       C  
ATOM    951  O   LYS A 174       0.307   1.330 -25.918  1.00 39.20           O  
ANISOU  951  O   LYS A 174     4543   5197   5153    236    184    426       O  
ATOM    952  CB  LYS A 174      -1.289  -1.339 -26.676  1.00 47.36           C  
ANISOU  952  CB  LYS A 174     5812   5967   6216    150    320    550       C  
ATOM    953  CG  LYS A 174      -1.156  -2.866 -26.549  1.00 62.63           C  
ANISOU  953  CG  LYS A 174     7893   7776   8129    173    366    666       C  
ATOM    954  CD  LYS A 174      -1.744  -3.601 -27.757  1.00 75.10           C  
ANISOU  954  CD  LYS A 174     9573   9192   9768    106    415    648       C  
ATOM    955  CE  LYS A 174      -1.703  -5.124 -27.572  1.00 81.02           C  
ANISOU  955  CE  LYS A 174    10506   9791  10487    113    466    759       C  
ATOM    956  NZ  LYS A 174      -2.335  -5.855 -28.715  1.00 81.08           N  
ANISOU  956  NZ  LYS A 174    10631   9635  10542     23    514    731       N  
ATOM    957  N   ALA A 175      -1.868   1.681 -25.499  1.00 34.21           N  
ANISOU  957  N   ALA A 175     3913   4600   4485    107    233    354       N  
ATOM    958  CA  ALA A 175      -1.778   3.123 -25.692  1.00 29.69           C  
ANISOU  958  CA  ALA A 175     3269   4083   3928    110    188    246       C  
ATOM    959  C   ALA A 175      -0.769   3.746 -24.744  1.00 36.41           C  
ANISOU  959  C   ALA A 175     4078   5038   4717    150    133    245       C  
ATOM    960  O   ALA A 175      -0.139   4.741 -25.087  1.00 36.31           O  
ANISOU  960  O   ALA A 175     4029   5040   4727    155     87    179       O  
ATOM    961  CB  ALA A 175      -3.180   3.790 -25.509  1.00 28.47           C  
ANISOU  961  CB  ALA A 175     3083   3983   3752     59    209    165       C  
ATOM    962  N   LEU A 176      -0.621   3.166 -23.548  1.00 35.42           N  
ANISOU  962  N   LEU A 176     3964   4991   4503    165    136    319       N  
ATOM    963  CA  LEU A 176       0.340   3.672 -22.567  1.00 39.01           C  
ANISOU  963  CA  LEU A 176     4376   5567   4880    197     77    324       C  
ATOM    964  C   LEU A 176       1.766   3.629 -23.099  1.00 44.43           C  
ANISOU  964  C   LEU A 176     5028   6249   5606    251     32    355       C  
ATOM    965  O   LEU A 176       2.594   4.488 -22.758  1.00 39.76           O  
ANISOU  965  O   LEU A 176     4377   5753   4979    245    -28    313       O  
ATOM    966  CB  LEU A 176       0.247   2.869 -21.242  1.00 33.03           C  
ANISOU  966  CB  LEU A 176     3645   4893   4011    211     90    419       C  
ATOM    967  CG  LEU A 176      -1.091   2.975 -20.516  1.00 36.28           C  
ANISOU  967  CG  LEU A 176     4071   5357   4357    149    137    388       C  
ATOM    968  CD1 LEU A 176      -1.167   1.949 -19.360  1.00 41.50           C  
ANISOU  968  CD1 LEU A 176     4781   6078   4910    153    161    510       C  
ATOM    969  CD2 LEU A 176      -1.313   4.408 -19.989  1.00 31.87           C  
ANISOU  969  CD2 LEU A 176     3461   4900   3747    129    105    260       C  
ATOM    970  N   ASP A 177       2.063   2.618 -23.919  1.00 46.20           N  
ANISOU  970  N   ASP A 177     5290   6369   5893    299     64    428       N  
ATOM    971  CA  ASP A 177       3.387   2.490 -24.536  1.00 46.28           C  
ANISOU  971  CA  ASP A 177     5257   6384   5942    368     35    459       C  
ATOM    972  C   ASP A 177       3.474   3.254 -25.866  1.00 46.54           C  
ANISOU  972  C   ASP A 177     5266   6349   6067    328     35    370       C  
ATOM    973  O   ASP A 177       4.493   3.848 -26.174  1.00 44.76           O  
ANISOU  973  O   ASP A 177     4970   6186   5851    334     -6    347       O  
ATOM    974  CB  ASP A 177       3.742   1.018 -24.775  1.00 59.77           C  
ANISOU  974  CB  ASP A 177     7033   8010   7666    464     73    577       C  
ATOM    975  CG  ASP A 177       3.754   0.195 -23.484  1.00 84.41           C  
ANISOU  975  CG  ASP A 177    10197  11187  10688    513     71    685       C  
ATOM    976  OD1 ASP A 177       4.256   0.693 -22.452  1.00 91.01           O  
ANISOU  976  OD1 ASP A 177    10964  12178  11437    521     14    692       O  
ATOM    977  OD2 ASP A 177       3.252  -0.951 -23.504  1.00 90.70           O1-
ANISOU  977  OD2 ASP A 177    11108  11869  11486    534    124    764       O1-
ATOM    978  N   PHE A 178       2.403   3.249 -26.648  1.00 40.44           N  
ANISOU  978  N   PHE A 178     4549   5463   5355    281     78    325       N  
ATOM    979  CA  PHE A 178       2.457   3.886 -27.960  1.00 36.36           C  
ANISOU  979  CA  PHE A 178     4024   4875   4918    250     79    254       C  
ATOM    980  C   PHE A 178       2.474   5.419 -27.904  1.00 42.74           C  
ANISOU  980  C   PHE A 178     4790   5735   5715    188     31    153       C  
ATOM    981  O   PHE A 178       3.156   6.055 -28.706  1.00 40.94           O  
ANISOU  981  O   PHE A 178     4535   5495   5524    168     10    118       O  
ATOM    982  CB  PHE A 178       1.281   3.422 -28.832  1.00 41.10           C  
ANISOU  982  CB  PHE A 178     4693   5351   5574    216    131    236       C  
ATOM    983  CG  PHE A 178       1.236   4.088 -30.192  1.00 46.74           C  
ANISOU  983  CG  PHE A 178     5405   5995   6358    186    129    167       C  
ATOM    984  CD1 PHE A 178       2.183   3.785 -31.157  1.00 55.75           C  
ANISOU  984  CD1 PHE A 178     6544   7095   7544    222    138    188       C  
ATOM    985  CD2 PHE A 178       0.253   5.022 -30.497  1.00 47.65           C  
ANISOU  985  CD2 PHE A 178     5523   6096   6487    132    119     85       C  
ATOM    986  CE1 PHE A 178       2.154   4.396 -32.409  1.00 51.47           C  
ANISOU  986  CE1 PHE A 178     6008   6495   7054    187    138    131       C  
ATOM    987  CE2 PHE A 178       0.222   5.642 -31.748  1.00 51.97           C  
ANISOU  987  CE2 PHE A 178     6080   6577   7088    110    112     32       C  
ATOM    988  CZ  PHE A 178       1.179   5.321 -32.703  1.00 46.52           C  
ANISOU  988  CZ  PHE A 178     5393   5844   6438    129    121     57       C  
ATOM    989  N   ARG A 179       1.740   6.020 -26.966  1.00 33.55           N  
ANISOU  989  N   ARG A 179     3630   4625   4494    156     17    107       N  
ATOM    990  CA  ARG A 179       1.431   7.449 -27.087  1.00 31.50           C  
ANISOU  990  CA  ARG A 179     3374   4362   4233    106    -14     -1       C  
ATOM    991  C   ARG A 179       2.373   8.352 -26.329  1.00 34.90           C  
ANISOU  991  C   ARG A 179     3773   4890   4599     74    -75    -37       C  
ATOM    992  O   ARG A 179       1.949   9.286 -25.645  1.00 46.39           O  
ANISOU  992  O   ARG A 179     5251   6375   5999     44    -97   -114       O  
ATOM    993  CB  ARG A 179      -0.005   7.708 -26.653  1.00 33.31           C  
ANISOU  993  CB  ARG A 179     3632   4588   4437    101     12    -52       C  
ATOM    994  CG  ARG A 179      -1.003   6.888 -27.451  1.00 36.29           C  
ANISOU  994  CG  ARG A 179     4032   4888   4871    105     66    -25       C  
ATOM    995  CD  ARG A 179      -2.422   7.287 -27.105  1.00 35.13           C  
ANISOU  995  CD  ARG A 179     3883   4770   4694     99     88    -84       C  
ATOM    996  NE  ARG A 179      -2.860   8.450 -27.872  1.00 33.22           N  
ANISOU  996  NE  ARG A 179     3655   4478   4488    106     67   -175       N  
ATOM    997  CZ  ARG A 179      -3.874   9.228 -27.525  1.00 39.83           C  
ANISOU  997  CZ  ARG A 179     4489   5352   5291    131     70   -250       C  
ATOM    998  NH1 ARG A 179      -4.536   9.009 -26.389  1.00 35.61           N1+
ANISOU  998  NH1 ARG A 179     3926   4922   4682    140     99   -251       N1+
ATOM    999  NH2 ARG A 179      -4.207  10.246 -28.301  1.00 38.44           N  
ANISOU  999  NH2 ARG A 179     4342   5114   5148    156     47   -321       N  
ATOM   1000  N   THR A 180       3.659   8.074 -26.482  1.00 36.54           N  
ANISOU 1000  N   THR A 180     3925   5152   4807     79   -100     14       N  
ATOM   1001  CA  THR A 180       4.712   8.855 -25.855  1.00 40.75           C  
ANISOU 1001  CA  THR A 180     4408   5801   5274     27   -163    -13       C  
ATOM   1002  C   THR A 180       5.318   9.803 -26.873  1.00 42.66           C  
ANISOU 1002  C   THR A 180     4648   5998   5560    -48   -185    -69       C  
ATOM   1003  O   THR A 180       5.296   9.510 -28.068  1.00 36.44           O  
ANISOU 1003  O   THR A 180     3870   5122   4852    -32   -150    -51       O  
ATOM   1004  CB  THR A 180       5.816   7.962 -25.317  1.00 40.43           C  
ANISOU 1004  CB  THR A 180     4283   5890   5190     80   -183     86       C  
ATOM   1005  OG1 THR A 180       6.383   7.221 -26.405  1.00 39.43           O  
ANISOU 1005  OG1 THR A 180     4125   5719   5137    134   -152    146       O  
ATOM   1006  CG2 THR A 180       5.267   6.979 -24.271  1.00 44.41           C  
ANISOU 1006  CG2 THR A 180     4807   6430   5637    151   -163    158       C  
ATOM   1007  N   PRO A 181       5.868  10.936 -26.404  1.00 41.54           N  
ANISOU 1007  N   PRO A 181     4507   5917   5360   -143   -241   -137       N  
ATOM   1008  CA  PRO A 181       6.598  11.821 -27.314  1.00 35.06           C  
ANISOU 1008  CA  PRO A 181     3687   5066   4567   -240   -263   -179       C  
ATOM   1009  C   PRO A 181       7.733  11.084 -28.052  1.00 41.78           C  
ANISOU 1009  C   PRO A 181     4430   5992   5452   -220   -251    -97       C  
ATOM   1010  O   PRO A 181       7.987  11.353 -29.219  1.00 35.74           O  
ANISOU 1010  O   PRO A 181     3673   5161   4743   -258   -231   -106       O  
ATOM   1011  CB  PRO A 181       7.158  12.923 -26.385  1.00 35.10           C  
ANISOU 1011  CB  PRO A 181     3702   5157   4476   -356   -330   -251       C  
ATOM   1012  CG  PRO A 181       6.874  12.467 -24.953  1.00 40.47           C  
ANISOU 1012  CG  PRO A 181     4362   5943   5071   -302   -346   -235       C  
ATOM   1013  CD  PRO A 181       5.714  11.513 -25.049  1.00 38.24           C  
ANISOU 1013  CD  PRO A 181     4110   5580   4840   -178   -282   -190       C  
ATOM   1014  N   ARG A 182       8.396  10.150 -27.382  1.00 37.20           N  
ANISOU 1014  N   ARG A 182     3750   5552   4831   -148   -260    -17       N  
ATOM   1015  CA  ARG A 182       9.476   9.403 -28.020  1.00 37.50           C  
ANISOU 1015  CA  ARG A 182     3679   5677   4894    -95   -245     60       C  
ATOM   1016  C   ARG A 182       8.997   8.604 -29.233  1.00 39.34           C  
ANISOU 1016  C   ARG A 182     3958   5768   5223    -10   -171     94       C  
ATOM   1017  O   ARG A 182       9.637   8.596 -30.287  1.00 38.76           O  
ANISOU 1017  O   ARG A 182     3843   5696   5190    -20   -147    103       O  
ATOM   1018  CB  ARG A 182      10.127   8.467 -27.018  1.00 43.24           C  
ANISOU 1018  CB  ARG A 182     4309   6567   5555      4   -269    148       C  
ATOM   1019  CG  ARG A 182      11.373   7.788 -27.557  1.00 51.55           C  
ANISOU 1019  CG  ARG A 182     5228   7744   6614     78   -260    224       C  
ATOM   1020  CD  ARG A 182      12.017   6.928 -26.483  1.00 62.69           C  
ANISOU 1020  CD  ARG A 182     6546   9325   7947    194   -294    317       C  
ATOM   1021  NE  ARG A 182      13.409   6.624 -26.793  1.00 73.95           N  
ANISOU 1021  NE  ARG A 182     7807  10941   9350    247   -309    372       N  
ATOM   1022  CZ  ARG A 182      13.803   5.558 -27.480  1.00 76.81           C  
ANISOU 1022  CZ  ARG A 182     8136  11291   9757    409   -255    448       C  
ATOM   1023  NH1 ARG A 182      12.904   4.690 -27.928  1.00 71.28           N  
ANISOU 1023  NH1 ARG A 182     7574  10383   9127    512   -186    475       N  
ATOM   1024  NH2 ARG A 182      15.094   5.361 -27.715  1.00 81.75           N  
ANISOU 1024  NH2 ARG A 182     8592  12119  10351    465   -268    493       N  
ATOM   1025  N   ASN A 183       7.874   7.919 -29.078  1.00 36.87           N  
ANISOU 1025  N   ASN A 183     3730   5341   4938     65   -133    111       N  
ATOM   1026  CA  ASN A 183       7.343   7.117 -30.164  1.00 41.22           C  
ANISOU 1026  CA  ASN A 183     4337   5756   5569    131    -68    137       C  
ATOM   1027  C   ASN A 183       6.799   7.945 -31.309  1.00 38.06           C  
ANISOU 1027  C   ASN A 183     4002   5233   5224     53    -53     65       C  
ATOM   1028  O   ASN A 183       6.864   7.527 -32.456  1.00 36.19           O  
ANISOU 1028  O   ASN A 183     3781   4927   5042     78    -10     79       O  
ATOM   1029  CB  ASN A 183       6.259   6.182 -29.648  1.00 37.35           C  
ANISOU 1029  CB  ASN A 183     3921   5189   5081    200    -34    173       C  
ATOM   1030  CG  ASN A 183       6.835   4.891 -29.115  1.00 52.88           C  
ANISOU 1030  CG  ASN A 183     5859   7213   7020    318    -19    277       C  
ATOM   1031  OD1 ASN A 183       7.933   4.487 -29.504  1.00 59.95           O  
ANISOU 1031  OD1 ASN A 183     6685   8175   7919    382    -16    323       O  
ATOM   1032  ND2 ASN A 183       6.101   4.234 -28.232  1.00 62.08           N  
ANISOU 1032  ND2 ASN A 183     7080   8357   8151    353     -8    319       N  
ATOM   1033  N   ALA A 184       6.248   9.109 -30.993  1.00 38.29           N  
ANISOU 1033  N   ALA A 184     4081   5233   5233    -33    -89    -12       N  
ATOM   1034  CA  ALA A 184       5.700   9.978 -32.012  1.00 39.67           C  
ANISOU 1034  CA  ALA A 184     4333   5287   5451    -94    -83    -75       C  
ATOM   1035  C   ALA A 184       6.829  10.469 -32.919  1.00 40.59           C  
ANISOU 1035  C   ALA A 184     4409   5437   5576   -166    -88    -75       C  
ATOM   1036  O   ALA A 184       6.662  10.565 -34.141  1.00 39.73           O  
ANISOU 1036  O   ALA A 184     4342   5239   5515   -179    -59    -82       O  
ATOM   1037  CB  ALA A 184       4.957  11.137 -31.380  1.00 31.66           C  
ANISOU 1037  CB  ALA A 184     3393   4235   4402   -147   -121   -155       C  
ATOM   1038  N   LYS A 185       7.982  10.758 -32.322  1.00 36.08           N  
ANISOU 1038  N   LYS A 185     3747   5009   4950   -219   -125    -64       N  
ATOM   1039  CA  LYS A 185       9.147  11.145 -33.115  1.00 39.26           C  
ANISOU 1039  CA  LYS A 185     4084   5485   5350   -300   -124    -56       C  
ATOM   1040  C   LYS A 185       9.659   9.978 -33.950  1.00 43.64           C  
ANISOU 1040  C   LYS A 185     4566   6072   5943   -197    -65     12       C  
ATOM   1041  O   LYS A 185      10.001  10.153 -35.118  1.00 40.99           O  
ANISOU 1041  O   LYS A 185     4231   5709   5634   -234    -32      9       O  
ATOM   1042  CB  LYS A 185      10.269  11.691 -32.227  1.00 37.72           C  
ANISOU 1042  CB  LYS A 185     3789   5470   5075   -393   -181    -62       C  
ATOM   1043  CG  LYS A 185       9.998  13.125 -31.764  1.00 51.30           C  
ANISOU 1043  CG  LYS A 185     5606   7135   6750   -541   -235   -149       C  
ATOM   1044  CD  LYS A 185      10.892  13.556 -30.618  1.00 64.93           C  
ANISOU 1044  CD  LYS A 185     7250   9038   8383   -634   -300   -163       C  
ATOM   1045  CE  LYS A 185      10.561  14.984 -30.193  1.00 85.25           C  
ANISOU 1045  CE  LYS A 185     9959  11523  10908   -782   -348   -262       C  
ATOM   1046  NZ  LYS A 185      11.127  15.356 -28.861  1.00 96.72           N1+
ANISOU 1046  NZ  LYS A 185    11364  13128  12258   -864   -416   -293       N1+
ATOM   1047  N   ILE A 186       9.709   8.789 -33.361  1.00 35.66           N  
ANISOU 1047  N   ILE A 186     3508   5112   4929    -63    -48     73       N  
ATOM   1048  CA  ILE A 186      10.110   7.620 -34.121  1.00 40.91           C  
ANISOU 1048  CA  ILE A 186     4137   5779   5628     58     13    132       C  
ATOM   1049  C   ILE A 186       9.162   7.377 -35.318  1.00 41.58           C  
ANISOU 1049  C   ILE A 186     4341   5679   5780     71     66    109       C  
ATOM   1050  O   ILE A 186       9.612   7.082 -36.430  1.00 35.25           O  
ANISOU 1050  O   ILE A 186     3525   4867   5002     92    114    118       O  
ATOM   1051  CB  ILE A 186      10.145   6.374 -33.235  1.00 38.55           C  
ANISOU 1051  CB  ILE A 186     3814   5521   5312    207     21    205       C  
ATOM   1052  CG1 ILE A 186      11.292   6.492 -32.229  1.00 43.25           C  
ANISOU 1052  CG1 ILE A 186     4267   6335   5832    215    -33    242       C  
ATOM   1053  CG2 ILE A 186      10.311   5.129 -34.093  1.00 37.51           C  
ANISOU 1053  CG2 ILE A 186     3702   5329   5221    344     93    255       C  
ATOM   1054  CD1 ILE A 186      11.262   5.430 -31.149  1.00 44.95           C  
ANISOU 1054  CD1 ILE A 186     4475   6593   6012    355    -41    319       C  
ATOM   1055  N   VAL A 187       7.860   7.513 -35.083  1.00 35.30           N  
ANISOU 1055  N   VAL A 187     3652   4757   5006     57     58     76       N  
ATOM   1056  CA  VAL A 187       6.862   7.298 -36.131  1.00 40.53           C  
ANISOU 1056  CA  VAL A 187     4416   5265   5719     61     97     52       C  
ATOM   1057  C   VAL A 187       7.021   8.313 -37.270  1.00 40.75           C  
ANISOU 1057  C   VAL A 187     4469   5255   5759    -36     94      8       C  
ATOM   1058  O   VAL A 187       6.944   7.953 -38.452  1.00 37.62           O  
ANISOU 1058  O   VAL A 187     4108   4795   5391    -21    138      9       O  
ATOM   1059  CB  VAL A 187       5.433   7.368 -35.563  1.00 40.44           C  
ANISOU 1059  CB  VAL A 187     4485   5167   5715     57     81     24       C  
ATOM   1060  CG1 VAL A 187       4.403   7.547 -36.679  1.00 32.48           C  
ANISOU 1060  CG1 VAL A 187     3563   4031   4747     30    100    -15       C  
ATOM   1061  CG2 VAL A 187       5.132   6.113 -34.748  1.00 42.68           C  
ANISOU 1061  CG2 VAL A 187     4772   5455   5990    146    105     80       C  
ATOM   1062  N   ASN A 188       7.247   9.574 -36.913  1.00 35.05           N  
ANISOU 1062  N   ASN A 188     3745   4566   5007   -139     44    -31       N  
ATOM   1063  CA  ASN A 188       7.521  10.608 -37.903  1.00 40.70           C  
ANISOU 1063  CA  ASN A 188     4499   5245   5721   -246     38    -62       C  
ATOM   1064  C   ASN A 188       8.743  10.244 -38.760  1.00 40.60           C  
ANISOU 1064  C   ASN A 188     4398   5326   5701   -254     82    -26       C  
ATOM   1065  O   ASN A 188       8.739  10.451 -39.961  1.00 39.00           O  
ANISOU 1065  O   ASN A 188     4241   5068   5511   -290    113    -32       O  
ATOM   1066  CB  ASN A 188       7.727  11.967 -37.223  1.00 36.50           C  
ANISOU 1066  CB  ASN A 188     3991   4732   5145   -365    -23   -106       C  
ATOM   1067  CG  ASN A 188       6.413  12.604 -36.762  1.00 37.18           C  
ANISOU 1067  CG  ASN A 188     4195   4697   5236   -355    -57   -159       C  
ATOM   1068  OD1 ASN A 188       5.330  12.203 -37.176  1.00 36.90           O  
ANISOU 1068  OD1 ASN A 188     4216   4568   5238   -282    -37   -163       O  
ATOM   1069  ND2 ASN A 188       6.518  13.626 -35.931  1.00 35.07           N  
ANISOU 1069  ND2 ASN A 188     3963   4439   4924   -431   -107   -204       N  
ATOM   1070  N   VAL A 189       9.776   9.672 -38.151  1.00 38.67           N  
ANISOU 1070  N   VAL A 189     4026   5237   5430   -209     87     15       N  
ATOM   1071  CA  VAL A 189      10.947   9.267 -38.926  1.00 39.31           C  
ANISOU 1071  CA  VAL A 189     4002   5435   5497   -192    136     49       C  
ATOM   1072  C   VAL A 189      10.621   8.096 -39.873  1.00 35.19           C  
ANISOU 1072  C   VAL A 189     3524   4830   5016    -64    209     69       C  
ATOM   1073  O   VAL A 189      10.999   8.114 -41.048  1.00 37.58           O  
ANISOU 1073  O   VAL A 189     3826   5135   5319    -85    257     65       O  
ATOM   1074  CB  VAL A 189      12.117   8.885 -37.997  1.00 42.77           C  
ANISOU 1074  CB  VAL A 189     4277   6084   5891   -148    120     91       C  
ATOM   1075  CG1 VAL A 189      13.255   8.199 -38.777  1.00 41.84           C  
ANISOU 1075  CG1 VAL A 189     4035   6103   5760    -73    184    132       C  
ATOM   1076  CG2 VAL A 189      12.633  10.120 -37.274  1.00 41.17           C  
ANISOU 1076  CG2 VAL A 189     4025   5985   5633   -313     51     63       C  
ATOM   1077  N   CYS A 190       9.939   7.077 -39.343  1.00 34.20           N  
ANISOU 1077  N   CYS A 190     3445   4634   4917     57    219     89       N  
ATOM   1078  CA  CYS A 190       9.509   5.935 -40.141  1.00 37.70           C  
ANISOU 1078  CA  CYS A 190     3962   4971   5393    163    283     99       C  
ATOM   1079  C   CYS A 190       8.656   6.378 -41.340  1.00 38.74           C  
ANISOU 1079  C   CYS A 190     4204   4967   5547     87    297     53       C  
ATOM   1080  O   CYS A 190       8.840   5.899 -42.454  1.00 36.64           O  
ANISOU 1080  O   CYS A 190     3966   4671   5284    118    354     49       O  
ATOM   1081  CB  CYS A 190       8.730   4.946 -39.273  1.00 36.61           C  
ANISOU 1081  CB  CYS A 190     3884   4756   5271    260    281    125       C  
ATOM   1082  SG  CYS A 190       9.805   4.054 -38.071  1.00 41.80           S  
ANISOU 1082  SG  CYS A 190     4430   5560   5892    402    279    202       S  
ATOM   1083  N   ASN A 191       7.720   7.285 -41.088  1.00 31.82           N  
ANISOU 1083  N   ASN A 191     3394   4018   4678     -1    243     18       N  
ATOM   1084  CA  ASN A 191       6.885   7.818 -42.145  1.00 33.74           C  
ANISOU 1084  CA  ASN A 191     3737   4148   4934    -65    241    -19       C  
ATOM   1085  C   ASN A 191       7.723   8.573 -43.161  1.00 38.16           C  
ANISOU 1085  C   ASN A 191     4278   4754   5468   -149    258    -24       C  
ATOM   1086  O   ASN A 191       7.458   8.538 -44.355  1.00 37.70           O  
ANISOU 1086  O   ASN A 191     4283   4633   5408   -165    288    -35       O  
ATOM   1087  CB  ASN A 191       5.805   8.727 -41.563  1.00 30.84           C  
ANISOU 1087  CB  ASN A 191     3432   3714   4572   -118    178    -53       C  
ATOM   1088  CG  ASN A 191       4.677   7.944 -40.937  1.00 38.60           C  
ANISOU 1088  CG  ASN A 191     4450   4639   5576    -52    175    -54       C  
ATOM   1089  OD1 ASN A 191       4.526   6.757 -41.198  1.00 41.77           O  
ANISOU 1089  OD1 ASN A 191     4867   5011   5992     13    220    -34       O  
ATOM   1090  ND2 ASN A 191       3.881   8.602 -40.114  1.00 37.57           N  
ANISOU 1090  ND2 ASN A 191     4340   4493   5441    -71    127    -80       N  
ATOM   1091  N   TRP A 192       8.746   9.260 -42.686  1.00 33.69           N  
ANISOU 1091  N   TRP A 192     3623   4306   4870   -215    239    -13       N  
ATOM   1092  CA  TRP A 192       9.585   9.987 -43.599  1.00 35.41           C  
ANISOU 1092  CA  TRP A 192     3818   4582   5055   -319    259    -11       C  
ATOM   1093  C   TRP A 192      10.394   9.016 -44.479  1.00 42.88           C  
ANISOU 1093  C   TRP A 192     4695   5607   5989   -242    342     12       C  
ATOM   1094  O   TRP A 192      10.576   9.241 -45.686  1.00 38.65           O  
ANISOU 1094  O   TRP A 192     4193   5060   5432   -292    382      6       O  
ATOM   1095  CB  TRP A 192      10.512  10.922 -42.837  1.00 33.03           C  
ANISOU 1095  CB  TRP A 192     3432   4404   4713   -433    218     -8       C  
ATOM   1096  CG  TRP A 192      11.370  11.709 -43.784  1.00 44.56           C  
ANISOU 1096  CG  TRP A 192     4873   5930   6129   -571    242     -2       C  
ATOM   1097  CD1 TRP A 192      11.022  12.852 -44.450  1.00 46.26           C  
ANISOU 1097  CD1 TRP A 192     5211   6040   6326   -705    220    -19       C  
ATOM   1098  CD2 TRP A 192      12.707  11.397 -44.191  1.00 42.89           C  
ANISOU 1098  CD2 TRP A 192     4512   5907   5878   -586    298     27       C  
ATOM   1099  NE1 TRP A 192      12.065  13.274 -45.235  1.00 48.12           N  
ANISOU 1099  NE1 TRP A 192     5391   6382   6511   -823    260      1       N  
ATOM   1100  CE2 TRP A 192      13.115  12.400 -45.092  1.00 49.41           C  
ANISOU 1100  CE2 TRP A 192     5374   6740   6660   -755    310     26       C  
ATOM   1101  CE3 TRP A 192      13.602  10.365 -43.879  1.00 47.90           C  
ANISOU 1101  CE3 TRP A 192     4985   6712   6504   -463    341     57       C  
ATOM   1102  CZ2 TRP A 192      14.373  12.402 -45.693  1.00 50.91           C  
ANISOU 1102  CZ2 TRP A 192     5430   7119   6796   -821    369     51       C  
ATOM   1103  CZ3 TRP A 192      14.857  10.370 -44.473  1.00 55.59           C  
ANISOU 1103  CZ3 TRP A 192     5817   7878   7427   -505    396     79       C  
ATOM   1104  CH2 TRP A 192      15.231  11.385 -45.365  1.00 56.00           C  
ANISOU 1104  CH2 TRP A 192     5893   7950   7433   -691    412     74       C  
ATOM   1105  N   ILE A 193      10.857   7.926 -43.877  1.00 36.60           N  
ANISOU 1105  N   ILE A 193     3815   4889   5202   -109    370     38       N  
ATOM   1106  CA  ILE A 193      11.608   6.914 -44.612  1.00 35.56           C  
ANISOU 1106  CA  ILE A 193     3628   4826   5058      3    453     56       C  
ATOM   1107  C   ILE A 193      10.727   6.329 -45.706  1.00 37.82           C  
ANISOU 1107  C   ILE A 193     4054   4953   5363     42    496     28       C  
ATOM   1108  O   ILE A 193      11.161   6.156 -46.851  1.00 40.45           O  
ANISOU 1108  O   ILE A 193     4390   5310   5668     46    560     19       O  
ATOM   1109  CB  ILE A 193      12.120   5.803 -43.679  1.00 37.63           C  
ANISOU 1109  CB  ILE A 193     3805   5168   5324    168    468     94       C  
ATOM   1110  CG1 ILE A 193      13.220   6.366 -42.782  1.00 40.35           C  
ANISOU 1110  CG1 ILE A 193     3980   5722   5630    125    429    123       C  
ATOM   1111  CG2 ILE A 193      12.644   4.610 -44.482  1.00 38.98           C  
ANISOU 1111  CG2 ILE A 193     3970   5355   5487    324    560    104       C  
ATOM   1112  CD1 ILE A 193      13.591   5.483 -41.598  1.00 44.46           C  
ANISOU 1112  CD1 ILE A 193     4422   6324   6147    277    414    169       C  
ATOM   1113  N   LEU A 194       9.473   6.067 -45.357  1.00 38.97           N  
ANISOU 1113  N   LEU A 194     4311   4950   5546     58    461     12       N  
ATOM   1114  CA  LEU A 194       8.516   5.531 -46.311  1.00 43.32           C  
ANISOU 1114  CA  LEU A 194     4993   5359   6108     74    487    -18       C  
ATOM   1115  C   LEU A 194       8.273   6.530 -47.445  1.00 47.33           C  
ANISOU 1115  C   LEU A 194     5555   5838   6590    -47    478    -42       C  
ATOM   1116  O   LEU A 194       8.298   6.169 -48.616  1.00 44.24           O  
ANISOU 1116  O   LEU A 194     5215   5419   6174    -40    529    -59       O  
ATOM   1117  CB  LEU A 194       7.212   5.181 -45.602  1.00 40.93           C  
ANISOU 1117  CB  LEU A 194     4771   4937   5842     88    443    -27       C  
ATOM   1118  CG  LEU A 194       6.115   4.498 -46.417  1.00 48.77           C  
ANISOU 1118  CG  LEU A 194     5891   5797   6842     92    461    -59       C  
ATOM   1119  CD1 LEU A 194       6.587   3.127 -46.921  1.00 44.04           C  
ANISOU 1119  CD1 LEU A 194     5331   5169   6234    200    543    -59       C  
ATOM   1120  CD2 LEU A 194       4.813   4.392 -45.592  1.00 47.56           C  
ANISOU 1120  CD2 LEU A 194     5786   5569   6717     75    409    -66       C  
ATOM   1121  N   SER A 195       8.038   7.789 -47.090  1.00 39.19           N  
ANISOU 1121  N   SER A 195     4528   4806   5558   -155    411    -42       N  
ATOM   1122  CA  SER A 195       7.880   8.845 -48.079  1.00 39.87           C  
ANISOU 1122  CA  SER A 195     4679   4857   5611   -269    396    -51       C  
ATOM   1123  C   SER A 195       9.083   8.940 -49.024  1.00 39.17           C  
ANISOU 1123  C   SER A 195     4534   4877   5472   -311    463    -37       C  
ATOM   1124  O   SER A 195       8.935   9.282 -50.185  1.00 39.02           O  
ANISOU 1124  O   SER A 195     4587   4823   5416   -369    482    -42       O  
ATOM   1125  CB  SER A 195       7.666  10.185 -47.374  1.00 34.44           C  
ANISOU 1125  CB  SER A 195     4010   4151   4923   -367    319    -51       C  
ATOM   1126  OG  SER A 195       6.460  10.146 -46.637  1.00 44.22           O  
ANISOU 1126  OG  SER A 195     5304   5300   6200   -322    264    -70       O  
ATOM   1127  N   SER A 196      10.272   8.651 -48.507  1.00 36.09           N  
ANISOU 1127  N   SER A 196     4006   4635   5071   -280    498    -15       N  
ATOM   1128  CA  SER A 196      11.495   8.723 -49.298  1.00 42.02           C  
ANISOU 1128  CA  SER A 196     4667   5531   5766   -316    569     -1       C  
ATOM   1129  C   SER A 196      11.514   7.712 -50.443  1.00 41.60           C  
ANISOU 1129  C   SER A 196     4654   5459   5692   -219    654    -19       C  
ATOM   1130  O   SER A 196      12.213   7.918 -51.431  1.00 43.62           O  
ANISOU 1130  O   SER A 196     4881   5802   5891   -268    716    -16       O  
ATOM   1131  CB  SER A 196      12.717   8.504 -48.407  1.00 42.01           C  
ANISOU 1131  CB  SER A 196     4485   5721   5755   -277    584     26       C  
ATOM   1132  OG  SER A 196      12.792   9.487 -47.394  1.00 46.65           O  
ANISOU 1132  OG  SER A 196     5040   6339   6346   -389    505     35       O  
ATOM   1133  N   ALA A 197      10.760   6.619 -50.305  1.00 43.51           N  
ANISOU 1133  N   ALA A 197     4969   5590   5973    -91    663    -40       N  
ATOM   1134  CA  ALA A 197      10.683   5.604 -51.357  1.00 47.17           C  
ANISOU 1134  CA  ALA A 197     5502   6009   6413     -2    741    -70       C  
ATOM   1135  C   ALA A 197      10.220   6.203 -52.684  1.00 48.41           C  
ANISOU 1135  C   ALA A 197     5762   6110   6521   -111    746    -90       C  
ATOM   1136  O   ALA A 197      10.567   5.705 -53.752  1.00 50.86           O  
ANISOU 1136  O   ALA A 197     6099   6446   6780    -78    824   -112       O  
ATOM   1137  CB  ALA A 197       9.754   4.474 -50.940  1.00 49.80           C  
ANISOU 1137  CB  ALA A 197     5932   6198   6791    107    733    -91       C  
ATOM   1138  N   ILE A 198       9.436   7.274 -52.619  1.00 43.77           N  
ANISOU 1138  N   ILE A 198     5239   5450   5943   -231    663    -82       N  
ATOM   1139  CA  ILE A 198       9.034   7.976 -53.829  1.00 43.84           C  
ANISOU 1139  CA  ILE A 198     5347   5413   5896   -334    656    -86       C  
ATOM   1140  C   ILE A 198       9.714   9.343 -53.882  1.00 49.96           C  
ANISOU 1140  C   ILE A 198     6083   6264   6635   -477    636    -46       C  
ATOM   1141  O   ILE A 198      10.108   9.810 -54.952  1.00 45.15           O  
ANISOU 1141  O   ILE A 198     5505   5696   5956   -562    675    -34       O  
ATOM   1142  CB  ILE A 198       7.485   8.105 -53.923  1.00 46.92           C  
ANISOU 1142  CB  ILE A 198     5868   5651   6310   -345    577   -105       C  
ATOM   1143  CG1 ILE A 198       6.885   6.748 -54.316  1.00 50.77           C  
ANISOU 1143  CG1 ILE A 198     6417   6071   6802   -251    614   -150       C  
ATOM   1144  CG2 ILE A 198       7.082   9.165 -54.956  1.00 45.06           C  
ANISOU 1144  CG2 ILE A 198     5729   5377   6016   -456    542    -91       C  
ATOM   1145  CD1 ILE A 198       5.366   6.640 -54.179  1.00 48.47           C  
ANISOU 1145  CD1 ILE A 198     6215   5664   6537   -257    537   -172       C  
ATOM   1146  N   GLY A 199       9.886   9.968 -52.722  1.00 42.99           N  
ANISOU 1146  N   GLY A 199     5142   5402   5791   -516    580    -27       N  
ATOM   1147  CA  GLY A 199      10.476  11.297 -52.660  1.00 40.71           C  
ANISOU 1147  CA  GLY A 199     4841   5161   5465   -674    553      5       C  
ATOM   1148  C   GLY A 199      11.874  11.410 -53.226  1.00 46.65           C  
ANISOU 1148  C   GLY A 199     5481   6093   6151   -748    635     27       C  
ATOM   1149  O   GLY A 199      12.199  12.388 -53.898  1.00 48.34           O  
ANISOU 1149  O   GLY A 199     5742   6323   6303   -901    639     54       O  
ATOM   1150  N   LEU A 200      12.710  10.413 -52.957  1.00 49.82           N  
ANISOU 1150  N   LEU A 200     5737   6637   6558   -638    702     21       N  
ATOM   1151  CA  LEU A 200      14.086  10.420 -53.456  1.00 51.43           C  
ANISOU 1151  CA  LEU A 200     5798   7052   6692   -685    790     40       C  
ATOM   1152  C   LEU A 200      14.220  10.045 -54.938  1.00 47.00           C  
ANISOU 1152  C   LEU A 200     5285   6512   6062   -671    880     28       C  
ATOM   1153  O   LEU A 200      14.929  10.741 -55.674  1.00 42.31           O  
ANISOU 1153  O   LEU A 200     4661   6027   5389   -812    924     54       O  
ATOM   1154  CB  LEU A 200      14.967   9.488 -52.616  1.00 57.24           C  
ANISOU 1154  CB  LEU A 200     6346   7951   7449   -541    828     40       C  
ATOM   1155  CG  LEU A 200      15.415  10.026 -51.270  1.00 62.55           C  
ANISOU 1155  CG  LEU A 200     6906   8714   8147   -601    760     62       C  
ATOM   1156  CD1 LEU A 200      16.146   8.937 -50.504  1.00 69.97           C  
ANISOU 1156  CD1 LEU A 200     7678   9804   9104   -418    794     68       C  
ATOM   1157  CD2 LEU A 200      16.307  11.218 -51.496  1.00 65.58           C  
ANISOU 1157  CD2 LEU A 200     7218   9240   8460   -825    763     90       C  
ATOM   1158  N   PRO A 201      13.577   8.941 -55.383  1.00 39.84           N  
ANISOU 1158  N   PRO A 201     4455   5507   5173   -515    912    -11       N  
ATOM   1159  CA  PRO A 201      13.653   8.660 -56.827  1.00 44.05           C  
ANISOU 1159  CA  PRO A 201     5054   6054   5627   -517    993    -30       C  
ATOM   1160  C   PRO A 201      13.198   9.822 -57.724  1.00 50.57           C  
ANISOU 1160  C   PRO A 201     6012   6810   6394   -698    958     -4       C  
ATOM   1161  O   PRO A 201      13.846  10.044 -58.751  1.00 52.32           O  
ANISOU 1161  O   PRO A 201     6219   7138   6522   -772   1034      8       O  
ATOM   1162  CB  PRO A 201      12.714   7.463 -56.998  1.00 39.11           C  
ANISOU 1162  CB  PRO A 201     4541   5279   5038   -357    997    -83       C  
ATOM   1163  CG  PRO A 201      12.791   6.751 -55.685  1.00 44.51           C  
ANISOU 1163  CG  PRO A 201     5144   5962   5806   -224    975    -85       C  
ATOM   1164  CD  PRO A 201      12.906   7.845 -54.653  1.00 39.31           C  
ANISOU 1164  CD  PRO A 201     4417   5335   5183   -341    889    -42       C  
ATOM   1165  N   VAL A 202      12.142  10.556 -57.357  1.00 44.91           N  
ANISOU 1165  N   VAL A 202     5418   5926   5719   -761    848      9       N  
ATOM   1166  CA  VAL A 202      11.674  11.632 -58.244  1.00 47.06           C  
ANISOU 1166  CA  VAL A 202     5835   6117   5927   -905    811     42       C  
ATOM   1167  C   VAL A 202      12.700  12.749 -58.331  1.00 45.93           C  
ANISOU 1167  C   VAL A 202     5641   6088   5723  -1091    832     96       C  
ATOM   1168  O   VAL A 202      12.764  13.456 -59.328  1.00 51.02           O  
ANISOU 1168  O   VAL A 202     6380   6724   6282  -1217    848    131       O  
ATOM   1169  CB  VAL A 202      10.291  12.226 -57.825  1.00 38.80           C  
ANISOU 1169  CB  VAL A 202     4934   4873   4935   -908    687     46       C  
ATOM   1170  CG1 VAL A 202       9.207  11.140 -57.864  1.00 37.46           C  
ANISOU 1170  CG1 VAL A 202     4816   4608   4811   -759    667     -5       C  
ATOM   1171  CG2 VAL A 202      10.353  12.931 -56.479  1.00 42.49           C  
ANISOU 1171  CG2 VAL A 202     5359   5316   5468   -950    616     62       C  
ATOM   1172  N   MET A 203      13.533  12.884 -57.308  1.00 46.94           N  
ANISOU 1172  N   MET A 203     5619   6330   5884  -1119    833    104       N  
ATOM   1173  CA  MET A 203      14.626  13.844 -57.360  1.00 53.22           C  
ANISOU 1173  CA  MET A 203     6342   7266   6613  -1317    861    150       C  
ATOM   1174  C   MET A 203      15.606  13.490 -58.483  1.00 53.81           C  
ANISOU 1174  C   MET A 203     6324   7534   6585  -1348    988    158       C  
ATOM   1175  O   MET A 203      16.196  14.367 -59.135  1.00 51.78           O  
ANISOU 1175  O   MET A 203     6085   7352   6237  -1543   1022    204       O  
ATOM   1176  CB  MET A 203      15.335  13.896 -56.003  1.00 61.99           C  
ANISOU 1176  CB  MET A 203     7287   8494   7773  -1328    836    148       C  
ATOM   1177  CG  MET A 203      16.654  14.640 -56.014  1.00 70.72           C  
ANISOU 1177  CG  MET A 203     8261   9809   8801  -1531    880    186       C  
ATOM   1178  SD  MET A 203      16.780  15.765 -54.618  1.00147.10           S  
ANISOU 1178  SD  MET A 203    17936  19446  18508  -1696    772    198       S  
ATOM   1179  CE  MET A 203      15.635  17.041 -55.130  1.00 82.76           C  
ANISOU 1179  CE  MET A 203    10103  10996  10345  -1827    690    223       C  
ATOM   1180  N   PHE A 204      15.770  12.197 -58.734  1.00 55.88           N  
ANISOU 1180  N   PHE A 204     6502   7873   6857  -1156   1064    113       N  
ATOM   1181  CA  PHE A 204      16.621  11.764 -59.843  1.00 51.56           C  
ANISOU 1181  CA  PHE A 204     5877   7506   6208  -1151   1194    109       C  
ATOM   1182  C   PHE A 204      15.872  11.795 -61.155  1.00 48.23           C  
ANISOU 1182  C   PHE A 204     5645   6961   5719  -1169   1209    103       C  
ATOM   1183  O   PHE A 204      16.414  12.216 -62.183  1.00 50.39           O  
ANISOU 1183  O   PHE A 204     5928   7340   5880  -1292   1282    131       O  
ATOM   1184  CB  PHE A 204      17.167  10.362 -59.579  1.00 61.68           C  
ANISOU 1184  CB  PHE A 204     7004   8917   7516   -919   1275     59       C  
ATOM   1185  CG  PHE A 204      18.292  10.340 -58.595  1.00 60.17           C  
ANISOU 1185  CG  PHE A 204     6576   8944   7343   -912   1293     77       C  
ATOM   1186  CD1 PHE A 204      19.599  10.497 -59.019  1.00 65.95           C  
ANISOU 1186  CD1 PHE A 204     7120   9958   7980   -985   1394     98       C  
ATOM   1187  CD2 PHE A 204      18.043  10.193 -57.247  1.00 63.47           C  
ANISOU 1187  CD2 PHE A 204     6950   9305   7860   -840   1206     75       C  
ATOM   1188  CE1 PHE A 204      20.640  10.489 -58.112  1.00 71.64           C  
ANISOU 1188  CE1 PHE A 204     7602  10911   8707   -983   1402    116       C  
ATOM   1189  CE2 PHE A 204      19.080  10.184 -56.330  1.00 65.33           C  
ANISOU 1189  CE2 PHE A 204     6964   9759   8101   -836   1213     94       C  
ATOM   1190  CZ  PHE A 204      20.381  10.334 -56.765  1.00 66.94           C  
ANISOU 1190  CZ  PHE A 204     6971  10254   8211   -907   1307    115       C  
ATOM   1191  N   MET A 205      14.612  11.368 -61.124  1.00 40.62           N  
ANISOU 1191  N   MET A 205     4831   5788   4815  -1058   1138     69       N  
ATOM   1192  CA  MET A 205      13.825  11.264 -62.352  1.00 43.53           C  
ANISOU 1192  CA  MET A 205     5373   6052   5116  -1058   1143     56       C  
ATOM   1193  C   MET A 205      13.423  12.619 -62.914  1.00 47.95           C  
ANISOU 1193  C   MET A 205     6083   6522   5612  -1249   1080    124       C  
ATOM   1194  O   MET A 205      13.290  12.785 -64.131  1.00 47.04           O  
ANISOU 1194  O   MET A 205     6073   6409   5392  -1307   1115    138       O  
ATOM   1195  CB  MET A 205      12.570  10.441 -62.106  1.00 42.16           C  
ANISOU 1195  CB  MET A 205     5301   5698   5018   -904   1077      1       C  
ATOM   1196  CG  MET A 205      12.835   8.983 -61.766  1.00 50.51           C  
ANISOU 1196  CG  MET A 205     6270   6800   6120   -707   1145    -66       C  
ATOM   1197  SD  MET A 205      11.451   8.261 -60.864  1.00 61.16           S  
ANISOU 1197  SD  MET A 205     7707   7941   7591   -578   1043   -109       S  
ATOM   1198  CE  MET A 205      10.077   9.175 -61.554  1.00139.12           C  
ANISOU 1198  CE  MET A 205    17773  17655  17431   -693    932    -85       C  
ATOM   1199  N   ALA A 206      13.207  13.581 -62.027  1.00 43.63           N  
ANISOU 1199  N   ALA A 206     5564   5889   5123  -1341    985    165       N  
ATOM   1200  CA  ALA A 206      12.711  14.887 -62.449  1.00 44.53           C  
ANISOU 1200  CA  ALA A 206     5857   5875   5187  -1498    912    231       C  
ATOM   1201  C   ALA A 206      13.732  15.588 -63.314  1.00 47.18           C  
ANISOU 1201  C   ALA A 206     6187   6346   5396  -1692    995    289       C  
ATOM   1202  O   ALA A 206      14.928  15.611 -63.013  1.00 51.92           O  
ANISOU 1202  O   ALA A 206     6618   7135   5975  -1773   1070    297       O  
ATOM   1203  CB  ALA A 206      12.349  15.761 -61.242  1.00 40.23           C  
ANISOU 1203  CB  ALA A 206     5352   5206   4728  -1547    803    252       C  
ATOM   1204  N   THR A 207      13.251  16.162 -64.402  1.00 50.88           N  
ANISOU 1204  N   THR A 207     6834   6729   5768  -1770    979    336       N  
ATOM   1205  CA  THR A 207      14.121  16.925 -65.266  1.00 55.02           C  
ANISOU 1205  CA  THR A 207     7386   7362   6159  -1977   1053    404       C  
ATOM   1206  C   THR A 207      13.289  17.855 -66.113  1.00 46.12           C  
ANISOU 1206  C   THR A 207     6514   6058   4952  -2060    982    474       C  
ATOM   1207  O   THR A 207      12.086  17.660 -66.275  1.00 54.51           O  
ANISOU 1207  O   THR A 207     7701   6965   6045  -1929    896    458       O  
ATOM   1208  CB  THR A 207      14.974  16.008 -66.173  1.00 61.25           C  
ANISOU 1208  CB  THR A 207     8038   8379   6854  -1943   1202    370       C  
ATOM   1209  OG1 THR A 207      16.102  16.738 -66.664  1.00 71.03           O  
ANISOU 1209  OG1 THR A 207     9228   9785   7977  -2165   1289    434       O  
ATOM   1210  CG2 THR A 207      14.150  15.477 -67.340  1.00 49.82           C  
ANISOU 1210  CG2 THR A 207     6731   6864   5336  -1845   1208    347       C  
ATOM   1211  N   THR A 208      13.932  18.884 -66.633  1.00 56.76           N  
ANISOU 1211  N   THR A 208     7939   7437   6190  -2284   1014    559       N  
ATOM   1212  CA  THR A 208      13.322  19.701 -67.658  1.00 61.87           C  
ANISOU 1212  CA  THR A 208     8833   7948   6728  -2367    970    639       C  
ATOM   1213  C   THR A 208      13.711  19.135 -69.011  1.00 67.07           C  
ANISOU 1213  C   THR A 208     9470   8768   7247  -2381   1083    640       C  
ATOM   1214  O   THR A 208      14.868  18.783 -69.225  1.00 73.79           O  
ANISOU 1214  O   THR A 208    10150   9847   8041  -2460   1213    626       O  
ATOM   1215  CB  THR A 208      13.773  21.156 -67.557  1.00 57.72           C  
ANISOU 1215  CB  THR A 208     8446   7343   6144  -2617    946    739       C  
ATOM   1216  OG1 THR A 208      15.205  21.205 -67.609  1.00 56.70           O  
ANISOU 1216  OG1 THR A 208     8147   7448   5948  -2806   1070    752       O  
ATOM   1217  CG2 THR A 208      13.292  21.769 -66.232  1.00 48.65           C  
ANISOU 1217  CG2 THR A 208     7353   6007   5123  -2593    828    729       C  
ATOM   1218  N   LYS A 209      12.746  19.028 -69.914  1.00 61.25           N  
ANISOU 1218  N   LYS A 209     8896   7929   6446  -2299   1034    652       N  
ATOM   1219  CA  LYS A 209      13.057  18.712 -71.300  1.00 75.72           C  
ANISOU 1219  CA  LYS A 209    10758   9895   8116  -2343   1132    667       C  
ATOM   1220  C   LYS A 209      12.169  19.532 -72.230  1.00 84.77           C  
ANISOU 1220  C   LYS A 209    12173  10882   9152  -2390   1044    758       C  
ATOM   1221  O   LYS A 209      11.089  19.986 -71.836  1.00 78.80           O  
ANISOU 1221  O   LYS A 209    11556   9921   8464  -2306    903    781       O  
ATOM   1222  CB  LYS A 209      12.886  17.217 -71.577  1.00 73.15           C  
ANISOU 1222  CB  LYS A 209    10308   9676   7810  -2143   1191    549       C  
ATOM   1223  CG  LYS A 209      11.506  16.695 -71.263  1.00 68.94           C  
ANISOU 1223  CG  LYS A 209     9847   8974   7374  -1948   1067    493       C  
ATOM   1224  CD  LYS A 209      11.244  15.379 -71.967  1.00 70.04           C  
ANISOU 1224  CD  LYS A 209     9948   9195   7470  -1805   1126    394       C  
ATOM   1225  CE  LYS A 209      11.237  15.574 -73.468  1.00 81.11           C  
ANISOU 1225  CE  LYS A 209    11483  10657   8677  -1889   1170    436       C  
ATOM   1226  NZ  LYS A 209      10.802  14.339 -74.174  1.00 82.29           N  
ANISOU 1226  NZ  LYS A 209    11633  10855   8776  -1753   1206    331       N  
ATOM   1227  N   TYR A 210      12.623  19.720 -73.466  1.00 88.88           N  
ANISOU 1227  N   TYR A 210    12765  11511   9496  -2513   1128    814       N  
ATOM   1228  CA  TYR A 210      11.884  20.536 -74.420  1.00 89.01           C  
ANISOU 1228  CA  TYR A 210    13042  11393   9383  -2567   1049    917       C  
ATOM   1229  C   TYR A 210      10.645  19.834 -74.960  1.00 87.45           C  
ANISOU 1229  C   TYR A 210    12916  11136   9175  -2367    966    866       C  
ATOM   1230  O   TYR A 210      10.646  18.631 -75.225  1.00 87.39           O  
ANISOU 1230  O   TYR A 210    12782  11253   9169  -2249   1028    758       O  
ATOM   1231  CB  TYR A 210      12.789  20.962 -75.569  1.00 92.02           C  
ANISOU 1231  CB  TYR A 210    13478  11921   9564  -2778   1170    999       C  
ATOM   1232  CG  TYR A 210      13.577  22.205 -75.252  1.00103.24           C  
ANISOU 1232  CG  TYR A 210    14968  13304  10953  -3030   1189   1108       C  
ATOM   1233  CD1 TYR A 210      12.963  23.451 -75.249  1.00110.94           C  
ANISOU 1233  CD1 TYR A 210    16195  14036  11922  -3080   1057   1212       C  
ATOM   1234  CD2 TYR A 210      14.930  22.138 -74.947  1.00106.94           C  
ANISOU 1234  CD2 TYR A 210    15219  13978  11437  -3155   1307   1077       C  
ATOM   1235  CE1 TYR A 210      13.676  24.597 -74.954  1.00117.06           C  
ANISOU 1235  CE1 TYR A 210    17005  14755  12719  -3237   1035   1259       C  
ATOM   1236  CE2 TYR A 210      15.653  23.277 -74.651  1.00112.31           C  
ANISOU 1236  CE2 TYR A 210    15918  14621  12135  -3323   1278   1130       C  
ATOM   1237  CZ  TYR A 210      15.020  24.505 -74.657  1.00118.58           C  
ANISOU 1237  CZ  TYR A 210    16973  15154  12927  -3371   1145   1217       C  
ATOM   1238  OH  TYR A 210      15.732  25.647 -74.364  1.00122.71           O  
ANISOU 1238  OH  TYR A 210    17539  15629  13457  -3544   1120   1259       O  
ATOM   1239  N   ARG A 211       9.587  20.618 -75.115  1.00 86.09           N  
ANISOU 1239  N   ARG A 211    12954  10771   8985  -2330    822    944       N  
ATOM   1240  CA  ARG A 211       8.283  20.119 -75.511  1.00 89.93           C  
ANISOU 1240  CA  ARG A 211    13508  11197   9465  -2148    713    908       C  
ATOM   1241  C   ARG A 211       7.574  21.187 -76.339  1.00102.04           C  
ANISOU 1241  C   ARG A 211    15303  12603  10863  -2185    608   1043       C  
ATOM   1242  O   ARG A 211       6.866  22.037 -75.792  1.00108.04           O  
ANISOU 1242  O   ARG A 211    16189  13175  11686  -2133    481   1107       O  
ATOM   1243  CB  ARG A 211       7.455  19.745 -74.278  1.00 93.64           C  
ANISOU 1243  CB  ARG A 211    13890  11559  10132  -1972    611    830       C  
ATOM   1244  CG  ARG A 211       6.082  19.188 -74.586  1.00 93.85           C  
ANISOU 1244  CG  ARG A 211    13954  11545  10158  -1796    496    784       C  
ATOM   1245  CD  ARG A 211       6.176  17.792 -75.143  1.00100.85           C  
ANISOU 1245  CD  ARG A 211    14721  12590  11006  -1740    579    666       C  
ATOM   1246  NE  ARG A 211       5.032  17.474 -75.989  1.00109.37           N  
ANISOU 1246  NE  ARG A 211    15894  13669  11991  -1654    484    655       N  
ATOM   1247  CZ  ARG A 211       4.923  16.357 -76.699  1.00115.93           C  
ANISOU 1247  CZ  ARG A 211    16680  14618  12750  -1618    536    559       C  
ATOM   1248  NH1 ARG A 211       5.891  15.451 -76.662  1.00115.73           N  
ANISOU 1248  NH1 ARG A 211    16524  14708  12738  -1637    686    466       N  
ATOM   1249  NH2 ARG A 211       3.848  16.144 -77.446  1.00120.51           N  
ANISOU 1249  NH2 ARG A 211    17347  15204  13236  -1558    435    552       N  
ATOM   1250  N   GLN A 212       7.794  21.144 -77.654  1.00100.15           N  
ANISOU 1250  N   GLN A 212    15151  12471  10431  -2267    666   1088       N  
ATOM   1251  CA  GLN A 212       7.197  22.082 -78.605  1.00 95.29           C  
ANISOU 1251  CA  GLN A 212    14792  11761   9655  -2304    576   1227       C  
ATOM   1252  C   GLN A 212       7.620  23.522 -78.327  1.00 96.94           C  
ANISOU 1252  C   GLN A 212    15178  11810   9844  -2460    556   1371       C  
ATOM   1253  O   GLN A 212       6.783  24.423 -78.238  1.00 93.85           O  
ANISOU 1253  O   GLN A 212    14986  11223   9451  -2395    418   1465       O  
ATOM   1254  CB  GLN A 212       5.670  21.963 -78.586  1.00 90.38           C  
ANISOU 1254  CB  GLN A 212    14237  11037   9067  -2092    401   1215       C  
ATOM   1255  CG  GLN A 212       5.178  20.525 -78.629  1.00 93.73           C  
ANISOU 1255  CG  GLN A 212    14485  11591   9538  -1951    408   1059       C  
ATOM   1256  CD  GLN A 212       3.681  20.421 -78.822  1.00 98.42           C  
ANISOU 1256  CD  GLN A 212    15143  12130  10124  -1778    239   1056       C  
ATOM   1257  OE1 GLN A 212       3.130  20.972 -79.772  1.00103.99           O  
ANISOU 1257  OE1 GLN A 212    16020  12821  10670  -1776    159   1155       O  
ATOM   1258  NE2 GLN A 212       3.014  19.710 -77.918  1.00 95.47           N  
ANISOU 1258  NE2 GLN A 212    14623  11739   9913  -1634    182    947       N  
ATOM   1259  N   GLY A 213       8.927  23.732 -78.192  1.00100.98           N  
ANISOU 1259  N   GLY A 213    15619  12411  10337  -2666    696   1386       N  
ATOM   1260  CA  GLY A 213       9.464  25.043 -77.873  1.00107.66           C  
ANISOU 1260  CA  GLY A 213    16589  13121  11197  -2821    681   1484       C  
ATOM   1261  C   GLY A 213       9.365  25.354 -76.390  1.00111.27           C  
ANISOU 1261  C   GLY A 213    17007  13428  11842  -2786    623   1452       C  
ATOM   1262  O   GLY A 213      10.302  25.887 -75.794  1.00116.61           O  
ANISOU 1262  O   GLY A 213    17609  14109  12587  -2921    671   1440       O  
ATOM   1263  N   SER A 214       8.223  25.011 -75.796  1.00104.82           N  
ANISOU 1263  N   SER A 214    16187  12503  11136  -2564    504   1402       N  
ATOM   1264  CA  SER A 214       7.956  25.252 -74.380  1.00 88.53           C  
ANISOU 1264  CA  SER A 214    14076  10300   9263  -2482    433   1353       C  
ATOM   1265  C   SER A 214       8.601  24.181 -73.494  1.00 87.89           C  
ANISOU 1265  C   SER A 214    13687  10383   9324  -2458    524   1210       C  
ATOM   1266  O   SER A 214       9.004  23.126 -73.980  1.00 90.10           O  
ANISOU 1266  O   SER A 214    13795  10867   9570  -2443    622   1136       O  
ATOM   1267  CB  SER A 214       6.449  25.303 -74.140  1.00 78.17           C  
ANISOU 1267  CB  SER A 214    12849   8837   8015  -2227    268   1345       C  
ATOM   1268  OG  SER A 214       6.028  24.204 -73.354  1.00 81.02           O  
ANISOU 1268  OG  SER A 214    12977   9279   8530  -2056    255   1203       O  
ATOM   1269  N   ILE A 215       8.689  24.447 -72.194  1.00 81.62           N  
ANISOU 1269  N   ILE A 215    12835   9496   8683  -2444    490   1171       N  
ATOM   1270  CA  ILE A 215       9.414  23.558 -71.286  1.00 71.50           C  
ANISOU 1270  CA  ILE A 215    11274   8366   7526  -2437    574   1054       C  
ATOM   1271  C   ILE A 215       8.515  22.852 -70.269  1.00 71.89           C  
ANISOU 1271  C   ILE A 215    11205   8365   7747  -2203    490    949       C  
ATOM   1272  O   ILE A 215       7.748  23.487 -69.530  1.00 66.65           O  
ANISOU 1272  O   ILE A 215    10647   7515   7163  -2118    376    964       O  
ATOM   1273  CB  ILE A 215      10.512  24.318 -70.519  1.00 68.38           C  
ANISOU 1273  CB  ILE A 215    10859   7964   7159  -2653    627   1084       C  
ATOM   1274  CG1 ILE A 215      11.553  24.873 -71.489  1.00 68.68           C  
ANISOU 1274  CG1 ILE A 215    10968   8103   7024  -2917    735   1178       C  
ATOM   1275  CG2 ILE A 215      11.159  23.421 -69.469  1.00 62.78           C  
ANISOU 1275  CG2 ILE A 215     9859   7411   6585  -2614    690    967       C  
ATOM   1276  CD1 ILE A 215      12.584  25.763 -70.823  1.00 68.24           C  
ANISOU 1276  CD1 ILE A 215    10868   8051   7007  -3092    749   1178       C  
ATOM   1277  N   ASP A 216       8.619  21.526 -70.256  1.00 62.49           N  
ANISOU 1277  N   ASP A 216     9801   7339   6602  -2099    553    843       N  
ATOM   1278  CA  ASP A 216       7.906  20.693 -69.307  1.00 57.27           C  
ANISOU 1278  CA  ASP A 216     9006   6659   6096  -1903    498    741       C  
ATOM   1279  C   ASP A 216       8.864  20.327 -68.174  1.00 65.00           C  
ANISOU 1279  C   ASP A 216     9783   7726   7187  -1944    570    678       C  
ATOM   1280  O   ASP A 216      10.004  19.915 -68.423  1.00 65.92           O  
ANISOU 1280  O   ASP A 216     9767   8019   7260  -2045    695    661       O  
ATOM   1281  CB  ASP A 216       7.355  19.436 -69.994  1.00 65.49           C  
ANISOU 1281  CB  ASP A 216     9969   7804   7110  -1765    515    664       C  
ATOM   1282  CG  ASP A 216       6.404  18.631 -69.107  1.00 78.85           C  
ANISOU 1282  CG  ASP A 216    11561   9454   8944  -1573    441    571       C  
ATOM   1283  OD1 ASP A 216       5.957  19.133 -68.049  1.00 81.98           O  
ANISOU 1283  OD1 ASP A 216    11968   9730   9449  -1520    359    574       O  
ATOM   1284  OD2 ASP A 216       6.089  17.485 -69.488  1.00 87.14           O  
ANISOU 1284  OD2 ASP A 216    12530  10590   9988  -1481    468    492       O  
ATOM   1285  N   CYS A 217       8.418  20.530 -66.937  1.00 63.64           N  
ANISOU 1285  N   CYS A 217     9587   7443   7148  -1865    491    647       N  
ATOM   1286  CA  CYS A 217       9.109  19.962 -65.787  1.00 54.22           C  
ANISOU 1286  CA  CYS A 217     8187   6342   6071  -1854    540    574       C  
ATOM   1287  C   CYS A 217       8.460  18.602 -65.574  1.00 53.18           C  
ANISOU 1287  C   CYS A 217     7925   6263   6020  -1652    536    477       C  
ATOM   1288  O   CYS A 217       7.293  18.518 -65.201  1.00 56.53           O  
ANISOU 1288  O   CYS A 217     8398   6573   6508  -1514    436    454       O  
ATOM   1289  CB  CYS A 217       8.994  20.857 -64.550  1.00 49.51           C  
ANISOU 1289  CB  CYS A 217     7641   5607   5566  -1884    462    586       C  
ATOM   1290  SG  CYS A 217       9.710  20.128 -63.017  1.00 59.27           S  
ANISOU 1290  SG  CYS A 217     8618   6958   6942  -1849    501    496       S  
ATOM   1291  N   THR A 218       9.201  17.534 -65.842  1.00 58.16           N  
ANISOU 1291  N   THR A 218     8395   7066   6637  -1634    648    420       N  
ATOM   1292  CA  THR A 218       8.566  16.227 -65.957  1.00 61.30           C  
ANISOU 1292  CA  THR A 218     8723   7495   7074  -1463    653    335       C  
ATOM   1293  C   THR A 218       9.453  15.122 -65.370  1.00 53.26           C  
ANISOU 1293  C   THR A 218     7497   6620   6120  -1404    755    260       C  
ATOM   1294  O   THR A 218      10.554  15.397 -64.894  1.00 53.68           O  
ANISOU 1294  O   THR A 218     7441   6772   6182  -1492    816    277       O  
ATOM   1295  CB  THR A 218       8.201  15.938 -67.461  1.00 56.99           C  
ANISOU 1295  CB  THR A 218     8282   6982   6392  -1464    676    343       C  
ATOM   1296  OG1 THR A 218       7.276  14.850 -67.553  1.00 64.80           O  
ANISOU 1296  OG1 THR A 218     9253   7954   7415  -1313    644    262       O  
ATOM   1297  CG2 THR A 218       9.438  15.651 -68.292  1.00 48.04           C  
ANISOU 1297  CG2 THR A 218     7082   6023   5149  -1561    821    345       C  
ATOM   1298  N   LEU A 219       8.957  13.887 -65.379  1.00 49.07           N  
ANISOU 1298  N   LEU A 219     6917   6099   5629  -1255    767    179       N  
ATOM   1299  CA  LEU A 219       9.702  12.735 -64.869  1.00 44.43           C  
ANISOU 1299  CA  LEU A 219     6161   5624   5097  -1163    861    109       C  
ATOM   1300  C   LEU A 219      10.203  11.874 -66.030  1.00 49.16           C  
ANISOU 1300  C   LEU A 219     6749   6342   5590  -1136    979     66       C  
ATOM   1301  O   LEU A 219       9.478  11.633 -66.986  1.00 50.94           O  
ANISOU 1301  O   LEU A 219     7093   6521   5740  -1121    960     48       O  
ATOM   1302  CB  LEU A 219       8.826  11.894 -63.927  1.00 41.92           C  
ANISOU 1302  CB  LEU A 219     5813   5214   4902  -1012    799     47       C  
ATOM   1303  CG  LEU A 219       8.282  12.628 -62.701  1.00 47.82           C  
ANISOU 1303  CG  LEU A 219     6562   5854   5753  -1014    690     75       C  
ATOM   1304  CD1 LEU A 219       7.241  11.795 -61.942  1.00 44.20           C  
ANISOU 1304  CD1 LEU A 219     6091   5309   5392   -877    628     17       C  
ATOM   1305  CD2 LEU A 219       9.418  13.005 -61.797  1.00 44.98           C  
ANISOU 1305  CD2 LEU A 219     6074   5580   5435  -1072    729     98       C  
ATOM   1306  N   THR A 220      11.453  11.438 -65.963  1.00 44.04           N  
ANISOU 1306  N   THR A 220     5952   5857   4923  -1129   1100     48       N  
ATOM   1307  CA  THR A 220      11.969  10.501 -66.960  1.00 53.10           C  
ANISOU 1307  CA  THR A 220     7080   7123   5975  -1068   1225     -9       C  
ATOM   1308  C   THR A 220      12.118   9.130 -66.311  1.00 51.89           C  
ANISOU 1308  C   THR A 220     6829   6982   5905   -878   1274    -96       C  
ATOM   1309  O   THR A 220      12.558   9.018 -65.164  1.00 56.13           O  
ANISOU 1309  O   THR A 220     7237   7548   6543   -826   1268    -91       O  
ATOM   1310  CB  THR A 220      13.309  10.959 -67.540  1.00 62.87           C  
ANISOU 1310  CB  THR A 220     8221   8563   7103  -1184   1345     33       C  
ATOM   1311  OG1 THR A 220      14.205  11.262 -66.464  1.00 74.35           O  
ANISOU 1311  OG1 THR A 220     9502  10116   8631  -1212   1360     61       O  
ATOM   1312  CG2 THR A 220      13.121  12.198 -68.398  1.00 61.44           C  
ANISOU 1312  CG2 THR A 220     8178   8354   6811  -1375   1308    120       C  
ATOM   1313  N   PHE A 221      11.727   8.087 -67.027  1.00 45.44           N  
ANISOU 1313  N   PHE A 221     6092   6133   5042   -776   1318   -174       N  
ATOM   1314  CA  PHE A 221      11.626   6.763 -66.421  1.00 44.73           C  
ANISOU 1314  CA  PHE A 221     5968   5994   5031   -595   1347   -256       C  
ATOM   1315  C   PHE A 221      12.579   5.798 -67.084  1.00 46.20           C  
ANISOU 1315  C   PHE A 221     6107   6310   5136   -486   1504   -322       C  
ATOM   1316  O   PHE A 221      13.047   6.057 -68.177  1.00 46.45           O  
ANISOU 1316  O   PHE A 221     6159   6452   5037   -553   1581   -319       O  
ATOM   1317  CB  PHE A 221      10.200   6.235 -66.530  1.00 43.85           C  
ANISOU 1317  CB  PHE A 221     6013   5700   4947   -561   1255   -305       C  
ATOM   1318  CG  PHE A 221       9.203   7.029 -65.746  1.00 48.97           C  
ANISOU 1318  CG  PHE A 221     6691   6228   5686   -624   1106   -252       C  
ATOM   1319  CD1 PHE A 221       8.939   6.717 -64.427  1.00 44.45           C  
ANISOU 1319  CD1 PHE A 221     6055   5587   5247   -549   1055   -257       C  
ATOM   1320  CD2 PHE A 221       8.532   8.093 -66.329  1.00 47.63           C  
ANISOU 1320  CD2 PHE A 221     6619   6019   5459   -748   1020   -195       C  
ATOM   1321  CE1 PHE A 221       8.016   7.458 -63.692  1.00 50.07           C  
ANISOU 1321  CE1 PHE A 221     6790   6199   6033   -597    926   -214       C  
ATOM   1322  CE2 PHE A 221       7.618   8.826 -65.615  1.00 46.14           C  
ANISOU 1322  CE2 PHE A 221     6459   5724   5347   -779    888   -150       C  
ATOM   1323  CZ  PHE A 221       7.357   8.516 -64.288  1.00 44.45           C  
ANISOU 1323  CZ  PHE A 221     6172   5451   5267   -704    844   -164       C  
ATOM   1324  N   SER A 222      12.865   4.676 -66.431  1.00 49.99           N  
ANISOU 1324  N   SER A 222     6533   6775   5685   -308   1553   -380       N  
ATOM   1325  CA  SER A 222      13.645   3.614 -67.078  1.00 54.53           C  
ANISOU 1325  CA  SER A 222     7096   7443   6181   -161   1703   -458       C  
ATOM   1326  C   SER A 222      12.837   2.946 -68.188  1.00 48.36           C  
ANISOU 1326  C   SER A 222     6519   6546   5308   -153   1716   -543       C  
ATOM   1327  O   SER A 222      11.615   3.112 -68.278  1.00 48.02           O  
ANISOU 1327  O   SER A 222     6613   6349   5284   -236   1601   -545       O  
ATOM   1328  CB  SER A 222      14.075   2.549 -66.063  1.00 62.99           C  
ANISOU 1328  CB  SER A 222     8088   8497   7349     48   1743   -495       C  
ATOM   1329  OG  SER A 222      14.639   3.126 -64.900  1.00 65.04           O  
ANISOU 1329  OG  SER A 222     8166   8845   7699     36   1703   -419       O  
ATOM   1330  N   HIS A 223      13.515   2.158 -69.007  1.00 49.96           N  
ANISOU 1330  N   HIS A 223     6740   6835   5407    -46   1857   -618       N  
ATOM   1331  CA  HIS A 223      12.840   1.352 -70.010  1.00 56.04           C  
ANISOU 1331  CA  HIS A 223     7714   7495   6083    -21   1882   -718       C  
ATOM   1332  C   HIS A 223      12.184   0.139 -69.357  1.00 52.57           C  
ANISOU 1332  C   HIS A 223     7385   6854   5735    114   1853   -794       C  
ATOM   1333  O   HIS A 223      12.730  -0.429 -68.408  1.00 59.04           O  
ANISOU 1333  O   HIS A 223     8117   7670   6648    268   1889   -794       O  
ATOM   1334  CB  HIS A 223      13.829   0.906 -71.088  1.00 62.25           C  
ANISOU 1334  CB  HIS A 223     8492   8441   6719     58   2053   -782       C  
ATOM   1335  CG  HIS A 223      14.645   2.024 -71.654  1.00 83.89           C  
ANISOU 1335  CG  HIS A 223    11103  11407   9364    -74   2104   -702       C  
ATOM   1336  ND1 HIS A 223      14.083   3.087 -72.329  1.00 89.83           N  
ANISOU 1336  ND1 HIS A 223    11927  12160  10045   -286   2026   -638       N  
ATOM   1337  CD2 HIS A 223      15.981   2.241 -71.654  1.00 95.32           C  
ANISOU 1337  CD2 HIS A 223    12354  13092  10769    -32   2226   -672       C  
ATOM   1338  CE1 HIS A 223      15.039   3.910 -72.721  1.00 96.76           C  
ANISOU 1338  CE1 HIS A 223    12677  13247  10839   -381   2100   -570       C  
ATOM   1339  NE2 HIS A 223      16.199   3.421 -72.323  1.00100.43           N  
ANISOU 1339  NE2 HIS A 223    12967  13871  11319   -239   2223   -592       N  
ATOM   1340  N   PRO A 224      10.986  -0.235 -69.829  1.00 53.89           N  
ANISOU 1340  N   PRO A 224     7746   6857   5872     45   1780   -853       N  
ATOM   1341  CA  PRO A 224      10.192   0.548 -70.779  1.00 51.23           C  
ANISOU 1341  CA  PRO A 224     7500   6527   5439   -141   1701   -833       C  
ATOM   1342  C   PRO A 224       9.392   1.604 -70.036  1.00 42.48           C  
ANISOU 1342  C   PRO A 224     6338   5370   4431   -268   1541   -731       C  
ATOM   1343  O   PRO A 224       8.853   1.335 -68.963  1.00 40.63           O  
ANISOU 1343  O   PRO A 224     6088   5021   4327   -231   1465   -722       O  
ATOM   1344  CB  PRO A 224       9.280  -0.493 -71.411  1.00 57.98           C  
ANISOU 1344  CB  PRO A 224     8569   7232   6230   -135   1690   -950       C  
ATOM   1345  CG  PRO A 224       9.039  -1.472 -70.293  1.00 57.44           C  
ANISOU 1345  CG  PRO A 224     8523   7008   6294    -15   1677   -987       C  
ATOM   1346  CD  PRO A 224      10.319  -1.502 -69.471  1.00 53.81           C  
ANISOU 1346  CD  PRO A 224     7886   6648   5911    141   1769   -942       C  
ATOM   1347  N   THR A 225       9.342   2.811 -70.577  1.00 38.44           N  
ANISOU 1347  N   THR A 225     5805   4945   3854   -410   1494   -651       N  
ATOM   1348  CA  THR A 225       8.755   3.932 -69.849  1.00 41.56           C  
ANISOU 1348  CA  THR A 225     6147   5303   4340   -510   1355   -548       C  
ATOM   1349  C   THR A 225       7.292   3.685 -69.528  1.00 38.61           C  
ANISOU 1349  C   THR A 225     5873   4774   4024   -536   1219   -572       C  
ATOM   1350  O   THR A 225       6.815   4.088 -68.465  1.00 43.49           O  
ANISOU 1350  O   THR A 225     6431   5329   4765   -540   1124   -521       O  
ATOM   1351  CB  THR A 225       8.878   5.245 -70.640  1.00 43.65           C  
ANISOU 1351  CB  THR A 225     6421   5661   4503   -659   1328   -459       C  
ATOM   1352  OG1 THR A 225       8.304   5.049 -71.937  1.00 49.47           O  
ANISOU 1352  OG1 THR A 225     7308   6395   5092   -713   1324   -504       O  
ATOM   1353  CG2 THR A 225      10.337   5.625 -70.800  1.00 44.04           C  
ANISOU 1353  CG2 THR A 225     6345   5885   4505   -666   1457   -420       C  
ATOM   1354  N   TRP A 226       6.580   3.008 -70.434  1.00 41.06           N  
ANISOU 1354  N   TRP A 226     6328   5035   4237   -557   1212   -653       N  
ATOM   1355  CA  TRP A 226       5.147   2.794 -70.223  1.00 44.54           C  
ANISOU 1355  CA  TRP A 226     6848   5361   4712   -605   1079   -675       C  
ATOM   1356  C   TRP A 226       4.873   1.872 -69.034  1.00 48.65           C  
ANISOU 1356  C   TRP A 226     7347   5768   5371   -519   1071   -718       C  
ATOM   1357  O   TRP A 226       3.794   1.907 -68.442  1.00 43.55           O  
ANISOU 1357  O   TRP A 226     6707   5047   4793   -560    957   -707       O  
ATOM   1358  CB  TRP A 226       4.468   2.246 -71.482  1.00 44.79           C  
ANISOU 1358  CB  TRP A 226     7038   5384   4594   -668   1070   -759       C  
ATOM   1359  CG  TRP A 226       5.242   1.206 -72.247  1.00 47.51           C  
ANISOU 1359  CG  TRP A 226     7466   5746   4839   -600   1220   -865       C  
ATOM   1360  CD1 TRP A 226       6.029   1.414 -73.343  1.00 50.82           C  
ANISOU 1360  CD1 TRP A 226     7913   6283   5115   -611   1320   -875       C  
ATOM   1361  CD2 TRP A 226       5.279  -0.202 -71.988  1.00 42.42           C  
ANISOU 1361  CD2 TRP A 226     6905   4991   4222   -506   1291   -979       C  
ATOM   1362  NE1 TRP A 226       6.560   0.222 -73.780  1.00 51.73           N  
ANISOU 1362  NE1 TRP A 226     8114   6375   5166   -516   1451   -995       N  
ATOM   1363  CE2 TRP A 226       6.118  -0.783 -72.960  1.00 52.27           C  
ANISOU 1363  CE2 TRP A 226     8228   6292   5339   -447   1435  -1060       C  
ATOM   1364  CE3 TRP A 226       4.691  -1.025 -71.023  1.00 43.79           C  
ANISOU 1364  CE3 TRP A 226     7107   5021   4511   -468   1251  -1017       C  
ATOM   1365  CZ2 TRP A 226       6.383  -2.155 -72.996  1.00 57.01           C  
ANISOU 1365  CZ2 TRP A 226     8945   6792   5925   -334   1537  -1183       C  
ATOM   1366  CZ3 TRP A 226       4.959  -2.393 -71.065  1.00 41.69           C  
ANISOU 1366  CZ3 TRP A 226     6964   4649   4229   -373   1352  -1131       C  
ATOM   1367  CH2 TRP A 226       5.792  -2.936 -72.040  1.00 42.99           C  
ANISOU 1367  CH2 TRP A 226     7214   4854   4266   -300   1491  -1214       C  
ATOM   1368  N   TYR A 227       5.839   1.052 -68.655  1.00 38.73           N  
ANISOU 1368  N   TYR A 227     6062   4504   4151   -395   1192   -760       N  
ATOM   1369  CA  TYR A 227       5.614   0.251 -67.457  1.00 35.37           C  
ANISOU 1369  CA  TYR A 227     5621   3963   3853   -311   1180   -781       C  
ATOM   1370  C   TYR A 227       5.869   1.108 -66.226  1.00 33.92           C  
ANISOU 1370  C   TYR A 227     5275   3814   3798   -297   1126   -679       C  
ATOM   1371  O   TYR A 227       4.980   1.302 -65.375  1.00 38.78           O  
ANISOU 1371  O   TYR A 227     5870   4361   4503   -333   1020   -649       O  
ATOM   1372  CB  TYR A 227       6.500  -1.004 -67.473  1.00 38.10           C  
ANISOU 1372  CB  TYR A 227     6018   4273   4187   -159   1323   -862       C  
ATOM   1373  CG  TYR A 227       6.296  -1.924 -66.288  1.00 38.83           C  
ANISOU 1373  CG  TYR A 227     6127   4230   4398    -65   1317   -878       C  
ATOM   1374  CD1 TYR A 227       6.892  -1.654 -65.058  1.00 41.54           C  
ANISOU 1374  CD1 TYR A 227     6319   4605   4860     21   1316   -803       C  
ATOM   1375  CD2 TYR A 227       5.508  -3.069 -66.402  1.00 36.52           C  
ANISOU 1375  CD2 TYR A 227     6011   3778   4088    -76   1312   -968       C  
ATOM   1376  CE1 TYR A 227       6.699  -2.488 -63.970  1.00 44.53           C  
ANISOU 1376  CE1 TYR A 227     6722   4863   5337    106   1309   -808       C  
ATOM   1377  CE2 TYR A 227       5.303  -3.900 -65.328  1.00 40.02           C  
ANISOU 1377  CE2 TYR A 227     6488   4089   4630     -6   1308   -974       C  
ATOM   1378  CZ  TYR A 227       5.910  -3.612 -64.116  1.00 37.80           C  
ANISOU 1378  CZ  TYR A 227     6054   3843   4464     93   1308   -890       C  
ATOM   1379  OH  TYR A 227       5.733  -4.453 -63.061  1.00 41.89           O  
ANISOU 1379  OH  TYR A 227     6616   4232   5069    168   1306   -888       O  
ATOM   1380  N   TRP A 228       7.074   1.654 -66.119  1.00 39.92           N  
ANISOU 1380  N   TRP A 228     5914   4694   4560   -254   1198   -628       N  
ATOM   1381  CA  TRP A 228       7.463   2.294 -64.863  1.00 39.11           C  
ANISOU 1381  CA  TRP A 228     5661   4624   4575   -232   1161   -547       C  
ATOM   1382  C   TRP A 228       6.671   3.577 -64.581  1.00 36.39           C  
ANISOU 1382  C   TRP A 228     5292   4271   4263   -357   1027   -470       C  
ATOM   1383  O   TRP A 228       6.417   3.909 -63.416  1.00 35.94           O  
ANISOU 1383  O   TRP A 228     5162   4179   4314   -347    959   -426       O  
ATOM   1384  CB  TRP A 228       8.980   2.567 -64.864  1.00 39.63           C  
ANISOU 1384  CB  TRP A 228     5591   4846   4620   -175   1270   -514       C  
ATOM   1385  CG  TRP A 228       9.744   1.285 -64.972  1.00 35.14           C  
ANISOU 1385  CG  TRP A 228     5035   4286   4030     -9   1399   -587       C  
ATOM   1386  CD1 TRP A 228      10.462   0.841 -66.040  1.00 35.23           C  
ANISOU 1386  CD1 TRP A 228     5080   4379   3925     44   1522   -643       C  
ATOM   1387  CD2 TRP A 228       9.799   0.245 -63.989  1.00 35.05           C  
ANISOU 1387  CD2 TRP A 228     5025   4183   4109    138   1417   -614       C  
ATOM   1388  NE1 TRP A 228      10.975  -0.403 -65.776  1.00 43.83           N  
ANISOU 1388  NE1 TRP A 228     6193   5429   5030    230   1617   -707       N  
ATOM   1389  CE2 TRP A 228      10.586  -0.787 -64.517  1.00 40.61           C  
ANISOU 1389  CE2 TRP A 228     5771   4910   4749    289   1552   -685       C  
ATOM   1390  CE3 TRP A 228       9.269   0.096 -62.700  1.00 41.90           C  
ANISOU 1390  CE3 TRP A 228     5868   4954   5099    161   1335   -582       C  
ATOM   1391  CZ2 TRP A 228      10.862  -1.953 -63.814  1.00 44.21           C  
ANISOU 1391  CZ2 TRP A 228     6258   5279   5260    470   1604   -720       C  
ATOM   1392  CZ3 TRP A 228       9.542  -1.057 -62.004  1.00 42.11           C  
ANISOU 1392  CZ3 TRP A 228     5920   4904   5177    322   1386   -611       C  
ATOM   1393  CH2 TRP A 228      10.324  -2.074 -62.566  1.00 37.74           C  
ANISOU 1393  CH2 TRP A 228     5423   4358   4560    478   1516   -678       C  
ATOM   1394  N   GLU A 229       6.268   4.289 -65.629  1.00 37.13           N  
ANISOU 1394  N   GLU A 229     5455   4394   4258   -462    989   -452       N  
ATOM   1395  CA  GLU A 229       5.499   5.514 -65.429  1.00 41.39           C  
ANISOU 1395  CA  GLU A 229     5994   4914   4819   -556    862   -377       C  
ATOM   1396  C   GLU A 229       4.129   5.167 -64.862  1.00 35.51           C  
ANISOU 1396  C   GLU A 229     5289   4065   4139   -551    754   -402       C  
ATOM   1397  O   GLU A 229       3.625   5.819 -63.950  1.00 38.34           O  
ANISOU 1397  O   GLU A 229     5595   4392   4582   -558    666   -353       O  
ATOM   1398  CB  GLU A 229       5.339   6.309 -66.733  1.00 43.13           C  
ANISOU 1398  CB  GLU A 229     6298   5184   4905   -656    842   -345       C  
ATOM   1399  CG  GLU A 229       4.508   7.573 -66.510  1.00 64.10           C  
ANISOU 1399  CG  GLU A 229     8973   7802   7581   -725    707   -264       C  
ATOM   1400  CD  GLU A 229       4.249   8.374 -67.774  1.00 80.02           C  
ANISOU 1400  CD  GLU A 229    11092   9854   9459   -814    673   -218       C  
ATOM   1401  OE1 GLU A 229       4.566   7.880 -68.879  1.00 75.50           O  
ANISOU 1401  OE1 GLU A 229    10580   9338   8768   -834    746   -260       O  
ATOM   1402  OE2 GLU A 229       3.722   9.503 -67.651  1.00 86.84           O1-
ANISOU 1402  OE2 GLU A 229    11985  10683  10328   -856    572   -140       O1-
ATOM   1403  N   ASN A 230       3.525   4.117 -65.388  1.00 34.60           N  
ANISOU 1403  N   ASN A 230     5266   3901   3977   -543    765   -483       N  
ATOM   1404  CA  ASN A 230       2.223   3.739 -64.882  1.00 39.39           C  
ANISOU 1404  CA  ASN A 230     5901   4433   4635   -562    667   -509       C  
ATOM   1405  C   ASN A 230       2.311   3.070 -63.504  1.00 44.61           C  
ANISOU 1405  C   ASN A 230     6498   5029   5423   -486    684   -518       C  
ATOM   1406  O   ASN A 230       1.420   3.240 -62.663  1.00 38.98           O  
ANISOU 1406  O   ASN A 230     5748   4281   4783   -500    596   -498       O  
ATOM   1407  CB  ASN A 230       1.531   2.862 -65.911  1.00 39.25           C  
ANISOU 1407  CB  ASN A 230     6010   4391   4514   -610    668   -594       C  
ATOM   1408  CG  ASN A 230       1.109   3.662 -67.131  1.00 44.48           C  
ANISOU 1408  CG  ASN A 230     6727   5123   5049   -694    609   -570       C  
ATOM   1409  OD1 ASN A 230       0.457   4.692 -67.003  1.00 45.62           O  
ANISOU 1409  OD1 ASN A 230     6836   5293   5203   -728    502   -499       O  
ATOM   1410  ND2 ASN A 230       1.528   3.224 -68.309  1.00 41.94           N  
ANISOU 1410  ND2 ASN A 230     6499   4834   4602   -716    684   -623       N  
ATOM   1411  N   LEU A 231       3.397   2.347 -63.252  1.00 45.56           N  
ANISOU 1411  N   LEU A 231     6601   5145   5566   -396    797   -542       N  
ATOM   1412  CA  LEU A 231       3.627   1.817 -61.910  1.00 40.69           C  
ANISOU 1412  CA  LEU A 231     5919   4478   5063   -311    812   -532       C  
ATOM   1413  C   LEU A 231       3.673   2.949 -60.884  1.00 38.98           C  
ANISOU 1413  C   LEU A 231     5577   4304   4930   -322    742   -448       C  
ATOM   1414  O   LEU A 231       3.081   2.847 -59.802  1.00 44.05           O  
ANISOU 1414  O   LEU A 231     6183   4898   5656   -309    686   -433       O  
ATOM   1415  CB  LEU A 231       4.925   1.009 -61.845  1.00 39.30           C  
ANISOU 1415  CB  LEU A 231     5729   4317   4886   -187    944   -557       C  
ATOM   1416  CG  LEU A 231       5.228   0.448 -60.446  1.00 52.52           C  
ANISOU 1416  CG  LEU A 231     7340   5946   6669    -84    957   -535       C  
ATOM   1417  CD1 LEU A 231       4.056  -0.376 -59.891  1.00 43.68           C  
ANISOU 1417  CD1 LEU A 231     6311   4692   5592   -110    903   -568       C  
ATOM   1418  CD2 LEU A 231       6.487  -0.387 -60.473  1.00 51.79           C  
ANISOU 1418  CD2 LEU A 231     7237   5879   6564     65   1084   -559       C  
ATOM   1419  N   LEU A 232       4.375   4.029 -61.224  1.00 36.12           N  
ANISOU 1419  N   LEU A 232     5158   4030   4537   -355    749   -395       N  
ATOM   1420  CA  LEU A 232       4.459   5.174 -60.329  1.00 34.69           C  
ANISOU 1420  CA  LEU A 232     4884   3877   4422   -380    684   -323       C  
ATOM   1421  C   LEU A 232       3.079   5.733 -60.049  1.00 39.23           C  
ANISOU 1421  C   LEU A 232     5488   4396   5020   -429    560   -308       C  
ATOM   1422  O   LEU A 232       2.737   5.999 -58.890  1.00 38.81           O  
ANISOU 1422  O   LEU A 232     5375   4319   5051   -408    507   -284       O  
ATOM   1423  CB  LEU A 232       5.355   6.279 -60.899  1.00 35.14           C  
ANISOU 1423  CB  LEU A 232     4908   4023   4421   -442    709   -270       C  
ATOM   1424  CG  LEU A 232       5.367   7.564 -60.063  1.00 36.92           C  
ANISOU 1424  CG  LEU A 232     5075   4254   4700   -492    634   -201       C  
ATOM   1425  CD1 LEU A 232       5.914   7.278 -58.660  1.00 41.30           C  
ANISOU 1425  CD1 LEU A 232     5515   4824   5352   -426    648   -194       C  
ATOM   1426  CD2 LEU A 232       6.189   8.658 -60.710  1.00 38.23           C  
ANISOU 1426  CD2 LEU A 232     5238   4491   4796   -585    657   -146       C  
ATOM   1427  N   LYS A 233       2.291   5.925 -61.107  1.00 31.38           N  
ANISOU 1427  N   LYS A 233     4581   3397   3945   -488    515   -322       N  
ATOM   1428  CA  LYS A 233       0.946   6.472 -60.953  1.00 34.34           C  
ANISOU 1428  CA  LYS A 233     4972   3747   4329   -518    394   -306       C  
ATOM   1429  C   LYS A 233       0.087   5.601 -60.051  1.00 37.58           C  
ANISOU 1429  C   LYS A 233     5356   4113   4808   -491    365   -346       C  
ATOM   1430  O   LYS A 233      -0.654   6.104 -59.200  1.00 35.50           O  
ANISOU 1430  O   LYS A 233     5041   3844   4601   -481    288   -320       O  
ATOM   1431  CB  LYS A 233       0.274   6.632 -62.309  1.00 33.97           C  
ANISOU 1431  CB  LYS A 233     5017   3724   4168   -577    353   -318       C  
ATOM   1432  CG  LYS A 233       0.782   7.855 -63.043  1.00 34.44           C  
ANISOU 1432  CG  LYS A 233     5109   3818   4158   -616    343   -252       C  
ATOM   1433  CD  LYS A 233       0.169   7.969 -64.413  1.00 34.82           C  
ANISOU 1433  CD  LYS A 233     5254   3898   4079   -668    303   -257       C  
ATOM   1434  CE  LYS A 233       0.809   9.147 -65.158  1.00 37.00           C  
ANISOU 1434  CE  LYS A 233     5580   4201   4276   -713    308   -181       C  
ATOM   1435  NZ  LYS A 233       0.325   9.189 -66.577  1.00 43.47           N1+
ANISOU 1435  NZ  LYS A 233     6501   5062   4953   -762    278   -183       N1+
ATOM   1436  N   ILE A 234       0.199   4.295 -60.246  1.00 38.23           N  
ANISOU 1436  N   ILE A 234     5486   4162   4879   -481    432   -408       N  
ATOM   1437  CA  ILE A 234      -0.554   3.328 -59.459  1.00 34.73           C  
ANISOU 1437  CA  ILE A 234     5043   3665   4489   -477    418   -445       C  
ATOM   1438  C   ILE A 234      -0.137   3.342 -57.993  1.00 35.21           C  
ANISOU 1438  C   ILE A 234     5015   3707   4655   -410    432   -409       C  
ATOM   1439  O   ILE A 234      -1.000   3.305 -57.107  1.00 38.84           O  
ANISOU 1439  O   ILE A 234     5435   4156   5166   -420    374   -402       O  
ATOM   1440  CB  ILE A 234      -0.390   1.895 -60.024  1.00 38.55           C  
ANISOU 1440  CB  ILE A 234     5634   4086   4928   -482    499   -522       C  
ATOM   1441  CG1 ILE A 234      -1.069   1.786 -61.380  1.00 51.85           C  
ANISOU 1441  CG1 ILE A 234     7411   5792   6498   -569    468   -570       C  
ATOM   1442  CG2 ILE A 234      -0.941   0.849 -59.052  1.00 42.35           C  
ANISOU 1442  CG2 ILE A 234     6131   4490   5470   -480    502   -548       C  
ATOM   1443  CD1 ILE A 234      -2.431   2.416 -61.422  1.00 64.29           C  
ANISOU 1443  CD1 ILE A 234     8949   7421   8056   -642    342   -552       C  
ATOM   1444  N   CYS A 235       1.172   3.385 -57.731  1.00 39.99           N  
ANISOU 1444  N   CYS A 235     5582   4328   5285   -345    507   -386       N  
ATOM   1445  CA  CYS A 235       1.651   3.397 -56.347  1.00 40.89           C  
ANISOU 1445  CA  CYS A 235     5608   4442   5487   -281    516   -350       C  
ATOM   1446  C   CYS A 235       1.260   4.672 -55.646  1.00 47.19           C  
ANISOU 1446  C   CYS A 235     6331   5275   6324   -305    430   -301       C  
ATOM   1447  O   CYS A 235       0.976   4.657 -54.447  1.00 39.11           O  
ANISOU 1447  O   CYS A 235     5252   4243   5366   -278    401   -285       O  
ATOM   1448  CB  CYS A 235       3.170   3.230 -56.260  1.00 38.81           C  
ANISOU 1448  CB  CYS A 235     5297   4221   5229   -206    608   -334       C  
ATOM   1449  SG  CYS A 235       3.775   1.600 -56.791  1.00 53.43           S  
ANISOU 1449  SG  CYS A 235     7239   6017   7046   -120    726   -393       S  
ATOM   1450  N   VAL A 236       1.281   5.782 -56.377  1.00 40.86           N  
ANISOU 1450  N   VAL A 236     5541   4508   5476   -351    393   -276       N  
ATOM   1451  CA  VAL A 236       0.866   7.055 -55.804  1.00 36.09           C  
ANISOU 1451  CA  VAL A 236     4900   3914   4899   -366    310   -234       C  
ATOM   1452  C   VAL A 236      -0.592   6.985 -55.435  1.00 34.76           C  
ANISOU 1452  C   VAL A 236     4731   3728   4746   -366    230   -251       C  
ATOM   1453  O   VAL A 236      -0.983   7.363 -54.329  1.00 42.00           O  
ANISOU 1453  O   VAL A 236     5592   4645   5718   -338    188   -236       O  
ATOM   1454  CB  VAL A 236       1.085   8.226 -56.757  1.00 38.98           C  
ANISOU 1454  CB  VAL A 236     5314   4297   5201   -416    284   -199       C  
ATOM   1455  CG1 VAL A 236       0.335   9.463 -56.246  1.00 31.55           C  
ANISOU 1455  CG1 VAL A 236     4375   3335   4278   -415    186   -165       C  
ATOM   1456  CG2 VAL A 236       2.553   8.506 -56.880  1.00 34.09           C  
ANISOU 1456  CG2 VAL A 236     4665   3720   4569   -434    359   -174       C  
ATOM   1457  N   PHE A 237      -1.400   6.485 -56.360  1.00 32.58           N  
ANISOU 1457  N   PHE A 237     4513   3454   4414   -403    211   -284       N  
ATOM   1458  CA  PHE A 237      -2.818   6.291 -56.108  1.00 34.26           C  
ANISOU 1458  CA  PHE A 237     4706   3682   4627   -418    138   -304       C  
ATOM   1459  C   PHE A 237      -3.125   5.424 -54.875  1.00 42.21           C  
ANISOU 1459  C   PHE A 237     5662   4673   5703   -403    158   -321       C  
ATOM   1460  O   PHE A 237      -4.023   5.743 -54.098  1.00 41.38           O  
ANISOU 1460  O   PHE A 237     5497   4601   5626   -393     99   -314       O  
ATOM   1461  CB  PHE A 237      -3.489   5.661 -57.312  1.00 33.82           C  
ANISOU 1461  CB  PHE A 237     4718   3644   4490   -481    126   -347       C  
ATOM   1462  CG  PHE A 237      -4.980   5.502 -57.161  1.00 38.60           C  
ANISOU 1462  CG  PHE A 237     5284   4302   5080   -514     45   -367       C  
ATOM   1463  CD1 PHE A 237      -5.786   6.599 -56.898  1.00 40.64           C  
ANISOU 1463  CD1 PHE A 237     5483   4619   5340   -474    -47   -332       C  
ATOM   1464  CD2 PHE A 237      -5.576   4.265 -57.303  1.00 40.19           C  
ANISOU 1464  CD2 PHE A 237     5511   4500   5259   -587     61   -422       C  
ATOM   1465  CE1 PHE A 237      -7.151   6.471 -56.780  1.00 39.59           C  
ANISOU 1465  CE1 PHE A 237     5289   4569   5185   -496   -120   -350       C  
ATOM   1466  CE2 PHE A 237      -6.943   4.122 -57.193  1.00 40.95           C  
ANISOU 1466  CE2 PHE A 237     5554   4674   5332   -639    -13   -440       C  
ATOM   1467  CZ  PHE A 237      -7.737   5.221 -56.929  1.00 44.04           C  
ANISOU 1467  CZ  PHE A 237     5857   5153   5724   -589   -104   -403       C  
ATOM   1468  N  AILE A 238      -2.376   4.341 -54.684  0.54 40.06           N  
ANISOU 1468  N  AILE A 238     5419   4352   5450   -393    242   -340       N  
ATOM   1469  N  BILE A 238      -2.403   4.322 -54.715  0.46 40.26           N  
ANISOU 1469  N  BILE A 238     5446   4377   5473   -395    241   -342       N  
ATOM   1470  CA AILE A 238      -2.704   3.416 -53.601  0.54 41.91           C  
ANISOU 1470  CA AILE A 238     5633   4557   5735   -387    262   -349       C  
ATOM   1471  CA BILE A 238      -2.669   3.436 -53.591  0.46 40.84           C  
ANISOU 1471  CA BILE A 238     5497   4422   5600   -385    262   -348       C  
ATOM   1472  C  AILE A 238      -2.071   3.792 -52.255  0.54 36.91           C  
ANISOU 1472  C  AILE A 238     4922   3930   5171   -318    272   -306       C  
ATOM   1473  C  BILE A 238      -2.178   4.040 -52.285  0.46 37.57           C  
ANISOU 1473  C  BILE A 238     4998   4025   5253   -321    257   -304       C  
ATOM   1474  O  AILE A 238      -2.634   3.497 -51.215  0.54 41.58           O  
ANISOU 1474  O  AILE A 238     5474   4525   5799   -316    257   -300       O  
ATOM   1475  O  BILE A 238      -2.927   4.151 -51.320  0.46 40.35           O  
ANISOU 1475  O  BILE A 238     5295   4400   5637   -320    218   -295       O  
ATOM   1476  CB AILE A 238      -2.316   1.962 -53.961  0.54 47.91           C  
ANISOU 1476  CB AILE A 238     6488   5239   6476   -397    344   -388       C  
ATOM   1477  CB BILE A 238      -2.016   2.067 -53.776  0.46 47.21           C  
ANISOU 1477  CB BILE A 238     6385   5151   6401   -374    354   -377       C  
ATOM   1478  CG1AILE A 238      -0.800   1.814 -54.114  0.54 46.98           C  
ANISOU 1478  CG1AILE A 238     6385   5098   6366   -315    428   -375       C  
ATOM   1479  CG1BILE A 238      -2.569   1.386 -55.025  0.46 48.94           C  
ANISOU 1479  CG1BILE A 238     6708   5344   6544   -452    359   -435       C  
ATOM   1480  CG2AILE A 238      -3.062   1.512 -55.216  0.54 48.96           C  
ANISOU 1480  CG2AILE A 238     6707   5366   6529   -486    328   -443       C  
ATOM   1481  CG2BILE A 238      -2.272   1.201 -52.554  0.46 53.52           C  
ANISOU 1481  CG2BILE A 238     7178   5907   7251   -363    373   -368       C  
ATOM   1482  CD1AILE A 238      -0.388   0.588 -54.931  0.54 42.79           C  
ANISOU 1482  CD1AILE A 238     5974   4493   5789   -308    510   -426       C  
ATOM   1483  CD1BILE A 238      -1.812   0.142 -55.403  0.46 48.04           C  
ANISOU 1483  CD1BILE A 238     6706   5137   6411   -425    457   -473       C  
ATOM   1484  N   PHE A 239      -0.919   4.452 -52.270  1.00 36.14           N  
ANISOU 1484  N   PHE A 239     4800   3847   5083   -275    297   -278       N  
ATOM   1485  CA  PHE A 239      -0.307   4.912 -51.052  1.00 40.39           C  
ANISOU 1485  CA  PHE A 239     5263   4409   5675   -226    297   -242       C  
ATOM   1486  C   PHE A 239      -0.768   6.283 -50.607  1.00 46.64           C  
ANISOU 1486  C   PHE A 239     6010   5234   6476   -234    220   -223       C  
ATOM   1487  O   PHE A 239      -0.730   6.587 -49.415  1.00 36.59           O  
ANISOU 1487  O   PHE A 239     4681   3979   5242   -205    202   -207       O  
ATOM   1488  CB  PHE A 239       1.203   4.913 -51.192  1.00 44.06           C  
ANISOU 1488  CB  PHE A 239     5708   4894   6139   -187    362   -222       C  
ATOM   1489  CG  PHE A 239       1.809   3.574 -50.966  1.00 49.03           C  
ANISOU 1489  CG  PHE A 239     6357   5494   6780   -126    439   -228       C  
ATOM   1490  CD1 PHE A 239       1.985   3.095 -49.673  1.00 52.35           C  
ANISOU 1490  CD1 PHE A 239     6734   5912   7246    -71    446   -203       C  
ATOM   1491  CD2 PHE A 239       2.181   2.779 -52.031  1.00 49.06           C  
ANISOU 1491  CD2 PHE A 239     6435   5464   6742   -113    504   -259       C  
ATOM   1492  CE1 PHE A 239       2.534   1.853 -49.450  1.00 48.94           C  
ANISOU 1492  CE1 PHE A 239     6338   5438   6819      4    515   -199       C  
ATOM   1493  CE2 PHE A 239       2.740   1.532 -51.814  1.00 57.52           C  
ANISOU 1493  CE2 PHE A 239     7545   6488   7820    -34    578   -267       C  
ATOM   1494  CZ  PHE A 239       2.914   1.068 -50.521  1.00 52.19           C  
ANISOU 1494  CZ  PHE A 239     6834   5804   7194     30    582   -232       C  
ATOM   1495  N   ALA A 240      -1.195   7.126 -51.538  1.00 34.52           N  
ANISOU 1495  N   ALA A 240     4513   3704   4899   -264    174   -224       N  
ATOM   1496  CA  ALA A 240      -1.600   8.455 -51.118  1.00 36.21           C  
ANISOU 1496  CA  ALA A 240     4712   3929   5120   -251    103   -206       C  
ATOM   1497  C   ALA A 240      -3.103   8.538 -51.020  1.00 34.72           C  
ANISOU 1497  C   ALA A 240     4509   3763   4921   -238     38   -224       C  
ATOM   1498  O   ALA A 240      -3.651   9.474 -50.444  1.00 41.50           O  
ANISOU 1498  O   ALA A 240     5346   4633   5788   -198    -19   -218       O  
ATOM   1499  CB  ALA A 240      -1.062   9.512 -52.062  1.00 35.61           C  
ANISOU 1499  CB  ALA A 240     4694   3837   5000   -279     89   -182       C  
ATOM   1500  N   PHE A 241      -3.798   7.555 -51.561  1.00 32.58           N  
ANISOU 1500  N   PHE A 241     4246   3507   4626   -272     45   -251       N  
ATOM   1501  CA  PHE A 241      -5.240   7.674 -51.535  1.00 29.82           C  
ANISOU 1501  CA  PHE A 241     3860   3215   4256   -271    -22   -267       C  
ATOM   1502  C   PHE A 241      -5.936   6.432 -50.989  1.00 40.42           C  
ANISOU 1502  C   PHE A 241     5163   4585   5611   -315      1   -294       C  
ATOM   1503  O   PHE A 241      -6.646   6.517 -49.985  1.00 37.60           O  
ANISOU 1503  O   PHE A 241     4733   4279   5276   -294    -21   -295       O  
ATOM   1504  CB  PHE A 241      -5.790   7.996 -52.933  1.00 35.07           C  
ANISOU 1504  CB  PHE A 241     4572   3905   4849   -295    -70   -271       C  
ATOM   1505  CG  PHE A 241      -7.253   8.268 -52.916  1.00 33.49           C  
ANISOU 1505  CG  PHE A 241     4311   3795   4619   -277   -149   -282       C  
ATOM   1506  CD1 PHE A 241      -7.738   9.438 -52.331  1.00 34.53           C  
ANISOU 1506  CD1 PHE A 241     4405   3954   4762   -185   -208   -262       C  
ATOM   1507  CD2 PHE A 241      -8.160   7.329 -53.390  1.00 40.80           C  
ANISOU 1507  CD2 PHE A 241     5212   4786   5503   -350   -162   -316       C  
ATOM   1508  CE1 PHE A 241      -9.099   9.679 -52.258  1.00 34.98           C  
ANISOU 1508  CE1 PHE A 241     4384   4119   4788   -145   -277   -272       C  
ATOM   1509  CE2 PHE A 241      -9.532   7.570 -53.321  1.00 44.65           C  
ANISOU 1509  CE2 PHE A 241     5612   5395   5957   -336   -237   -325       C  
ATOM   1510  CZ  PHE A 241     -10.001   8.744 -52.762  1.00 41.18           C  
ANISOU 1510  CZ  PHE A 241     5119   4999   5529   -222   -293   -301       C  
ATOM   1511  N   ILE A 242      -5.761   5.291 -51.656  1.00 40.67           N  
ANISOU 1511  N   ILE A 242     5253   4582   5619   -380     48   -318       N  
ATOM   1512  CA  ILE A 242      -6.502   4.087 -51.277  1.00 43.36           C  
ANISOU 1512  CA  ILE A 242     5586   4932   5958   -450     67   -344       C  
ATOM   1513  C   ILE A 242      -6.217   3.641 -49.839  1.00 37.36           C  
ANISOU 1513  C   ILE A 242     4791   4149   5255   -423    109   -323       C  
ATOM   1514  O   ILE A 242      -7.134   3.459 -49.050  1.00 44.55           O  
ANISOU 1514  O   ILE A 242     5639   5120   6170   -450     89   -324       O  
ATOM   1515  CB  ILE A 242      -6.186   2.899 -52.185  1.00 44.92           C  
ANISOU 1515  CB  ILE A 242     5890   5058   6118   -521    122   -378       C  
ATOM   1516  CG1 ILE A 242      -6.583   3.203 -53.634  1.00 45.80           C  
ANISOU 1516  CG1 ILE A 242     6040   5206   6154   -565     79   -405       C  
ATOM   1517  CG2 ILE A 242      -6.883   1.641 -51.654  1.00 43.40           C  
ANISOU 1517  CG2 ILE A 242     5716   4849   5924   -608    148   -401       C  
ATOM   1518  CD1 ILE A 242      -8.027   3.592 -53.805  1.00 41.53           C  
ANISOU 1518  CD1 ILE A 242     5422   4786   5571   -609    -11   -415       C  
ATOM   1519  N   MET A 243      -4.941   3.446 -49.541  1.00 34.46           N  
ANISOU 1519  N   MET A 243     4460   3711   4922   -371    168   -302       N  
ATOM   1520  CA  MET A 243      -4.493   3.008 -48.234  1.00 46.27           C  
ANISOU 1520  CA  MET A 243     5932   5186   6464   -333    206   -273       C  
ATOM   1521  C   MET A 243      -4.926   3.999 -47.141  1.00 48.93           C  
ANISOU 1521  C   MET A 243     6171   5598   6822   -292    157   -255       C  
ATOM   1522  O   MET A 243      -5.445   3.585 -46.107  1.00 38.94           O  
ANISOU 1522  O   MET A 243     4867   4361   5568   -304    163   -246       O  
ATOM   1523  CB  MET A 243      -2.966   2.821 -48.224  1.00 45.59           C  
ANISOU 1523  CB  MET A 243     5879   5044   6399   -265    266   -251       C  
ATOM   1524  CG  MET A 243      -2.362   2.438 -46.856  1.00 52.49           C  
ANISOU 1524  CG  MET A 243     6721   5911   7312   -208    297   -211       C  
ATOM   1525  SD  MET A 243      -0.555   2.540 -46.727  1.00 86.50           S  
ANISOU 1525  SD  MET A 243    11013  10216  11638   -112    347   -178       S  
ATOM   1526  CE  MET A 243      -0.320   4.298 -46.497  1.00 68.12           C  
ANISOU 1526  CE  MET A 243     8598   7967   9317   -112    283   -171       C  
ATOM   1527  N   PRO A 244      -4.712   5.309 -47.359  1.00 42.17           N  
ANISOU 1527  N   PRO A 244     5288   4768   5966   -247    112   -252       N  
ATOM   1528  CA  PRO A 244      -5.141   6.225 -46.287  1.00 41.16           C  
ANISOU 1528  CA  PRO A 244     5090   4697   5853   -199     71   -246       C  
ATOM   1529  C   PRO A 244      -6.657   6.242 -46.076  1.00 36.59           C  
ANISOU 1529  C   PRO A 244     4449   4202   5250   -217     29   -267       C  
ATOM   1530  O   PRO A 244      -7.100   6.301 -44.927  1.00 36.69           O  
ANISOU 1530  O   PRO A 244     4401   4269   5272   -196     28   -265       O  
ATOM   1531  CB  PRO A 244      -4.640   7.586 -46.769  1.00 39.55           C  
ANISOU 1531  CB  PRO A 244     4908   4476   5643   -158     33   -241       C  
ATOM   1532  CG  PRO A 244      -3.492   7.250 -47.673  1.00 37.20           C  
ANISOU 1532  CG  PRO A 244     4670   4123   5342   -183     77   -229       C  
ATOM   1533  CD  PRO A 244      -3.865   5.991 -48.356  1.00 37.36           C  
ANISOU 1533  CD  PRO A 244     4725   4128   5344   -232    111   -247       C  
ATOM   1534  N   VAL A 245      -7.442   6.165 -47.145  1.00 32.93           N  
ANISOU 1534  N   VAL A 245     3994   3771   4748   -257     -3   -287       N  
ATOM   1535  CA  VAL A 245      -8.891   6.114 -46.974  1.00 36.99           C  
ANISOU 1535  CA  VAL A 245     4424   4400   5231   -280    -43   -306       C  
ATOM   1536  C   VAL A 245      -9.298   4.853 -46.171  1.00 41.52           C  
ANISOU 1536  C   VAL A 245     4972   4997   5807   -365      5   -307       C  
ATOM   1537  O   VAL A 245     -10.143   4.932 -45.280  1.00 41.75           O  
ANISOU 1537  O   VAL A 245     4911   5127   5827   -362     -4   -309       O  
ATOM   1538  CB  VAL A 245      -9.646   6.143 -48.323  1.00 40.22           C  
ANISOU 1538  CB  VAL A 245     4838   4858   5584   -321    -92   -327       C  
ATOM   1539  CG1 VAL A 245     -11.125   5.819 -48.114  1.00 38.34           C  
ANISOU 1539  CG1 VAL A 245     4491   4770   5306   -371   -126   -347       C  
ATOM   1540  CG2 VAL A 245      -9.519   7.510 -48.972  1.00 42.98           C  
ANISOU 1540  CG2 VAL A 245     5209   5202   5919   -227   -151   -316       C  
ATOM   1541  N   LEU A 246      -8.673   3.713 -46.459  1.00 34.41           N  
ANISOU 1541  N   LEU A 246     4160   4000   4913   -434     62   -302       N  
ATOM   1542  CA  LEU A 246      -8.956   2.488 -45.707  1.00 36.88           C  
ANISOU 1542  CA  LEU A 246     4487   4299   5225   -518    112   -292       C  
ATOM   1543  C   LEU A 246      -8.524   2.624 -44.245  1.00 33.27           C  
ANISOU 1543  C   LEU A 246     3994   3845   4801   -454    139   -257       C  
ATOM   1544  O   LEU A 246      -9.249   2.226 -43.340  1.00 38.81           O  
ANISOU 1544  O   LEU A 246     4645   4613   5488   -501    151   -247       O  
ATOM   1545  CB  LEU A 246      -8.254   1.279 -46.327  1.00 37.05           C  
ANISOU 1545  CB  LEU A 246     4645   4186   5245   -577    170   -295       C  
ATOM   1546  CG  LEU A 246      -8.824   0.803 -47.663  1.00 50.34           C  
ANISOU 1546  CG  LEU A 246     6383   5867   6878   -679    153   -339       C  
ATOM   1547  CD1 LEU A 246      -7.983  -0.337 -48.182  1.00 50.77           C  
ANISOU 1547  CD1 LEU A 246     6593   5766   6930   -709    221   -347       C  
ATOM   1548  CD2 LEU A 246     -10.271   0.371 -47.487  1.00 46.21           C  
ANISOU 1548  CD2 LEU A 246     5793   5456   6308   -810    126   -358       C  
ATOM   1549  N   ILE A 247      -7.336   3.178 -44.024  1.00 33.87           N  
ANISOU 1549  N   ILE A 247     4095   3861   4913   -359    148   -237       N  
ATOM   1550  CA  ILE A 247      -6.806   3.298 -42.670  1.00 40.61           C  
ANISOU 1550  CA  ILE A 247     4919   4721   5788   -302    168   -204       C  
ATOM   1551  C   ILE A 247      -7.699   4.157 -41.765  1.00 40.48           C  
ANISOU 1551  C   ILE A 247     4800   4825   5757   -271    131   -217       C  
ATOM   1552  O   ILE A 247      -8.079   3.731 -40.666  1.00 36.83           O  
ANISOU 1552  O   ILE A 247     4300   4412   5282   -292    155   -199       O  
ATOM   1553  CB  ILE A 247      -5.385   3.867 -42.677  1.00 36.63           C  
ANISOU 1553  CB  ILE A 247     4442   4162   5315   -220    173   -187       C  
ATOM   1554  CG1 ILE A 247      -4.407   2.789 -43.138  1.00 38.53           C  
ANISOU 1554  CG1 ILE A 247     4770   4303   5566   -223    230   -166       C  
ATOM   1555  CG2 ILE A 247      -4.973   4.331 -41.266  1.00 39.11           C  
ANISOU 1555  CG2 ILE A 247     4705   4518   5638   -162    171   -164       C  
ATOM   1556  CD1 ILE A 247      -3.001   3.303 -43.334  1.00 39.89           C  
ANISOU 1556  CD1 ILE A 247     4947   4451   5758   -152    239   -151       C  
ATOM   1557  N   ILE A 248      -8.044   5.354 -42.217  1.00 40.60           N  
ANISOU 1557  N   ILE A 248     4776   4885   5767   -216     77   -246       N  
ATOM   1558  CA  ILE A 248      -8.799   6.269 -41.370  1.00 36.24           C  
ANISOU 1558  CA  ILE A 248     4138   4435   5196   -153     46   -265       C  
ATOM   1559  C   ILE A 248     -10.261   5.834 -41.233  1.00 37.67           C  
ANISOU 1559  C   ILE A 248     4229   4747   5337   -208     42   -281       C  
ATOM   1560  O   ILE A 248     -10.849   5.980 -40.168  1.00 40.44           O  
ANISOU 1560  O   ILE A 248     4504   5196   5667   -188     52   -286       O  
ATOM   1561  CB  ILE A 248      -8.716   7.730 -41.882  1.00 34.05           C  
ANISOU 1561  CB  ILE A 248     3871   4146   4919    -59    -12   -289       C  
ATOM   1562  CG1 ILE A 248      -9.432   7.895 -43.224  1.00 40.98           C  
ANISOU 1562  CG1 ILE A 248     4749   5048   5774    -72    -54   -305       C  
ATOM   1563  CG2 ILE A 248      -7.235   8.182 -41.948  1.00 29.62           C  
ANISOU 1563  CG2 ILE A 248     3391   3474   4390    -35     -4   -272       C  
ATOM   1564  CD1 ILE A 248      -9.612   9.347 -43.669  1.00 44.63           C  
ANISOU 1564  CD1 ILE A 248     5229   5506   6224     35   -116   -320       C  
ATOM   1565  N   THR A 249     -10.858   5.261 -42.271  1.00 32.00           N  
ANISOU 1565  N   THR A 249     3513   4047   4599   -291     31   -292       N  
ATOM   1566  CA  THR A 249     -12.237   4.803 -42.107  1.00 34.69           C  
ANISOU 1566  CA  THR A 249     3750   4538   4891   -368     27   -306       C  
ATOM   1567  C   THR A 249     -12.310   3.575 -41.165  1.00 37.32           C  
ANISOU 1567  C   THR A 249     4094   4871   5216   -481     93   -277       C  
ATOM   1568  O   THR A 249     -13.232   3.465 -40.355  1.00 39.73           O  
ANISOU 1568  O   THR A 249     4297   5316   5483   -515    106   -279       O  
ATOM   1569  CB  THR A 249     -12.917   4.468 -43.457  1.00 40.94           C  
ANISOU 1569  CB  THR A 249     4535   5370   5649   -451     -9   -328       C  
ATOM   1570  OG1 THR A 249     -12.190   3.428 -44.121  1.00 45.01           O  
ANISOU 1570  OG1 THR A 249     5179   5743   6178   -550     27   -318       O  
ATOM   1571  CG2 THR A 249     -12.962   5.709 -44.357  1.00 38.15           C  
ANISOU 1571  CG2 THR A 249     4174   5031   5292   -334    -79   -346       C  
ATOM   1572  N   VAL A 250     -11.347   2.662 -41.242  1.00 39.80           N  
ANISOU 1572  N   VAL A 250     4534   5033   5557   -530    138   -247       N  
ATOM   1573  CA  VAL A 250     -11.428   1.472 -40.387  1.00 40.44           C  
ANISOU 1573  CA  VAL A 250     4652   5091   5622   -632    198   -209       C  
ATOM   1574  C   VAL A 250     -11.070   1.835 -38.941  1.00 36.73           C  
ANISOU 1574  C   VAL A 250     4146   4654   5157   -551    220   -179       C  
ATOM   1575  O   VAL A 250     -11.740   1.407 -38.002  1.00 37.89           O  
ANISOU 1575  O   VAL A 250     4243   4889   5264   -615    251   -160       O  
ATOM   1576  CB  VAL A 250     -10.525   0.332 -40.903  1.00 41.77           C  
ANISOU 1576  CB  VAL A 250     4984   5075   5810   -686    242   -185       C  
ATOM   1577  CG1 VAL A 250     -10.441  -0.819 -39.888  1.00 42.14           C  
ANISOU 1577  CG1 VAL A 250     5103   5068   5842   -760    304   -131       C  
ATOM   1578  CG2 VAL A 250     -11.070  -0.185 -42.225  1.00 43.14           C  
ANISOU 1578  CG2 VAL A 250     5201   5231   5959   -799    227   -223       C  
ATOM   1579  N   CYS A 251     -10.028   2.636 -38.770  1.00 28.60           N  
ANISOU 1579  N   CYS A 251     3140   3562   4164   -424    203   -176       N  
ATOM   1580  CA  CYS A 251      -9.595   3.045 -37.436  1.00 30.74           C  
ANISOU 1580  CA  CYS A 251     3384   3866   4432   -350    215   -155       C  
ATOM   1581  C   CYS A 251     -10.681   3.855 -36.751  1.00 40.02           C  
ANISOU 1581  C   CYS A 251     4433   5207   5566   -317    197   -190       C  
ATOM   1582  O   CYS A 251     -11.042   3.564 -35.611  1.00 36.35           O  
ANISOU 1582  O   CYS A 251     3927   4821   5062   -341    231   -169       O  
ATOM   1583  CB  CYS A 251      -8.297   3.856 -37.504  1.00 28.72           C  
ANISOU 1583  CB  CYS A 251     3168   3528   4215   -240    192   -156       C  
ATOM   1584  SG  CYS A 251      -6.862   2.811 -37.798  1.00 42.04           S  
ANISOU 1584  SG  CYS A 251     4977   5062   5936   -245    231   -102       S  
ATOM   1585  N   TYR A 252     -11.218   4.853 -37.450  1.00 34.83           N  
ANISOU 1585  N   TYR A 252     3718   4606   4909   -255    147   -240       N  
ATOM   1586  CA  TYR A 252     -12.265   5.677 -36.862  1.00 34.07           C  
ANISOU 1586  CA  TYR A 252     3502   4672   4770   -191    132   -278       C  
ATOM   1587  C   TYR A 252     -13.554   4.904 -36.683  1.00 41.46           C  
ANISOU 1587  C   TYR A 252     4336   5763   5653   -302    159   -276       C  
ATOM   1588  O   TYR A 252     -14.248   5.065 -35.674  1.00 37.72           O  
ANISOU 1588  O   TYR A 252     3766   5434   5132   -287    184   -285       O  
ATOM   1589  CB  TYR A 252     -12.512   6.928 -37.699  1.00 30.07           C  
ANISOU 1589  CB  TYR A 252     2976   4176   4273    -76     68   -325       C  
ATOM   1590  CG  TYR A 252     -11.441   7.986 -37.509  1.00 34.92           C  
ANISOU 1590  CG  TYR A 252     3672   4676   4918     35     44   -337       C  
ATOM   1591  CD1 TYR A 252     -10.943   8.277 -36.238  1.00 37.75           C  
ANISOU 1591  CD1 TYR A 252     4041   5036   5266     77     66   -338       C  
ATOM   1592  CD2 TYR A 252     -10.935   8.700 -38.596  1.00 33.47           C  
ANISOU 1592  CD2 TYR A 252     3561   4392   4765     82     -2   -346       C  
ATOM   1593  CE1 TYR A 252      -9.971   9.243 -36.052  1.00 37.28           C  
ANISOU 1593  CE1 TYR A 252     4059   4882   5226    152     40   -354       C  
ATOM   1594  CE2 TYR A 252      -9.950   9.672 -38.424  1.00 36.60           C  
ANISOU 1594  CE2 TYR A 252     4040   4686   5182    154    -23   -356       C  
ATOM   1595  CZ  TYR A 252      -9.481   9.944 -37.148  1.00 40.23           C  
ANISOU 1595  CZ  TYR A 252     4505   5151   5631    184     -3   -363       C  
ATOM   1596  OH  TYR A 252      -8.513  10.910 -36.960  1.00 36.02           O  
ANISOU 1596  OH  TYR A 252     4053   4524   5108    230    -27   -378       O  
ATOM   1597  N   GLY A 253     -13.868   4.052 -37.653  1.00 34.21           N  
ANISOU 1597  N   GLY A 253     3440   4823   4736   -426    158   -267       N  
ATOM   1598  CA  GLY A 253     -15.054   3.223 -37.552  1.00 35.85           C  
ANISOU 1598  CA  GLY A 253     3558   5176   4886   -574    184   -263       C  
ATOM   1599  C   GLY A 253     -14.988   2.296 -36.343  1.00 42.68           C  
ANISOU 1599  C   GLY A 253     4450   6043   5723   -672    254   -213       C  
ATOM   1600  O   GLY A 253     -15.964   2.130 -35.639  1.00 39.95           O  
ANISOU 1600  O   GLY A 253     3990   5874   5317   -735    283   -213       O  
ATOM   1601  N   LEU A 254     -13.839   1.676 -36.117  1.00 40.13           N  
ANISOU 1601  N   LEU A 254     4276   5534   5436   -681    283   -167       N  
ATOM   1602  CA  LEU A 254     -13.682   0.771 -34.983  1.00 40.57           C  
ANISOU 1602  CA  LEU A 254     4384   5571   5461   -761    345   -106       C  
ATOM   1603  C   LEU A 254     -13.659   1.539 -33.660  1.00 40.97           C  
ANISOU 1603  C   LEU A 254     4357   5729   5482   -653    356   -106       C  
ATOM   1604  O   LEU A 254     -14.118   1.045 -32.636  1.00 39.96           O  
ANISOU 1604  O   LEU A 254     4198   5691   5293   -726    405    -71       O  
ATOM   1605  CB  LEU A 254     -12.405  -0.054 -35.130  1.00 29.21           C  
ANISOU 1605  CB  LEU A 254     3127   3908   4065   -763    367    -53       C  
ATOM   1606  CG  LEU A 254     -12.483  -1.176 -36.180  1.00 38.94           C  
ANISOU 1606  CG  LEU A 254     4473   5017   5303   -902    382    -45       C  
ATOM   1607  CD1 LEU A 254     -11.198  -2.000 -36.179  1.00 37.73           C  
ANISOU 1607  CD1 LEU A 254     4503   4647   5185   -868    412      9       C  
ATOM   1608  CD2 LEU A 254     -13.695  -2.059 -35.948  1.00 38.60           C  
ANISOU 1608  CD2 LEU A 254     4402   5071   5192  -1104    418    -32       C  
ATOM   1609  N   MET A 255     -13.119   2.753 -33.696  1.00 34.34           N  
ANISOU 1609  N   MET A 255     3498   4875   4675   -488    312   -147       N  
ATOM   1610  CA  MET A 255     -13.103   3.617 -32.527  1.00 43.20           C  
ANISOU 1610  CA  MET A 255     4559   6091   5763   -379    316   -167       C  
ATOM   1611  C   MET A 255     -14.540   3.960 -32.100  1.00 45.65           C  
ANISOU 1611  C   MET A 255     4709   6632   6005   -388    333   -206       C  
ATOM   1612  O   MET A 255     -14.915   3.804 -30.940  1.00 43.95           O  
ANISOU 1612  O   MET A 255     4441   6532   5724   -409    379   -192       O  
ATOM   1613  CB  MET A 255     -12.283   4.869 -32.824  1.00 37.76           C  
ANISOU 1613  CB  MET A 255     3903   5322   5121   -223    261   -211       C  
ATOM   1614  CG  MET A 255     -12.246   5.881 -31.694  1.00 46.58           C  
ANISOU 1614  CG  MET A 255     4980   6520   6198   -108    259   -249       C  
ATOM   1615  SD  MET A 255     -11.515   7.445 -32.229  1.00 41.53           S  
ANISOU 1615  SD  MET A 255     4393   5781   5604     47    190   -313       S  
ATOM   1616  CE  MET A 255     -12.961   8.245 -32.941  1.00 35.92           C  
ANISOU 1616  CE  MET A 255     3573   5199   4874    123    162   -378       C  
ATOM   1617  N   ILE A 256     -15.355   4.383 -33.055  1.00 37.57           N  
ANISOU 1617  N   ILE A 256     3600   5690   4986   -372    296   -253       N  
ATOM   1618  CA  ILE A 256     -16.743   4.712 -32.787  1.00 42.56           C  
ANISOU 1618  CA  ILE A 256     4054   6567   5549   -365    308   -292       C  
ATOM   1619  C   ILE A 256     -17.531   3.488 -32.321  1.00 47.86           C  
ANISOU 1619  C   ILE A 256     4667   7361   6156   -568    372   -247       C  
ATOM   1620  O   ILE A 256     -18.354   3.587 -31.419  1.00 43.66           O  
ANISOU 1620  O   ILE A 256     4008   7032   5549   -576    415   -257       O  
ATOM   1621  CB  ILE A 256     -17.401   5.319 -34.020  1.00 42.27           C  
ANISOU 1621  CB  ILE A 256     3941   6593   5528   -307    246   -340       C  
ATOM   1622  CG1 ILE A 256     -16.960   6.771 -34.167  1.00 44.12           C  
ANISOU 1622  CG1 ILE A 256     4207   6763   5794    -85    194   -390       C  
ATOM   1623  CG2 ILE A 256     -18.932   5.240 -33.944  1.00 41.45           C  
ANISOU 1623  CG2 ILE A 256     3633   6771   5345   -354    261   -364       C  
ATOM   1624  CD1 ILE A 256     -17.357   7.363 -35.507  1.00 59.79           C  
ANISOU 1624  CD1 ILE A 256     6163   8755   7799    -16    123   -420       C  
ATOM   1625  N   LEU A 257     -17.260   2.333 -32.917  1.00 42.38           N  
ANISOU 1625  N   LEU A 257     4076   6542   5485   -737    382   -198       N  
ATOM   1626  CA  LEU A 257     -17.932   1.098 -32.508  1.00 45.36           C  
ANISOU 1626  CA  LEU A 257     4439   6998   5799   -959    444   -149       C  
ATOM   1627  C   LEU A 257     -17.619   0.735 -31.049  1.00 41.67           C  
ANISOU 1627  C   LEU A 257     4015   6535   5284   -978    509    -93       C  
ATOM   1628  O   LEU A 257     -18.509   0.309 -30.307  1.00 45.68           O  
ANISOU 1628  O   LEU A 257     4427   7223   5707  -1098    566    -73       O  
ATOM   1629  CB  LEU A 257     -17.536  -0.049 -33.440  1.00 52.81           C  
ANISOU 1629  CB  LEU A 257     5537   7750   6777  -1121    442   -112       C  
ATOM   1630  CG  LEU A 257     -18.603  -0.618 -34.382  1.00 69.19           C  
ANISOU 1630  CG  LEU A 257     7539   9935   8815  -1305    430   -135       C  
ATOM   1631  CD1 LEU A 257     -19.732   0.369 -34.675  1.00 66.30           C  
ANISOU 1631  CD1 LEU A 257     6937   9841   8412  -1228    389   -202       C  
ATOM   1632  CD2 LEU A 257     -17.932  -1.054 -35.681  1.00 75.22           C  
ANISOU 1632  CD2 LEU A 257     8459  10481   9641  -1340    392   -142       C  
ATOM   1633  N  AARG A 258     -16.362   0.896 -30.633  0.62 43.99           N  
ANISOU 1633  N  AARG A 258     4444   6648   5622   -867    502    -66       N  
ATOM   1634  N  BARG A 258     -16.363   0.913 -30.647  0.38 43.73           N  
ANISOU 1634  N  BARG A 258     4410   6615   5590   -865    501    -67       N  
ATOM   1635  CA AARG A 258     -16.008   0.616 -29.237  0.62 45.94           C  
ANISOU 1635  CA AARG A 258     4732   6907   5815   -869    553    -11       C  
ATOM   1636  CA BARG A 258     -15.963   0.641 -29.270  0.38 45.50           C  
ANISOU 1636  CA BARG A 258     4680   6844   5764   -863    550    -12       C  
ATOM   1637  C  AARG A 258     -16.760   1.576 -28.321  0.62 49.21           C  
ANISOU 1637  C  AARG A 258     4981   7558   6159   -774    571    -64       C  
ATOM   1638  C  BARG A 258     -16.702   1.578 -28.316  0.38 48.43           C  
ANISOU 1638  C  BARG A 258     4889   7450   6063   -770    570    -62       C  
ATOM   1639  O  AARG A 258     -17.359   1.162 -27.320  0.62 51.15           O  
ANISOU 1639  O  AARG A 258     5170   7950   6314   -863    635    -31       O  
ATOM   1640  O  BARG A 258     -17.235   1.150 -27.287  0.38 51.87           O  
ANISOU 1640  O  BARG A 258     5278   8022   6410   -856    633    -27       O  
ATOM   1641  CB AARG A 258     -14.498   0.723 -28.999  0.62 43.89           C  
ANISOU 1641  CB AARG A 258     4624   6441   5611   -752    528     23       C  
ATOM   1642  CB BARG A 258     -14.449   0.789 -29.107  0.38 44.37           C  
ANISOU 1642  CB BARG A 258     4686   6492   5679   -742    522     17       C  
ATOM   1643  CG AARG A 258     -14.072   0.555 -27.527  0.62 42.91           C  
ANISOU 1643  CG AARG A 258     4537   6346   5421   -732    567     78       C  
ATOM   1644  CG BARG A 258     -13.902   0.315 -27.768  0.38 45.07           C  
ANISOU 1644  CG BARG A 258     4849   6565   5712   -750    564     91       C  
ATOM   1645  CD AARG A 258     -14.323  -0.874 -27.002  0.62 44.47           C  
ANISOU 1645  CD AARG A 258     4821   6518   5557   -916    633    179       C  
ATOM   1646  CD BARG A 258     -13.668  -1.201 -27.740  0.38 49.39           C  
ANISOU 1646  CD BARG A 258     5545   6975   6246   -906    607    193       C  
ATOM   1647  NE AARG A 258     -13.663  -1.866 -27.851  0.62 48.23           N  
ANISOU 1647  NE AARG A 258     5464   6767   6095   -982    625    231       N  
ATOM   1648  NE BARG A 258     -14.882  -1.980 -27.499  0.38 46.51           N  
ANISOU 1648  NE BARG A 258     5134   6736   5804  -1104    667    221       N  
ATOM   1649  CZ AARG A 258     -12.410  -2.277 -27.683  0.62 46.71           C  
ANISOU 1649  CZ AARG A 258     5421   6392   5935   -908    614    293       C  
ATOM   1650  CZ BARG A 258     -15.540  -2.664 -28.433  0.38 49.85           C  
ANISOU 1650  CZ BARG A 258     5569   7135   6237  -1263    675    216       C  
ATOM   1651  NH1AARG A 258     -11.681  -1.805 -26.677  0.62 48.06           N  
ANISOU 1651  NH1AARG A 258     5591   6589   6079   -786    603    315       N  
ATOM   1652  NH1BARG A 258     -16.633  -3.344 -28.111  0.38 55.48           N  
ANISOU 1652  NH1BARG A 258     6230   7982   6866  -1465    731    243       N  
ATOM   1653  NH2AARG A 258     -11.887  -3.165 -28.516  0.62 46.97           N  
ANISOU 1653  NH2AARG A 258     5602   6225   6019   -951    614    330       N  
ATOM   1654  NH2BARG A 258     -15.111  -2.671 -29.687  0.38 42.53           N  
ANISOU 1654  NH2BARG A 258     4705   6060   5393  -1234    629    182       N  
ATOM   1655  N   LEU A 259     -16.744   2.856 -28.675  1.00 44.31           N  
ANISOU 1655  N   LEU A 259     4293   6970   5572   -592    519   -146       N  
ATOM   1656  CA  LEU A 259     -17.413   3.866 -27.857  1.00 51.19           C  
ANISOU 1656  CA  LEU A 259     5027   8046   6377   -465    535   -210       C  
ATOM   1657  C   LEU A 259     -18.922   3.635 -27.757  1.00 56.34           C  
ANISOU 1657  C   LEU A 259     5489   8972   6948   -557    581   -227       C  
ATOM   1658  O   LEU A 259     -19.516   3.847 -26.703  1.00 55.81           O  
ANISOU 1658  O   LEU A 259     5319   9097   6790   -536    637   -242       O  
ATOM   1659  CB  LEU A 259     -17.129   5.266 -28.407  1.00 42.10           C  
ANISOU 1659  CB  LEU A 259     3871   6846   5280   -253    467   -294       C  
ATOM   1660  CG  LEU A 259     -15.685   5.709 -28.190  1.00 39.79           C  
ANISOU 1660  CG  LEU A 259     3736   6341   5040   -160    431   -289       C  
ATOM   1661  CD1 LEU A 259     -15.406   7.011 -28.922  1.00 42.29           C  
ANISOU 1661  CD1 LEU A 259     4075   6582   5412     10    363   -364       C  
ATOM   1662  CD2 LEU A 259     -15.373   5.841 -26.688  1.00 36.50           C  
ANISOU 1662  CD2 LEU A 259     3337   5983   4549   -128    472   -282       C  
ATOM   1663  N   LYS A 260     -19.539   3.192 -28.847  1.00 47.56           N  
ANISOU 1663  N   LYS A 260     4321   7893   5858   -665    559   -227       N  
ATOM   1664  CA  LYS A 260     -20.975   2.976 -28.858  1.00 56.03           C  
ANISOU 1664  CA  LYS A 260     5190   9251   6849   -766    594   -245       C  
ATOM   1665  C   LYS A 260     -21.344   1.738 -28.036  1.00 60.52           C  
ANISOU 1665  C   LYS A 260     5762   9896   7335  -1007    679   -168       C  
ATOM   1666  O   LYS A 260     -22.499   1.561 -27.641  1.00 62.19           O  
ANISOU 1666  O   LYS A 260     5794  10383   7453  -1104    731   -175       O  
ATOM   1667  CB  LYS A 260     -21.485   2.857 -30.303  1.00 65.07           C  
ANISOU 1667  CB  LYS A 260     6278  10412   8032   -825    535   -268       C  
ATOM   1668  CG  LYS A 260     -21.950   1.468 -30.740  1.00 74.77           C  
ANISOU 1668  CG  LYS A 260     7521  11656   9233  -1120    562   -213       C  
ATOM   1669  CD  LYS A 260     -22.414   1.500 -32.200  1.00 85.12           C  
ANISOU 1669  CD  LYS A 260     8775  12994  10575  -1158    491   -250       C  
ATOM   1670  CE  LYS A 260     -22.993   0.161 -32.653  1.00 91.57           C  
ANISOU 1670  CE  LYS A 260     9600  13845  11348  -1472    516   -211       C  
ATOM   1671  NZ  LYS A 260     -23.435   0.183 -34.085  1.00 92.27           N  
ANISOU 1671  NZ  LYS A 260     9635  13970  11454  -1519    441   -251       N  
ATOM   1672  N   SER A 261     -20.350   0.903 -27.754  1.00 55.90           N  
ANISOU 1672  N   SER A 261     5385   9076   6780  -1097    695    -90       N  
ATOM   1673  CA  SER A 261     -20.588  -0.358 -27.063  1.00 57.96           C  
ANISOU 1673  CA  SER A 261     5702   9353   6966  -1334    771     -1       C  
ATOM   1674  C   SER A 261     -20.654  -0.201 -25.549  1.00 62.56           C  
ANISOU 1674  C   SER A 261     6249  10067   7454  -1300    838     24       C  
ATOM   1675  O   SER A 261     -21.191  -1.065 -24.860  1.00 69.98           O  
ANISOU 1675  O   SER A 261     7178  11111   8300  -1496    913     90       O  
ATOM   1676  CB  SER A 261     -19.495  -1.363 -27.407  1.00 56.41           C  
ANISOU 1676  CB  SER A 261     5760   8839   6833  -1424    760     78       C  
ATOM   1677  OG  SER A 261     -18.272  -0.981 -26.800  1.00 59.37           O  
ANISOU 1677  OG  SER A 261     6260   9052   7245  -1253    743     99       O  
ATOM   1678  N   VAL A 262     -20.101   0.887 -25.026  1.00 64.35           N  
ANISOU 1678  N   VAL A 262     6470  10285   7694  -1065    814    -27       N  
ATOM   1679  CA  VAL A 262     -19.963   1.009 -23.583  1.00 67.89           C  
ANISOU 1679  CA  VAL A 262     6923  10823   8051  -1028    872     -3       C  
ATOM   1680  C   VAL A 262     -21.322   1.187 -22.926  1.00 77.56           C  
ANISOU 1680  C   VAL A 262     7926  12391   9151  -1077    946    -36       C  
ATOM   1681  O   VAL A 262     -22.190   1.899 -23.437  1.00 71.58           O  
ANISOU 1681  O   VAL A 262     6985  11821   8392   -994    932   -120       O  
ATOM   1682  CB  VAL A 262     -19.036   2.180 -23.171  1.00 72.42           C  
ANISOU 1682  CB  VAL A 262     7550  11307   8658   -775    825    -63       C  
ATOM   1683  CG1 VAL A 262     -19.547   3.490 -23.697  1.00 71.95           C  
ANISOU 1683  CG1 VAL A 262     7355  11357   8627   -582    784   -183       C  
ATOM   1684  CG2 VAL A 262     -18.914   2.249 -21.646  1.00 73.56           C  
ANISOU 1684  CG2 VAL A 262     7704  11557   8690   -753    884    -40       C  
ATOM   1685  N   ARG A 263     -21.510   0.496 -21.808  1.00 86.58           N  
ANISOU 1685  N   ARG A 263     9087  13625  10184  -1215   1028     37       N  
ATOM   1686  CA  ARG A 263     -22.698   0.670 -20.998  1.00 95.29           C  
ANISOU 1686  CA  ARG A 263     9983  15072  11152  -1258   1113     11       C  
ATOM   1687  C   ARG A 263     -22.290   1.255 -19.664  1.00107.65           C  
ANISOU 1687  C   ARG A 263    11575  16691  12635  -1115   1150     -4       C  
ATOM   1688  O   ARG A 263     -21.238   0.930 -19.119  1.00118.47           O  
ANISOU 1688  O   ARG A 263    13138  17863  14013  -1111   1137     63       O  
ATOM   1689  CB  ARG A 263     -23.439  -0.653 -20.815  1.00 96.98           C  
ANISOU 1689  CB  ARG A 263    10178  15390  11279  -1579   1190    109       C  
ATOM   1690  CG  ARG A 263     -23.891  -1.275 -22.124  1.00103.82           C  
ANISOU 1690  CG  ARG A 263    11023  16212  12210  -1750   1154    115       C  
ATOM   1691  CD  ARG A 263     -24.668  -0.269 -22.965  1.00114.91           C  
ANISOU 1691  CD  ARG A 263    12226  17779  13654  -1583   1092     -4       C  
ATOM   1692  NE  ARG A 263     -24.662  -0.620 -24.385  1.00120.97           N  
ANISOU 1692  NE  ARG A 263    13022  18424  14515  -1671   1025    -11       N  
ATOM   1693  CZ  ARG A 263     -25.156   0.149 -25.351  1.00120.87           C  
ANISOU 1693  CZ  ARG A 263    12877  18497  14552  -1536    954    -97       C  
ATOM   1694  NH1 ARG A 263     -25.702   1.322 -25.059  1.00119.99           N  
ANISOU 1694  NH1 ARG A 263    12606  18576  14409  -1294    941   -182       N  
ATOM   1695  NH2 ARG A 263     -25.103  -0.255 -26.613  1.00121.83           N  
ANISOU 1695  NH2 ARG A 263    13041  18503  14746  -1635    895    -97       N  
ATOM   1696  N   MET A 264     -23.128   2.143 -19.156  1.00113.48           N  
ANISOU 1696  N   MET A 264    12117  17710  13289   -986   1193    -96       N  
ATOM   1697  CA  MET A 264     -22.907   2.766 -17.867  1.00114.76           C  
ANISOU 1697  CA  MET A 264    12287  17964  13351   -850   1237   -130       C  
ATOM   1698  C   MET A 264     -24.246   2.795 -17.149  1.00112.84           C  
ANISOU 1698  C   MET A 264    11854  18049  12972   -891   1318   -157       C  
ATOM   1699  O   MET A 264     -25.230   3.310 -17.683  1.00112.55           O  
ANISOU 1699  O   MET A 264    11670  18144  12951   -806   1288   -233       O  
ATOM   1700  CB  MET A 264     -22.315   4.164 -18.041  1.00116.53           C  
ANISOU 1700  CB  MET A 264    12548  18085  13645   -551   1164   -250       C  
ATOM   1701  CG  MET A 264     -23.115   5.072 -18.965  1.00118.57           C  
ANISOU 1701  CG  MET A 264    12638  18462  13953   -393   1131   -360       C  
ATOM   1702  SD  MET A 264     -23.815   4.263 -20.417  1.00149.06           S  
ANISOU 1702  SD  MET A 264    16400  22344  17893   -579   1100   -314       S  
ATOM   1703  CE  MET A 264     -22.388   4.290 -21.500  1.00104.63           C  
ANISOU 1703  CE  MET A 264    11017  16294  12445   -530    979   -291       C  
ATOM   1704  N   LEU A 265     -24.293   2.216 -15.953  1.00113.39           N  
ANISOU 1704  N   LEU A 265    11974  18190  12919  -1009   1388    -86       N  
ATOM   1705  CA  LEU A 265     -25.568   1.994 -15.278  1.00114.55           C  
ANISOU 1705  CA  LEU A 265    11997  18574  12953  -1087   1437    -87       C  
ATOM   1706  C   LEU A 265     -26.315   3.311 -15.058  1.00116.32           C  
ANISOU 1706  C   LEU A 265    12063  18991  13143   -825   1430   -230       C  
ATOM   1707  O   LEU A 265     -27.546   3.353 -15.111  1.00122.83           O  
ANISOU 1707  O   LEU A 265    12731  20019  13920   -842   1439   -261       O  
ATOM   1708  CB  LEU A 265     -25.352   1.257 -13.953  1.00109.48           C  
ANISOU 1708  CB  LEU A 265    11456  17961  12181  -1232   1512     11       C  
ATOM   1709  CG  LEU A 265     -26.518   0.386 -13.456  1.00107.97           C  
ANISOU 1709  CG  LEU A 265    11191  17943  11887  -1450   1566     72       C  
ATOM   1710  CD1 LEU A 265     -27.554   0.105 -14.553  1.00111.01           C  
ANISOU 1710  CD1 LEU A 265    11444  18403  12329  -1549   1528     50       C  
ATOM   1711  CD2 LEU A 265     -26.002  -0.917 -12.864  1.00103.44           C  
ANISOU 1711  CD2 LEU A 265    10806  17238  11259  -1698   1609    230       C  
ATOM   1712  N   SER A 266     -25.565   4.387 -14.846  1.00109.00           N  
ANISOU 1712  N   SER A 266    11188  17992  12235   -582   1410   -318       N  
ATOM   1713  CA  SER A 266     -26.154   5.715 -14.739  1.00105.99           C  
ANISOU 1713  CA  SER A 266    10703  17735  11835   -307   1395   -458       C  
ATOM   1714  C   SER A 266     -26.081   6.449 -16.072  1.00109.08           C  
ANISOU 1714  C   SER A 266    11067  18018  12362   -145   1309   -529       C  
ATOM   1715  O   SER A 266     -27.080   6.556 -16.786  1.00112.57           O  
ANISOU 1715  O   SER A 266    11374  18572  12825   -127   1279   -552       O  
ATOM   1716  CB  SER A 266     -25.456   6.531 -13.652  1.00103.06           C  
ANISOU 1716  CB  SER A 266    10426  17344  11389   -131   1422   -526       C  
ATOM   1717  OG  SER A 266     -25.991   7.840 -13.587  1.00103.99           O  
ANISOU 1717  OG  SER A 266    10477  17543  11493    142   1405   -665       O  
ATOM   1718  N   GLY A 267     -24.890   6.948 -16.397  1.00108.98           N  
ANISOU 1718  N   GLY A 267    11183  17794  12429    -29   1268   -561       N  
ATOM   1719  CA  GLY A 267     -24.671   7.713 -17.611  1.00115.02           C  
ANISOU 1719  CA  GLY A 267    11952  18430  13322    136   1185   -629       C  
ATOM   1720  C   GLY A 267     -25.586   8.910 -17.726  1.00123.58           C  
ANISOU 1720  C   GLY A 267    12942  19625  14386    390   1158   -743       C  
ATOM   1721  O   GLY A 267     -25.659   9.727 -16.810  1.00126.41           O  
ANISOU 1721  O   GLY A 267    13325  20041  14664    559   1189   -823       O  
ATOM   1722  N   SER A 268     -26.288   9.025 -18.849  1.00126.97           N  
ANISOU 1722  N   SER A 268    13274  20086  14882    420   1101   -750       N  
ATOM   1723  CA  SER A 268     -26.161   8.108 -19.978  1.00123.09           C  
ANISOU 1723  CA  SER A 268    12770  19514  14484    223   1060   -667       C  
ATOM   1724  C   SER A 268     -26.374   8.915 -21.245  1.00122.17           C  
ANISOU 1724  C   SER A 268    12626  19333  14461    401    969   -725       C  
ATOM   1725  O   SER A 268     -25.857   8.582 -22.313  1.00128.87           O  
ANISOU 1725  O   SER A 268    13518  20033  15416    327    914   -690       O  
ATOM   1726  CB  SER A 268     -27.174   6.961 -19.892  1.00122.88           C  
ANISOU 1726  CB  SER A 268    12624  19676  14390    -35   1099   -585       C  
ATOM   1727  OG  SER A 268     -26.955   6.003 -20.913  1.00117.92           O  
ANISOU 1727  OG  SER A 268    12020  18940  13844   -248   1063   -507       O  
ATOM   1728  N   LYS A 269     -27.150   9.986 -21.111  1.00111.38           N  
ANISOU 1728  N   LYS A 269    11194  18077  13048    639    955   -810       N  
ATOM   1729  CA  LYS A 269     -27.316  10.952 -22.183  1.00102.03           C  
ANISOU 1729  CA  LYS A 269    10013  16817  11937    856    870   -866       C  
ATOM   1730  C   LYS A 269     -25.995  11.686 -22.389  1.00100.73           C  
ANISOU 1730  C   LYS A 269    10039  16373  11862   1001    830   -914       C  
ATOM   1731  O   LYS A 269     -25.746  12.245 -23.454  1.00103.80           O  
ANISOU 1731  O   LYS A 269    10479  16622  12340   1119    751   -935       O  
ATOM   1732  CB  LYS A 269     -28.446  11.936 -21.865  1.00 93.63           C  
ANISOU 1732  CB  LYS A 269     8854  15934  10788   1088    873   -941       C  
ATOM   1733  N   GLU A 270     -25.155  11.674 -21.357  1.00 99.25           N  
ANISOU 1733  N   GLU A 270     9958  16113  11639    985    882   -929       N  
ATOM   1734  CA  GLU A 270     -23.810  12.232 -21.439  1.00100.95           C  
ANISOU 1734  CA  GLU A 270    10356  16077  11924   1082    850   -973       C  
ATOM   1735  C   GLU A 270     -22.957  11.429 -22.418  1.00102.12           C  
ANISOU 1735  C   GLU A 270    10607  15995  12199    888    781   -877       C  
ATOM   1736  O   GLU A 270     -22.064  11.972 -23.068  1.00106.39           O  
ANISOU 1736  O   GLU A 270    11322  16263  12838    959    698   -889       O  
ATOM   1737  CB  GLU A 270     -23.152  12.260 -20.057  1.00 98.24           C  
ANISOU 1737  CB  GLU A 270    10119  15710  11496   1063    910   -994       C  
ATOM   1738  N   LYS A 271     -23.243  10.134 -22.520  1.00 98.08           N  
ANISOU 1738  N   LYS A 271    10006  15581  11679    634    815   -779       N  
ATOM   1739  CA  LYS A 271     -22.535   9.259 -23.450  1.00 87.86           C  
ANISOU 1739  CA  LYS A 271     8818  14070  10495    442    755   -686       C  
ATOM   1740  C   LYS A 271     -23.023   9.470 -24.882  1.00 86.52           C  
ANISOU 1740  C   LYS A 271     8573  13901  10401    488    685   -697       C  
ATOM   1741  O   LYS A 271     -22.225   9.539 -25.815  1.00 86.98           O  
ANISOU 1741  O   LYS A 271     8773  13709  10566    483    606   -676       O  
ATOM   1742  CB  LYS A 271     -22.709   7.793 -23.045  1.00 80.42           C  
ANISOU 1742  CB  LYS A 271     7835  13215   9508    153    820   -580       C  
ATOM   1743  CG  LYS A 271     -22.083   6.800 -24.009  1.00 78.89           C  
ANISOU 1743  CG  LYS A 271     7754  12806   9417    -43    769   -489       C  
ATOM   1744  CD  LYS A 271     -23.122   5.850 -24.597  1.00 80.20           C  
ANISOU 1744  CD  LYS A 271     7761  13155   9555   -247    795   -443       C  
ATOM   1745  CE  LYS A 271     -22.459   4.703 -25.349  1.00 73.49           C  
ANISOU 1745  CE  LYS A 271     7059  12079   8787   -465    763   -351       C  
ATOM   1746  NZ  LYS A 271     -23.399   3.571 -25.603  1.00 77.71           N  
ANISOU 1746  NZ  LYS A 271     7477  12781   9266   -727    808   -296       N  
ATOM   1747  N   ASP A 272     -24.338   9.566 -25.048  1.00 82.00           N  
ANISOU 1747  N   ASP A 272     7767  13628   9760    531    715   -729       N  
ATOM   1748  CA  ASP A 272     -24.930   9.820 -26.356  1.00 84.79           C  
ANISOU 1748  CA  ASP A 272     8033  14020  10162    590    641   -739       C  
ATOM   1749  C   ASP A 272     -24.430  11.134 -26.948  1.00 79.26           C  
ANISOU 1749  C   ASP A 272     7454  13131   9531    864    562   -807       C  
ATOM   1750  O   ASP A 272     -24.139  11.214 -28.146  1.00 74.40           O  
ANISOU 1750  O   ASP A 272     6904  12363   9001    864    479   -787       O  
ATOM   1751  CB  ASP A 272     -26.458   9.845 -26.265  1.00 89.69           C  
ANISOU 1751  CB  ASP A 272     8486  14907  10687    602    651   -744       C  
ATOM   1752  CG  ASP A 272     -27.077   8.474 -26.447  1.00100.69           C  
ANISOU 1752  CG  ASP A 272     9777  16436  12044    293    678   -663       C  
ATOM   1753  OD1 ASP A 272     -26.409   7.467 -26.132  1.00105.31           O  
ANISOU 1753  OD1 ASP A 272    10433  16934  12646     67    722   -600       O  
ATOM   1754  OD2 ASP A 272     -28.234   8.404 -26.911  1.00106.54           O  
ANISOU 1754  OD2 ASP A 272    10379  17368  12734    275    654   -662       O  
ATOM   1755  N   ARG A 273     -24.331  12.153 -26.098  1.00 72.99           N  
ANISOU 1755  N   ARG A 273     6714  12329   8689   1084    588   -887       N  
ATOM   1756  CA  ARG A 273     -23.942  13.486 -26.530  1.00 70.13           C  
ANISOU 1756  CA  ARG A 273     6494  11780   8373   1348    520   -957       C  
ATOM   1757  C   ARG A 273     -22.522  13.492 -27.062  1.00 75.84           C  
ANISOU 1757  C   ARG A 273     7472  12135   9209   1267    450   -918       C  
ATOM   1758  O   ARG A 273     -22.271  13.974 -28.164  1.00 71.69           O  
ANISOU 1758  O   ARG A 273     7027  11454   8757   1342    369   -915       O  
ATOM   1759  CB  ARG A 273     -24.076  14.488 -25.384  1.00 67.40           C  
ANISOU 1759  CB  ARG A 273     6213  11453   7944   1553    563  -1045       C  
ATOM   1760  N   ASN A 274     -21.596  12.957 -26.273  1.00 82.20           N  
ANISOU 1760  N   ASN A 274     8397  12817  10019   1117    481   -885       N  
ATOM   1761  CA  ASN A 274     -20.197  12.888 -26.679  1.00 82.95           C  
ANISOU 1761  CA  ASN A 274     8711  12596  10210   1031    423   -844       C  
ATOM   1762  C   ASN A 274     -20.013  12.082 -27.952  1.00 70.93           C  
ANISOU 1762  C   ASN A 274     7188  10988   8776    875    372   -765       C  
ATOM   1763  O   ASN A 274     -19.214  12.439 -28.812  1.00 69.32           O  
ANISOU 1763  O   ASN A 274     7125  10557   8655    896    303   -755       O  
ATOM   1764  CB  ASN A 274     -19.341  12.290 -25.563  1.00 94.74           C  
ANISOU 1764  CB  ASN A 274    10294  14028  11676    892    468   -810       C  
ATOM   1765  CG  ASN A 274     -18.548  13.339 -24.816  1.00100.49           C  
ANISOU 1765  CG  ASN A 274    11185  14613  12383   1026    455   -883       C  
ATOM   1766  OD1 ASN A 274     -18.607  13.417 -23.590  1.00106.87           O  
ANISOU 1766  OD1 ASN A 274    11985  15521  13099   1043    512   -917       O  
ATOM   1767  ND2 ASN A 274     -17.799  14.156 -25.554  1.00 96.88           N  
ANISOU 1767  ND2 ASN A 274    10885  13924  12002   1107    379   -909       N  
ATOM   1768  N   LEU A 275     -20.756  10.991 -28.067  1.00 64.55           N  
ANISOU 1768  N   LEU A 275     6223  10362   7939    708    411   -711       N  
ATOM   1769  CA  LEU A 275     -20.709  10.167 -29.264  1.00 63.02           C  
ANISOU 1769  CA  LEU A 275     6026  10106   7812    549    369   -647       C  
ATOM   1770  C   LEU A 275     -21.223  10.896 -30.504  1.00 62.96           C  
ANISOU 1770  C   LEU A 275     5972  10114   7837    688    294   -679       C  
ATOM   1771  O   LEU A 275     -20.733  10.648 -31.602  1.00 64.36           O  
ANISOU 1771  O   LEU A 275     6233  10132   8086    618    236   -642       O  
ATOM   1772  CB  LEU A 275     -21.512   8.889 -29.062  1.00 65.69           C  
ANISOU 1772  CB  LEU A 275     6212  10651   8096    328    429   -592       C  
ATOM   1773  CG  LEU A 275     -20.709   7.626 -28.777  1.00 72.02           C  
ANISOU 1773  CG  LEU A 275     7132  11310   8923     91    461   -506       C  
ATOM   1774  CD1 LEU A 275     -21.665   6.481 -28.557  1.00 82.52           C  
ANISOU 1774  CD1 LEU A 275     8318  12855  10182   -126    524   -459       C  
ATOM   1775  CD2 LEU A 275     -19.762   7.316 -29.932  1.00 68.33           C  
ANISOU 1775  CD2 LEU A 275     6822  10579   8562     28    395   -468       C  
ATOM   1776  N   ARG A 276     -22.216  11.769 -30.339  1.00 62.56           N  
ANISOU 1776  N   ARG A 276     5788  10260   7723    892    297   -744       N  
ATOM   1777  CA  ARG A 276     -22.696  12.579 -31.461  1.00 55.81           C  
ANISOU 1777  CA  ARG A 276     4901   9416   6887   1064    220   -771       C  
ATOM   1778  C   ARG A 276     -21.590  13.495 -31.945  1.00 53.57           C  
ANISOU 1778  C   ARG A 276     4861   8815   6680   1183    154   -784       C  
ATOM   1779  O   ARG A 276     -21.387  13.653 -33.144  1.00 50.76           O  
ANISOU 1779  O   ARG A 276     4565   8344   6378   1190     82   -759       O  
ATOM   1780  CB  ARG A 276     -23.911  13.426 -31.085  1.00 60.19           C  
ANISOU 1780  CB  ARG A 276     5280  10238   7353   1305    238   -840       C  
ATOM   1781  CG  ARG A 276     -25.235  12.686 -31.060  1.00 78.82           C  
ANISOU 1781  CG  ARG A 276     7370  12945   9632   1203    275   -821       C  
ATOM   1782  CD  ARG A 276     -26.422  13.651 -31.169  1.00 89.14           C  
ANISOU 1782  CD  ARG A 276     8606  14399  10863   1430    246   -855       C  
ATOM   1783  NE  ARG A 276     -26.304  14.820 -30.293  1.00100.21           N  
ANISOU 1783  NE  ARG A 276    10119  15725  12232   1679    270   -925       N  
ATOM   1784  CZ  ARG A 276     -26.681  14.854 -29.014  1.00100.10           C  
ANISOU 1784  CZ  ARG A 276    10062  15837  12136   1696    351   -958       C  
ATOM   1785  NH1 ARG A 276     -27.196  13.778 -28.432  1.00 96.00           N  
ANISOU 1785  NH1 ARG A 276     9393  15525  11559   1477    418   -920       N  
ATOM   1786  NH2 ARG A 276     -26.535  15.969 -28.312  1.00 99.42           N  
ANISOU 1786  NH2 ARG A 276    10096  15660  12017   1925    366  -1029       N  
ATOM   1787  N   ARG A 277     -20.881  14.104 -30.999  1.00 49.22           N  
ANISOU 1787  N   ARG A 277     4448   8130   6122   1263    181   -825       N  
ATOM   1788  CA  ARG A 277     -19.816  15.040 -31.328  1.00 54.77           C  
ANISOU 1788  CA  ARG A 277     5385   8539   6884   1357    125   -845       C  
ATOM   1789  C   ARG A 277     -18.637  14.340 -32.013  1.00 54.61           C  
ANISOU 1789  C   ARG A 277     5496   8301   6953   1154     93   -773       C  
ATOM   1790  O   ARG A 277     -18.046  14.865 -32.956  1.00 45.14           O  
ANISOU 1790  O   ARG A 277     4429   6911   5810   1191     29   -762       O  
ATOM   1791  CB  ARG A 277     -19.339  15.764 -30.069  1.00 63.18           C  
ANISOU 1791  CB  ARG A 277     6563   9535   7909   1454    164   -911       C  
ATOM   1792  CG  ARG A 277     -18.402  16.932 -30.332  1.00 80.49           C  
ANISOU 1792  CG  ARG A 277     8996  11446  10140   1566    107   -948       C  
ATOM   1793  CD  ARG A 277     -18.281  17.818 -29.099  1.00 98.50           C  
ANISOU 1793  CD  ARG A 277    11369  13703  12352   1703    144  -1039       C  
ATOM   1794  NE  ARG A 277     -17.728  19.132 -29.417  1.00109.71           N  
ANISOU 1794  NE  ARG A 277    13014  14880  13789   1848     89  -1092       N  
ATOM   1795  CZ  ARG A 277     -17.676  20.148 -28.561  1.00117.20           C  
ANISOU 1795  CZ  ARG A 277    14088  15766  14676   2001    107  -1187       C  
ATOM   1796  NH1 ARG A 277     -18.146  20.006 -27.328  1.00117.88           N  
ANISOU 1796  NH1 ARG A 277    14082  16030  14676   2039    180  -1242       N  
ATOM   1797  NH2 ARG A 277     -17.157  21.309 -28.938  1.00120.70           N  
ANISOU 1797  NH2 ARG A 277    14761  15964  15135   2109     54  -1228       N  
ATOM   1798  N   ILE A 278     -18.294  13.152 -31.541  1.00 47.31           N  
ANISOU 1798  N   ILE A 278     4538   7404   6034    947    141   -721       N  
ATOM   1799  CA  ILE A 278     -17.134  12.453 -32.079  1.00 46.93           C  
ANISOU 1799  CA  ILE A 278     4614   7154   6062    778    120   -657       C  
ATOM   1800  C   ILE A 278     -17.439  11.906 -33.465  1.00 45.96           C  
ANISOU 1800  C   ILE A 278     4449   7033   5980    696     78   -614       C  
ATOM   1801  O   ILE A 278     -16.626  12.003 -34.381  1.00 51.94           O  
ANISOU 1801  O   ILE A 278     5330   7604   6800    668     32   -589       O  
ATOM   1802  CB  ILE A 278     -16.685  11.317 -31.130  1.00 50.46           C  
ANISOU 1802  CB  ILE A 278     5054   7624   6495    602    184   -609       C  
ATOM   1803  CG1 ILE A 278     -16.184  11.914 -29.812  1.00 55.51           C  
ANISOU 1803  CG1 ILE A 278     5761   8240   7091    677    213   -651       C  
ATOM   1804  CG2 ILE A 278     -15.575  10.492 -31.747  1.00 43.59           C  
ANISOU 1804  CG2 ILE A 278     4297   6566   5699    448    167   -540       C  
ATOM   1805  CD1 ILE A 278     -15.963  10.884 -28.718  1.00 60.42           C  
ANISOU 1805  CD1 ILE A 278     6357   8930   7671    535    278   -604       C  
ATOM   1806  N   THR A 279     -18.630  11.351 -33.612  1.00 43.45           N  
ANISOU 1806  N   THR A 279     3951   6942   5615    653     96   -609       N  
ATOM   1807  CA  THR A 279     -19.054  10.783 -34.868  1.00 46.70           C  
ANISOU 1807  CA  THR A 279     4307   7391   6046    558     56   -576       C  
ATOM   1808  C   THR A 279     -19.112  11.872 -35.938  1.00 45.59           C  
ANISOU 1808  C   THR A 279     4219   7178   5926    730    -25   -598       C  
ATOM   1809  O   THR A 279     -18.676  11.671 -37.063  1.00 46.05           O  
ANISOU 1809  O   THR A 279     4355   7113   6029    665    -73   -567       O  
ATOM   1810  CB  THR A 279     -20.418  10.107 -34.717  1.00 52.31           C  
ANISOU 1810  CB  THR A 279     4794   8397   6684    479     88   -575       C  
ATOM   1811  OG1 THR A 279     -20.321   9.113 -33.693  1.00 64.53           O  
ANISOU 1811  OG1 THR A 279     6320   9993   8205    310    167   -545       O  
ATOM   1812  CG2 THR A 279     -20.834   9.447 -36.001  1.00 45.91           C  
ANISOU 1812  CG2 THR A 279     3931   7631   5883    350     43   -545       C  
ATOM   1813  N   ARG A 280     -19.636  13.027 -35.556  1.00 43.24           N  
ANISOU 1813  N   ARG A 280     3893   6949   5589    956    -38   -653       N  
ATOM   1814  CA  ARG A 280     -19.697  14.178 -36.432  1.00 50.24           C  
ANISOU 1814  CA  ARG A 280     4856   7748   6484   1148   -113   -671       C  
ATOM   1815  C   ARG A 280     -18.292  14.565 -36.881  1.00 49.52           C  
ANISOU 1815  C   ARG A 280     5003   7347   6464   1117   -145   -650       C  
ATOM   1816  O   ARG A 280     -18.059  14.805 -38.075  1.00 43.57           O  
ANISOU 1816  O   ARG A 280     4326   6491   5739   1124   -206   -622       O  
ATOM   1817  CB  ARG A 280     -20.385  15.339 -35.716  1.00 53.60           C  
ANISOU 1817  CB  ARG A 280     5245   8269   6850   1409   -106   -738       C  
ATOM   1818  CG  ARG A 280     -21.041  16.357 -36.616  1.00 72.02           C  
ANISOU 1818  CG  ARG A 280     7577  10627   9160   1636   -181   -751       C  
ATOM   1819  CD  ARG A 280     -21.805  17.387 -35.783  1.00 89.86           C  
ANISOU 1819  CD  ARG A 280     9791  13001  11351   1909   -159   -824       C  
ATOM   1820  NE  ARG A 280     -20.916  18.141 -34.899  1.00 97.71           N  
ANISOU 1820  NE  ARG A 280    10992  13775  12358   1976   -131   -871       N  
ATOM   1821  CZ  ARG A 280     -21.186  18.430 -33.629  1.00 98.20           C  
ANISOU 1821  CZ  ARG A 280    11021  13926  12365   2069    -65   -938       C  
ATOM   1822  NH1 ARG A 280     -22.324  18.027 -33.083  1.00 99.80           N  
ANISOU 1822  NH1 ARG A 280    10981  14442  12497   2111    -13   -960       N  
ATOM   1823  NH2 ARG A 280     -20.317  19.122 -32.906  1.00 95.71           N  
ANISOU 1823  NH2 ARG A 280    10911  13399  12057   2109    -49   -984       N  
ATOM   1824  N   MET A 281     -17.353  14.597 -35.935  1.00 39.60           N  
ANISOU 1824  N   MET A 281     3854   5962   5228   1072   -102   -662       N  
ATOM   1825  CA  MET A 281     -15.971  14.954 -36.250  1.00 47.54           C  
ANISOU 1825  CA  MET A 281     5065   6705   6293   1026   -127   -644       C  
ATOM   1826  C   MET A 281     -15.313  13.933 -37.172  1.00 47.79           C  
ANISOU 1826  C   MET A 281     5122   6657   6378    834   -134   -580       C  
ATOM   1827  O   MET A 281     -14.574  14.300 -38.082  1.00 40.57           O  
ANISOU 1827  O   MET A 281     4335   5577   5502    824   -176   -558       O  
ATOM   1828  CB  MET A 281     -15.123  15.107 -34.984  1.00 44.75           C  
ANISOU 1828  CB  MET A 281     4796   6269   5937   1001    -83   -670       C  
ATOM   1829  CG  MET A 281     -14.829  16.556 -34.619  1.00 63.78           C  
ANISOU 1829  CG  MET A 281     7354   8551   8329   1167   -108   -731       C  
ATOM   1830  SD  MET A 281     -13.903  17.431 -35.902  1.00 73.83           S  
ANISOU 1830  SD  MET A 281     8835   9565   9652   1179   -181   -707       S  
ATOM   1831  CE  MET A 281     -12.329  16.591 -35.772  1.00 92.89           C  
ANISOU 1831  CE  MET A 281    11316  11856  12123    947   -158   -657       C  
ATOM   1832  N   VAL A 282     -15.572  12.655 -36.924  1.00 47.22           N  
ANISOU 1832  N   VAL A 282     4941   6697   6302    681    -89   -550       N  
ATOM   1833  CA  VAL A 282     -15.073  11.609 -37.803  1.00 43.15           C  
ANISOU 1833  CA  VAL A 282     4455   6111   5828    510    -90   -498       C  
ATOM   1834  C   VAL A 282     -15.591  11.794 -39.224  1.00 44.58           C  
ANISOU 1834  C   VAL A 282     4620   6312   6006    534   -152   -489       C  
ATOM   1835  O   VAL A 282     -14.823  11.718 -40.189  1.00 44.13           O  
ANISOU 1835  O   VAL A 282     4672   6108   5986    479   -178   -462       O  
ATOM   1836  CB  VAL A 282     -15.460  10.212 -37.305  1.00 40.79           C  
ANISOU 1836  CB  VAL A 282     4056   5932   5512    345    -32   -470       C  
ATOM   1837  CG1 VAL A 282     -15.183   9.185 -38.393  1.00 38.94           C  
ANISOU 1837  CG1 VAL A 282     3857   5630   5307    188    -39   -429       C  
ATOM   1838  CG2 VAL A 282     -14.682   9.882 -36.047  1.00 37.54           C  
ANISOU 1838  CG2 VAL A 282     3693   5464   5106    302     24   -458       C  
ATOM   1839  N   LEU A 283     -16.889  12.049 -39.354  1.00 42.14           N  
ANISOU 1839  N   LEU A 283     4169   6199   5644    620   -175   -512       N  
ATOM   1840  CA  LEU A 283     -17.475  12.217 -40.673  1.00 44.99           C  
ANISOU 1840  CA  LEU A 283     4496   6611   5985    649   -242   -501       C  
ATOM   1841  C   LEU A 283     -16.871  13.427 -41.380  1.00 45.07           C  
ANISOU 1841  C   LEU A 283     4667   6441   6015    790   -301   -498       C  
ATOM   1842  O   LEU A 283     -16.618  13.386 -42.580  1.00 38.82           O  
ANISOU 1842  O   LEU A 283     3940   5577   5232    750   -346   -468       O  
ATOM   1843  CB  LEU A 283     -18.993  12.348 -40.575  1.00 50.05           C  
ANISOU 1843  CB  LEU A 283     4932   7530   6555    738   -260   -525       C  
ATOM   1844  CG  LEU A 283     -19.688  11.090 -40.043  1.00 55.22           C  
ANISOU 1844  CG  LEU A 283     5421   8383   7177    557   -204   -521       C  
ATOM   1845  CD1 LEU A 283     -21.166  11.321 -39.789  1.00 49.38           C  
ANISOU 1845  CD1 LEU A 283     4453   7952   6357    652   -213   -550       C  
ATOM   1846  CD2 LEU A 283     -19.497   9.931 -41.002  1.00 56.61           C  
ANISOU 1846  CD2 LEU A 283     5620   8522   7367    334   -213   -487       C  
ATOM   1847  N   VAL A 284     -16.618  14.499 -40.636  1.00 43.51           N  
ANISOU 1847  N   VAL A 284     4550   6165   5819    945   -298   -529       N  
ATOM   1848  CA  VAL A 284     -16.018  15.675 -41.245  1.00 42.11           C  
ANISOU 1848  CA  VAL A 284     4552   5795   5654   1061   -350   -523       C  
ATOM   1849  C   VAL A 284     -14.597  15.391 -41.751  1.00 40.24           C  
ANISOU 1849  C   VAL A 284     4468   5347   5472    909   -341   -487       C  
ATOM   1850  O   VAL A 284     -14.312  15.657 -42.920  1.00 40.80           O  
ANISOU 1850  O   VAL A 284     4627   5329   5547    901   -387   -454       O  
ATOM   1851  CB  VAL A 284     -15.991  16.876 -40.287  1.00 46.00           C  
ANISOU 1851  CB  VAL A 284     5127   6222   6128   1241   -344   -573       C  
ATOM   1852  CG1 VAL A 284     -15.159  18.007 -40.888  1.00 41.16           C  
ANISOU 1852  CG1 VAL A 284     4742   5367   5532   1307   -390   -562       C  
ATOM   1853  CG2 VAL A 284     -17.412  17.365 -40.022  1.00 48.06           C  
ANISOU 1853  CG2 VAL A 284     5249   6687   6325   1444   -361   -610       C  
ATOM   1854  N   VAL A 285     -13.711  14.838 -40.917  1.00 35.20           N  
ANISOU 1854  N   VAL A 285     3858   4647   4871    792   -283   -488       N  
ATOM   1855  CA  VAL A 285     -12.320  14.706 -41.365  1.00 35.86           C  
ANISOU 1855  CA  VAL A 285     4077   4549   5001    677   -275   -456       C  
ATOM   1856  C   VAL A 285     -12.219  13.709 -42.520  1.00 40.19           C  
ANISOU 1856  C   VAL A 285     4601   5108   5562    548   -278   -415       C  
ATOM   1857  O   VAL A 285     -11.358  13.862 -43.386  1.00 38.43           O  
ANISOU 1857  O   VAL A 285     4488   4756   5358    498   -291   -387       O  
ATOM   1858  CB  VAL A 285     -11.322  14.306 -40.232  1.00 41.23           C  
ANISOU 1858  CB  VAL A 285     4781   5175   5709    590   -219   -461       C  
ATOM   1859  CG1 VAL A 285     -11.526  15.175 -38.999  1.00 46.36           C  
ANISOU 1859  CG1 VAL A 285     5445   5838   6331    704   -212   -512       C  
ATOM   1860  CG2 VAL A 285     -11.399  12.819 -39.880  1.00 39.94           C  
ANISOU 1860  CG2 VAL A 285     4511   5107   5558    458   -166   -438       C  
ATOM   1861  N   VAL A 286     -13.109  12.719 -42.558  1.00 37.58           N  
ANISOU 1861  N   VAL A 286     4134   4934   5213    487   -264   -415       N  
ATOM   1862  CA  VAL A 286     -13.075  11.733 -43.640  1.00 41.47           C  
ANISOU 1862  CA  VAL A 286     4617   5432   5706    355   -265   -388       C  
ATOM   1863  C   VAL A 286     -13.644  12.338 -44.921  1.00 41.44           C  
ANISOU 1863  C   VAL A 286     4627   5453   5665    423   -338   -379       C  
ATOM   1864  O   VAL A 286     -13.073  12.174 -45.999  1.00 41.75           O  
ANISOU 1864  O   VAL A 286     4753   5403   5708    357   -353   -355       O  
ATOM   1865  CB  VAL A 286     -13.841  10.435 -43.253  1.00 38.42           C  
ANISOU 1865  CB  VAL A 286     4099   5195   5304    236   -226   -392       C  
ATOM   1866  CG1 VAL A 286     -13.975   9.504 -44.444  1.00 35.10           C  
ANISOU 1866  CG1 VAL A 286     3683   4784   4869    104   -237   -378       C  
ATOM   1867  CG2 VAL A 286     -13.111   9.715 -42.108  1.00 34.33           C  
ANISOU 1867  CG2 VAL A 286     3599   4625   4820    158   -154   -384       C  
ATOM   1868  N   ALA A 287     -14.756  13.058 -44.799  1.00 38.60           N  
ANISOU 1868  N   ALA A 287     4184   5222   5262    566   -384   -398       N  
ATOM   1869  CA  ALA A 287     -15.359  13.708 -45.952  1.00 41.89           C  
ANISOU 1869  CA  ALA A 287     4609   5676   5630    661   -463   -382       C  
ATOM   1870  C   ALA A 287     -14.401  14.741 -46.554  1.00 42.86           C  
ANISOU 1870  C   ALA A 287     4929   5589   5768    724   -491   -355       C  
ATOM   1871  O   ALA A 287     -14.262  14.831 -47.772  1.00 43.24           O  
ANISOU 1871  O   ALA A 287     5043   5595   5791    700   -534   -322       O  
ATOM   1872  CB  ALA A 287     -16.680  14.368 -45.573  1.00 38.14           C  
ANISOU 1872  CB  ALA A 287     4004   5384   5103    841   -503   -405       C  
ATOM   1873  N   VAL A 288     -13.727  15.509 -45.705  1.00 42.21           N  
ANISOU 1873  N   VAL A 288     4946   5377   5716    788   -467   -368       N  
ATOM   1874  CA  VAL A 288     -12.772  16.490 -46.218  1.00 43.01           C  
ANISOU 1874  CA  VAL A 288     5243   5274   5825    815   -489   -342       C  
ATOM   1875  C   VAL A 288     -11.633  15.819 -46.995  1.00 40.24           C  
ANISOU 1875  C   VAL A 288     4964   4824   5501    638   -460   -309       C  
ATOM   1876  O   VAL A 288     -11.300  16.250 -48.103  1.00 36.82           O  
ANISOU 1876  O   VAL A 288     4638   4309   5044    630   -494   -271       O  
ATOM   1877  CB  VAL A 288     -12.199  17.365 -45.093  1.00 41.13           C  
ANISOU 1877  CB  VAL A 288     5102   4917   5608    880   -466   -372       C  
ATOM   1878  CG1 VAL A 288     -10.997  18.142 -45.584  1.00 42.77           C  
ANISOU 1878  CG1 VAL A 288     5511   4914   5827    832   -474   -344       C  
ATOM   1879  CG2 VAL A 288     -13.275  18.317 -44.599  1.00 34.98           C  
ANISOU 1879  CG2 VAL A 288     4305   4198   4788   1097   -503   -405       C  
ATOM   1880  N   PHE A 289     -11.060  14.753 -46.441  1.00 34.89           N  
ANISOU 1880  N   PHE A 289     4230   4161   4866    505   -394   -319       N  
ATOM   1881  CA  PHE A 289     -10.000  14.036 -47.136  1.00 37.69           C  
ANISOU 1881  CA  PHE A 289     4641   4439   5243    361   -357   -293       C  
ATOM   1882  C   PHE A 289     -10.486  13.536 -48.499  1.00 37.27           C  
ANISOU 1882  C   PHE A 289     4573   4441   5147    316   -388   -275       C  
ATOM   1883  O   PHE A 289      -9.793  13.661 -49.524  1.00 37.18           O  
ANISOU 1883  O   PHE A 289     4660   4345   5121    265   -392   -246       O  
ATOM   1884  CB  PHE A 289      -9.482  12.849 -46.299  1.00 34.71           C  
ANISOU 1884  CB  PHE A 289     4196   4083   4908    254   -284   -305       C  
ATOM   1885  CG  PHE A 289      -8.285  12.166 -46.908  1.00 35.31           C  
ANISOU 1885  CG  PHE A 289     4335   4076   5006    138   -239   -282       C  
ATOM   1886  CD1 PHE A 289      -8.441  11.179 -47.872  1.00 36.28           C  
ANISOU 1886  CD1 PHE A 289     4444   4228   5111     55   -226   -277       C  
ATOM   1887  CD2 PHE A 289      -7.002  12.535 -46.541  1.00 32.41           C  
ANISOU 1887  CD2 PHE A 289     4038   3611   4668    112   -208   -270       C  
ATOM   1888  CE1 PHE A 289      -7.342  10.571 -48.455  1.00 36.26           C  
ANISOU 1888  CE1 PHE A 289     4504   4153   5122    -29   -178   -262       C  
ATOM   1889  CE2 PHE A 289      -5.891  11.926 -47.114  1.00 39.09           C  
ANISOU 1889  CE2 PHE A 289     4922   4405   5527     23   -162   -249       C  
ATOM   1890  CZ  PHE A 289      -6.061  10.943 -48.090  1.00 30.99           C  
ANISOU 1890  CZ  PHE A 289     3888   3401   4484    -37   -143   -246       C  
ATOM   1891  N   ILE A 290     -11.687  12.977 -48.505  1.00 37.44           N  
ANISOU 1891  N   ILE A 290     4466   4619   5140    325   -410   -293       N  
ATOM   1892  CA  ILE A 290     -12.223  12.371 -49.706  1.00 39.55           C  
ANISOU 1892  CA  ILE A 290     4704   4964   5358    260   -443   -286       C  
ATOM   1893  C   ILE A 290     -12.567  13.427 -50.743  1.00 45.00           C  
ANISOU 1893  C   ILE A 290     5462   5645   5991    365   -523   -255       C  
ATOM   1894  O   ILE A 290     -12.265  13.252 -51.917  1.00 39.86           O  
ANISOU 1894  O   ILE A 290     4880   4962   5304    300   -539   -233       O  
ATOM   1895  CB  ILE A 290     -13.443  11.499 -49.383  1.00 39.35           C  
ANISOU 1895  CB  ILE A 290     4513   5129   5308    218   -448   -315       C  
ATOM   1896  CG1 ILE A 290     -12.958  10.199 -48.742  1.00 43.65           C  
ANISOU 1896  CG1 ILE A 290     5038   5650   5896     70   -365   -331       C  
ATOM   1897  CG2 ILE A 290     -14.233  11.169 -50.639  1.00 42.88           C  
ANISOU 1897  CG2 ILE A 290     4920   5690   5683    174   -508   -312       C  
ATOM   1898  CD1 ILE A 290     -14.074   9.328 -48.233  1.00 48.71           C  
ANISOU 1898  CD1 ILE A 290     5532   6463   6514      1   -357   -356       C  
ATOM   1899  N   VAL A 291     -13.179  14.523 -50.319  1.00 40.25           N  
ANISOU 1899  N   VAL A 291     4854   5064   5373    534   -571   -252       N  
ATOM   1900  CA  VAL A 291     -13.551  15.577 -51.260  1.00 43.47           C  
ANISOU 1900  CA  VAL A 291     5344   5453   5721    659   -653   -213       C  
ATOM   1901  C   VAL A 291     -12.320  16.257 -51.877  1.00 44.89           C  
ANISOU 1901  C   VAL A 291     5726   5424   5905    626   -644   -171       C  
ATOM   1902  O   VAL A 291     -12.305  16.575 -53.072  1.00 42.54           O  
ANISOU 1902  O   VAL A 291     5512   5103   5550    628   -690   -128       O  
ATOM   1903  CB  VAL A 291     -14.433  16.641 -50.576  1.00 44.85           C  
ANISOU 1903  CB  VAL A 291     5487   5675   5877    877   -700   -222       C  
ATOM   1904  CG1 VAL A 291     -14.526  17.884 -51.435  1.00 42.94           C  
ANISOU 1904  CG1 VAL A 291     5393   5342   5580   1023   -776   -171       C  
ATOM   1905  CG2 VAL A 291     -15.825  16.068 -50.289  1.00 42.72           C  
ANISOU 1905  CG2 VAL A 291     4996   5663   5573    921   -724   -253       C  
ATOM   1906  N   CYS A 292     -11.287  16.462 -51.066  1.00 42.39           N  
ANISOU 1906  N   CYS A 292     5483   4974   5648    582   -583   -182       N  
ATOM   1907  CA  CYS A 292     -10.088  17.175 -51.515  1.00 45.36           C  
ANISOU 1907  CA  CYS A 292     6040   5169   6026    534   -569   -144       C  
ATOM   1908  C   CYS A 292      -9.161  16.346 -52.395  1.00 43.82           C  
ANISOU 1908  C   CYS A 292     5871   4950   5829    366   -521   -126       C  
ATOM   1909  O   CYS A 292      -8.545  16.877 -53.312  1.00 36.64           O  
ANISOU 1909  O   CYS A 292     5091   3949   4881    330   -531    -81       O  
ATOM   1910  CB  CYS A 292      -9.298  17.691 -50.311  1.00 41.42           C  
ANISOU 1910  CB  CYS A 292     5597   4558   5581    531   -525   -167       C  
ATOM   1911  SG  CYS A 292     -10.097  19.127 -49.483  1.00 45.00           S  
ANISOU 1911  SG  CYS A 292     6120   4961   6017    748   -581   -185       S  
ATOM   1912  N   TRP A 293      -9.066  15.051 -52.120  1.00 36.99           N  
ANISOU 1912  N   TRP A 293     4893   4165   4998    266   -467   -160       N  
ATOM   1913  CA  TRP A 293      -8.067  14.211 -52.765  1.00 36.21           C  
ANISOU 1913  CA  TRP A 293     4823   4032   4903    125   -405   -155       C  
ATOM   1914  C   TRP A 293      -8.598  13.275 -53.858  1.00 40.46           C  
ANISOU 1914  C   TRP A 293     5323   4662   5389     62   -417   -162       C  
ATOM   1915  O   TRP A 293      -7.835  12.853 -54.737  1.00 38.35           O  
ANISOU 1915  O   TRP A 293     5119   4356   5098    -29   -378   -153       O  
ATOM   1916  CB  TRP A 293      -7.341  13.379 -51.703  1.00 32.39           C  
ANISOU 1916  CB  TRP A 293     4277   3539   4491     59   -326   -185       C  
ATOM   1917  CG  TRP A 293      -6.168  14.071 -51.078  1.00 39.26           C  
ANISOU 1917  CG  TRP A 293     5216   4305   5397     45   -292   -171       C  
ATOM   1918  CD1 TRP A 293      -5.978  14.354 -49.747  1.00 33.78           C  
ANISOU 1918  CD1 TRP A 293     4491   3594   4749     78   -278   -191       C  
ATOM   1919  CD2 TRP A 293      -5.004  14.556 -51.763  1.00 36.67           C  
ANISOU 1919  CD2 TRP A 293     4993   3890   5050    -23   -267   -137       C  
ATOM   1920  NE1 TRP A 293      -4.767  14.990 -49.573  1.00 37.83           N  
ANISOU 1920  NE1 TRP A 293     5085   4018   5273     28   -253   -174       N  
ATOM   1921  CE2 TRP A 293      -4.152  15.120 -50.794  1.00 38.83           C  
ANISOU 1921  CE2 TRP A 293     5289   4103   5361    -38   -243   -139       C  
ATOM   1922  CE3 TRP A 293      -4.606  14.568 -53.108  1.00 40.44           C  
ANISOU 1922  CE3 TRP A 293     5545   4348   5473    -82   -262   -105       C  
ATOM   1923  CZ2 TRP A 293      -2.923  15.688 -51.123  1.00 41.77           C  
ANISOU 1923  CZ2 TRP A 293     5745   4405   5719   -122   -215   -109       C  
ATOM   1924  CZ3 TRP A 293      -3.387  15.139 -53.435  1.00 42.94           C  
ANISOU 1924  CZ3 TRP A 293     5947   4591   5775   -156   -227    -73       C  
ATOM   1925  CH2 TRP A 293      -2.554  15.680 -52.445  1.00 42.27           C  
ANISOU 1925  CH2 TRP A 293     5873   4456   5731   -182   -203    -74       C  
ATOM   1926  N   THR A 294      -9.879  12.923 -53.813  1.00 37.19           N  
ANISOU 1926  N   THR A 294     4803   4379   4950     99   -466   -185       N  
ATOM   1927  CA  THR A 294     -10.408  12.001 -54.821  1.00 38.50           C  
ANISOU 1927  CA  THR A 294     4934   4639   5056     15   -481   -201       C  
ATOM   1928  C   THR A 294     -10.372  12.599 -56.248  1.00 39.29           C  
ANISOU 1928  C   THR A 294     5136   4725   5070     25   -536   -159       C  
ATOM   1929  O   THR A 294      -9.990  11.897 -57.185  1.00 37.09           O  
ANISOU 1929  O   THR A 294     4901   4444   4748    -81   -508   -169       O  
ATOM   1930  CB  THR A 294     -11.869  11.547 -54.497  1.00 36.56           C  
ANISOU 1930  CB  THR A 294     4535   4569   4786     34   -532   -232       C  
ATOM   1931  OG1 THR A 294     -11.925  10.998 -53.176  1.00 42.35           O  
ANISOU 1931  OG1 THR A 294     5182   5321   5590     16   -478   -263       O  
ATOM   1932  CG2 THR A 294     -12.336  10.495 -55.477  1.00 37.83           C  
ANISOU 1932  CG2 THR A 294     4668   4824   4883    -91   -543   -258       C  
ATOM   1933  N   PRO A 295     -10.769  13.884 -56.425  1.00 35.96           N  
ANISOU 1933  N   PRO A 295     4763   4287   4612    158   -610   -113       N  
ATOM   1934  CA  PRO A 295     -10.822  14.357 -57.816  1.00 39.69           C  
ANISOU 1934  CA  PRO A 295     5334   4758   4988    164   -666    -65       C  
ATOM   1935  C   PRO A 295      -9.473  14.335 -58.541  1.00 41.58           C  
ANISOU 1935  C   PRO A 295     5712   4874   5215     56   -600    -41       C  
ATOM   1936  O   PRO A 295      -9.438  13.856 -59.674  1.00 39.36           O  
ANISOU 1936  O   PRO A 295     5463   4634   4856    -21   -604    -39       O  
ATOM   1937  CB  PRO A 295     -11.346  15.792 -57.685  1.00 34.73           C  
ANISOU 1937  CB  PRO A 295     4763   4096   4335    342   -747    -13       C  
ATOM   1938  CG  PRO A 295     -12.160  15.769 -56.384  1.00 37.21           C  
ANISOU 1938  CG  PRO A 295     4938   4491   4709    440   -756    -55       C  
ATOM   1939  CD  PRO A 295     -11.356  14.867 -55.488  1.00 36.07           C  
ANISOU 1939  CD  PRO A 295     4750   4301   4654    316   -653   -104       C  
ATOM   1940  N   ILE A 296      -8.393  14.817 -57.930  1.00 35.10           N  
ANISOU 1940  N   ILE A 296     4961   3920   4455     43   -540    -27       N  
ATOM   1941  CA  ILE A 296      -7.124  14.818 -58.658  1.00 31.58           C  
ANISOU 1941  CA  ILE A 296     4625   3391   3985    -63   -474     -2       C  
ATOM   1942  C   ILE A 296      -6.648  13.381 -58.892  1.00 42.76           C  
ANISOU 1942  C   ILE A 296     5981   4854   5412   -180   -393    -56       C  
ATOM   1943  O   ILE A 296      -6.160  13.062 -59.987  1.00 38.32           O  
ANISOU 1943  O   ILE A 296     5483   4296   4782   -256   -363    -50       O  
ATOM   1944  CB  ILE A 296      -6.014  15.664 -57.966  1.00 31.20           C  
ANISOU 1944  CB  ILE A 296     4656   3211   3990    -75   -428     26       C  
ATOM   1945  CG1 ILE A 296      -4.776  15.783 -58.875  1.00 32.08           C  
ANISOU 1945  CG1 ILE A 296     4869   3266   4052   -190   -367     62       C  
ATOM   1946  CG2 ILE A 296      -5.631  15.108 -56.561  1.00 37.06           C  
ANISOU 1946  CG2 ILE A 296     5294   3951   4837    -87   -368    -25       C  
ATOM   1947  CD1 ILE A 296      -5.089  16.206 -60.331  1.00 32.20           C  
ANISOU 1947  CD1 ILE A 296     4992   3293   3949   -195   -417    116       C  
ATOM   1948  N   HIS A 297      -6.842  12.495 -57.915  1.00 34.27           N  
ANISOU 1948  N   HIS A 297     4796   3813   4411   -189   -357   -110       N  
ATOM   1949  CA  HIS A 297      -6.397  11.112 -58.116  1.00 34.80           C  
ANISOU 1949  CA  HIS A 297     4836   3900   4486   -287   -279   -161       C  
ATOM   1950  C   HIS A 297      -7.122  10.410 -59.250  1.00 39.06           C  
ANISOU 1950  C   HIS A 297     5382   4521   4936   -342   -310   -188       C  
ATOM   1951  O   HIS A 297      -6.503   9.671 -60.005  1.00 38.10           O  
ANISOU 1951  O   HIS A 297     5315   4385   4776   -421   -249   -214       O  
ATOM   1952  CB  HIS A 297      -6.524  10.303 -56.831  1.00 31.18           C  
ANISOU 1952  CB  HIS A 297     4278   3452   4116   -286   -239   -203       C  
ATOM   1953  CG  HIS A 297      -5.351  10.485 -55.925  1.00 36.89           C  
ANISOU 1953  CG  HIS A 297     5004   4098   4914   -279   -171   -191       C  
ATOM   1954  ND1 HIS A 297      -4.093  10.019 -56.244  1.00 37.28           N  
ANISOU 1954  ND1 HIS A 297     5093   4105   4966   -333    -85   -193       N  
ATOM   1955  CD2 HIS A 297      -5.223  11.137 -54.745  1.00 37.69           C  
ANISOU 1955  CD2 HIS A 297     5071   4170   5077   -222   -179   -178       C  
ATOM   1956  CE1 HIS A 297      -3.245  10.359 -55.291  1.00 37.03           C  
ANISOU 1956  CE1 HIS A 297     5038   4035   4997   -315    -48   -177       C  
ATOM   1957  NE2 HIS A 297      -3.909  11.029 -54.365  1.00 40.44           N  
ANISOU 1957  NE2 HIS A 297     5432   4467   5464   -255   -105   -170       N  
ATOM   1958  N   ILE A 298      -8.421  10.649 -59.376  1.00 39.12           N  
ANISOU 1958  N   ILE A 298     5335   4627   4904   -299   -406   -186       N  
ATOM   1959  CA  ILE A 298      -9.193   9.990 -60.404  1.00 40.51           C  
ANISOU 1959  CA  ILE A 298     5503   4904   4985   -365   -449   -216       C  
ATOM   1960  C   ILE A 298      -8.846  10.609 -61.751  1.00 44.36           C  
ANISOU 1960  C   ILE A 298     6108   5380   5369   -371   -476   -172       C  
ATOM   1961  O   ILE A 298      -8.745   9.908 -62.749  1.00 45.12           O  
ANISOU 1961  O   ILE A 298     6252   5507   5386   -461   -457   -204       O  
ATOM   1962  CB  ILE A 298     -10.707  10.079 -60.133  1.00 44.92           C  
ANISOU 1962  CB  ILE A 298     5940   5609   5520   -318   -549   -225       C  
ATOM   1963  CG1 ILE A 298     -11.040   9.344 -58.826  1.00 47.07           C  
ANISOU 1963  CG1 ILE A 298     6100   5904   5882   -339   -510   -269       C  
ATOM   1964  CG2 ILE A 298     -11.509   9.484 -61.297  1.00 41.44           C  
ANISOU 1964  CG2 ILE A 298     5488   5295   4961   -402   -608   -253       C  
ATOM   1965  CD1 ILE A 298     -10.526   7.916 -58.775  1.00 45.12           C  
ANISOU 1965  CD1 ILE A 298     5879   5607   5657   -475   -418   -329       C  
ATOM   1966  N   TYR A 299      -8.641  11.922 -61.766  1.00 41.04           N  
ANISOU 1966  N   TYR A 299     5747   4904   4943   -279   -515    -99       N  
ATOM   1967  CA  TYR A 299      -8.318  12.619 -62.999  1.00 41.69           C  
ANISOU 1967  CA  TYR A 299     5954   4967   4921   -284   -542    -41       C  
ATOM   1968  C   TYR A 299      -7.014  12.074 -63.587  1.00 41.95           C  
ANISOU 1968  C   TYR A 299     6068   4936   4934   -395   -430    -58       C  
ATOM   1969  O   TYR A 299      -6.934  11.769 -64.782  1.00 45.38           O  
ANISOU 1969  O   TYR A 299     6567   5412   5261   -460   -428    -62       O  
ATOM   1970  CB  TYR A 299      -8.217  14.118 -62.738  1.00 46.51           C  
ANISOU 1970  CB  TYR A 299     6641   5493   5540   -174   -590     43       C  
ATOM   1971  CG  TYR A 299      -8.610  15.008 -63.907  1.00 49.84           C  
ANISOU 1971  CG  TYR A 299     7171   5931   5835   -125   -678    119       C  
ATOM   1972  CD1 TYR A 299      -8.280  14.675 -65.212  1.00 53.51           C  
ANISOU 1972  CD1 TYR A 299     7714   6431   6187   -219   -663    129       C  
ATOM   1973  CD2 TYR A 299      -9.302  16.197 -63.694  1.00 48.96           C  
ANISOU 1973  CD2 TYR A 299     7097   5797   5709     25   -773    184       C  
ATOM   1974  CE1 TYR A 299      -8.633  15.500 -66.279  1.00 57.05           C  
ANISOU 1974  CE1 TYR A 299     8270   6897   6509   -174   -747    210       C  
ATOM   1975  CE2 TYR A 299      -9.663  17.022 -64.754  1.00 50.72           C  
ANISOU 1975  CE2 TYR A 299     7434   6027   5811     86   -858    267       C  
ATOM   1976  CZ  TYR A 299      -9.323  16.675 -66.038  1.00 56.09           C  
ANISOU 1976  CZ  TYR A 299     8187   6747   6378    -19   -846    283       C  
ATOM   1977  OH  TYR A 299      -9.676  17.510 -67.089  1.00 63.09           O  
ANISOU 1977  OH  TYR A 299     9196   7643   7132     43   -934    375       O  
ATOM   1978  N   VAL A 300      -6.010  11.926 -62.733  1.00 38.71           N  
ANISOU 1978  N   VAL A 300     5644   4443   4622   -412   -338    -71       N  
ATOM   1979  CA  VAL A 300      -4.712  11.406 -63.143  1.00 42.43           C  
ANISOU 1979  CA  VAL A 300     6164   4874   5083   -495   -223    -89       C  
ATOM   1980  C   VAL A 300      -4.856   9.995 -63.745  1.00 45.97           C  
ANISOU 1980  C   VAL A 300     6603   5377   5487   -566   -179   -169       C  
ATOM   1981  O   VAL A 300      -4.311   9.709 -64.813  1.00 39.00           O  
ANISOU 1981  O   VAL A 300     5797   4507   4514   -625   -130   -180       O  
ATOM   1982  CB  VAL A 300      -3.716  11.408 -61.944  1.00 36.72           C  
ANISOU 1982  CB  VAL A 300     5394   4082   4478   -486   -143    -92       C  
ATOM   1983  CG1 VAL A 300      -2.497  10.551 -62.225  1.00 39.31           C  
ANISOU 1983  CG1 VAL A 300     5728   4404   4803   -549    -20   -128       C  
ATOM   1984  CG2 VAL A 300      -3.279  12.827 -61.631  1.00 33.58           C  
ANISOU 1984  CG2 VAL A 300     5050   3614   4093   -457   -169    -17       C  
ATOM   1985  N   ILE A 301      -5.619   9.130 -63.086  1.00 43.78           N  
ANISOU 1985  N   ILE A 301     6243   5130   5261   -567   -195   -228       N  
ATOM   1986  CA  ILE A 301      -5.890   7.804 -63.639  1.00 45.80           C  
ANISOU 1986  CA  ILE A 301     6515   5421   5467   -648   -163   -309       C  
ATOM   1987  C   ILE A 301      -6.571   7.854 -65.005  1.00 48.56           C  
ANISOU 1987  C   ILE A 301     6922   5855   5672   -698   -232   -314       C  
ATOM   1988  O   ILE A 301      -6.157   7.169 -65.949  1.00 49.22           O  
ANISOU 1988  O   ILE A 301     7088   5941   5673   -769   -177   -361       O  
ATOM   1989  CB  ILE A 301      -6.771   6.981 -62.711  1.00 42.85           C  
ANISOU 1989  CB  ILE A 301     6051   5072   5159   -662   -184   -359       C  
ATOM   1990  CG1 ILE A 301      -6.060   6.730 -61.379  1.00 44.43           C  
ANISOU 1990  CG1 ILE A 301     6203   5190   5488   -620   -108   -360       C  
ATOM   1991  CG2 ILE A 301      -7.155   5.655 -63.373  1.00 42.00           C  
ANISOU 1991  CG2 ILE A 301     5987   4988   4982   -771   -162   -445       C  
ATOM   1992  CD1 ILE A 301      -4.642   6.206 -61.516  1.00 53.90           C  
ANISOU 1992  CD1 ILE A 301     7465   6311   6705   -627     14   -376       C  
ATOM   1993  N   ILE A 302      -7.622   8.657 -65.114  1.00 46.16           N  
ANISOU 1993  N   ILE A 302     6578   5631   5331   -651   -354   -267       N  
ATOM   1994  CA  ILE A 302      -8.354   8.737 -66.364  1.00 49.60           C  
ANISOU 1994  CA  ILE A 302     7054   6170   5621   -689   -437   -264       C  
ATOM   1995  C   ILE A 302      -7.446   9.214 -67.486  1.00 51.76           C  
ANISOU 1995  C   ILE A 302     7458   6410   5798   -709   -397   -223       C  
ATOM   1996  O   ILE A 302      -7.519   8.699 -68.601  1.00 49.50           O  
ANISOU 1996  O   ILE A 302     7239   6181   5390   -788   -396   -261       O  
ATOM   1997  CB  ILE A 302      -9.571   9.661 -66.252  1.00 45.64           C  
ANISOU 1997  CB  ILE A 302     6478   5768   5094   -598   -578   -205       C  
ATOM   1998  CG1 ILE A 302     -10.513   9.118 -65.181  1.00 55.23           C  
ANISOU 1998  CG1 ILE A 302     7546   7048   6389   -592   -610   -252       C  
ATOM   1999  CG2 ILE A 302     -10.309   9.735 -67.575  1.00 49.68           C  
ANISOU 1999  CG2 ILE A 302     7025   6408   5443   -632   -673   -196       C  
ATOM   2000  CD1 ILE A 302     -11.807   9.852 -65.088  1.00 49.47           C  
ANISOU 2000  CD1 ILE A 302     6716   6456   5623   -498   -744   -210       C  
ATOM   2001  N   LYS A 303      -6.559  10.163 -67.198  1.00 49.32           N  
ANISOU 2001  N   LYS A 303     7190   6013   5535   -655   -358   -151       N  
ATOM   2002  CA  LYS A 303      -5.687  10.664 -68.261  1.00 54.07           C  
ANISOU 2002  CA  LYS A 303     7914   6595   6036   -692   -315   -103       C  
ATOM   2003  C   LYS A 303      -4.648   9.617 -68.623  1.00 50.38           C  
ANISOU 2003  C   LYS A 303     7481   6106   5554   -772   -177   -177       C  
ATOM   2004  O   LYS A 303      -4.101   9.640 -69.721  1.00 47.99           O  
ANISOU 2004  O   LYS A 303     7271   5828   5134   -825   -133   -170       O  
ATOM   2005  CB  LYS A 303      -5.004  11.981 -67.875  1.00 46.43           C  
ANISOU 2005  CB  LYS A 303     6992   5539   5111   -639   -308     -4       C  
ATOM   2006  CG  LYS A 303      -5.949  13.173 -67.894  1.00 55.80           C  
ANISOU 2006  CG  LYS A 303     8203   6732   6266   -544   -444     83       C  
ATOM   2007  CD  LYS A 303      -5.274  14.460 -68.364  1.00 72.51           C  
ANISOU 2007  CD  LYS A 303    10457   8768   8325   -540   -444    191       C  
ATOM   2008  CE  LYS A 303      -4.210  14.949 -67.402  1.00 80.75           C  
ANISOU 2008  CE  LYS A 303    11504   9696   9481   -552   -362    211       C  
ATOM   2009  NZ  LYS A 303      -2.967  14.129 -67.479  1.00 88.64           N1+
ANISOU 2009  NZ  LYS A 303    12478  10702  10498   -655   -220    158       N1+
ATOM   2010  N   ALA A 304      -4.381   8.681 -67.718  1.00 43.36           N  
ANISOU 2010  N   ALA A 304     6524   5175   4774   -772   -105   -248       N  
ATOM   2011  CA  ALA A 304      -3.485   7.587 -68.081  1.00 51.11           C  
ANISOU 2011  CA  ALA A 304     7549   6136   5735   -822     23   -326       C  
ATOM   2012  C   ALA A 304      -4.140   6.642 -69.093  1.00 56.72           C  
ANISOU 2012  C   ALA A 304     8323   6905   6324   -897      5   -408       C  
ATOM   2013  O   ALA A 304      -3.452   6.021 -69.904  1.00 58.26           O  
ANISOU 2013  O   ALA A 304     8600   7098   6437   -939     97   -462       O  
ATOM   2014  CB  ALA A 304      -3.056   6.819 -66.860  1.00 41.93           C  
ANISOU 2014  CB  ALA A 304     6315   4905   4712   -788     98   -372       C  
ATOM   2015  N   LEU A 305      -5.467   6.555 -69.050  1.00 53.57           N  
ANISOU 2015  N   LEU A 305     7882   6567   5904   -917   -114   -421       N  
ATOM   2016  CA  LEU A 305      -6.198   5.503 -69.749  1.00 50.38           C  
ANISOU 2016  CA  LEU A 305     7521   6220   5403  -1013   -137   -516       C  
ATOM   2017  C   LEU A 305      -6.790   5.941 -71.069  1.00 63.43           C  
ANISOU 2017  C   LEU A 305     9233   7985   6883  -1059   -228   -495       C  
ATOM   2018  O   LEU A 305      -6.800   5.174 -72.038  1.00 64.54           O  
ANISOU 2018  O   LEU A 305     9463   8158   6900  -1148   -202   -573       O  
ATOM   2019  CB  LEU A 305      -7.317   4.971 -68.866  1.00 47.11           C  
ANISOU 2019  CB  LEU A 305     7008   5831   5061  -1036   -207   -554       C  
ATOM   2020  CG  LEU A 305      -6.853   4.122 -67.691  1.00 53.95           C  
ANISOU 2020  CG  LEU A 305     7845   6586   6067  -1024   -112   -601       C  
ATOM   2021  CD1 LEU A 305      -8.011   3.883 -66.740  1.00 51.05           C  
ANISOU 2021  CD1 LEU A 305     7365   6263   5769  -1044   -191   -610       C  
ATOM   2022  CD2 LEU A 305      -6.294   2.797 -68.208  1.00 58.09           C  
ANISOU 2022  CD2 LEU A 305     8492   7039   6542  -1095     -3   -707       C  
ATOM   2023  N   ILE A 306      -7.320   7.159 -71.097  1.00 56.90           N  
ANISOU 2023  N   ILE A 306     8364   7217   6040   -993   -339   -392       N  
ATOM   2024  CA  ILE A 306      -7.960   7.670 -72.294  1.00 66.11           C  
ANISOU 2024  CA  ILE A 306     9581   8501   7039  -1016   -443   -352       C  
ATOM   2025  C   ILE A 306      -7.409   9.040 -72.665  1.00 73.00           C  
ANISOU 2025  C   ILE A 306    10516   9346   7874   -941   -457   -225       C  
ATOM   2026  O   ILE A 306      -6.854   9.754 -71.824  1.00 74.57           O  
ANISOU 2026  O   ILE A 306    10691   9451   8191   -866   -423   -162       O  
ATOM   2027  CB  ILE A 306      -9.489   7.759 -72.118  1.00 73.00           C  
ANISOU 2027  CB  ILE A 306    10343   9505   7888  -1006   -599   -348       C  
ATOM   2028  CG1 ILE A 306      -9.879   9.036 -71.380  1.00 71.46           C  
ANISOU 2028  CG1 ILE A 306    10072   9308   7773   -861   -683   -235       C  
ATOM   2029  CG2 ILE A 306     -10.010   6.556 -71.350  1.00 77.69           C  
ANISOU 2029  CG2 ILE A 306    10856  10103   8561  -1082   -579   -454       C  
ATOM   2030  CD1 ILE A 306     -11.366   9.154 -71.144  1.00 77.55           C  
ANISOU 2030  CD1 ILE A 306    10709  10233   8523   -825   -829   -229       C  
ATOM   2031  N   THR A 307      -7.548   9.386 -73.940  1.00 60.83           N  
ANISOU 2031  N   THR A 307     9069   7885   6160   -974   -506   -190       N  
ATOM   2032  CA  THR A 307      -7.203  10.712 -74.437  1.00 68.30           C  
ANISOU 2032  CA  THR A 307    10099   8811   7039   -917   -539    -57       C  
ATOM   2033  C   THR A 307      -8.458  11.578 -74.441  1.00 77.71           C  
ANISOU 2033  C   THR A 307    11248  10085   8194   -820   -713     27       C  
ATOM   2034  O   THR A 307      -9.462  11.221 -75.052  1.00 88.28           O  
ANISOU 2034  O   THR A 307    12554  11566   9421   -845   -817     -2       O  
ATOM   2035  CB  THR A 307      -6.600  10.653 -75.863  1.00 81.34           C  
ANISOU 2035  CB  THR A 307    11890  10509   8506  -1002   -489    -52       C  
ATOM   2036  OG1 THR A 307      -5.260  10.143 -75.803  1.00 88.31           O  
ANISOU 2036  OG1 THR A 307    12811  11314   9430  -1055   -315   -103       O  
ATOM   2037  CG2 THR A 307      -6.578  12.035 -76.488  1.00 78.94           C  
ANISOU 2037  CG2 THR A 307    11685  10205   8102   -951   -559     99       C  
ATOM   2038  N   ILE A 308      -8.398  12.713 -73.754  1.00 81.14           N  
ANISOU 2038  N   ILE A 308    11682  10434   8713   -705   -747    129       N  
ATOM   2039  CA  ILE A 308      -9.572  13.556 -73.559  1.00 91.23           C  
ANISOU 2039  CA  ILE A 308    12912  11774   9977   -572   -904    206       C  
ATOM   2040  C   ILE A 308      -9.439  14.888 -74.297  1.00 95.01           C  
ANISOU 2040  C   ILE A 308    13541  12212  10345   -498   -966    351       C  
ATOM   2041  O   ILE A 308      -8.340  15.439 -74.391  1.00 91.19           O  
ANISOU 2041  O   ILE A 308    13180  11599   9870   -533   -875    408       O  
ATOM   2042  CB  ILE A 308      -9.822  13.820 -72.055  1.00 95.66           C  
ANISOU 2042  CB  ILE A 308    13359  12263  10725   -469   -908    202       C  
ATOM   2043  CG1 ILE A 308      -8.502  14.050 -71.320  1.00 90.74           C  
ANISOU 2043  CG1 ILE A 308    12788  11464  10227   -493   -772    209       C  
ATOM   2044  CG2 ILE A 308     -10.561  12.654 -71.419  1.00 97.76           C  
ANISOU 2044  CG2 ILE A 308    13458  12626  11059   -512   -915     85       C  
ATOM   2045  CD1 ILE A 308      -8.684  14.326 -69.848  1.00 90.32           C  
ANISOU 2045  CD1 ILE A 308    12636  11339  10344   -400   -773    202       C  
ATOM   2046  N   PRO A 309     -10.564  15.412 -74.820  1.00 99.55           N  
ANISOU 2046  N   PRO A 309    14110  12907  10810   -398  -1122    417       N  
ATOM   2047  CA  PRO A 309     -10.557  16.645 -75.618  1.00103.01           C  
ANISOU 2047  CA  PRO A 309    14712  13309  11119   -316  -1196    565       C  
ATOM   2048  C   PRO A 309     -10.159  17.879 -74.815  1.00 98.81           C  
ANISOU 2048  C   PRO A 309    14268  12584  10691   -198  -1186    664       C  
ATOM   2049  O   PRO A 309     -10.701  18.115 -73.737  1.00103.01           O  
ANISOU 2049  O   PRO A 309    14699  13088  11351    -77  -1225    651       O  
ATOM   2050  CB  PRO A 309     -12.009  16.759 -76.097  1.00105.29           C  
ANISOU 2050  CB  PRO A 309    14920  13793  11291   -207  -1375    594       C  
ATOM   2051  CG  PRO A 309     -12.800  16.015 -75.083  1.00102.24           C  
ANISOU 2051  CG  PRO A 309    14316  13499  11032   -182  -1397    488       C  
ATOM   2052  CD  PRO A 309     -11.925  14.868 -74.667  1.00 99.17           C  
ANISOU 2052  CD  PRO A 309    13892  13044  10745   -355  -1240    360       C  
ATOM   2053  N   GLU A 310      -9.221  18.656 -75.344  1.00 93.79           N  
ANISOU 2053  N   GLU A 310    13825  11817   9992   -245  -1131    760       N  
ATOM   2054  CA  GLU A 310      -8.786  19.880 -74.684  1.00 95.30           C  
ANISOU 2054  CA  GLU A 310    14140  11808  10261   -163  -1121    858       C  
ATOM   2055  C   GLU A 310      -9.818  20.983 -74.807  1.00 92.29           C  
ANISOU 2055  C   GLU A 310    13836  11416   9814     46  -1281    975       C  
ATOM   2056  O   GLU A 310      -9.755  21.798 -75.724  1.00100.97           O  
ANISOU 2056  O   GLU A 310    15124  12472  10767     70  -1331   1101       O  
ATOM   2057  CB  GLU A 310      -7.464  20.363 -75.266  1.00108.91           C  
ANISOU 2057  CB  GLU A 310    16052  13407  11921   -306  -1011    928       C  
ATOM   2058  CG  GLU A 310      -6.324  19.394 -75.080  1.00122.14           C  
ANISOU 2058  CG  GLU A 310    17652  15090  13665   -486   -843    821       C  
ATOM   2059  CD  GLU A 310      -5.129  19.754 -75.932  1.00132.05           C  
ANISOU 2059  CD  GLU A 310    19068  16295  14810   -637   -740    888       C  
ATOM   2060  OE1 GLU A 310      -5.058  20.916 -76.390  1.00136.89           O  
ANISOU 2060  OE1 GLU A 310    19870  16811  15330   -615   -788   1028       O  
ATOM   2061  OE2 GLU A 310      -4.270  18.874 -76.153  1.00132.97           O  
ANISOU 2061  OE2 GLU A 310    19126  16470  14926   -775   -609    804       O  
ATOM   2062  N   THR A 311     -10.773  20.999 -73.885  1.00 85.94           N  
ANISOU 2062  N   THR A 311    12889  10655   9111    206  -1357    937       N  
ATOM   2063  CA  THR A 311     -11.734  22.088 -73.801  1.00 83.54           C  
ANISOU 2063  CA  THR A 311    12646  10330   8766    446  -1499   1042       C  
ATOM   2064  C   THR A 311     -11.357  23.020 -72.657  1.00 86.08           C  
ANISOU 2064  C   THR A 311    13059  10421   9226    539  -1462   1071       C  
ATOM   2065  O   THR A 311     -10.496  22.698 -71.833  1.00 81.44           O  
ANISOU 2065  O   THR A 311    12436   9732   8775    419  -1339    997       O  
ATOM   2066  CB  THR A 311     -13.177  21.577 -73.583  1.00 79.50           C  
ANISOU 2066  CB  THR A 311    11904  10054   8250    587  -1621    985       C  
ATOM   2067  OG1 THR A 311     -13.204  20.661 -72.476  1.00 73.68           O  
ANISOU 2067  OG1 THR A 311    10959   9360   7677    527  -1548    846       O  
ATOM   2068  CG2 THR A 311     -13.701  20.886 -74.837  1.00 75.02           C  
ANISOU 2068  CG2 THR A 311    11278   9717   7507    513  -1694    977       C  
ATOM   2069  N   THR A 312     -12.004  24.177 -72.617  1.00 83.07           N  
ANISOU 2069  N   THR A 312    12803   9958   8801    761  -1571   1178       N  
ATOM   2070  CA  THR A 312     -11.851  25.091 -71.504  1.00 77.80           C  
ANISOU 2070  CA  THR A 312    12229   9078   8255    881  -1554   1196       C  
ATOM   2071  C   THR A 312     -12.232  24.381 -70.210  1.00 81.33           C  
ANISOU 2071  C   THR A 312    12426   9607   8868    915  -1520   1059       C  
ATOM   2072  O   THR A 312     -11.509  24.447 -69.214  1.00 78.21           O  
ANISOU 2072  O   THR A 312    12043   9066   8608    847  -1423   1006       O  
ATOM   2073  CB  THR A 312     -12.713  26.343 -71.693  1.00 74.93           C  
ANISOU 2073  CB  THR A 312    12025   8639   7806   1159  -1691   1323       C  
ATOM   2074  OG1 THR A 312     -12.247  27.064 -72.840  1.00 86.65           O  
ANISOU 2074  OG1 THR A 312    13777  10011   9134   1112  -1713   1464       O  
ATOM   2075  CG2 THR A 312     -12.643  27.240 -70.465  1.00 66.95           C  
ANISOU 2075  CG2 THR A 312    11111   7407   6920   1298  -1673   1320       C  
ATOM   2076  N   PHE A 313     -13.359  23.677 -70.246  1.00 83.00           N  
ANISOU 2076  N   PHE A 313    12409  10068   9060   1004  -1601   1003       N  
ATOM   2077  CA  PHE A 313     -13.854  22.975 -69.073  1.00 84.45           C  
ANISOU 2077  CA  PHE A 313    12348  10356   9382   1036  -1576    881       C  
ATOM   2078  C   PHE A 313     -12.851  21.929 -68.584  1.00 77.29           C  
ANISOU 2078  C   PHE A 313    11357   9421   8588    789  -1428    771       C  
ATOM   2079  O   PHE A 313     -12.690  21.744 -67.385  1.00 74.81           O  
ANISOU 2079  O   PHE A 313    10954   9055   8416    791  -1366    698       O  
ATOM   2080  CB  PHE A 313     -15.203  22.315 -69.363  1.00 83.96           C  
ANISOU 2080  CB  PHE A 313    12050  10596   9254   1126  -1686    843       C  
ATOM   2081  CG  PHE A 313     -15.836  21.695 -68.151  1.00 86.40           C  
ANISOU 2081  CG  PHE A 313    12111  11026   9690   1169  -1668    732       C  
ATOM   2082  CD1 PHE A 313     -16.558  22.473 -67.257  1.00 92.89           C  
ANISOU 2082  CD1 PHE A 313    12896  11833  10565   1416  -1720    747       C  
ATOM   2083  CD2 PHE A 313     -15.696  20.339 -67.897  1.00 80.74           C  
ANISOU 2083  CD2 PHE A 313    11213  10431   9034    966  -1593    614       C  
ATOM   2084  CE1 PHE A 313     -17.137  21.907 -66.133  1.00 95.54           C  
ANISOU 2084  CE1 PHE A 313    13000  12293  11006   1449  -1697    646       C  
ATOM   2085  CE2 PHE A 313     -16.269  19.766 -66.777  1.00 85.96           C  
ANISOU 2085  CE2 PHE A 313    11658  11199   9802    991  -1573    521       C  
ATOM   2086  CZ  PHE A 313     -16.991  20.552 -65.891  1.00 91.67           C  
ANISOU 2086  CZ  PHE A 313    12331  11927  10574   1227  -1624    537       C  
ATOM   2087  N   GLN A 314     -12.172  21.264 -69.514  1.00 68.04           N  
ANISOU 2087  N   GLN A 314    10221   8286   7347    589  -1372    761       N  
ATOM   2088  CA  GLN A 314     -11.164  20.270 -69.162  1.00 65.22           C  
ANISOU 2088  CA  GLN A 314     9799   7901   7080    375  -1230    664       C  
ATOM   2089  C   GLN A 314      -9.943  20.903 -68.497  1.00 63.31           C  
ANISOU 2089  C   GLN A 314     9696   7428   6932    313  -1126    686       C  
ATOM   2090  O   GLN A 314      -9.427  20.393 -67.501  1.00 55.13           O  
ANISOU 2090  O   GLN A 314     8564   6354   6029    245  -1036    604       O  
ATOM   2091  CB  GLN A 314     -10.733  19.487 -70.397  1.00 73.89           C  
ANISOU 2091  CB  GLN A 314    10921   9091   8061    200  -1194    650       C  
ATOM   2092  CG  GLN A 314      -9.269  19.112 -70.404  1.00 91.60           C  
ANISOU 2092  CG  GLN A 314    13234  11222  10349      8  -1040    619       C  
ATOM   2093  CD  GLN A 314      -9.025  17.811 -71.117  1.00115.31           C  
ANISOU 2093  CD  GLN A 314    16161  14355  13295   -152   -979    533       C  
ATOM   2094  OE1 GLN A 314      -9.912  16.962 -71.190  1.00125.08           O  
ANISOU 2094  OE1 GLN A 314    17257  15752  14515   -147  -1032    460       O  
ATOM   2095  NE2 GLN A 314      -7.821  17.643 -71.655  1.00122.70           N  
ANISOU 2095  NE2 GLN A 314    17196  15230  14195   -298   -865    536       N  
ATOM   2096  N   THR A 315      -9.487  22.019 -69.050  1.00 57.56           N  
ANISOU 2096  N   THR A 315     9196   6550   6126    330  -1142    800       N  
ATOM   2097  CA  THR A 315      -8.367  22.748 -68.474  1.00 55.95           C  
ANISOU 2097  CA  THR A 315     9140   6129   5991    255  -1056    830       C  
ATOM   2098  C   THR A 315      -8.692  23.291 -67.086  1.00 52.08           C  
ANISOU 2098  C   THR A 315     8622   5536   5629    394  -1072    799       C  
ATOM   2099  O   THR A 315      -7.929  23.091 -66.138  1.00 52.30           O  
ANISOU 2099  O   THR A 315     8606   5491   5776    302   -980    737       O  
ATOM   2100  CB  THR A 315      -7.946  23.902 -69.379  1.00 60.07           C  
ANISOU 2100  CB  THR A 315     9933   6504   6385    242  -1081    969       C  
ATOM   2101  OG1 THR A 315      -7.280  23.364 -70.524  1.00 67.55           O  
ANISOU 2101  OG1 THR A 315    10911   7531   7225     62  -1022    985       O  
ATOM   2102  CG2 THR A 315      -7.003  24.849 -68.645  1.00 58.65           C  
ANISOU 2102  CG2 THR A 315     9921   6088   6275    183  -1016   1003       C  
ATOM   2103  N   VAL A 316      -9.825  23.976 -66.978  1.00 46.65           N  
ANISOU 2103  N   VAL A 316     7959   4855   4911    624  -1191    843       N  
ATOM   2104  CA  VAL A 316     -10.231  24.567 -65.717  1.00 54.24           C  
ANISOU 2104  CA  VAL A 316     8909   5724   5975    784  -1211    813       C  
ATOM   2105  C   VAL A 316     -10.445  23.500 -64.647  1.00 48.42           C  
ANISOU 2105  C   VAL A 316     7910   5120   5369    756  -1159    682       C  
ATOM   2106  O   VAL A 316      -9.993  23.649 -63.515  1.00 50.46           O  
ANISOU 2106  O   VAL A 316     8159   5274   5738    740  -1098    631       O  
ATOM   2107  CB  VAL A 316     -11.511  25.393 -65.876  1.00 49.14           C  
ANISOU 2107  CB  VAL A 316     8311   5100   5258   1067  -1349    879       C  
ATOM   2108  CG1 VAL A 316     -11.953  25.917 -64.522  1.00 52.22           C  
ANISOU 2108  CG1 VAL A 316     8674   5412   5754   1243  -1358    830       C  
ATOM   2109  CG2 VAL A 316     -11.261  26.537 -66.816  1.00 52.55           C  
ANISOU 2109  CG2 VAL A 316     9040   5363   5565   1107  -1399   1020       C  
ATOM   2110  N   SER A 317     -11.110  22.412 -65.018  1.00 51.55           N  
ANISOU 2110  N   SER A 317     8103   5743   5741    735  -1184    629       N  
ATOM   2111  CA  SER A 317     -11.401  21.362 -64.062  1.00 49.77           C  
ANISOU 2111  CA  SER A 317     7641   5644   5624    701  -1139    514       C  
ATOM   2112  C   SER A 317     -10.111  20.687 -63.588  1.00 45.20           C  
ANISOU 2112  C   SER A 317     7048   4988   5138    492  -1003    453       C  
ATOM   2113  O   SER A 317     -10.005  20.287 -62.431  1.00 42.82           O  
ANISOU 2113  O   SER A 317     6634   4685   4951    483   -950    380       O  
ATOM   2114  CB  SER A 317     -12.365  20.344 -64.665  1.00 49.59           C  
ANISOU 2114  CB  SER A 317     7430   5874   5539    691  -1196    474       C  
ATOM   2115  OG  SER A 317     -11.752  19.656 -65.728  1.00 56.08           O  
ANISOU 2115  OG  SER A 317     8289   6730   6288    509  -1154    473       O  
ATOM   2116  N   TRP A 318      -9.121  20.581 -64.470  1.00 40.68           N  
ANISOU 2116  N   TRP A 318     6588   4361   4509    333   -945    488       N  
ATOM   2117  CA  TRP A 318      -7.835  19.998 -64.083  1.00 42.25           C  
ANISOU 2117  CA  TRP A 318     6768   4502   4782    152   -815    438       C  
ATOM   2118  C   TRP A 318      -7.149  20.810 -62.984  1.00 45.17           C  
ANISOU 2118  C   TRP A 318     7216   4702   5244    159   -772    444       C  
ATOM   2119  O   TRP A 318      -6.682  20.268 -61.976  1.00 36.25           O  
ANISOU 2119  O   TRP A 318     5979   3573   4222    104   -701    373       O  
ATOM   2120  CB  TRP A 318      -6.922  19.903 -65.295  1.00 44.48           C  
ANISOU 2120  CB  TRP A 318     7164   4769   4968     -1   -762    484       C  
ATOM   2121  CG  TRP A 318      -5.498  19.527 -65.010  1.00 43.40           C  
ANISOU 2121  CG  TRP A 318     7026   4576   4887   -171   -629    452       C  
ATOM   2122  CD1 TRP A 318      -4.406  20.334 -65.113  1.00 45.20           C  
ANISOU 2122  CD1 TRP A 318     7401   4676   5098   -267   -574    513       C  
ATOM   2123  CD2 TRP A 318      -5.006  18.238 -64.617  1.00 41.56           C  
ANISOU 2123  CD2 TRP A 318     6637   4427   4727   -264   -535    357       C  
ATOM   2124  NE1 TRP A 318      -3.270  19.632 -64.820  1.00 46.40           N  
ANISOU 2124  NE1 TRP A 318     7473   4853   5305   -408   -454    460       N  
ATOM   2125  CE2 TRP A 318      -3.611  18.343 -64.505  1.00 41.95           C  
ANISOU 2125  CE2 TRP A 318     6731   4410   4799   -394   -429    366       C  
ATOM   2126  CE3 TRP A 318      -5.614  17.002 -64.361  1.00 41.68           C  
ANISOU 2126  CE3 TRP A 318     6488   4566   4783   -252   -532    269       C  
ATOM   2127  CZ2 TRP A 318      -2.806  17.263 -64.128  1.00 45.74           C  
ANISOU 2127  CZ2 TRP A 318     7089   4946   5343   -481   -322    291       C  
ATOM   2128  CZ3 TRP A 318      -4.819  15.934 -63.993  1.00 39.52           C  
ANISOU 2128  CZ3 TRP A 318     6123   4319   4574   -348   -424    196       C  
ATOM   2129  CH2 TRP A 318      -3.429  16.069 -63.885  1.00 42.31           C  
ANISOU 2129  CH2 TRP A 318     6517   4608   4950   -447   -321    209       C  
ATOM   2130  N   HIS A 319      -7.082  22.118 -63.183  1.00 39.31           N  
ANISOU 2130  N   HIS A 319     6676   3809   4452    222   -819    530       N  
ATOM   2131  CA  HIS A 319      -6.414  22.955 -62.209  1.00 44.05           C  
ANISOU 2131  CA  HIS A 319     7379   4234   5122    207   -782    532       C  
ATOM   2132  C   HIS A 319      -7.218  23.049 -60.918  1.00 44.02           C  
ANISOU 2132  C   HIS A 319     7277   4238   5211    369   -818    469       C  
ATOM   2133  O   HIS A 319      -6.639  23.135 -59.834  1.00 44.73           O  
ANISOU 2133  O   HIS A 319     7349   4255   5390    322   -762    421       O  
ATOM   2134  CB  HIS A 319      -6.138  24.330 -62.810  1.00 36.04           C  
ANISOU 2134  CB  HIS A 319     6641   3035   4019    218   -821    643       C  
ATOM   2135  CG  HIS A 319      -5.073  24.286 -63.853  1.00 47.18           C  
ANISOU 2135  CG  HIS A 319     8150   4427   5348     16   -756    700       C  
ATOM   2136  ND1 HIS A 319      -3.751  24.051 -63.543  1.00 43.99           N  
ANISOU 2136  ND1 HIS A 319     7729   3998   4989   -188   -644    673       N  
ATOM   2137  CD2 HIS A 319      -5.139  24.357 -65.204  1.00 43.60           C  
ANISOU 2137  CD2 HIS A 319     7791   4012   4765    -16   -783    778       C  
ATOM   2138  CE1 HIS A 319      -3.041  24.022 -64.658  1.00 51.13           C  
ANISOU 2138  CE1 HIS A 319     8712   4922   5795   -334   -599    732       C  
ATOM   2139  NE2 HIS A 319      -3.859  24.204 -65.679  1.00 47.40           N  
ANISOU 2139  NE2 HIS A 319     8316   4481   5214   -238   -680    796       N  
ATOM   2140  N   PHE A 320      -8.545  22.999 -61.032  1.00 43.19           N  
ANISOU 2140  N   PHE A 320     7092   4241   5076    554   -909    468       N  
ATOM   2141  CA  PHE A 320      -9.386  22.988 -59.847  1.00 46.59           C  
ANISOU 2141  CA  PHE A 320     7398   4719   5583    711   -936    403       C  
ATOM   2142  C   PHE A 320      -9.143  21.721 -59.026  1.00 47.79           C  
ANISOU 2142  C   PHE A 320     7331   4993   5835    600   -857    304       C  
ATOM   2143  O   PHE A 320      -9.022  21.786 -57.800  1.00 46.78           O  
ANISOU 2143  O   PHE A 320     7156   4825   5792    625   -822    250       O  
ATOM   2144  CB  PHE A 320     -10.869  23.111 -60.212  1.00 46.07           C  
ANISOU 2144  CB  PHE A 320     7258   4793   5454    925  -1047    422       C  
ATOM   2145  CG  PHE A 320     -11.758  23.324 -59.019  1.00 68.59           C  
ANISOU 2145  CG  PHE A 320    10003   7691   8368   1112  -1074    366       C  
ATOM   2146  CD1 PHE A 320     -11.985  24.601 -58.528  1.00 74.46           C  
ANISOU 2146  CD1 PHE A 320    10914   8274   9105   1295  -1114    395       C  
ATOM   2147  CD2 PHE A 320     -12.342  22.249 -58.366  1.00 72.60           C  
ANISOU 2147  CD2 PHE A 320    10255   8396   8933   1100  -1053    281       C  
ATOM   2148  CE1 PHE A 320     -12.787  24.800 -57.416  1.00 74.83           C  
ANISOU 2148  CE1 PHE A 320    10862   8371   9200   1477  -1130    334       C  
ATOM   2149  CE2 PHE A 320     -13.148  22.449 -57.256  1.00 74.23           C  
ANISOU 2149  CE2 PHE A 320    10355   8662   9186   1266  -1069    229       C  
ATOM   2150  CZ  PHE A 320     -13.367  23.724 -56.781  1.00 71.46           C  
ANISOU 2150  CZ  PHE A 320    10161   8165   8827   1461  -1106    253       C  
ATOM   2151  N   CYS A 321      -9.053  20.575 -59.699  1.00 40.20           N  
ANISOU 2151  N   CYS A 321     6253   4167   4854    479   -827    282       N  
ATOM   2152  CA  CYS A 321      -8.770  19.323 -59.002  1.00 39.17           C  
ANISOU 2152  CA  CYS A 321     5946   4130   4808    372   -749    197       C  
ATOM   2153  C   CYS A 321      -7.400  19.351 -58.343  1.00 38.16           C  
ANISOU 2153  C   CYS A 321     5866   3881   4751    244   -652    181       C  
ATOM   2154  O   CYS A 321      -7.235  18.879 -57.213  1.00 37.94           O  
ANISOU 2154  O   CYS A 321     5732   3872   4812    230   -605    121       O  
ATOM   2155  CB  CYS A 321      -8.873  18.137 -59.959  1.00 40.80           C  
ANISOU 2155  CB  CYS A 321     6063   4474   4966    264   -734    176       C  
ATOM   2156  SG  CYS A 321     -10.594  17.831 -60.470  1.00 47.43           S  
ANISOU 2156  SG  CYS A 321     6774   5517   5730    388   -850    170       S  
ATOM   2157  N   ILE A 322      -6.415  19.902 -59.049  1.00 35.15           N  
ANISOU 2157  N   ILE A 322     5639   3392   4322    144   -622    238       N  
ATOM   2158  CA  ILE A 322      -5.100  20.105 -58.455  1.00 36.73           C  
ANISOU 2158  CA  ILE A 322     5886   3494   4575     18   -540    231       C  
ATOM   2159  C   ILE A 322      -5.228  20.957 -57.183  1.00 40.98           C  
ANISOU 2159  C   ILE A 322     6467   3929   5175    104   -561    212       C  
ATOM   2160  O   ILE A 322      -4.674  20.633 -56.125  1.00 36.74           O  
ANISOU 2160  O   ILE A 322     5850   3393   4716     52   -506    160       O  
ATOM   2161  CB  ILE A 322      -4.135  20.792 -59.445  1.00 42.37           C  
ANISOU 2161  CB  ILE A 322     6776   4113   5211   -102   -514    307       C  
ATOM   2162  CG1 ILE A 322      -3.740  19.827 -60.563  1.00 41.30           C  
ANISOU 2162  CG1 ILE A 322     6585   4088   5018   -211   -464    308       C  
ATOM   2163  CG2 ILE A 322      -2.887  21.287 -58.729  1.00 41.64           C  
ANISOU 2163  CG2 ILE A 322     6739   3919   5162   -226   -447    306       C  
ATOM   2164  CD1 ILE A 322      -2.926  20.484 -61.649  1.00 43.94           C  
ANISOU 2164  CD1 ILE A 322     7085   4357   5255   -325   -440    389       C  
ATOM   2165  N   ALA A 323      -5.975  22.051 -57.300  1.00 42.41           N  
ANISOU 2165  N   ALA A 323     6783   4021   5311    246   -643    254       N  
ATOM   2166  CA  ALA A 323      -6.126  22.974 -56.194  1.00 41.20           C  
ANISOU 2166  CA  ALA A 323     6709   3747   5197    342   -664    233       C  
ATOM   2167  C   ALA A 323      -6.817  22.301 -55.007  1.00 45.64           C  
ANISOU 2167  C   ALA A 323     7076   4425   5838    435   -659    148       C  
ATOM   2168  O   ALA A 323      -6.434  22.536 -53.868  1.00 40.80           O  
ANISOU 2168  O   ALA A 323     6464   3756   5284    423   -627    102       O  
ATOM   2169  CB  ALA A 323      -6.895  24.235 -56.637  1.00 37.91           C  
ANISOU 2169  CB  ALA A 323     6487   3209   4707    512   -755    296       C  
ATOM   2170  N   LEU A 324      -7.812  21.458 -55.274  1.00 42.77           N  
ANISOU 2170  N   LEU A 324     6550   4233   5470    511   -688    128       N  
ATOM   2171  CA  LEU A 324      -8.512  20.744 -54.202  1.00 44.02           C  
ANISOU 2171  CA  LEU A 324     6515   4519   5691    579   -677     54       C  
ATOM   2172  C   LEU A 324      -7.558  19.914 -53.372  1.00 37.12           C  
ANISOU 2172  C   LEU A 324     5549   3660   4894    431   -587      5       C  
ATOM   2173  O   LEU A 324      -7.670  19.872 -52.143  1.00 38.62           O  
ANISOU 2173  O   LEU A 324     5672   3863   5140    471   -568    -47       O  
ATOM   2174  CB  LEU A 324      -9.605  19.841 -54.768  1.00 39.97           C  
ANISOU 2174  CB  LEU A 324     5839   4201   5147    626   -716     44       C  
ATOM   2175  CG  LEU A 324     -10.936  20.547 -54.961  1.00 41.99           C  
ANISOU 2175  CG  LEU A 324     6093   4515   5346    840   -812     65       C  
ATOM   2176  CD1 LEU A 324     -11.933  19.583 -55.586  1.00 46.22           C  
ANISOU 2176  CD1 LEU A 324     6450   5271   5841    843   -851     53       C  
ATOM   2177  CD2 LEU A 324     -11.449  21.062 -53.613  1.00 43.42           C  
ANISOU 2177  CD2 LEU A 324     6237   4687   5573    988   -815     16       C  
ATOM   2178  N   GLY A 325      -6.614  19.261 -54.043  1.00 41.09           N  
ANISOU 2178  N   GLY A 325     6050   4170   5394    271   -532     21       N  
ATOM   2179  CA  GLY A 325      -5.563  18.527 -53.363  1.00 41.51           C  
ANISOU 2179  CA  GLY A 325     6028   4233   5510    142   -447    -13       C  
ATOM   2180  C   GLY A 325      -4.828  19.372 -52.328  1.00 40.99           C  
ANISOU 2180  C   GLY A 325     6040   4056   5479    122   -429    -25       C  
ATOM   2181  O   GLY A 325      -4.588  18.931 -51.201  1.00 38.91           O  
ANISOU 2181  O   GLY A 325     5680   3830   5274    107   -393    -71       O  
ATOM   2182  N   TYR A 326      -4.479  20.601 -52.698  1.00 38.41           N  
ANISOU 2182  N   TYR A 326     5898   3588   5107    114   -458     19       N  
ATOM   2183  CA  TYR A 326      -3.705  21.448 -51.805  1.00 37.83           C  
ANISOU 2183  CA  TYR A 326     5923   3397   5053     61   -443      5       C  
ATOM   2184  C   TYR A 326      -4.587  22.080 -50.733  1.00 40.36           C  
ANISOU 2184  C   TYR A 326     6267   3675   5391    220   -487    -41       C  
ATOM   2185  O   TYR A 326      -4.077  22.539 -49.710  1.00 42.33           O  
ANISOU 2185  O   TYR A 326     6559   3860   5666    185   -471    -78       O  
ATOM   2186  CB  TYR A 326      -2.940  22.523 -52.604  1.00 35.31           C  
ANISOU 2186  CB  TYR A 326     5816   2929   4671    -39   -450     69       C  
ATOM   2187  CG  TYR A 326      -1.827  21.883 -53.404  1.00 39.13           C  
ANISOU 2187  CG  TYR A 326     6251   3477   5138   -218   -383    101       C  
ATOM   2188  CD1 TYR A 326      -0.591  21.602 -52.823  1.00 35.54           C  
ANISOU 2188  CD1 TYR A 326     5730   3056   4716   -369   -315     80       C  
ATOM   2189  CD2 TYR A 326      -2.029  21.506 -54.718  1.00 34.63           C  
ANISOU 2189  CD2 TYR A 326     5687   2955   4514   -226   -385    147       C  
ATOM   2190  CE1 TYR A 326       0.413  20.977 -53.555  1.00 41.08           C  
ANISOU 2190  CE1 TYR A 326     6370   3841   5399   -509   -247    106       C  
ATOM   2191  CE2 TYR A 326      -1.037  20.899 -55.454  1.00 34.11           C  
ANISOU 2191  CE2 TYR A 326     5576   2958   4426   -374   -315    168       C  
ATOM   2192  CZ  TYR A 326       0.174  20.628 -54.881  1.00 38.05           C  
ANISOU 2192  CZ  TYR A 326     6004   3493   4961   -508   -244    148       C  
ATOM   2193  OH  TYR A 326       1.145  20.003 -55.640  1.00 36.99           O  
ANISOU 2193  OH  TYR A 326     5811   3446   4797   -632   -169    166       O  
ATOM   2194  N  ATHR A 327      -5.897  22.075 -50.973  0.62 34.72           N  
ANISOU 2194  N  ATHR A 327     5517   3017   4658    394   -543    -42       N  
ATOM   2195  N  BTHR A 327      -5.902  22.100 -50.952  0.38 36.29           N  
ANISOU 2195  N  BTHR A 327     5718   3213   4857    396   -543    -42       N  
ATOM   2196  CA ATHR A 327      -6.873  22.613 -50.028  0.62 41.30           C  
ANISOU 2196  CA ATHR A 327     6350   3843   5500    576   -581    -88       C  
ATOM   2197  CA BTHR A 327      -6.816  22.656 -49.953  0.38 41.19           C  
ANISOU 2197  CA BTHR A 327     6342   3821   5487    572   -579    -90       C  
ATOM   2198  C  ATHR A 327      -6.942  21.731 -48.782  0.62 38.90           C  
ANISOU 2198  C  ATHR A 327     5859   3664   5258    563   -534   -157       C  
ATOM   2199  C  BTHR A 327      -6.930  21.732 -48.751  0.38 39.20           C  
ANISOU 2199  C  BTHR A 327     5897   3702   5297    563   -533   -159       C  
ATOM   2200  O  ATHR A 327      -7.264  22.197 -47.687  0.62 40.57           O  
ANISOU 2200  O  ATHR A 327     6081   3852   5481    655   -538   -209       O  
ATOM   2201  O  BTHR A 327      -7.314  22.162 -47.663  0.38 40.34           O  
ANISOU 2201  O  BTHR A 327     6043   3830   5452    660   -538   -211       O  
ATOM   2202  CB ATHR A 327      -8.268  22.730 -50.677  0.62 38.22           C  
ANISOU 2202  CB ATHR A 327     5930   3529   5064    768   -651    -66       C  
ATOM   2203  CB BTHR A 327      -8.226  22.896 -50.508  0.38 39.23           C  
ANISOU 2203  CB BTHR A 327     6079   3633   5194    777   -651    -71       C  
ATOM   2204  OG1ATHR A 327      -8.187  23.581 -51.831  0.62 40.41           O  
ANISOU 2204  OG1ATHR A 327     6398   3684   5273    788   -699     10       O  
ATOM   2205  OG1BTHR A 327      -8.797  21.647 -50.912  0.38 41.61           O  
ANISOU 2205  OG1BTHR A 327     6172   4133   5505    759   -644    -76       O  
ATOM   2206  CG2ATHR A 327      -9.284  23.311 -49.706  0.62 33.41           C  
ANISOU 2206  CG2ATHR A 327     5308   2932   4455    979   -684   -116       C  
ATOM   2207  CG2BTHR A 327      -8.188  23.857 -51.688  0.38 40.81           C  
ANISOU 2207  CG2BTHR A 327     6488   3697   5321    810   -704      7       C  
ATOM   2208  N   ASN A 328      -6.609  20.460 -48.952  1.00 39.06           N  
ANISOU 2208  N   ASN A 328     5723   3807   5311    450   -487   -158       N  
ATOM   2209  CA  ASN A 328      -6.525  19.538 -47.832  1.00 33.76           C  
ANISOU 2209  CA  ASN A 328     4892   3241   4693    416   -438   -209       C  
ATOM   2210  C   ASN A 328      -5.497  20.057 -46.827  1.00 42.36           C  
ANISOU 2210  C   ASN A 328     6051   4241   5804    341   -408   -235       C  
ATOM   2211  O   ASN A 328      -5.713  20.007 -45.615  1.00 39.30           O  
ANISOU 2211  O   ASN A 328     5604   3891   5436    386   -396   -285       O  
ATOM   2212  CB  ASN A 328      -6.153  18.125 -48.299  1.00 34.06           C  
ANISOU 2212  CB  ASN A 328     4799   3386   4756    298   -389   -196       C  
ATOM   2213  CG  ASN A 328      -6.400  17.082 -47.218  1.00 41.97           C  
ANISOU 2213  CG  ASN A 328     5641   4504   5803    294   -349   -238       C  
ATOM   2214  OD1 ASN A 328      -5.469  16.447 -46.708  1.00 40.50           O  
ANISOU 2214  OD1 ASN A 328     5411   4328   5651    195   -294   -243       O  
ATOM   2215  ND2 ASN A 328      -7.663  16.919 -46.850  1.00 33.91           N  
ANISOU 2215  ND2 ASN A 328     4530   3581   4774    403   -375   -265       N  
ATOM   2216  N   SER A 329      -4.388  20.580 -47.340  1.00 41.76           N  
ANISOU 2216  N   SER A 329     6098   4057   5711    216   -398   -200       N  
ATOM   2217  CA  SER A 329      -3.359  21.183 -46.499  1.00 44.52           C  
ANISOU 2217  CA  SER A 329     6523   4326   6065    118   -378   -223       C  
ATOM   2218  C   SER A 329      -3.835  22.472 -45.851  1.00 49.78           C  
ANISOU 2218  C   SER A 329     7348   4862   6703    222   -423   -259       C  
ATOM   2219  O   SER A 329      -3.356  22.838 -44.780  1.00 46.74           O  
ANISOU 2219  O   SER A 329     6994   4443   6322    179   -412   -307       O  
ATOM   2220  CB  SER A 329      -2.090  21.460 -47.307  1.00 42.38           C  
ANISOU 2220  CB  SER A 329     6339   3991   5771    -57   -355   -174       C  
ATOM   2221  OG  SER A 329      -1.537  20.247 -47.758  1.00 42.92           O  
ANISOU 2221  OG  SER A 329     6259   4184   5864   -141   -303   -153       O  
ATOM   2222  N   CYS A 330      -4.762  23.161 -46.514  1.00 41.55           N  
ANISOU 2222  N   CYS A 330     6416   3747   5624    363   -474   -238       N  
ATOM   2223  CA  CYS A 330      -5.389  24.350 -45.957  1.00 45.13           C  
ANISOU 2223  CA  CYS A 330     7030   4073   6046    512   -517   -275       C  
ATOM   2224  C   CYS A 330      -6.346  24.029 -44.816  1.00 50.81           C  
ANISOU 2224  C   CYS A 330     7616   4907   6784    667   -513   -346       C  
ATOM   2225  O   CYS A 330      -6.469  24.807 -43.882  1.00 42.32           O  
ANISOU 2225  O   CYS A 330     6641   3748   5692    739   -519   -404       O  
ATOM   2226  CB  CYS A 330      -6.158  25.120 -47.032  1.00 45.30           C  
ANISOU 2226  CB  CYS A 330     7197   3998   6016    651   -576   -222       C  
ATOM   2227  SG  CYS A 330      -5.129  25.838 -48.303  1.00 47.56           S  
ANISOU 2227  SG  CYS A 330     7706   4111   6255    484   -585   -134       S  
ATOM   2228  N   LEU A 331      -7.042  22.899 -44.909  1.00 43.49           N  
ANISOU 2228  N   LEU A 331     6472   4168   5883    712   -499   -343       N  
ATOM   2229  CA  LEU A 331      -8.073  22.567 -43.931  1.00 44.22           C  
ANISOU 2229  CA  LEU A 331     6425   4394   5982    856   -493   -401       C  
ATOM   2230  C   LEU A 331      -7.531  21.773 -42.746  1.00 43.79           C  
ANISOU 2230  C   LEU A 331     6243   4432   5965    750   -437   -444       C  
ATOM   2231  O   LEU A 331      -8.073  21.852 -41.654  1.00 43.40           O  
ANISOU 2231  O   LEU A 331     6142   4441   5906    844   -425   -503       O  
ATOM   2232  CB  LEU A 331      -9.208  21.792 -44.608  1.00 40.63           C  
ANISOU 2232  CB  LEU A 331     5804   4108   5524    948   -511   -376       C  
ATOM   2233  CG  LEU A 331      -9.961  22.629 -45.642  1.00 46.57           C  
ANISOU 2233  CG  LEU A 331     6667   4802   6226   1100   -579   -336       C  
ATOM   2234  CD1 LEU A 331     -10.953  21.777 -46.406  1.00 45.47           C  
ANISOU 2234  CD1 LEU A 331     6349   4853   6076   1149   -602   -309       C  
ATOM   2235  CD2 LEU A 331     -10.668  23.812 -44.986  1.00 49.87           C  
ANISOU 2235  CD2 LEU A 331     7200   5142   6607   1318   -610   -381       C  
ATOM   2236  N   ASN A 332      -6.464  21.011 -42.965  1.00 34.33           N  
ANISOU 2236  N   ASN A 332     4992   3253   4798    567   -401   -412       N  
ATOM   2237  CA  ASN A 332      -5.842  20.245 -41.890  1.00 43.25           C  
ANISOU 2237  CA  ASN A 332     6009   4467   5956    471   -353   -438       C  
ATOM   2238  C   ASN A 332      -5.488  21.033 -40.618  1.00 44.41           C  
ANISOU 2238  C   ASN A 332     6239   4553   6080    477   -353   -501       C  
ATOM   2239  O   ASN A 332      -5.641  20.487 -39.539  1.00 43.89           O  
ANISOU 2239  O   ASN A 332     6064   4594   6020    488   -325   -536       O  
ATOM   2240  CB  ASN A 332      -4.590  19.540 -42.407  1.00 35.54           C  
ANISOU 2240  CB  ASN A 332     4998   3497   5007    292   -321   -391       C  
ATOM   2241  CG  ASN A 332      -4.922  18.282 -43.189  1.00 39.37           C  
ANISOU 2241  CG  ASN A 332     5350   4092   5518    275   -298   -352       C  
ATOM   2242  OD1 ASN A 332      -6.052  17.801 -43.158  1.00 43.56           O  
ANISOU 2242  OD1 ASN A 332     5787   4715   6048    368   -305   -362       O  
ATOM   2243  ND2 ASN A 332      -3.940  17.747 -43.890  1.00 36.63           N  
ANISOU 2243  ND2 ASN A 332     4991   3740   5185    152   -270   -310       N  
ATOM   2244  N   PRO A 333      -5.013  22.299 -40.734  1.00 42.16           N  
ANISOU 2244  N   PRO A 333     6160   4094   5763    458   -382   -514       N  
ATOM   2245  CA  PRO A 333      -4.802  23.082 -39.512  1.00 48.90           C  
ANISOU 2245  CA  PRO A 333     7112   4885   6584    468   -385   -588       C  
ATOM   2246  C   PRO A 333      -6.077  23.257 -38.718  1.00 50.93           C  
ANISOU 2246  C   PRO A 333     7332   5200   6818    672   -386   -651       C  
ATOM   2247  O   PRO A 333      -6.030  23.318 -37.494  1.00 55.37           O  
ANISOU 2247  O   PRO A 333     7877   5803   7359    681   -368   -714       O  
ATOM   2248  CB  PRO A 333      -4.325  24.447 -40.027  1.00 51.07           C  
ANISOU 2248  CB  PRO A 333     7646   4938   6820    429   -421   -587       C  
ATOM   2249  CG  PRO A 333      -3.773  24.185 -41.336  1.00 43.63           C  
ANISOU 2249  CG  PRO A 333     6707   3973   5896    319   -423   -504       C  
ATOM   2250  CD  PRO A 333      -4.529  23.027 -41.921  1.00 40.83           C  
ANISOU 2250  CD  PRO A 333     6157   3778   5579    396   -410   -464       C  
ATOM   2251  N   VAL A 334      -7.209  23.348 -39.408  1.00 45.57           N  
ANISOU 2251  N   VAL A 334     6635   4544   6134    838   -408   -633       N  
ATOM   2252  CA  VAL A 334      -8.469  23.509 -38.712  1.00 40.03           C  
ANISOU 2252  CA  VAL A 334     5874   3931   5404   1045   -406   -690       C  
ATOM   2253  C   VAL A 334      -8.874  22.199 -38.067  1.00 49.19           C  
ANISOU 2253  C   VAL A 334     6785   5319   6587   1021   -360   -693       C  
ATOM   2254  O   VAL A 334      -9.162  22.148 -36.868  1.00 47.01           O  
ANISOU 2254  O   VAL A 334     6455   5122   6285   1070   -331   -754       O  
ATOM   2255  CB  VAL A 334      -9.590  23.975 -39.632  1.00 48.22           C  
ANISOU 2255  CB  VAL A 334     6940   4959   6421   1241   -447   -666       C  
ATOM   2256  CG1 VAL A 334     -10.880  24.097 -38.831  1.00 50.98           C  
ANISOU 2256  CG1 VAL A 334     7194   5440   6735   1462   -437   -730       C  
ATOM   2257  CG2 VAL A 334      -9.235  25.319 -40.251  1.00 55.62           C  
ANISOU 2257  CG2 VAL A 334     8157   5648   7327   1278   -493   -655       C  
ATOM   2258  N   LEU A 335      -8.876  21.141 -38.872  1.00 40.47           N  
ANISOU 2258  N   LEU A 335     5544   4309   5522    938   -353   -627       N  
ATOM   2259  CA  LEU A 335      -9.338  19.828 -38.435  1.00 43.56           C  
ANISOU 2259  CA  LEU A 335     5719   4901   5932    904   -311   -618       C  
ATOM   2260  C   LEU A 335      -8.486  19.234 -37.322  1.00 46.11           C  
ANISOU 2260  C   LEU A 335     5994   5262   6265    778   -267   -632       C  
ATOM   2261  O   LEU A 335      -9.009  18.619 -36.402  1.00 41.78           O  
ANISOU 2261  O   LEU A 335     5320   4854   5702    802   -232   -654       O  
ATOM   2262  CB  LEU A 335      -9.370  18.854 -39.618  1.00 41.84           C  
ANISOU 2262  CB  LEU A 335     5409   4738   5749    820   -313   -548       C  
ATOM   2263  CG  LEU A 335     -10.304  19.201 -40.784  1.00 50.92           C  
ANISOU 2263  CG  LEU A 335     6567   5900   6882    933   -361   -524       C  
ATOM   2264  CD1 LEU A 335     -10.237  18.134 -41.870  1.00 48.32           C  
ANISOU 2264  CD1 LEU A 335     6152   5631   6578    819   -359   -465       C  
ATOM   2265  CD2 LEU A 335     -11.731  19.370 -40.296  1.00 51.16           C  
ANISOU 2265  CD2 LEU A 335     6490   6076   6873   1113   -368   -565       C  
ATOM   2266  N   TYR A 336      -7.174  19.416 -37.403  1.00 37.24           N  
ANISOU 2266  N   TYR A 336     4965   4029   5158    642   -271   -615       N  
ATOM   2267  CA  TYR A 336      -6.275  18.639 -36.559  1.00 36.14           C  
ANISOU 2267  CA  TYR A 336     4751   3952   5029    515   -236   -606       C  
ATOM   2268  C   TYR A 336      -5.512  19.471 -35.529  1.00 44.26           C  
ANISOU 2268  C   TYR A 336     5886   4914   6018    476   -244   -661       C  
ATOM   2269  O   TYR A 336      -4.929  18.923 -34.603  1.00 46.82           O  
ANISOU 2269  O   TYR A 336     6141   5315   6332    401   -222   -663       O  
ATOM   2270  CB  TYR A 336      -5.285  17.867 -37.428  1.00 39.14           C  
ANISOU 2270  CB  TYR A 336     5100   4318   5454    374   -226   -536       C  
ATOM   2271  CG  TYR A 336      -5.945  16.784 -38.242  1.00 36.91           C  
ANISOU 2271  CG  TYR A 336     4704   4118   5202    384   -208   -489       C  
ATOM   2272  CD1 TYR A 336      -6.341  15.591 -37.640  1.00 41.94           C  
ANISOU 2272  CD1 TYR A 336     5202   4886   5846    370   -169   -477       C  
ATOM   2273  CD2 TYR A 336      -6.180  16.950 -39.603  1.00 38.22           C  
ANISOU 2273  CD2 TYR A 336     4913   4229   5379    394   -233   -458       C  
ATOM   2274  CE1 TYR A 336      -6.946  14.593 -38.364  1.00 40.01           C  
ANISOU 2274  CE1 TYR A 336     4872   4708   5623    355   -153   -441       C  
ATOM   2275  CE2 TYR A 336      -6.793  15.950 -40.350  1.00 35.35           C  
ANISOU 2275  CE2 TYR A 336     4452   3947   5034    387   -221   -425       C  
ATOM   2276  CZ  TYR A 336      -7.165  14.774 -39.721  1.00 37.93           C  
ANISOU 2276  CZ  TYR A 336     4648   4394   5369    361   -180   -420       C  
ATOM   2277  OH  TYR A 336      -7.770  13.786 -40.431  1.00 37.37           O  
ANISOU 2277  OH  TYR A 336     4498   4392   5308    332   -169   -393       O  
ATOM   2278  N   ALA A 337      -5.510  20.787 -35.685  1.00 41.08           N  
ANISOU 2278  N   ALA A 337     5660   4363   5585    524   -279   -704       N  
ATOM   2279  CA  ALA A 337      -4.838  21.627 -34.707  1.00 41.17           C  
ANISOU 2279  CA  ALA A 337     5793   4301   5548    473   -290   -769       C  
ATOM   2280  C   ALA A 337      -5.851  22.455 -33.928  1.00 44.06           C  
ANISOU 2280  C   ALA A 337     6237   4645   5858    648   -292   -857       C  
ATOM   2281  O   ALA A 337      -6.012  22.279 -32.723  1.00 45.45           O  
ANISOU 2281  O   ALA A 337     6358   4915   5994    671   -268   -909       O  
ATOM   2282  CB  ALA A 337      -3.809  22.536 -35.388  1.00 40.32           C  
ANISOU 2282  CB  ALA A 337     5864   4020   5436    350   -324   -757       C  
ATOM   2283  N   PHE A 338      -6.534  23.360 -34.621  1.00 41.44           N  
ANISOU 2283  N   PHE A 338     6037   4191   5516    782   -319   -871       N  
ATOM   2284  CA  PHE A 338      -7.414  24.316 -33.961  1.00 49.88           C  
ANISOU 2284  CA  PHE A 338     7216   5211   6526    972   -322   -960       C  
ATOM   2285  C   PHE A 338      -8.610  23.647 -33.297  1.00 53.88           C  
ANISOU 2285  C   PHE A 338     7530   5926   7017   1122   -282   -986       C  
ATOM   2286  O   PHE A 338      -9.175  24.188 -32.356  1.00 50.09           O  
ANISOU 2286  O   PHE A 338     7091   5464   6476   1253   -265  -1072       O  
ATOM   2287  CB  PHE A 338      -7.893  25.382 -34.949  1.00 51.70           C  
ANISOU 2287  CB  PHE A 338     7632   5263   6747   1106   -363   -955       C  
ATOM   2288  CG  PHE A 338      -6.788  26.274 -35.455  1.00 65.69           C  
ANISOU 2288  CG  PHE A 338     9642   6806   8513    959   -398   -943       C  
ATOM   2289  CD1 PHE A 338      -6.055  27.053 -34.577  1.00 75.62           C  
ANISOU 2289  CD1 PHE A 338    11070   7944   9720    867   -402  -1018       C  
ATOM   2290  CD2 PHE A 338      -6.485  26.333 -36.808  1.00 70.39           C  
ANISOU 2290  CD2 PHE A 338    10290   7313   9141    897   -426   -856       C  
ATOM   2291  CE1 PHE A 338      -5.036  27.869 -35.037  1.00 79.49           C  
ANISOU 2291  CE1 PHE A 338    11777   8232  10195    702   -433  -1006       C  
ATOM   2292  CE2 PHE A 338      -5.470  27.153 -37.275  1.00 69.47           C  
ANISOU 2292  CE2 PHE A 338    10391   6997   9010    743   -452   -840       C  
ATOM   2293  CZ  PHE A 338      -4.744  27.916 -36.389  1.00 75.53           C  
ANISOU 2293  CZ  PHE A 338    11322   7648   9728    638   -455   -913       C  
ATOM   2294  N   LEU A 339      -8.992  22.471 -33.779  1.00 53.19           N  
ANISOU 2294  N   LEU A 339     7236   5997   6976   1095   -264   -915       N  
ATOM   2295  CA  LEU A 339     -10.069  21.722 -33.140  1.00 52.17           C  
ANISOU 2295  CA  LEU A 339     6909   6086   6827   1192   -221   -930       C  
ATOM   2296  C   LEU A 339      -9.557  20.631 -32.187  1.00 53.42           C  
ANISOU 2296  C   LEU A 339     6932   6379   6985   1046   -177   -914       C  
ATOM   2297  O   LEU A 339     -10.342  19.890 -31.611  1.00 58.19           O  
ANISOU 2297  O   LEU A 339     7375   7167   7569   1086   -135   -915       O  
ATOM   2298  CB  LEU A 339     -10.971  21.105 -34.200  1.00 49.51           C  
ANISOU 2298  CB  LEU A 339     6435   5853   6525   1250   -229   -869       C  
ATOM   2299  CG  LEU A 339     -11.801  22.162 -34.935  1.00 55.42           C  
ANISOU 2299  CG  LEU A 339     7283   6524   7251   1454   -271   -888       C  
ATOM   2300  CD1 LEU A 339     -12.714  21.511 -35.954  1.00 56.60           C  
ANISOU 2300  CD1 LEU A 339     7273   6810   7421   1503   -286   -828       C  
ATOM   2301  CD2 LEU A 339     -12.595  23.001 -33.951  1.00 52.33           C  
ANISOU 2301  CD2 LEU A 339     6933   6162   6788   1660   -252   -984       C  
ATOM   2302  N   ASP A 340      -8.244  20.523 -32.034  1.00 48.37           N  
ANISOU 2302  N   ASP A 340     6356   5660   6362    877   -188   -893       N  
ATOM   2303  CA  ASP A 340      -7.693  19.581 -31.070  1.00 51.66           C  
ANISOU 2303  CA  ASP A 340     6664   6197   6768    760   -155   -875       C  
ATOM   2304  C   ASP A 340      -8.003  20.072 -29.653  1.00 55.79           C  
ANISOU 2304  C   ASP A 340     7215   6777   7206    831   -132   -964       C  
ATOM   2305  O   ASP A 340      -7.890  21.262 -29.372  1.00 56.82           O  
ANISOU 2305  O   ASP A 340     7513   6785   7293    889   -155  -1043       O  
ATOM   2306  CB  ASP A 340      -6.186  19.408 -31.262  1.00 53.59           C  
ANISOU 2306  CB  ASP A 340     6957   6364   7041    579   -177   -831       C  
ATOM   2307  CG  ASP A 340      -5.542  18.603 -30.133  1.00 57.40           C  
ANISOU 2307  CG  ASP A 340     7348   6966   7495    483   -153   -816       C  
ATOM   2308  OD1 ASP A 340      -5.540  17.354 -30.214  1.00 53.45           O  
ANISOU 2308  OD1 ASP A 340     6712   6570   7027    437   -125   -742       O  
ATOM   2309  OD2 ASP A 340      -5.049  19.224 -29.165  1.00 53.74           O  
ANISOU 2309  OD2 ASP A 340     6962   6488   6969    454   -165   -877       O  
ATOM   2310  N   GLU A 341      -8.396  19.155 -28.771  1.00 55.65           N  
ANISOU 2310  N   GLU A 341     7050   6938   7158    823    -86   -952       N  
ATOM   2311  CA  GLU A 341      -8.844  19.512 -27.420  1.00 66.26           C  
ANISOU 2311  CA  GLU A 341     8398   8371   8409    900    -54  -1035       C  
ATOM   2312  C   GLU A 341      -7.821  20.339 -26.629  1.00 56.63           C  
ANISOU 2312  C   GLU A 341     7336   7049   7133    832    -82  -1102       C  
ATOM   2313  O   GLU A 341      -8.156  21.367 -26.044  1.00 58.73           O  
ANISOU 2313  O   GLU A 341     7724   7263   7329    936    -81  -1206       O  
ATOM   2314  CB  GLU A 341      -9.189  18.242 -26.636  1.00 85.92           C  
ANISOU 2314  CB  GLU A 341    10708  11066  10873    852      1   -986       C  
ATOM   2315  CG  GLU A 341     -10.457  18.337 -25.795  1.00105.54           C  
ANISOU 2315  CG  GLU A 341    13111  13711  13277    990     56  -1048       C  
ATOM   2316  CD  GLU A 341     -11.721  18.107 -26.609  1.00120.83           C  
ANISOU 2316  CD  GLU A 341    14930  15736  15245   1097     75  -1028       C  
ATOM   2317  OE1 GLU A 341     -12.442  17.127 -26.321  1.00126.29           O  
ANISOU 2317  OE1 GLU A 341    15454  16612  15917   1071    125   -985       O  
ATOM   2318  OE2 GLU A 341     -11.995  18.904 -27.532  1.00125.98           O  
ANISOU 2318  OE2 GLU A 341    15659  16278  15932   1200     37  -1051       O  
ATOM   2319  N   ASN A 342      -6.573  19.881 -26.610  1.00 47.56           N  
ANISOU 2319  N   ASN A 342     6183   5880   6007    659   -107  -1047       N  
ATOM   2320  CA  ASN A 342      -5.529  20.569 -25.859  1.00 50.17           C  
ANISOU 2320  CA  ASN A 342     6638   6146   6276    561   -140  -1104       C  
ATOM   2321  C   ASN A 342      -5.090  21.852 -26.549  1.00 58.66           C  
ANISOU 2321  C   ASN A 342     7919   7006   7363    546   -188  -1156       C  
ATOM   2322  O   ASN A 342      -5.002  22.907 -25.919  1.00 52.28           O  
ANISOU 2322  O   ASN A 342     7274   6109   6480    566   -204  -1259       O  
ATOM   2323  CB  ASN A 342      -4.333  19.640 -25.655  1.00 56.33           C  
ANISOU 2323  CB  ASN A 342     7326   7004   7073    390   -155  -1020       C  
ATOM   2324  CG  ASN A 342      -4.631  18.518 -24.669  1.00 58.83           C  
ANISOU 2324  CG  ASN A 342     7492   7515   7348    395   -112   -979       C  
ATOM   2325  OD1 ASN A 342      -4.990  18.779 -23.525  1.00 61.04           O  
ANISOU 2325  OD1 ASN A 342     7786   7873   7533    439    -93  -1046       O  
ATOM   2326  ND2 ASN A 342      -4.508  17.272 -25.116  1.00 55.01           N  
ANISOU 2326  ND2 ASN A 342     6875   7101   6926    351    -94   -868       N  
ATOM   2327  N   PHE A 343      -4.834  21.747 -27.852  1.00 57.17           N  
ANISOU 2327  N   PHE A 343     7733   6728   7259    507   -209  -1084       N  
ATOM   2328  CA  PHE A 343      -4.389  22.869 -28.674  1.00 62.07           C  
ANISOU 2328  CA  PHE A 343     8550   7139   7894    473   -253  -1109       C  
ATOM   2329  C   PHE A 343      -5.397  24.006 -28.634  1.00 66.94           C  
ANISOU 2329  C   PHE A 343     9329   7637   8469    660   -253  -1200       C  
ATOM   2330  O   PHE A 343      -5.019  25.171 -28.579  1.00 68.56           O  
ANISOU 2330  O   PHE A 343     9755   7663   8632    637   -283  -1269       O  
ATOM   2331  CB  PHE A 343      -4.165  22.410 -30.121  1.00 61.48           C  
ANISOU 2331  CB  PHE A 343     8425   7022   7911    426   -264  -1007       C  
ATOM   2332  CG  PHE A 343      -3.461  23.416 -30.987  1.00 53.57           C  
ANISOU 2332  CG  PHE A 343     7614   5821   6920    340   -306  -1008       C  
ATOM   2333  CD1 PHE A 343      -4.156  24.476 -31.558  1.00 55.18           C  
ANISOU 2333  CD1 PHE A 343     7996   5857   7114    468   -324  -1047       C  
ATOM   2334  CD2 PHE A 343      -2.108  23.291 -31.247  1.00 49.23           C  
ANISOU 2334  CD2 PHE A 343     7063   5261   6383    134   -326   -964       C  
ATOM   2335  CE1 PHE A 343      -3.506  25.405 -32.371  1.00 54.62           C  
ANISOU 2335  CE1 PHE A 343     8121   5587   7044    376   -361  -1038       C  
ATOM   2336  CE2 PHE A 343      -1.455  24.205 -32.050  1.00 50.57           C  
ANISOU 2336  CE2 PHE A 343     7404   5258   6553     31   -359   -960       C  
ATOM   2337  CZ  PHE A 343      -2.153  25.263 -32.621  1.00 42.81           C  
ANISOU 2337  CZ  PHE A 343     6621   4086   5559    144   -376   -994       C  
ATOM   2338  N   LYS A 344      -6.677  23.647 -28.653  1.00 68.44           N  
ANISOU 2338  N   LYS A 344     9409   7930   8665    844   -217  -1200       N  
ATOM   2339  CA  LYS A 344      -7.766  24.613 -28.625  1.00 74.74           C  
ANISOU 2339  CA  LYS A 344    10323   8654   9421   1067   -210  -1281       C  
ATOM   2340  C   LYS A 344      -7.607  25.616 -27.491  1.00 75.20           C  
ANISOU 2340  C   LYS A 344    10564   8629   9380   1098   -208  -1408       C  
ATOM   2341  O   LYS A 344      -7.964  26.782 -27.638  1.00 85.55           O  
ANISOU 2341  O   LYS A 344    12085   9764  10654   1228   -224  -1481       O  
ATOM   2342  CB  LYS A 344      -9.113  23.893 -28.491  1.00 77.63           C  
ANISOU 2342  CB  LYS A 344    10483   9226   9788   1236   -162  -1268       C  
ATOM   2343  CG  LYS A 344     -10.298  24.626 -29.100  1.00 80.03           C  
ANISOU 2343  CG  LYS A 344    10840   9483  10084   1479   -166  -1298       C  
ATOM   2344  CD  LYS A 344     -11.593  23.831 -28.930  1.00 82.30           C  
ANISOU 2344  CD  LYS A 344    10885  10022  10364   1616   -117  -1283       C  
ATOM   2345  CE  LYS A 344     -11.540  22.491 -29.652  1.00 85.49           C  
ANISOU 2345  CE  LYS A 344    11083  10555  10845   1480   -115  -1166       C  
ATOM   2346  NZ  LYS A 344     -12.828  21.738 -29.568  1.00 87.98           N  
ANISOU 2346  NZ  LYS A 344    11168  11113  11146   1584    -71  -1149       N  
ATOM   2347  N   ARG A 345      -7.039  25.166 -26.375  1.00 79.98           N  
ANISOU 2347  N   ARG A 345    11102   9351   9934    977   -193  -1433       N  
ATOM   2348  CA  ARG A 345      -7.049  25.934 -25.127  1.00 82.48           C  
ANISOU 2348  CA  ARG A 345    11557   9643  10138   1015   -181  -1562       C  
ATOM   2349  C   ARG A 345      -6.101  27.136 -25.094  1.00 94.39           C  
ANISOU 2349  C   ARG A 345    13346  10913  11603    897   -232  -1636       C  
ATOM   2350  O   ARG A 345      -5.824  27.686 -24.031  1.00 97.46           O  
ANISOU 2350  O   ARG A 345    13857  11281  11893    863   -232  -1742       O  
ATOM   2351  CB  ARG A 345      -6.744  24.998 -23.960  1.00 79.02           C  
ANISOU 2351  CB  ARG A 345    10951   9426   9650    916   -153  -1555       C  
ATOM   2352  CG  ARG A 345      -7.901  24.066 -23.643  1.00 83.98           C  
ANISOU 2352  CG  ARG A 345    11355  10279  10276   1055    -88  -1522       C  
ATOM   2353  CD  ARG A 345      -7.438  22.744 -23.057  1.00 91.69           C  
ANISOU 2353  CD  ARG A 345    12130  11455  11252    910    -70  -1438       C  
ATOM   2354  NE  ARG A 345      -6.767  22.903 -21.772  1.00 99.17           N  
ANISOU 2354  NE  ARG A 345    13131  12455  12094    815    -75  -1501       N  
ATOM   2355  CZ  ARG A 345      -5.545  22.449 -21.509  1.00 95.58           C  
ANISOU 2355  CZ  ARG A 345    12649  12029  11636    619   -115  -1449       C  
ATOM   2356  NH1 ARG A 345      -4.859  21.808 -22.444  1.00 85.35           N  
ANISOU 2356  NH1 ARG A 345    11276  10711  10442    507   -144  -1335       N  
ATOM   2357  NH2 ARG A 345      -5.010  22.635 -20.309  1.00101.62           N  
ANISOU 2357  NH2 ARG A 345    13460  12861  12291    542   -125  -1511       N  
ATOM   2358  N   CYS A 346      -5.623  27.553 -26.261  1.00106.52           N  
ANISOU 2358  N   CYS A 346    14995  12272  13205    825   -274  -1581       N  
ATOM   2359  CA  CYS A 346      -4.860  28.789 -26.386  1.00113.34           C  
ANISOU 2359  CA  CYS A 346    16154  12883  14027    715   -320  -1645       C  
ATOM   2360  C   CYS A 346      -5.511  29.643 -27.482  1.00114.95           C  
ANISOU 2360  C   CYS A 346    16541  12871  14265    878   -334  -1636       C  
ATOM   2361  O   CYS A 346      -5.532  29.211 -28.634  1.00117.96           O  
ANISOU 2361  O   CYS A 346    16832  13254  14733    868   -346  -1525       O  
ATOM   2362  CB  CYS A 346      -3.397  28.481 -26.709  1.00112.37           C  
ANISOU 2362  CB  CYS A 346    16000  12763  13935    413   -361  -1574       C  
ATOM   2363  SG  CYS A 346      -2.778  26.971 -25.908  1.00117.40           S  
ANISOU 2363  SG  CYS A 346    16316  13713  14576    275   -346  -1508       S  
ATOM   2364  N   PHE A 347      -6.040  30.835 -27.172  1.00111.99           N  
ANISOU 2364  N   PHE A 347    16428  12305  13817   1038   -333  -1748       N  
ATOM   2365  CA  PHE A 347      -5.915  31.540 -25.886  1.00108.61           C  
ANISOU 2365  CA  PHE A 347    16172  11822  13273   1035   -322  -1896       C  
ATOM   2366  C   PHE A 347      -6.570  30.840 -24.699  1.00108.79           C  
ANISOU 2366  C   PHE A 347    15987  12106  13243   1150   -266  -1950       C  
ATOM   2367  O   PHE A 347      -6.737  31.441 -23.637  1.00112.06           O  
ANISOU 2367  O   PHE A 347    16539  12489  13549   1211   -246  -2083       O  
ATOM   2368  CB  PHE A 347      -6.522  32.951 -25.983  1.00108.42           C  
ANISOU 2368  CB  PHE A 347    16400  11582  13211   1196   -309  -1945       C  
ATOM   2369  CG  PHE A 347      -6.187  33.694 -27.254  1.00116.13           C  
ANISOU 2369  CG  PHE A 347    17530  12346  14248   1125   -346  -1845       C  
ATOM   2370  CD1 PHE A 347      -4.872  33.977 -27.589  1.00120.40           C  
ANISOU 2370  CD1 PHE A 347    18186  12766  14794    820   -389  -1813       C  
ATOM   2371  CD2 PHE A 347      -7.199  34.146 -28.094  1.00117.30           C  
ANISOU 2371  CD2 PHE A 347    17701  12434  14432   1361   -337  -1782       C  
ATOM   2372  CE1 PHE A 347      -4.572  34.673 -28.756  1.00120.94           C  
ANISOU 2372  CE1 PHE A 347    18393  12655  14905    751   -416  -1717       C  
ATOM   2373  CE2 PHE A 347      -6.905  34.842 -29.258  1.00114.43           C  
ANISOU 2373  CE2 PHE A 347    17490  11884  14107   1301   -372  -1688       C  
ATOM   2374  CZ  PHE A 347      -5.592  35.106 -29.588  1.00116.19           C  
ANISOU 2374  CZ  PHE A 347    17830  11982  14334    995   -408  -1656       C  
TER    2375      PHE A 347                                                      
ATOM   2376  N   GLN B   3     -21.182   5.496  -1.003  1.00 75.91           N  
ANISOU 2376  N   GLN B   3     7916  14411   6514   -402   1799   -261       N  
ATOM   2377  CA  GLN B   3     -21.447   5.969  -2.359  1.00 80.32           C  
ANISOU 2377  CA  GLN B   3     8383  14884   7252   -307   1765   -343       C  
ATOM   2378  C   GLN B   3     -20.455   5.421  -3.411  1.00 86.49           C  
ANISOU 2378  C   GLN B   3     9251  15452   8160   -378   1694   -246       C  
ATOM   2379  O   GLN B   3     -20.573   4.272  -3.834  1.00 96.72           O  
ANISOU 2379  O   GLN B   3    10549  16697   9503   -569   1707    -90       O  
ATOM   2380  CB  GLN B   3     -21.442   7.495  -2.375  1.00 73.61           C  
ANISOU 2380  CB  GLN B   3     7522  14034   6413    -44   1739   -558       C  
ATOM   2381  CG  GLN B   3     -20.269   8.125  -1.645  1.00 75.44           C  
ANISOU 2381  CG  GLN B   3     7923  14195   6547     46   1689   -624       C  
ATOM   2382  CD  GLN B   3     -19.985   9.512  -2.162  1.00 79.48           C  
ANISOU 2382  CD  GLN B   3     8468  14599   7130    278   1634   -819       C  
ATOM   2383  OE1 GLN B   3     -20.807  10.093  -2.875  1.00 88.77           O  
ANISOU 2383  OE1 GLN B   3     9537  15782   8408    400   1646   -911       O  
ATOM   2384  NE2 GLN B   3     -18.818  10.051  -1.820  1.00 70.13           N  
ANISOU 2384  NE2 GLN B   3     7444  13311   5891    337   1567   -880       N  
ATOM   2385  N   VAL B   4     -19.505   6.254  -3.843  1.00 84.21           N  
ANISOU 2385  N   VAL B   4     9039  15034   7925   -226   1622   -344       N  
ATOM   2386  CA  VAL B   4     -18.475   5.875  -4.815  1.00 71.87           C  
ANISOU 2386  CA  VAL B   4     7592  13170   6545   -260   1502   -262       C  
ATOM   2387  C   VAL B   4     -17.196   5.402  -4.123  1.00 70.30           C  
ANISOU 2387  C   VAL B   4     7579  12839   6292   -318   1425   -150       C  
ATOM   2388  O   VAL B   4     -16.729   6.017  -3.159  1.00 65.38           O  
ANISOU 2388  O   VAL B   4     7023  12280   5537   -239   1410   -220       O  
ATOM   2389  CB  VAL B   4     -18.140   7.056  -5.760  1.00 70.85           C  
ANISOU 2389  CB  VAL B   4     7473  12869   6577    -65   1412   -419       C  
ATOM   2390  CG1 VAL B   4     -16.764   6.888  -6.395  1.00 64.94           C  
ANISOU 2390  CG1 VAL B   4     6883  11812   5980    -75   1272   -355       C  
ATOM   2391  CG2 VAL B   4     -19.222   7.217  -6.820  1.00 65.34           C  
ANISOU 2391  CG2 VAL B   4     6608  12231   5987    -29   1452   -473       C  
ATOM   2392  N   GLN B   5     -16.637   4.304  -4.618  1.00 66.30           N  
ANISOU 2392  N   GLN B   5     7157  12154   5880   -450   1376     22       N  
ATOM   2393  CA  GLN B   5     -15.412   3.743  -4.061  1.00 68.47           C  
ANISOU 2393  CA  GLN B   5     7600  12303   6113   -491   1297    148       C  
ATOM   2394  C   GLN B   5     -14.306   3.590  -5.113  1.00 68.35           C  
ANISOU 2394  C   GLN B   5     7678  11991   6300   -456   1169    192       C  
ATOM   2395  O   GLN B   5     -14.319   2.651  -5.916  1.00 68.10           O  
ANISOU 2395  O   GLN B   5     7671  11822   6383   -553   1164    311       O  
ATOM   2396  CB  GLN B   5     -15.707   2.393  -3.418  1.00 75.68           C  
ANISOU 2396  CB  GLN B   5     8557  13294   6903   -682   1371    346       C  
ATOM   2397  CG  GLN B   5     -14.490   1.735  -2.805  1.00 84.37           C  
ANISOU 2397  CG  GLN B   5     9834  14279   7946   -708   1291    496       C  
ATOM   2398  CD  GLN B   5     -14.821   0.417  -2.146  1.00 98.31           C  
ANISOU 2398  CD  GLN B   5    11669  16107   9577   -892   1368    699       C  
ATOM   2399  OE1 GLN B   5     -15.623   0.361  -1.206  1.00102.87           O  
ANISOU 2399  OE1 GLN B   5    12192  16927   9967   -967   1476    703       O  
ATOM   2400  NE2 GLN B   5     -14.211  -0.659  -2.637  1.00 99.55           N  
ANISOU 2400  NE2 GLN B   5    11956  16043   9825   -965   1318    870       N  
ATOM   2401  N   LEU B   6     -13.351   4.514  -5.109  1.00 55.26           N  
ANISOU 2401  N   LEU B   6     6078  10242   4678   -324   1068     92       N  
ATOM   2402  CA  LEU B   6     -12.248   4.454  -6.057  1.00 55.08           C  
ANISOU 2402  CA  LEU B   6     6130   9967   4832   -287    950    125       C  
ATOM   2403  C   LEU B   6     -11.148   3.550  -5.522  1.00 60.42           C  
ANISOU 2403  C   LEU B   6     6931  10571   5455   -338    886    295       C  
ATOM   2404  O   LEU B   6     -10.628   3.753  -4.425  1.00 67.63           O  
ANISOU 2404  O   LEU B   6     7895  11588   6214   -318    860    300       O  
ATOM   2405  CB  LEU B   6     -11.703   5.856  -6.355  1.00 51.81           C  
ANISOU 2405  CB  LEU B   6     5721   9485   4480   -142    870    -55       C  
ATOM   2406  CG  LEU B   6     -12.732   6.821  -6.959  1.00 54.07           C  
ANISOU 2406  CG  LEU B   6     5904   9816   4825    -54    921   -223       C  
ATOM   2407  CD1 LEU B   6     -12.159   8.224  -7.158  1.00 55.89           C  
ANISOU 2407  CD1 LEU B   6     6180   9957   5097     83    843   -396       C  
ATOM   2408  CD2 LEU B   6     -13.256   6.260  -8.280  1.00 54.47           C  
ANISOU 2408  CD2 LEU B   6     5889   9758   5047   -100    936   -169       C  
ATOM   2409  N   VAL B   7     -10.808   2.542  -6.312  1.00 64.69           N  
ANISOU 2409  N   VAL B   7     7524  10936   6118   -397    861    433       N  
ATOM   2410  CA  VAL B   7      -9.777   1.586  -5.951  1.00 64.09           C  
ANISOU 2410  CA  VAL B   7     7572  10770   6009   -421    802    609       C  
ATOM   2411  C   VAL B   7      -8.510   1.883  -6.747  1.00 54.01           C  
ANISOU 2411  C   VAL B   7     6331   9309   4881   -323    678    591       C  
ATOM   2412  O   VAL B   7      -8.465   1.651  -7.945  1.00 46.26           O  
ANISOU 2412  O   VAL B   7     5345   8160   4072   -321    663    597       O  
ATOM   2413  CB  VAL B   7     -10.247   0.136  -6.220  1.00 70.19           C  
ANISOU 2413  CB  VAL B   7     8408  11463   6798   -553    868    788       C  
ATOM   2414  CG1 VAL B   7      -9.118  -0.852  -5.996  1.00 75.01           C  
ANISOU 2414  CG1 VAL B   7     9166  11941   7394   -540    799    971       C  
ATOM   2415  CG2 VAL B   7     -11.453  -0.201  -5.332  1.00 72.44           C  
ANISOU 2415  CG2 VAL B   7     8656  11957   6913   -677    994    820       C  
ATOM   2416  N   GLU B   8      -7.497   2.422  -6.079  1.00 49.60           N  
ANISOU 2416  N   GLU B   8     5801   8799   4245   -251    590    565       N  
ATOM   2417  CA  GLU B   8      -6.227   2.713  -6.727  1.00 57.19           C  
ANISOU 2417  CA  GLU B   8     6780   9624   5324   -171    473    553       C  
ATOM   2418  C   GLU B   8      -5.261   1.553  -6.542  1.00 60.00           C  
ANISOU 2418  C   GLU B   8     7226   9910   5663   -162    419    751       C  
ATOM   2419  O   GLU B   8      -5.170   0.984  -5.455  1.00 63.14           O  
ANISOU 2419  O   GLU B   8     7679  10416   5895   -186    428    863       O  
ATOM   2420  CB  GLU B   8      -5.625   3.999  -6.168  1.00 65.83           C  
ANISOU 2420  CB  GLU B   8     7850  10816   6345   -112    400    404       C  
ATOM   2421  CG  GLU B   8      -6.448   5.246  -6.456  1.00 69.51           C  
ANISOU 2421  CG  GLU B   8     8255  11313   6843    -86    442    199       C  
ATOM   2422  CD  GLU B   8      -6.439   6.227  -5.295  1.00 66.11           C  
ANISOU 2422  CD  GLU B   8     7832  11051   6234    -64    433     72       C  
ATOM   2423  OE1 GLU B   8      -6.341   5.769  -4.138  1.00 71.11           O  
ANISOU 2423  OE1 GLU B   8     8498  11830   6691    -97    444    152       O  
ATOM   2424  OE2 GLU B   8      -6.529   7.449  -5.535  1.00 53.04           O1-
ANISOU 2424  OE2 GLU B   8     6166   9378   4610    -14    416   -107       O1-
ATOM   2425  N   SER B   9      -4.550   1.195  -7.606  1.00 48.41           N  
ANISOU 2425  N   SER B   9     5774   8263   4356   -117    366    797       N  
ATOM   2426  CA  SER B   9      -3.574   0.117  -7.531  1.00 49.84           C  
ANISOU 2426  CA  SER B   9     6040   8365   4531    -72    313    979       C  
ATOM   2427  C   SER B   9      -2.259   0.501  -8.178  1.00 49.80           C  
ANISOU 2427  C   SER B   9     6001   8291   4630     27    202    952       C  
ATOM   2428  O   SER B   9      -2.211   1.409  -9.008  1.00 47.98           O  
ANISOU 2428  O   SER B   9     5701   8011   4519     38    181    810       O  
ATOM   2429  CB  SER B   9      -4.121  -1.137  -8.210  1.00 51.37           C  
ANISOU 2429  CB  SER B   9     6319   8392   4807   -125    386   1107       C  
ATOM   2430  OG  SER B   9      -5.464  -1.364  -7.825  1.00 64.37           O  
ANISOU 2430  OG  SER B   9     7968  10109   6379   -246    497   1105       O  
ATOM   2431  N   GLY B  10      -1.193  -0.204  -7.815  1.00 50.29           N  
ANISOU 2431  N   GLY B  10     6111   8356   4642    102    133   1096       N  
ATOM   2432  CA  GLY B  10       0.034  -0.139  -8.586  1.00 49.48           C  
ANISOU 2432  CA  GLY B  10     5970   8180   4651    198     43   1104       C  
ATOM   2433  C   GLY B  10       1.115   0.806  -8.094  1.00 59.97           C  
ANISOU 2433  C   GLY B  10     7211   9665   5910    240    -69   1030       C  
ATOM   2434  O   GLY B  10       2.158   0.935  -8.731  1.00 64.48           O  
ANISOU 2434  O   GLY B  10     7729  10206   6567    308   -143   1030       O  
ATOM   2435  N   GLY B  11       0.887   1.469  -6.968  1.00 58.89           N  
ANISOU 2435  N   GLY B  11     7057   9707   5612    192    -81    964       N  
ATOM   2436  CA  GLY B  11       1.900   2.365  -6.438  1.00 66.15           C  
ANISOU 2436  CA  GLY B  11     7904  10784   6447    206   -192    888       C  
ATOM   2437  C   GLY B  11       3.023   1.647  -5.709  1.00 63.91           C  
ANISOU 2437  C   GLY B  11     7621  10617   6044    288   -283   1050       C  
ATOM   2438  O   GLY B  11       3.209   0.441  -5.861  1.00 68.94           O  
ANISOU 2438  O   GLY B  11     8320  11171   6703    365   -269   1226       O  
ATOM   2439  N   GLY B  12       3.782   2.393  -4.916  1.00 61.54           N  
ANISOU 2439  N   GLY B  12     7259  10512   5612    274   -380    990       N  
ATOM   2440  CA  GLY B  12       4.811   1.793  -4.086  1.00 61.69           C  
ANISOU 2440  CA  GLY B  12     7263  10688   5487    352   -477   1140       C  
ATOM   2441  C   GLY B  12       6.215   2.307  -4.344  1.00 56.72           C  
ANISOU 2441  C   GLY B  12     6508  10169   4874    389   -607   1108       C  
ATOM   2442  O   GLY B  12       6.401   3.440  -4.792  1.00 53.86           O  
ANISOU 2442  O   GLY B  12     6077   9813   4573    309   -635    934       O  
ATOM   2443  N   LEU B  13       7.202   1.461  -4.067  1.00 57.63           N  
ANISOU 2443  N   LEU B  13     6595  10374   4929    511   -684   1280       N  
ATOM   2444  CA  LEU B  13       8.605   1.850  -4.162  1.00 61.24           C  
ANISOU 2444  CA  LEU B  13     6907  10996   5368    551   -815   1271       C  
ATOM   2445  C   LEU B  13       9.277   1.520  -5.488  1.00 60.09           C  
ANISOU 2445  C   LEU B  13     6690  10727   5415    644   -820   1305       C  
ATOM   2446  O   LEU B  13       9.196   0.396  -5.972  1.00 71.06           O  
ANISOU 2446  O   LEU B  13     8147  11968   6885    772   -769   1449       O  
ATOM   2447  CB  LEU B  13       9.388   1.196  -3.039  1.00 68.90           C  
ANISOU 2447  CB  LEU B  13     7857  12186   6138    649   -912   1437       C  
ATOM   2448  CG  LEU B  13       9.513   2.145  -1.862  1.00 74.32           C  
ANISOU 2448  CG  LEU B  13     8505  13115   6617    527   -988   1329       C  
ATOM   2449  CD1 LEU B  13       9.119   1.432  -0.599  1.00 75.50           C  
ANISOU 2449  CD1 LEU B  13     8758  13364   6563    563   -980   1467       C  
ATOM   2450  CD2 LEU B  13      10.936   2.678  -1.809  1.00 78.59           C  
ANISOU 2450  CD2 LEU B  13     8871  13886   7103    528  -1137   1300       C  
ATOM   2451  N   VAL B  14       9.959   2.514  -6.050  1.00 62.05           N  
ANISOU 2451  N   VAL B  14     6812  11040   5726    573   -879   1168       N  
ATOM   2452  CA  VAL B  14      10.731   2.355  -7.280  1.00 60.77           C  
ANISOU 2452  CA  VAL B  14     6555  10808   5726    646   -891   1183       C  
ATOM   2453  C   VAL B  14      12.082   3.023  -7.194  1.00 60.14           C  
ANISOU 2453  C   VAL B  14     6292  10973   5585    618  -1019   1141       C  
ATOM   2454  O   VAL B  14      12.210   4.082  -6.578  1.00 58.79           O  
ANISOU 2454  O   VAL B  14     6080  10950   5307    466  -1080   1011       O  
ATOM   2455  CB  VAL B  14      10.033   2.973  -8.503  1.00 61.82           C  
ANISOU 2455  CB  VAL B  14     6722  10715   6053    554   -803   1038       C  
ATOM   2456  CG1 VAL B  14       9.433   1.902  -9.391  1.00 67.03           C  
ANISOU 2456  CG1 VAL B  14     7480  11127   6860    660   -698   1136       C  
ATOM   2457  CG2 VAL B  14       9.044   4.029  -8.075  1.00 52.35           C  
ANISOU 2457  CG2 VAL B  14     5591   9488   4810    391   -765    869       C  
ATOM   2458  N   ARG B  15      13.080   2.435  -7.845  1.00 62.17           N  
ANISOU 2458  N   ARG B  15     6439  11275   5907    756  -1056   1242       N  
ATOM   2459  CA  ARG B  15      14.373   3.094  -7.959  1.00 66.62           C  
ANISOU 2459  CA  ARG B  15     6801  12081   6433    713  -1168   1194       C  
ATOM   2460  C   ARG B  15      14.233   4.235  -8.959  1.00 56.90           C  
ANISOU 2460  C   ARG B  15     5543  10740   5338    539  -1134   1005       C  
ATOM   2461  O   ARG B  15      13.405   4.160  -9.871  1.00 53.76           O  
ANISOU 2461  O   ARG B  15     5250  10078   5101    536  -1027    963       O  
ATOM   2462  CB  ARG B  15      15.468   2.111  -8.386  1.00 73.42           C  
ANISOU 2462  CB  ARG B  15     7539  13038   7319    933  -1208   1358       C  
ATOM   2463  CG  ARG B  15      15.766   1.018  -7.363  1.00 87.84           C  
ANISOU 2463  CG  ARG B  15     9389  14994   8993   1124  -1260   1557       C  
ATOM   2464  CD  ARG B  15      17.013   0.214  -7.740  1.00108.33           C  
ANISOU 2464  CD  ARG B  15    11838  17721  11601   1351  -1312   1698       C  
ATOM   2465  NE  ARG B  15      16.869  -0.466  -9.028  1.00123.32           N  
ANISOU 2465  NE  ARG B  15    13788  19380  13688   1487  -1214   1740       N  
ATOM   2466  CZ  ARG B  15      17.060  -1.769  -9.219  1.00133.28           C  
ANISOU 2466  CZ  ARG B  15    15126  20536  14980   1740  -1177   1910       C  
ATOM   2467  NH1 ARG B  15      17.413  -2.552  -8.206  1.00137.24           N  
ANISOU 2467  NH1 ARG B  15    15681  21099  15364   1868  -1208   2036       N  
ATOM   2468  NH2 ARG B  15      16.900  -2.293 -10.427  1.00134.74           N  
ANISOU 2468  NH2 ARG B  15    15369  20494  15334   1841  -1085   1923       N  
ATOM   2469  N   PRO B  16      15.022   5.306  -8.775  1.00 56.55           N  
ANISOU 2469  N   PRO B  16     5368  10899   5220    383  -1228    892       N  
ATOM   2470  CA  PRO B  16      15.023   6.430  -9.718  1.00 59.74           C  
ANISOU 2470  CA  PRO B  16     5754  11206   5740    208  -1206    722       C  
ATOM   2471  C   PRO B  16      15.303   5.960 -11.137  1.00 61.89           C  
ANISOU 2471  C   PRO B  16     5974  11342   6199    307  -1143    768       C  
ATOM   2472  O   PRO B  16      16.132   5.068 -11.327  1.00 62.15           O  
ANISOU 2472  O   PRO B  16     5891  11489   6233    478  -1170    908       O  
ATOM   2473  CB  PRO B  16      16.151   7.324  -9.201  1.00 52.78           C  
ANISOU 2473  CB  PRO B  16     4712  10623   4718     54  -1338    650       C  
ATOM   2474  CG  PRO B  16      16.229   7.017  -7.759  1.00 54.84           C  
ANISOU 2474  CG  PRO B  16     4975  11087   4774     88  -1414    716       C  
ATOM   2475  CD  PRO B  16      15.917   5.551  -7.635  1.00 53.30           C  
ANISOU 2475  CD  PRO B  16     4834  10818   4600    342  -1363    914       C  
ATOM   2476  N   GLY B  17      14.603   6.542 -12.108  1.00 58.75           N  
ANISOU 2476  N   GLY B  17     5669  10706   5949    213  -1060    653       N  
ATOM   2477  CA  GLY B  17      14.718   6.124 -13.492  1.00 62.55           C  
ANISOU 2477  CA  GLY B  17     6127  11034   6605    296   -989    684       C  
ATOM   2478  C   GLY B  17      13.798   4.952 -13.784  1.00 66.96           C  
ANISOU 2478  C   GLY B  17     6825  11365   7254    466   -888    788       C  
ATOM   2479  O   GLY B  17      13.653   4.540 -14.935  1.00 74.17           O  
ANISOU 2479  O   GLY B  17     7762  12107   8313    534   -814    805       O  
ATOM   2480  N   GLY B  18      13.174   4.416 -12.735  1.00 61.00           N  
ANISOU 2480  N   GLY B  18     6168  10610   6399    521   -884    855       N  
ATOM   2481  CA  GLY B  18      12.285   3.273 -12.870  1.00 49.56           C  
ANISOU 2481  CA  GLY B  18     4864   8956   5010    655   -791    961       C  
ATOM   2482  C   GLY B  18      10.892   3.649 -13.339  1.00 48.01           C  
ANISOU 2482  C   GLY B  18     4815   8514   4914    556   -691    856       C  
ATOM   2483  O   GLY B  18      10.609   4.814 -13.635  1.00 49.44           O  
ANISOU 2483  O   GLY B  18     4994   8662   5127    404   -691    701       O  
ATOM   2484  N   SER B  19      10.018   2.651 -13.416  1.00 49.05           N  
ANISOU 2484  N   SER B  19     5077   8472   5087    641   -607    944       N  
ATOM   2485  CA  SER B  19       8.662   2.846 -13.921  1.00 50.37           C  
ANISOU 2485  CA  SER B  19     5366   8423   5349    562   -509    862       C  
ATOM   2486  C   SER B  19       7.602   2.238 -13.006  1.00 44.31           C  
ANISOU 2486  C   SER B  19     4724   7614   4497    565   -456    924       C  
ATOM   2487  O   SER B  19       7.855   1.248 -12.323  1.00 52.19           O  
ANISOU 2487  O   SER B  19     5757   8663   5408    668   -469   1073       O  
ATOM   2488  CB  SER B  19       8.526   2.246 -15.320  1.00 50.41           C  
ANISOU 2488  CB  SER B  19     5406   8224   5524    627   -437    887       C  
ATOM   2489  OG  SER B  19       9.107   3.093 -16.298  1.00 67.85           O  
ANISOU 2489  OG  SER B  19     7522  10436   7823    570   -459    785       O  
ATOM   2490  N   LEU B  20       6.415   2.841 -13.005  1.00 41.44           N  
ANISOU 2490  N   LEU B  20     4427   7164   4154    455   -395    812       N  
ATOM   2491  CA  LEU B  20       5.263   2.307 -12.276  1.00 47.08           C  
ANISOU 2491  CA  LEU B  20     5250   7839   4798    437   -325    857       C  
ATOM   2492  C   LEU B  20       4.033   2.578 -13.100  1.00 43.73           C  
ANISOU 2492  C   LEU B  20     4881   7243   4493    366   -232    763       C  
ATOM   2493  O   LEU B  20       3.987   3.564 -13.817  1.00 43.34           O  
ANISOU 2493  O   LEU B  20     4790   7152   4527    310   -239    628       O  
ATOM   2494  CB  LEU B  20       5.089   2.952 -10.891  1.00 51.63           C  
ANISOU 2494  CB  LEU B  20     5821   8600   5198    370   -363    807       C  
ATOM   2495  CG  LEU B  20       6.030   2.633  -9.734  1.00 59.21           C  
ANISOU 2495  CG  LEU B  20     6742   9766   5988    424   -452    910       C  
ATOM   2496  CD1 LEU B  20       5.610   3.459  -8.534  1.00 65.89           C  
ANISOU 2496  CD1 LEU B  20     7599  10765   6670    328   -471    815       C  
ATOM   2497  CD2 LEU B  20       6.021   1.150  -9.390  1.00 51.54           C  
ANISOU 2497  CD2 LEU B  20     5852   8756   4974    539   -425   1115       C  
ATOM   2498  N   ARG B  21       3.035   1.713 -12.982  1.00 38.69           N  
ANISOU 2498  N   ARG B  21     4336   6513   3851    362   -148    836       N  
ATOM   2499  CA  ARG B  21       1.758   1.937 -13.636  1.00 44.11           C  
ANISOU 2499  CA  ARG B  21     5059   7076   4625    287    -62    750       C  
ATOM   2500  C   ARG B  21       0.680   1.984 -12.580  1.00 44.59           C  
ANISOU 2500  C   ARG B  21     5158   7223   4562    221     -8    738       C  
ATOM   2501  O   ARG B  21       0.480   1.019 -11.848  1.00 45.63           O  
ANISOU 2501  O   ARG B  21     5356   7380   4601    230     21    868       O  
ATOM   2502  CB  ARG B  21       1.452   0.839 -14.664  1.00 47.42           C  
ANISOU 2502  CB  ARG B  21     5548   7305   5166    315      1    837       C  
ATOM   2503  CG  ARG B  21       0.102   0.988 -15.370  1.00 46.85           C  
ANISOU 2503  CG  ARG B  21     5500   7126   5176    229     85    756       C  
ATOM   2504  CD  ARG B  21      -0.094  -0.077 -16.445  1.00 42.15           C  
ANISOU 2504  CD  ARG B  21     4980   6342   4694    243    137    832       C  
ATOM   2505  NE  ARG B  21       0.929   0.021 -17.482  1.00 52.60           N  
ANISOU 2505  NE  ARG B  21     6269   7589   6127    317     93    819       N  
ATOM   2506  CZ  ARG B  21       1.025  -0.791 -18.532  1.00 59.44           C  
ANISOU 2506  CZ  ARG B  21     7197   8293   7096    351    126    867       C  
ATOM   2507  NH1 ARG B  21       0.161  -1.780 -18.688  1.00 69.37           N1+
ANISOU 2507  NH1 ARG B  21     8563   9432   8362    303    198    932       N1+
ATOM   2508  NH2 ARG B  21       1.987  -0.608 -19.427  1.00 51.58           N  
ANISOU 2508  NH2 ARG B  21     6156   7257   6186    422     89    846       N  
ATOM   2509  N   LEU B  22       0.002   3.116 -12.478  1.00 39.90           N  
ANISOU 2509  N   LEU B  22     4527   6677   3955    160      8    583       N  
ATOM   2510  CA  LEU B  22      -1.135   3.200 -11.580  1.00 37.63           C  
ANISOU 2510  CA  LEU B  22     4263   6480   3555    104     75    556       C  
ATOM   2511  C   LEU B  22      -2.394   2.877 -12.348  1.00 41.94           C  
ANISOU 2511  C   LEU B  22     4824   6919   4194     59    172    538       C  
ATOM   2512  O   LEU B  22      -2.500   3.165 -13.541  1.00 40.27           O  
ANISOU 2512  O   LEU B  22     4590   6584   4126     63    175    476       O  
ATOM   2513  CB  LEU B  22      -1.259   4.590 -10.949  1.00 38.75           C  
ANISOU 2513  CB  LEU B  22     4367   6745   3613     80     48    391       C  
ATOM   2514  CG  LEU B  22       0.007   5.176 -10.337  1.00 49.59           C  
ANISOU 2514  CG  LEU B  22     5714   8228   4901     96    -60    368       C  
ATOM   2515  CD1 LEU B  22      -0.305   6.471  -9.598  1.00 44.97           C  
ANISOU 2515  CD1 LEU B  22     5127   7751   4209     57    -71    200       C  
ATOM   2516  CD2 LEU B  22       0.655   4.155  -9.406  1.00 50.61           C  
ANISOU 2516  CD2 LEU B  22     5863   8459   4906    129    -94    536       C  
ATOM   2517  N   SER B  23      -3.362   2.299 -11.658  1.00 38.97           N  
ANISOU 2517  N   SER B  23     4479   6605   3724      4    249    593       N  
ATOM   2518  CA  SER B  23      -4.667   2.149 -12.249  1.00 42.85           C  
ANISOU 2518  CA  SER B  23     4956   7049   4276    -59    340    556       C  
ATOM   2519  C   SER B  23      -5.739   2.443 -11.217  1.00 45.65           C  
ANISOU 2519  C   SER B  23     5283   7576   4488   -112    411    509       C  
ATOM   2520  O   SER B  23      -5.531   2.313 -10.007  1.00 47.69           O  
ANISOU 2520  O   SER B  23     5567   7963   4590   -117    406    559       O  
ATOM   2521  CB  SER B  23      -4.834   0.751 -12.837  1.00 43.81           C  
ANISOU 2521  CB  SER B  23     5153   7031   4461    -99    384    701       C  
ATOM   2522  OG  SER B  23      -4.872  -0.211 -11.816  1.00 47.43           O  
ANISOU 2522  OG  SER B  23     5690   7545   4788   -132    413    845       O  
ATOM   2523  N   CYS B  24      -6.886   2.882 -11.699  1.00 46.70           N  
ANISOU 2523  N   CYS B  24     5354   7725   4665   -144    476    410       N  
ATOM   2524  CA  CYS B  24      -7.977   3.224 -10.814  1.00 44.10           C  
ANISOU 2524  CA  CYS B  24     4975   7577   4204   -180    554    351       C  
ATOM   2525  C   CYS B  24      -9.279   2.791 -11.440  1.00 47.69           C  
ANISOU 2525  C   CYS B  24     5377   8035   4710   -257    646    352       C  
ATOM   2526  O   CYS B  24      -9.517   3.014 -12.627  1.00 46.07           O  
ANISOU 2526  O   CYS B  24     5136   7723   4647   -244    637    296       O  
ATOM   2527  CB  CYS B  24      -8.005   4.727 -10.539  1.00 38.50           C  
ANISOU 2527  CB  CYS B  24     4217   6951   3461   -101    526    168       C  
ATOM   2528  SG  CYS B  24      -9.458   5.282  -9.595  1.00 57.97           S  
ANISOU 2528  SG  CYS B  24     6607   9647   5772   -110    635     64       S  
ATOM   2529  N   VAL B  25     -10.130   2.169 -10.643  1.00 47.11           N  
ANISOU 2529  N   VAL B  25     5293   8097   4509   -349    733    418       N  
ATOM   2530  CA  VAL B  25     -11.400   1.708 -11.173  1.00 60.80           C  
ANISOU 2530  CA  VAL B  25     6961   9867   6273   -449    823    424       C  
ATOM   2531  C   VAL B  25     -12.547   2.089 -10.243  1.00 63.34           C  
ANISOU 2531  C   VAL B  25     7184  10440   6442   -482    917    361       C  
ATOM   2532  O   VAL B  25     -12.374   2.212  -9.027  1.00 60.87           O  
ANISOU 2532  O   VAL B  25     6896  10259   5973   -473    932    375       O  
ATOM   2533  CB  VAL B  25     -11.390   0.174 -11.393  1.00 66.55           C  
ANISOU 2533  CB  VAL B  25     7790  10480   7015   -582    854    604       C  
ATOM   2534  CG1 VAL B  25     -11.426  -0.562 -10.042  1.00 64.44           C  
ANISOU 2534  CG1 VAL B  25     7595  10325   6565   -659    902    732       C  
ATOM   2535  CG2 VAL B  25     -12.551  -0.255 -12.281  1.00 71.97           C  
ANISOU 2535  CG2 VAL B  25     8411  11164   7771   -699    923    595       C  
ATOM   2536  N   ASP B  26     -13.702   2.343 -10.843  1.00 79.26           N  
ANISOU 2536  N   ASP B  26     9078  12539   8500   -509    978    283       N  
ATOM   2537  CA  ASP B  26     -14.970   2.337 -10.126  1.00 90.51           C  
ANISOU 2537  CA  ASP B  26    10389  14216   9784   -578   1091    258       C  
ATOM   2538  C   ASP B  26     -15.829   1.291 -10.833  1.00 99.30           C  
ANISOU 2538  C   ASP B  26    11464  15321  10944   -750   1152    347       C  
ATOM   2539  O   ASP B  26     -16.434   1.558 -11.880  1.00 94.79           O  
ANISOU 2539  O   ASP B  26    10795  14738  10482   -743   1152    275       O  
ATOM   2540  CB  ASP B  26     -15.639   3.714 -10.119  1.00 79.18           C  
ANISOU 2540  CB  ASP B  26     8820  12931   8332   -434   1110     67       C  
ATOM   2541  CG  ASP B  26     -16.876   3.754  -9.245  1.00 78.33           C  
ANISOU 2541  CG  ASP B  26     8584  13120   8059   -481   1232     36       C  
ATOM   2542  OD1 ASP B  26     -16.983   2.912  -8.330  1.00 93.94           O  
ANISOU 2542  OD1 ASP B  26    10599  15194   9899   -612   1292    153       O  
ATOM   2543  OD2 ASP B  26     -17.738   4.632  -9.457  1.00 63.00           O  
ANISOU 2543  OD2 ASP B  26     6504  11320   6114   -379   1270   -103       O  
ATOM   2544  N   SER B  27     -15.838   0.088 -10.268  1.00 97.77           N  
ANISOU 2544  N   SER B  27    11362  15123  10663   -912   1200    507       N  
ATOM   2545  CA  SER B  27     -16.456  -1.071 -10.898  1.00 92.19           C  
ANISOU 2545  CA  SER B  27    10674  14359   9993  -1108   1250    613       C  
ATOM   2546  C   SER B  27     -17.969  -0.945 -10.946  1.00 86.35           C  
ANISOU 2546  C   SER B  27     9742  13876   9192  -1213   1351    550       C  
ATOM   2547  O   SER B  27     -18.634  -1.641 -11.711  1.00 85.74           O  
ANISOU 2547  O   SER B  27     9633  13778   9166  -1371   1383    591       O  
ATOM   2548  CB  SER B  27     -16.066  -2.346 -10.149  1.00 95.04           C  
ANISOU 2548  CB  SER B  27    11212  14645  10255  -1250   1278    805       C  
ATOM   2549  OG  SER B  27     -14.676  -2.370  -9.878  1.00 92.44           O  
ANISOU 2549  OG  SER B  27    11034  14142   9948  -1124   1186    861       O  
ATOM   2550  N   GLU B  28     -18.506  -0.056 -10.117  1.00 87.64           N  
ANISOU 2550  N   GLU B  28     9772  14290   9236  -1124   1401    447       N  
ATOM   2551  CA  GLU B  28     -19.948   0.129 -10.021  1.00 85.80           C  
ANISOU 2551  CA  GLU B  28     9329  14352   8920  -1197   1506    383       C  
ATOM   2552  C   GLU B  28     -20.462   1.019 -11.157  1.00 86.15           C  
ANISOU 2552  C   GLU B  28     9217  14421   9096  -1070   1470    235       C  
ATOM   2553  O   GLU B  28     -21.662   1.256 -11.276  1.00 88.50           O  
ANISOU 2553  O   GLU B  28     9314  14967   9344  -1099   1542    170       O  
ATOM   2554  CB  GLU B  28     -20.325   0.718  -8.648  1.00 69.32           C  
ANISOU 2554  CB  GLU B  28     7164  12535   6637  -1132   1584    329       C  
ATOM   2555  CG  GLU B  28     -19.838  -0.108  -7.449  1.00 77.18           C  
ANISOU 2555  CG  GLU B  28     8314  13531   7480  -1251   1618    478       C  
ATOM   2556  CD  GLU B  28     -18.428   0.271  -6.978  1.00 84.52           C  
ANISOU 2556  CD  GLU B  28     9415  14281   8420  -1095   1516    484       C  
ATOM   2557  OE1 GLU B  28     -18.258   1.383  -6.431  1.00 91.35           O  
ANISOU 2557  OE1 GLU B  28    10235  15248   9228   -920   1501    350       O  
ATOM   2558  OE2 GLU B  28     -17.492  -0.546  -7.140  1.00 75.55           O  
ANISOU 2558  OE2 GLU B  28     8458  12909   7338  -1148   1452    619       O  
ATOM   2559  N   ARG B  29     -19.548   1.503 -11.989  1.00 94.62           N  
ANISOU 2559  N   ARG B  29    10378  15246  10326   -928   1359    188       N  
ATOM   2560  CA  ARG B  29     -19.884   2.413 -13.088  1.00106.26           C  
ANISOU 2560  CA  ARG B  29    11739  16708  11926   -787   1310     56       C  
ATOM   2561  C   ARG B  29     -20.630   3.644 -12.582  1.00104.32           C  
ANISOU 2561  C   ARG B  29    11331  16712  11595   -608   1355    -98       C  
ATOM   2562  O   ARG B  29     -21.289   4.339 -13.359  1.00115.48           O  
ANISOU 2562  O   ARG B  29    12607  18198  13071   -501   1344   -202       O  
ATOM   2563  CB  ARG B  29     -20.731   1.712 -14.161  1.00108.87           C  
ANISOU 2563  CB  ARG B  29    11976  17063  12327   -948   1330     92       C  
ATOM   2564  CG  ARG B  29     -20.190   0.376 -14.633  1.00106.64           C  
ANISOU 2564  CG  ARG B  29    11861  16549  12108  -1147   1307    241       C  
ATOM   2565  CD  ARG B  29     -18.732   0.480 -15.033  1.00104.46           C  
ANISOU 2565  CD  ARG B  29    11778  15958  11954  -1029   1201    262       C  
ATOM   2566  NE  ARG B  29     -18.264  -0.735 -15.691  1.00106.77           N  
ANISOU 2566  NE  ARG B  29    12226  16019  12323  -1184   1178    386       N  
ATOM   2567  CZ  ARG B  29     -18.108  -0.859 -17.005  1.00104.93           C  
ANISOU 2567  CZ  ARG B  29    12017  15620  12233  -1188   1120    367       C  
ATOM   2568  NH1 ARG B  29     -18.377   0.164 -17.808  1.00103.60           N  
ANISOU 2568  NH1 ARG B  29    11725  15491  12147  -1050   1075    239       N  
ATOM   2569  NH2 ARG B  29     -17.676  -2.003 -17.517  1.00103.58           N  
ANISOU 2569  NH2 ARG B  29    12007  15234  12114  -1324   1109    476       N  
ATOM   2570  N   THR B  30     -20.529   3.912 -11.282  1.00 83.93           N  
ANISOU 2570  N   THR B  30     8769  14260   8861   -566   1405   -113       N  
ATOM   2571  CA  THR B  30     -21.214   5.055 -10.712  1.00 73.62           C  
ANISOU 2571  CA  THR B  30     7329  13187   7456   -386   1458   -265       C  
ATOM   2572  C   THR B  30     -20.442   6.333 -11.013  1.00 64.53           C  
ANISOU 2572  C   THR B  30     6266  11862   6392   -143   1363   -397       C  
ATOM   2573  O   THR B  30     -20.967   7.431 -10.873  1.00 78.83           O  
ANISOU 2573  O   THR B  30     7991  13798   8162     47   1386   -544       O  
ATOM   2574  CB  THR B  30     -21.431   4.897  -9.186  1.00 75.11           C  
ANISOU 2574  CB  THR B  30     7513  13594   7431   -433   1555   -242       C  
ATOM   2575  OG1 THR B  30     -20.183   4.640  -8.538  1.00 77.67           O  
ANISOU 2575  OG1 THR B  30     8044  13735   7731   -453   1497   -169       O  
ATOM   2576  CG2 THR B  30     -22.376   3.738  -8.908  1.00 72.33           C  
ANISOU 2576  CG2 THR B  30     7097  13363   7024   -668   1620   -120       C  
ATOM   2577  N   SER B  31     -19.195   6.192 -11.445  1.00 60.41           N  
ANISOU 2577  N   SER B  31     5919  11049   5985   -149   1258   -347       N  
ATOM   2578  CA  SER B  31     -18.417   7.362 -11.833  1.00 57.16           C  
ANISOU 2578  CA  SER B  31     5598  10459   5661     45   1164   -464       C  
ATOM   2579  C   SER B  31     -17.325   7.011 -12.823  1.00 49.13           C  
ANISOU 2579  C   SER B  31     4710   9144   4812      3   1056   -393       C  
ATOM   2580  O   SER B  31     -17.007   5.845 -13.039  1.00 51.53           O  
ANISOU 2580  O   SER B  31     5064   9363   5151   -160   1051   -252       O  
ATOM   2581  CB  SER B  31     -17.792   8.033 -10.607  1.00 60.61           C  
ANISOU 2581  CB  SER B  31     6134  10923   5971    135   1160   -529       C  
ATOM   2582  OG  SER B  31     -16.638   7.328 -10.189  1.00 61.21           O  
ANISOU 2582  OG  SER B  31     6357  10861   6041     28   1107   -410       O  
ATOM   2583  N   TYR B  32     -16.743   8.042 -13.414  1.00 46.95           N  
ANISOU 2583  N   TYR B  32     4499   8709   4631    153    973   -493       N  
ATOM   2584  CA  TYR B  32     -15.695   7.864 -14.404  1.00 52.08           C  
ANISOU 2584  CA  TYR B  32     5259   9094   5437    131    874   -443       C  
ATOM   2585  C   TYR B  32     -14.360   8.362 -13.869  1.00 51.09           C  
ANISOU 2585  C   TYR B  32     5282   8834   5297    181    799   -463       C  
ATOM   2586  O   TYR B  32     -14.148   9.568 -13.800  1.00 49.62           O  
ANISOU 2586  O   TYR B  32     5136   8611   5106    317    764   -592       O  
ATOM   2587  CB  TYR B  32     -16.020   8.627 -15.693  1.00 57.04           C  
ANISOU 2587  CB  TYR B  32     5847   9633   6195    240    829   -529       C  
ATOM   2588  CG  TYR B  32     -17.350   8.323 -16.332  1.00 62.04           C  
ANISOU 2588  CG  TYR B  32     6313  10417   6842    213    886   -529       C  
ATOM   2589  CD1 TYR B  32     -17.628   7.062 -16.838  1.00 71.35           C  
ANISOU 2589  CD1 TYR B  32     7452  11596   8060     29    908   -408       C  
ATOM   2590  CD2 TYR B  32     -18.317   9.312 -16.470  1.00 64.48           C  
ANISOU 2590  CD2 TYR B  32     6509  10867   7123    375    913   -653       C  
ATOM   2591  CE1 TYR B  32     -18.843   6.782 -17.438  1.00 74.43           C  
ANISOU 2591  CE1 TYR B  32     7682  12144   8455    -19    953   -412       C  
ATOM   2592  CE2 TYR B  32     -19.532   9.043 -17.071  1.00 70.84           C  
ANISOU 2592  CE2 TYR B  32     7138  11842   7934    353    957   -652       C  
ATOM   2593  CZ  TYR B  32     -19.788   7.777 -17.553  1.00 77.29           C  
ANISOU 2593  CZ  TYR B  32     7906  12675   8786    143    975   -532       C  
ATOM   2594  OH  TYR B  32     -20.993   7.498 -18.149  1.00 91.84           O  
ANISOU 2594  OH  TYR B  32     9565  14705  10624     97   1014   -533       O  
ATOM   2595  N   PRO B  33     -13.449   7.445 -13.503  1.00 46.93           N  
ANISOU 2595  N   PRO B  33     4841   8231   4758     71    772   -335       N  
ATOM   2596  CA  PRO B  33     -12.096   7.909 -13.183  1.00 45.55           C  
ANISOU 2596  CA  PRO B  33     4788   7933   4586    114    685   -350       C  
ATOM   2597  C   PRO B  33     -11.459   8.588 -14.393  1.00 46.78           C  
ANISOU 2597  C   PRO B  33     4989   7888   4898    180    600   -407       C  
ATOM   2598  O   PRO B  33     -11.366   7.980 -15.465  1.00 39.77           O  
ANISOU 2598  O   PRO B  33     4095   6882   4135    131    581   -337       O  
ATOM   2599  CB  PRO B  33     -11.353   6.618 -12.811  1.00 38.66           C  
ANISOU 2599  CB  PRO B  33     3979   7020   3691     -5    673   -179       C  
ATOM   2600  CG  PRO B  33     -12.430   5.657 -12.441  1.00 50.46           C  
ANISOU 2600  CG  PRO B  33     5404   8658   5109   -111    774    -96       C  
ATOM   2601  CD  PRO B  33     -13.590   5.993 -13.324  1.00 45.32           C  
ANISOU 2601  CD  PRO B  33     4637   8053   4528    -88    818   -174       C  
ATOM   2602  N   MET B  34     -11.036   9.839 -14.232  1.00 40.75           N  
ANISOU 2602  N   MET B  34     4282   7081   4120    281    552   -534       N  
ATOM   2603  CA  MET B  34     -10.508  10.596 -15.368  1.00 42.74           C  
ANISOU 2603  CA  MET B  34     4585   7147   4506    337    478   -594       C  
ATOM   2604  C   MET B  34      -9.328  11.482 -15.009  1.00 45.95           C  
ANISOU 2604  C   MET B  34     5105   7465   4891    360    397   -662       C  
ATOM   2605  O   MET B  34      -8.696  12.033 -15.888  1.00 45.11           O  
ANISOU 2605  O   MET B  34     5054   7201   4887    376    332   -693       O  
ATOM   2606  CB  MET B  34     -11.613  11.459 -15.989  1.00 44.29           C  
ANISOU 2606  CB  MET B  34     4729   7362   4737    452    508   -708       C  
ATOM   2607  CG  MET B  34     -12.645  10.694 -16.823  1.00 50.11           C  
ANISOU 2607  CG  MET B  34     5346   8151   5540    418    559   -646       C  
ATOM   2608  SD  MET B  34     -14.133  11.687 -17.131  1.00 59.01           S  
ANISOU 2608  SD  MET B  34     6372   9400   6648    579    609   -780       S  
ATOM   2609  CE  MET B  34     -13.475  12.997 -18.158  1.00 60.08           C  
ANISOU 2609  CE  MET B  34     6633   9299   6895    701    514   -876       C  
ATOM   2610  N   GLY B  35      -9.030  11.641 -13.724  1.00 45.42           N  
ANISOU 2610  N   GLY B  35     5072   7507   4679    350    401   -686       N  
ATOM   2611  CA  GLY B  35      -7.927  12.506 -13.343  1.00 39.04           C  
ANISOU 2611  CA  GLY B  35     4368   6632   3833    350    321   -759       C  
ATOM   2612  C   GLY B  35      -6.934  11.905 -12.364  1.00 43.42           C  
ANISOU 2612  C   GLY B  35     4945   7264   4290    266    282   -674       C  
ATOM   2613  O   GLY B  35      -7.267  11.000 -11.604  1.00 40.16           O  
ANISOU 2613  O   GLY B  35     4487   6984   3787    229    332   -583       O  
ATOM   2614  N   TRP B  36      -5.700  12.402 -12.415  1.00 43.57           N  
ANISOU 2614  N   TRP B  36     5031   7203   4320    230    189   -697       N  
ATOM   2615  CA  TRP B  36      -4.658  12.029 -11.475  1.00 46.14           C  
ANISOU 2615  CA  TRP B  36     5373   7618   4539    163    133   -634       C  
ATOM   2616  C   TRP B  36      -4.063  13.279 -10.868  1.00 43.87           C  
ANISOU 2616  C   TRP B  36     5175   7336   4157    151     72   -779       C  
ATOM   2617  O   TRP B  36      -3.681  14.201 -11.577  1.00 42.58           O  
ANISOU 2617  O   TRP B  36     5072   7035   4070    151     25   -869       O  
ATOM   2618  CB  TRP B  36      -3.542  11.234 -12.134  1.00 41.22           C  
ANISOU 2618  CB  TRP B  36     4722   6923   4016    111     67   -498       C  
ATOM   2619  CG  TRP B  36      -3.916   9.882 -12.635  1.00 41.31           C  
ANISOU 2619  CG  TRP B  36     4677   6916   4105    107    117   -345       C  
ATOM   2620  CD1 TRP B  36      -4.137   9.524 -13.929  1.00 36.07           C  
ANISOU 2620  CD1 TRP B  36     3988   6117   3599    117    133   -306       C  
ATOM   2621  CD2 TRP B  36      -4.070   8.692 -11.855  1.00 40.82           C  
ANISOU 2621  CD2 TRP B  36     4593   6960   3956     83    155   -208       C  
ATOM   2622  NE1 TRP B  36      -4.428   8.185 -14.009  1.00 45.00           N  
ANISOU 2622  NE1 TRP B  36     5091   7258   4749     94    180   -163       N  
ATOM   2623  CE2 TRP B  36      -4.396   7.650 -12.747  1.00 44.55           C  
ANISOU 2623  CE2 TRP B  36     5041   7342   4546     73    195    -96       C  
ATOM   2624  CE3 TRP B  36      -3.975   8.409 -10.488  1.00 43.53           C  
ANISOU 2624  CE3 TRP B  36     4949   7464   4125     63    160   -169       C  
ATOM   2625  CZ2 TRP B  36      -4.639   6.344 -12.317  1.00 42.56           C  
ANISOU 2625  CZ2 TRP B  36     4791   7135   4245     39    242     55       C  
ATOM   2626  CZ3 TRP B  36      -4.211   7.115 -10.063  1.00 48.00           C  
ANISOU 2626  CZ3 TRP B  36     5508   8085   4643     37    205    -11       C  
ATOM   2627  CH2 TRP B  36      -4.547   6.099 -10.974  1.00 40.17           C  
ANISOU 2627  CH2 TRP B  36     4506   6982   3773     23    247     99       C  
ATOM   2628  N   PHE B  37      -3.982  13.290  -9.548  1.00 42.94           N  
ANISOU 2628  N   PHE B  37     5077   7375   3863    131     74   -798       N  
ATOM   2629  CA  PHE B  37      -3.379  14.380  -8.812  1.00 47.55           C  
ANISOU 2629  CA  PHE B  37     5756   7984   4327     99     14   -935       C  
ATOM   2630  C   PHE B  37      -2.344  13.799  -7.871  1.00 49.31           C  
ANISOU 2630  C   PHE B  37     5957   8352   4427     16    -55   -842       C  
ATOM   2631  O   PHE B  37      -2.295  12.588  -7.665  1.00 50.46           O  
ANISOU 2631  O   PHE B  37     6028   8581   4564     11    -39   -679       O  
ATOM   2632  CB  PHE B  37      -4.439  15.157  -8.020  1.00 53.12           C  
ANISOU 2632  CB  PHE B  37     6521   8758   4903    174     90  -1086       C  
ATOM   2633  CG  PHE B  37      -5.346  15.970  -8.881  1.00 58.02           C  
ANISOU 2633  CG  PHE B  37     7180   9240   5626    277    140  -1201       C  
ATOM   2634  CD1 PHE B  37      -6.341  15.355  -9.643  1.00 56.50           C  
ANISOU 2634  CD1 PHE B  37     6890   9034   5544    345    217  -1131       C  
ATOM   2635  CD2 PHE B  37      -5.201  17.347  -8.951  1.00 50.74           C  
ANISOU 2635  CD2 PHE B  37     6397   8199   4684    304    108  -1375       C  
ATOM   2636  CE1 PHE B  37      -7.171  16.102 -10.459  1.00 55.13           C  
ANISOU 2636  CE1 PHE B  37     6740   8750   5458    453    254  -1229       C  
ATOM   2637  CE2 PHE B  37      -6.031  18.102  -9.763  1.00 54.06           C  
ANISOU 2637  CE2 PHE B  37     6864   8483   5194    421    150  -1470       C  
ATOM   2638  CZ  PHE B  37      -7.018  17.477 -10.519  1.00 58.45           C  
ANISOU 2638  CZ  PHE B  37     7303   9047   5859    503    221  -1395       C  
ATOM   2639  N   ARG B  38      -1.530  14.657  -7.276  1.00 43.52           N  
ANISOU 2639  N   ARG B  38     5296   7652   3587    -49   -135   -945       N  
ATOM   2640  CA  ARG B  38      -0.572  14.176  -6.306  1.00 49.64           C  
ANISOU 2640  CA  ARG B  38     6042   8596   4222   -123   -208   -865       C  
ATOM   2641  C   ARG B  38      -0.238  15.260  -5.307  1.00 49.19           C  
ANISOU 2641  C   ARG B  38     6087   8616   3985   -184   -257  -1028       C  
ATOM   2642  O   ARG B  38      -0.381  16.452  -5.583  1.00 56.57           O  
ANISOU 2642  O   ARG B  38     7130   9429   4937   -192   -261  -1199       O  
ATOM   2643  CB  ARG B  38       0.698  13.676  -6.992  1.00 45.67           C  
ANISOU 2643  CB  ARG B  38     5466   8065   3820   -180   -303   -744       C  
ATOM   2644  CG  ARG B  38       1.577  14.773  -7.557  1.00 48.38           C  
ANISOU 2644  CG  ARG B  38     5859   8310   4212   -265   -388   -858       C  
ATOM   2645  CD  ARG B  38       2.760  14.211  -8.298  1.00 48.93           C  
ANISOU 2645  CD  ARG B  38     5831   8377   4385   -310   -466   -732       C  
ATOM   2646  NE  ARG B  38       3.559  15.278  -8.884  1.00 50.14           N  
ANISOU 2646  NE  ARG B  38     6028   8442   4582   -414   -538   -840       N  
ATOM   2647  CZ  ARG B  38       4.592  15.083  -9.696  1.00 51.42           C  
ANISOU 2647  CZ  ARG B  38     6109   8589   4841   -467   -601   -767       C  
ATOM   2648  NH1 ARG B  38       4.960  13.854 -10.030  1.00 46.13           N1+
ANISOU 2648  NH1 ARG B  38     5315   7973   4238   -404   -600   -591       N1+
ATOM   2649  NH2 ARG B  38       5.256  16.121 -10.178  1.00 51.60           N  
ANISOU 2649  NH2 ARG B  38     6181   8537   4888   -584   -659   -873       N  
ATOM   2650  N   ARG B  39       0.192  14.825  -4.136  1.00 50.20           N  
ANISOU 2650  N   ARG B  39     6195   8944   3936   -226   -294   -974       N  
ATOM   2651  CA  ARG B  39       0.625  15.739  -3.102  1.00 54.63           C  
ANISOU 2651  CA  ARG B  39     6849   9605   4302   -304   -352  -1118       C  
ATOM   2652  C   ARG B  39       1.926  15.219  -2.541  1.00 54.66           C  
ANISOU 2652  C   ARG B  39     6781   9779   4208   -397   -472  -1007       C  
ATOM   2653  O   ARG B  39       1.976  14.126  -1.971  1.00 50.37           O  
ANISOU 2653  O   ARG B  39     6160   9384   3594   -366   -468   -844       O  
ATOM   2654  CB  ARG B  39      -0.422  15.878  -2.002  1.00 51.23           C  
ANISOU 2654  CB  ARG B  39     6477   9290   3696   -245   -259  -1199       C  
ATOM   2655  CG  ARG B  39      -0.050  16.897  -0.934  1.00 56.20           C  
ANISOU 2655  CG  ARG B  39     7229  10010   4114   -322   -312  -1374       C  
ATOM   2656  CD  ARG B  39      -1.065  16.854   0.196  1.00 71.88           C  
ANISOU 2656  CD  ARG B  39     9256  12142   5913   -253   -211  -1431       C  
ATOM   2657  NE  ARG B  39      -1.221  15.490   0.692  1.00 86.97           N  
ANISOU 2657  NE  ARG B  39    11051  14225   7770   -232   -179  -1224       N  
ATOM   2658  CZ  ARG B  39      -0.422  14.933   1.597  1.00108.59           C  
ANISOU 2658  CZ  ARG B  39    13757  17154  10349   -304   -259  -1122       C  
ATOM   2659  NH1 ARG B  39       0.587  15.627   2.113  1.00112.55           N  
ANISOU 2659  NH1 ARG B  39    14314  17722  10727   -411   -377  -1215       N  
ATOM   2660  NH2 ARG B  39      -0.631  13.683   1.990  1.00114.36           N  
ANISOU 2660  NH2 ARG B  39    14405  18011  11036   -274   -223   -924       N  
ATOM   2661  N   ALA B  40       2.982  15.993  -2.760  1.00 63.36           N  
ANISOU 2661  N   ALA B  40     7907  10857   5309   -513   -581  -1086       N  
ATOM   2662  CA  ALA B  40       4.296  15.702  -2.220  1.00 68.18           C  
ANISOU 2662  CA  ALA B  40     8439  11656   5810   -614   -710  -1008       C  
ATOM   2663  C   ALA B  40       4.322  16.164  -0.768  1.00 76.83           C  
ANISOU 2663  C   ALA B  40     9613  12935   6643   -677   -742  -1111       C  
ATOM   2664  O   ALA B  40       3.606  17.103  -0.409  1.00 73.03           O  
ANISOU 2664  O   ALA B  40     9274  12384   6088   -680   -686  -1297       O  
ATOM   2665  CB  ALA B  40       5.378  16.394  -3.053  1.00 64.57           C  
ANISOU 2665  CB  ALA B  40     7966  11120   5448   -736   -807  -1061       C  
ATOM   2666  N   PRO B  41       5.125  15.489   0.075  1.00 85.01           N  
ANISOU 2666  N   PRO B  41    10560  14209   7529   -714   -829   -990       N  
ATOM   2667  CA  PRO B  41       5.255  15.703   1.522  1.00 87.75           C  
ANISOU 2667  CA  PRO B  41    10959  14777   7606   -775   -873  -1049       C  
ATOM   2668  C   PRO B  41       5.051  17.140   2.024  1.00 94.90           C  
ANISOU 2668  C   PRO B  41    12038  15639   8382   -876   -876  -1313       C  
ATOM   2669  O   PRO B  41       4.302  17.345   2.983  1.00105.40           O  
ANISOU 2669  O   PRO B  41    13463  17041   9543   -844   -812  -1400       O  
ATOM   2670  CB  PRO B  41       6.686  15.254   1.790  1.00 84.27           C  
ANISOU 2670  CB  PRO B  41    10385  14543   7088   -856  -1026   -926       C  
ATOM   2671  CG  PRO B  41       6.904  14.136   0.809  1.00 78.13           C  
ANISOU 2671  CG  PRO B  41     9471  13701   6515   -747  -1012   -712       C  
ATOM   2672  CD  PRO B  41       6.019  14.407  -0.387  1.00 82.39           C  
ANISOU 2672  CD  PRO B  41    10065  13955   7286   -685   -897   -772       C  
ATOM   2673  N   GLY B  42       5.703  18.116   1.401  1.00 87.06           N  
ANISOU 2673  N   GLY B  42    11097  14525   7458  -1000   -945  -1441       N  
ATOM   2674  CA  GLY B  42       5.608  19.487   1.875  1.00 90.02           C  
ANISOU 2674  CA  GLY B  42    11665  14837   7702  -1110   -958  -1692       C  
ATOM   2675  C   GLY B  42       4.861  20.448   0.965  1.00 93.75           C  
ANISOU 2675  C   GLY B  42    12290  15002   8330  -1069   -872  -1850       C  
ATOM   2676  O   GLY B  42       4.628  21.601   1.335  1.00 95.89           O  
ANISOU 2676  O   GLY B  42    12758  15180   8498  -1129   -864  -2067       O  
ATOM   2677  N   LYS B  43       4.476  19.974  -0.218  1.00 87.68           N  
ANISOU 2677  N   LYS B  43    11443  14071   7800   -960   -809  -1742       N  
ATOM   2678  CA  LYS B  43       3.862  20.824  -1.235  1.00 82.40           C  
ANISOU 2678  CA  LYS B  43    10901  13112   7294   -914   -742  -1863       C  
ATOM   2679  C   LYS B  43       2.328  20.831  -1.192  1.00 72.72           C  
ANISOU 2679  C   LYS B  43     9744  11792   6096   -718   -590  -1917       C  
ATOM   2680  O   LYS B  43       1.701  20.130  -0.394  1.00 69.90           O  
ANISOU 2680  O   LYS B  43     9329  11596   5634   -626   -526  -1855       O  
ATOM   2681  CB  LYS B  43       4.318  20.380  -2.625  1.00 88.36           C  
ANISOU 2681  CB  LYS B  43    11535  13748   8291   -913   -763  -1727       C  
ATOM   2682  CG  LYS B  43       5.338  21.279  -3.307  1.00 94.28           C  
ANISOU 2682  CG  LYS B  43    12342  14385   9095  -1094   -859  -1806       C  
ATOM   2683  CD  LYS B  43       5.427  20.909  -4.784  1.00 93.56           C  
ANISOU 2683  CD  LYS B  43    12159  14137   9254  -1047   -838  -1691       C  
ATOM   2684  CE  LYS B  43       6.332  21.840  -5.572  1.00 94.42           C  
ANISOU 2684  CE  LYS B  43    12335  14115   9425  -1227   -915  -1768       C  
ATOM   2685  NZ  LYS B  43       6.265  21.502  -7.025  1.00 94.87           N  
ANISOU 2685  NZ  LYS B  43    12317  14011   9718  -1162   -877  -1664       N  
ATOM   2686  N   GLU B  44       1.738  21.640  -2.066  1.00 72.23           N  
ANISOU 2686  N   GLU B  44     9801  11478   6166   -655   -534  -2029       N  
ATOM   2687  CA  GLU B  44       0.292  21.650  -2.261  1.00 81.68           C  
ANISOU 2687  CA  GLU B  44    11032  12585   7420   -453   -393  -2068       C  
ATOM   2688  C   GLU B  44      -0.117  20.548  -3.248  1.00 73.99           C  
ANISOU 2688  C   GLU B  44     9878  11584   6652   -351   -341  -1871       C  
ATOM   2689  O   GLU B  44       0.723  20.038  -3.985  1.00 68.97           O  
ANISOU 2689  O   GLU B  44     9136  10928   6140   -426   -411  -1740       O  
ATOM   2690  CB  GLU B  44      -0.165  23.014  -2.778  1.00 91.59           C  
ANISOU 2690  CB  GLU B  44    12501  13579   8719   -410   -362  -2270       C  
ATOM   2691  CG  GLU B  44      -1.515  23.462  -2.251  1.00106.14           C  
ANISOU 2691  CG  GLU B  44    14446  15406  10475   -223   -236  -2407       C  
ATOM   2692  CD  GLU B  44      -1.393  24.283  -0.983  1.00121.50           C  
ANISOU 2692  CD  GLU B  44    16570  17422  12171   -279   -250  -2598       C  
ATOM   2693  OE1 GLU B  44      -0.592  25.242  -0.974  1.00127.54           O  
ANISOU 2693  OE1 GLU B  44    17509  18065  12887   -428   -338  -2726       O  
ATOM   2694  OE2 GLU B  44      -2.091  23.968   0.003  1.00128.42           O1-
ANISOU 2694  OE2 GLU B  44    17420  18479  12895   -188   -172  -2620       O1-
ATOM   2695  N   ARG B  45      -1.398  20.182  -3.252  1.00 74.83           N  
ANISOU 2695  N   ARG B  45     9946  11701   6785   -185   -217  -1856       N  
ATOM   2696  CA  ARG B  45      -1.912  19.223  -4.229  1.00 78.42           C  
ANISOU 2696  CA  ARG B  45    10253  12114   7430    -97   -161  -1692       C  
ATOM   2697  C   ARG B  45      -1.672  19.744  -5.639  1.00 70.28           C  
ANISOU 2697  C   ARG B  45     9260  10842   6603   -102   -192  -1710       C  
ATOM   2698  O   ARG B  45      -1.908  20.918  -5.911  1.00 75.39           O  
ANISOU 2698  O   ARG B  45    10065  11322   7257    -75   -186  -1874       O  
ATOM   2699  CB  ARG B  45      -3.405  18.958  -4.006  1.00 86.97           C  
ANISOU 2699  CB  ARG B  45    11300  13252   8492     65    -20  -1707       C  
ATOM   2700  CG  ARG B  45      -4.027  17.989  -5.013  1.00 97.36           C  
ANISOU 2700  CG  ARG B  45    12469  14528   9993    139     40  -1550       C  
ATOM   2701  CD  ARG B  45      -5.336  17.391  -4.499  1.00107.60           C  
ANISOU 2701  CD  ARG B  45    13684  15975  11223    246    169  -1519       C  
ATOM   2702  NE  ARG B  45      -6.508  18.192  -4.848  1.00116.81           N  
ANISOU 2702  NE  ARG B  45    14896  17066  12420    396    259  -1661       N  
ATOM   2703  CZ  ARG B  45      -7.637  18.213  -4.141  1.00123.42           C  
ANISOU 2703  CZ  ARG B  45    15705  18050  13138    501    373  -1722       C  
ATOM   2704  NH1 ARG B  45      -7.749  17.487  -3.035  1.00120.77           N1+
ANISOU 2704  NH1 ARG B  45    15310  17937  12640    455    412  -1653       N1+
ATOM   2705  NH2 ARG B  45      -8.654  18.968  -4.535  1.00128.41           N  
ANISOU 2705  NH2 ARG B  45    16368  18617  13804    659    448  -1849       N  
ATOM   2706  N   GLU B  46      -1.191  18.888  -6.534  1.00 61.61           N  
ANISOU 2706  N   GLU B  46     8031   9717   5661   -133   -224  -1542       N  
ATOM   2707  CA  GLU B  46      -0.968  19.326  -7.904  1.00 61.28           C  
ANISOU 2707  CA  GLU B  46     8019   9459   5807   -141   -248  -1549       C  
ATOM   2708  C   GLU B  46      -1.540  18.375  -8.962  1.00 55.24           C  
ANISOU 2708  C   GLU B  46     7122   8643   5222    -52   -191  -1403       C  
ATOM   2709  O   GLU B  46      -1.490  17.152  -8.833  1.00 50.08           O  
ANISOU 2709  O   GLU B  46     6333   8111   4582    -49   -176  -1244       O  
ATOM   2710  CB  GLU B  46       0.528  19.548  -8.154  1.00 68.52           C  
ANISOU 2710  CB  GLU B  46     8938  10361   6736   -314   -371  -1526       C  
ATOM   2711  CG  GLU B  46       1.376  18.294  -8.252  1.00 78.25           C  
ANISOU 2711  CG  GLU B  46     9991  11734   8008   -366   -420  -1328       C  
ATOM   2712  CD  GLU B  46       2.861  18.604  -8.211  1.00 86.28           C  
ANISOU 2712  CD  GLU B  46    10995  12804   8985   -537   -543  -1326       C  
ATOM   2713  OE1 GLU B  46       3.311  19.247  -7.233  1.00 99.70           O  
ANISOU 2713  OE1 GLU B  46    12772  14596  10513   -637   -600  -1432       O  
ATOM   2714  OE2 GLU B  46       3.579  18.211  -9.150  1.00 78.94           O1-
ANISOU 2714  OE2 GLU B  46     9973  11836   8186   -577   -582  -1223       O1-
ATOM   2715  N   PHE B  47      -2.099  18.972 -10.004  1.00 51.23           N  
ANISOU 2715  N   PHE B  47     6673   7948   4845     20   -159  -1462       N  
ATOM   2716  CA  PHE B  47      -2.573  18.244 -11.163  1.00 49.51           C  
ANISOU 2716  CA  PHE B  47     6350   7659   4803     86   -118  -1345       C  
ATOM   2717  C   PHE B  47      -1.432  17.481 -11.821  1.00 47.15           C  
ANISOU 2717  C   PHE B  47     5958   7355   4603    -18   -188  -1199       C  
ATOM   2718  O   PHE B  47      -0.340  18.020 -11.991  1.00 49.29           O  
ANISOU 2718  O   PHE B  47     6276   7578   4872   -130   -272  -1229       O  
ATOM   2719  CB  PHE B  47      -3.209  19.207 -12.167  1.00 55.12           C  
ANISOU 2719  CB  PHE B  47     7161   8165   5618    173    -94  -1447       C  
ATOM   2720  CG  PHE B  47      -3.632  18.552 -13.453  1.00 49.13           C  
ANISOU 2720  CG  PHE B  47     6303   7328   5035    227    -64  -1336       C  
ATOM   2721  CD1 PHE B  47      -4.823  17.842 -13.523  1.00 45.07           C  
ANISOU 2721  CD1 PHE B  47     5684   6894   4546    336     24  -1284       C  
ATOM   2722  CD2 PHE B  47      -2.846  18.657 -14.591  1.00 43.00           C  
ANISOU 2722  CD2 PHE B  47     5539   6411   4390    155   -123  -1289       C  
ATOM   2723  CE1 PHE B  47      -5.220  17.248 -14.705  1.00 44.92           C  
ANISOU 2723  CE1 PHE B  47     5581   6809   4679    370     46  -1191       C  
ATOM   2724  CE2 PHE B  47      -3.235  18.048 -15.784  1.00 44.79           C  
ANISOU 2724  CE2 PHE B  47     5682   6568   4767    202    -96  -1193       C  
ATOM   2725  CZ  PHE B  47      -4.417  17.349 -15.837  1.00 46.03           C  
ANISOU 2725  CZ  PHE B  47     5744   6800   4947    306    -15  -1148       C  
ATOM   2726  N   VAL B  48      -1.684  16.226 -12.177  1.00 43.73           N  
ANISOU 2726  N   VAL B  48     5393   6976   4246     18   -150  -1045       N  
ATOM   2727  CA  VAL B  48      -0.701  15.410 -12.899  1.00 41.89           C  
ANISOU 2727  CA  VAL B  48     5071   6729   4117    -45   -201   -903       C  
ATOM   2728  C   VAL B  48      -1.129  15.101 -14.332  1.00 43.12           C  
ANISOU 2728  C   VAL B  48     5192   6737   4453      5   -166   -849       C  
ATOM   2729  O   VAL B  48      -0.382  15.325 -15.296  1.00 46.38           O  
ANISOU 2729  O   VAL B  48     5611   7045   4968    -45   -213   -834       O  
ATOM   2730  CB  VAL B  48      -0.446  14.084 -12.165  1.00 43.20           C  
ANISOU 2730  CB  VAL B  48     5135   7062   4218    -50   -197   -751       C  
ATOM   2731  CG1 VAL B  48       0.506  13.215 -12.954  1.00 38.83           C  
ANISOU 2731  CG1 VAL B  48     4496   6485   3771    -79   -240   -607       C  
ATOM   2732  CG2 VAL B  48       0.100  14.346 -10.775  1.00 37.73           C  
ANISOU 2732  CG2 VAL B  48     4468   6532   3336   -107   -245   -791       C  
ATOM   2733  N   ALA B  49      -2.327  14.555 -14.470  1.00 45.02           N  
ANISOU 2733  N   ALA B  49     5391   6988   4725     93    -81   -818       N  
ATOM   2734  CA  ALA B  49      -2.847  14.200 -15.783  1.00 42.34           C  
ANISOU 2734  CA  ALA B  49     5015   6532   4542    136    -47   -769       C  
ATOM   2735  C   ALA B  49      -4.332  13.978 -15.720  1.00 43.76           C  
ANISOU 2735  C   ALA B  49     5159   6751   4715    227     44   -787       C  
ATOM   2736  O   ALA B  49      -4.890  13.684 -14.659  1.00 45.92           O  
ANISOU 2736  O   ALA B  49     5408   7167   4871    245     91   -788       O  
ATOM   2737  CB  ALA B  49      -2.157  12.944 -16.324  1.00 38.44           C  
ANISOU 2737  CB  ALA B  49     4436   6041   4129     96    -62   -608       C  
ATOM   2738  N   SER B  50      -4.976  14.107 -16.872  1.00 41.19           N  
ANISOU 2738  N   SER B  50     4824   6319   4509    278     68   -796       N  
ATOM   2739  CA  SER B  50      -6.368  13.748 -16.988  1.00 38.17           C  
ANISOU 2739  CA  SER B  50     4374   5996   4132    352    150   -793       C  
ATOM   2740  C   SER B  50      -6.639  13.316 -18.418  1.00 41.55           C  
ANISOU 2740  C   SER B  50     4759   6318   4710    357    154   -732       C  
ATOM   2741  O   SER B  50      -5.801  13.481 -19.301  1.00 37.90           O  
ANISOU 2741  O   SER B  50     4335   5727   4339    320     99   -712       O  
ATOM   2742  CB  SER B  50      -7.277  14.907 -16.596  1.00 40.26           C  
ANISOU 2742  CB  SER B  50     4690   6281   4327    461    183   -944       C  
ATOM   2743  OG  SER B  50      -7.149  15.968 -17.520  1.00 49.17           O  
ANISOU 2743  OG  SER B  50     5909   7238   5533    510    141  -1027       O  
ATOM   2744  N   ILE B  51      -7.812  12.751 -18.636  1.00 38.16           N  
ANISOU 2744  N   ILE B  51     4245   5960   4294    392    222   -704       N  
ATOM   2745  CA  ILE B  51      -8.144  12.233 -19.942  1.00 39.23           C  
ANISOU 2745  CA  ILE B  51     4335   6016   4555    383    227   -645       C  
ATOM   2746  C   ILE B  51      -9.638  12.341 -20.090  1.00 41.73           C  
ANISOU 2746  C   ILE B  51     4572   6427   4857    458    290   -689       C  
ATOM   2747  O   ILE B  51     -10.390  12.259 -19.107  1.00 40.41           O  
ANISOU 2747  O   ILE B  51     4352   6419   4583    483    349   -714       O  
ATOM   2748  CB  ILE B  51      -7.647  10.776 -20.124  1.00 44.99           C  
ANISOU 2748  CB  ILE B  51     5026   6745   5325    282    234   -497       C  
ATOM   2749  CG1 ILE B  51      -7.650  10.378 -21.608  1.00 40.06           C  
ANISOU 2749  CG1 ILE B  51     4389   5997   4835    263    221   -451       C  
ATOM   2750  CG2 ILE B  51      -8.467   9.811 -19.257  1.00 34.22           C  
ANISOU 2750  CG2 ILE B  51     3592   5537   3875    246    308   -434       C  
ATOM   2751  CD1 ILE B  51      -6.765   9.191 -21.925  1.00 37.45           C  
ANISOU 2751  CD1 ILE B  51     4068   5609   4555    185    209   -326       C  
ATOM   2752  N   THR B  52     -10.080  12.575 -21.316  1.00 43.71           N  
ANISOU 2752  N   THR B  52     4807   6597   5204    499    277   -702       N  
ATOM   2753  CA  THR B  52     -11.500  12.737 -21.569  1.00 42.61           C  
ANISOU 2753  CA  THR B  52     4573   6565   5051    583    327   -745       C  
ATOM   2754  C   THR B  52     -12.219  11.416 -21.371  1.00 38.45           C  
ANISOU 2754  C   THR B  52     3925   6184   4502    488    392   -652       C  
ATOM   2755  O   THR B  52     -11.594  10.352 -21.338  1.00 40.57           O  
ANISOU 2755  O   THR B  52     4206   6417   4791    367    391   -546       O  
ATOM   2756  CB  THR B  52     -11.767  13.224 -23.008  1.00 47.24           C  
ANISOU 2756  CB  THR B  52     5170   7036   5742    643    287   -766       C  
ATOM   2757  OG1 THR B  52     -11.165  12.299 -23.914  1.00 42.20           O  
ANISOU 2757  OG1 THR B  52     4532   6304   5200    528    262   -665       O  
ATOM   2758  CG2 THR B  52     -11.154  14.601 -23.237  1.00 44.56           C  
ANISOU 2758  CG2 THR B  52     4972   6540   5419    731    228   -857       C  
ATOM   2759  N   TRP B  53     -13.539  11.498 -21.281  1.00 32.77           N  
ANISOU 2759  N   TRP B  53     3090   5627   3734    546    448   -691       N  
ATOM   2760  CA  TRP B  53     -14.391  10.326 -21.195  1.00 47.02           C  
ANISOU 2760  CA  TRP B  53     4769   7585   5511    439    514   -612       C  
ATOM   2761  C   TRP B  53     -14.100   9.309 -22.309  1.00 50.54           C  
ANISOU 2761  C   TRP B  53     5222   7917   6064    313    489   -511       C  
ATOM   2762  O   TRP B  53     -14.025   8.105 -22.066  1.00 48.28           O  
ANISOU 2762  O   TRP B  53     4928   7653   5763    173    522   -411       O  
ATOM   2763  CB  TRP B  53     -15.862  10.760 -21.240  1.00 48.33           C  
ANISOU 2763  CB  TRP B  53     4789   7947   5626    536    564   -682       C  
ATOM   2764  CG  TRP B  53     -16.766   9.630 -21.485  1.00 63.78           C  
ANISOU 2764  CG  TRP B  53     6610  10052   7572    403    618   -605       C  
ATOM   2765  CD1 TRP B  53     -17.281   8.770 -20.554  1.00 71.62           C  
ANISOU 2765  CD1 TRP B  53     7525  11223   8465    287    698   -550       C  
ATOM   2766  CD2 TRP B  53     -17.250   9.187 -22.754  1.00 53.59           C  
ANISOU 2766  CD2 TRP B  53     5253   8744   6364    347    596   -570       C  
ATOM   2767  NE1 TRP B  53     -18.069   7.828 -21.172  1.00 73.91           N  
ANISOU 2767  NE1 TRP B  53     7707  11602   8772    151    728   -485       N  
ATOM   2768  CE2 TRP B  53     -18.060   8.061 -22.525  1.00 67.10           C  
ANISOU 2768  CE2 TRP B  53     6849  10625   8022    186    664   -500       C  
ATOM   2769  CE3 TRP B  53     -17.081   9.640 -24.063  1.00 53.86           C  
ANISOU 2769  CE3 TRP B  53     5321   8638   6504    408    525   -592       C  
ATOM   2770  CZ2 TRP B  53     -18.696   7.379 -23.556  1.00 70.10           C  
ANISOU 2770  CZ2 TRP B  53     7146  11040   8450     77    659   -459       C  
ATOM   2771  CZ3 TRP B  53     -17.711   8.962 -25.082  1.00 57.34           C  
ANISOU 2771  CZ3 TRP B  53     5676   9120   6990    315    520   -548       C  
ATOM   2772  CH2 TRP B  53     -18.510   7.847 -24.825  1.00 59.87           C  
ANISOU 2772  CH2 TRP B  53     5881   9612   7256    148    584   -487       C  
ATOM   2773  N   SER B  54     -13.914   9.806 -23.524  1.00 47.76           N  
ANISOU 2773  N   SER B  54     4902   7432   5810    366    430   -538       N  
ATOM   2774  CA  SER B  54     -13.708   8.948 -24.697  1.00 47.27           C  
ANISOU 2774  CA  SER B  54     4850   7265   5844    262    407   -461       C  
ATOM   2775  C   SER B  54     -12.391   8.173 -24.652  1.00 45.25           C  
ANISOU 2775  C   SER B  54     4705   6857   5629    167    385   -374       C  
ATOM   2776  O   SER B  54     -12.189   7.217 -25.415  1.00 47.32           O  
ANISOU 2776  O   SER B  54     4989   7039   5953     69    384   -300       O  
ATOM   2777  CB  SER B  54     -13.748   9.795 -25.963  1.00 38.27           C  
ANISOU 2777  CB  SER B  54     3731   6023   4787    355    347   -515       C  
ATOM   2778  OG  SER B  54     -12.664  10.709 -25.949  1.00 42.76           O  
ANISOU 2778  OG  SER B  54     4426   6437   5384    426    293   -555       O  
ATOM   2779  N   GLY B  55     -11.491   8.592 -23.770  1.00 41.05           N  
ANISOU 2779  N   GLY B  55     4246   6292   5059    202    367   -387       N  
ATOM   2780  CA  GLY B  55     -10.161   8.023 -23.733  1.00 37.16           C  
ANISOU 2780  CA  GLY B  55     3844   5674   4600    144    336   -311       C  
ATOM   2781  C   GLY B  55      -9.255   8.580 -24.821  1.00 35.16           C  
ANISOU 2781  C   GLY B  55     3661   5254   4446    178    270   -332       C  
ATOM   2782  O   GLY B  55      -8.107   8.184 -24.931  1.00 33.07           O  
ANISOU 2782  O   GLY B  55     3455   4895   4214    143    242   -275       O  
ATOM   2783  N   ILE B  56      -9.763   9.512 -25.621  1.00 42.91           N  
ANISOU 2783  N   ILE B  56     4632   6207   5466    250    246   -409       N  
ATOM   2784  CA  ILE B  56      -9.013   9.995 -26.781  1.00 37.87           C  
ANISOU 2784  CA  ILE B  56     4060   5411   4916    266    190   -420       C  
ATOM   2785  C   ILE B  56      -7.969  11.065 -26.433  1.00 37.05           C  
ANISOU 2785  C   ILE B  56     4045   5231   4802    306    140   -472       C  
ATOM   2786  O   ILE B  56      -6.817  10.981 -26.868  1.00 44.14           O  
ANISOU 2786  O   ILE B  56     4995   6029   5747    263    104   -437       O  
ATOM   2787  CB  ILE B  56      -9.971  10.559 -27.867  1.00 44.66           C  
ANISOU 2787  CB  ILE B  56     4888   6263   5817    327    177   -470       C  
ATOM   2788  CG1 ILE B  56     -10.871   9.436 -28.394  1.00 43.64           C  
ANISOU 2788  CG1 ILE B  56     4673   6207   5703    252    216   -415       C  
ATOM   2789  CG2 ILE B  56      -9.169  11.190 -29.017  1.00 40.81           C  
ANISOU 2789  CG2 ILE B  56     4487   5613   5406    343    119   -481       C  
ATOM   2790  CD1 ILE B  56     -12.002   9.890 -29.337  1.00 44.35           C  
ANISOU 2790  CD1 ILE B  56     4695   6347   5809    310    203   -460       C  
ATOM   2791  N   ASP B  57      -8.359  12.060 -25.646  1.00 36.88           N  
ANISOU 2791  N   ASP B  57     4039   5262   4711    383    139   -560       N  
ATOM   2792  CA  ASP B  57      -7.512  13.228 -25.428  1.00 42.63           C  
ANISOU 2792  CA  ASP B  57     4871   5902   5423    411     89   -629       C  
ATOM   2793  C   ASP B  57      -6.945  13.380 -24.007  1.00 45.37           C  
ANISOU 2793  C   ASP B  57     5243   6320   5674    389     88   -651       C  
ATOM   2794  O   ASP B  57      -7.642  13.850 -23.110  1.00 41.56           O  
ANISOU 2794  O   ASP B  57     4756   5928   5106    453    117   -721       O  
ATOM   2795  CB  ASP B  57      -8.309  14.480 -25.784  1.00 50.59           C  
ANISOU 2795  CB  ASP B  57     5927   6870   6425    530     78   -730       C  
ATOM   2796  CG  ASP B  57      -8.801  14.458 -27.224  1.00 55.17           C  
ANISOU 2796  CG  ASP B  57     6490   7382   7090    558     64   -707       C  
ATOM   2797  OD1 ASP B  57      -7.949  14.607 -28.121  1.00 53.03           O  
ANISOU 2797  OD1 ASP B  57     6286   6978   6884    508     22   -680       O  
ATOM   2798  OD2 ASP B  57     -10.020  14.276 -27.452  1.00 59.84           O  
ANISOU 2798  OD2 ASP B  57     6994   8068   7674    623     94   -716       O  
ATOM   2799  N   PRO B  58      -5.667  13.016 -23.811  1.00 40.83           N  
ANISOU 2799  N   PRO B  58     4692   5718   5105    305     55   -597       N  
ATOM   2800  CA  PRO B  58      -4.997  13.215 -22.516  1.00 40.98           C  
ANISOU 2800  CA  PRO B  58     4735   5810   5024    275     38   -617       C  
ATOM   2801  C   PRO B  58      -4.415  14.618 -22.362  1.00 48.95           C  
ANISOU 2801  C   PRO B  58     5855   6742   6001    276    -15   -723       C  
ATOM   2802  O   PRO B  58      -4.047  15.262 -23.352  1.00 43.10           O  
ANISOU 2802  O   PRO B  58     5177   5870   5330    266    -51   -747       O  
ATOM   2803  CB  PRO B  58      -3.874  12.186 -22.548  1.00 33.57           C  
ANISOU 2803  CB  PRO B  58     3762   4882   4110    195     18   -503       C  
ATOM   2804  CG  PRO B  58      -3.518  12.149 -24.047  1.00 32.31           C  
ANISOU 2804  CG  PRO B  58     3614   4592   4071    180     -1   -475       C  
ATOM   2805  CD  PRO B  58      -4.849  12.209 -24.730  1.00 32.71           C  
ANISOU 2805  CD  PRO B  58     3647   4618   4163    239     38   -503       C  
ATOM   2806  N   THR B  59      -4.327  15.065 -21.115  1.00 44.15           N  
ANISOU 2806  N   THR B  59     5282   6215   5280    278    -19   -786       N  
ATOM   2807  CA  THR B  59      -3.740  16.349 -20.772  1.00 41.26           C  
ANISOU 2807  CA  THR B  59     5039   5780   4858    256    -69   -895       C  
ATOM   2808  C   THR B  59      -2.725  16.125 -19.663  1.00 49.34           C  
ANISOU 2808  C   THR B  59     6051   6909   5785    164   -105   -877       C  
ATOM   2809  O   THR B  59      -3.042  15.513 -18.639  1.00 44.40           O  
ANISOU 2809  O   THR B  59     5370   6427   5075    179    -73   -851       O  
ATOM   2810  CB  THR B  59      -4.807  17.357 -20.316  1.00 46.28           C  
ANISOU 2810  CB  THR B  59     5754   6403   5427    371    -38  -1024       C  
ATOM   2811  OG1 THR B  59      -5.774  17.530 -21.359  1.00 45.97           O  
ANISOU 2811  OG1 THR B  59     5706   6288   5471    472    -11  -1031       O  
ATOM   2812  CG2 THR B  59      -4.180  18.706 -19.971  1.00 46.71           C  
ANISOU 2812  CG2 THR B  59     5974   6354   5419    338    -89  -1145       C  
ATOM   2813  N   TYR B  60      -1.501  16.596 -19.875  1.00 43.49           N  
ANISOU 2813  N   TYR B  60     5358   6114   5051     62   -172   -886       N  
ATOM   2814  CA  TYR B  60      -0.430  16.380 -18.918  1.00 45.51           C  
ANISOU 2814  CA  TYR B  60     5585   6491   5215    -33   -221   -862       C  
ATOM   2815  C   TYR B  60       0.076  17.682 -18.345  1.00 51.19           C  
ANISOU 2815  C   TYR B  60     6433   7176   5841   -106   -273   -993       C  
ATOM   2816  O   TYR B  60       0.139  18.682 -19.057  1.00 47.61           O  
ANISOU 2816  O   TYR B  60     6094   6566   5430   -129   -293  -1067       O  
ATOM   2817  CB  TYR B  60       0.732  15.642 -19.570  1.00 40.16           C  
ANISOU 2817  CB  TYR B  60     4819   5832   4608   -108   -259   -746       C  
ATOM   2818  CG  TYR B  60       0.329  14.336 -20.187  1.00 42.92           C  
ANISOU 2818  CG  TYR B  60     5069   6190   5047    -45   -209   -621       C  
ATOM   2819  CD1 TYR B  60       0.121  13.215 -19.393  1.00 38.83           C  
ANISOU 2819  CD1 TYR B  60     4477   5799   4479    -11   -179   -533       C  
ATOM   2820  CD2 TYR B  60       0.142  14.221 -21.564  1.00 39.73           C  
ANISOU 2820  CD2 TYR B  60     4664   5662   4770    -26   -190   -593       C  
ATOM   2821  CE1 TYR B  60      -0.262  12.011 -19.946  1.00 40.19           C  
ANISOU 2821  CE1 TYR B  60     4587   5959   4726     32   -131   -423       C  
ATOM   2822  CE2 TYR B  60      -0.239  13.022 -22.137  1.00 38.69           C  
ANISOU 2822  CE2 TYR B  60     4459   5529   4713     20   -145   -489       C  
ATOM   2823  CZ  TYR B  60      -0.438  11.917 -21.325  1.00 40.32           C  
ANISOU 2823  CZ  TYR B  60     4603   5847   4868     45   -114   -406       C  
ATOM   2824  OH  TYR B  60      -0.810  10.723 -21.875  1.00 34.03           O  
ANISOU 2824  OH  TYR B  60     3762   5030   4139     75    -68   -307       O  
ATOM   2825  N   ALA B  61       0.440  17.662 -17.065  1.00 47.13           N  
ANISOU 2825  N   ALA B  61     5913   6802   5191   -150   -297  -1018       N  
ATOM   2826  CA  ALA B  61       1.189  18.763 -16.468  1.00 46.07           C  
ANISOU 2826  CA  ALA B  61     5893   6656   4953   -263   -362  -1132       C  
ATOM   2827  C   ALA B  61       2.547  18.822 -17.141  1.00 51.06           C  
ANISOU 2827  C   ALA B  61     6489   7276   5637   -406   -433  -1081       C  
ATOM   2828  O   ALA B  61       3.135  17.778 -17.451  1.00 47.90           O  
ANISOU 2828  O   ALA B  61     5941   6969   5289   -415   -442   -948       O  
ATOM   2829  CB  ALA B  61       1.336  18.584 -14.945  1.00 41.20           C  
ANISOU 2829  CB  ALA B  61     5259   6224   4170   -287   -377  -1157       C  
ATOM   2830  N   ASP B  62       3.031  20.038 -17.389  1.00 56.45           N  
ANISOU 2830  N   ASP B  62     7309   7840   6298   -517   -479  -1186       N  
ATOM   2831  CA  ASP B  62       4.290  20.249 -18.106  1.00 60.23           C  
ANISOU 2831  CA  ASP B  62     7759   8306   6819   -675   -540  -1150       C  
ATOM   2832  C   ASP B  62       5.406  19.457 -17.454  1.00 59.60           C  
ANISOU 2832  C   ASP B  62     7512   8460   6672   -760   -595  -1061       C  
ATOM   2833  O   ASP B  62       6.258  18.875 -18.129  1.00 60.00           O  
ANISOU 2833  O   ASP B  62     7434   8573   6790   -805   -616   -958       O  
ATOM   2834  CB  ASP B  62       4.655  21.739 -18.141  1.00 73.36           C  
ANISOU 2834  CB  ASP B  62     9622   9827   8426   -816   -585  -1290       C  
ATOM   2835  CG  ASP B  62       4.003  22.477 -19.294  1.00 89.12           C  
ANISOU 2835  CG  ASP B  62    11765  11571  10524   -761   -550  -1331       C  
ATOM   2836  OD1 ASP B  62       3.783  21.853 -20.354  1.00 95.41           O  
ANISOU 2836  OD1 ASP B  62    12474  12328  11450   -687   -515  -1231       O  
ATOM   2837  OD2 ASP B  62       3.718  23.684 -19.144  1.00 95.76           O1-
ANISOU 2837  OD2 ASP B  62    12822  12250  11312   -788   -558  -1462       O1-
ATOM   2838  N   SER B  63       5.362  19.431 -16.126  1.00 45.51           N  
ANISOU 2838  N   SER B  63     5732   6814   4747   -764   -616  -1103       N  
ATOM   2839  CA  SER B  63       6.326  18.737 -15.300  1.00 53.26           C  
ANISOU 2839  CA  SER B  63     6568   8037   5633   -826   -675  -1026       C  
ATOM   2840  C   SER B  63       6.480  17.252 -15.634  1.00 52.14           C  
ANISOU 2840  C   SER B  63     6241   8000   5571   -717   -650   -848       C  
ATOM   2841  O   SER B  63       7.527  16.664 -15.379  1.00 56.81           O  
ANISOU 2841  O   SER B  63     6694   8770   6122   -763   -707   -759       O  
ATOM   2842  CB  SER B  63       5.924  18.885 -13.833  1.00 57.97           C  
ANISOU 2842  CB  SER B  63     7218   8745   6063   -810   -682  -1099       C  
ATOM   2843  OG  SER B  63       6.791  18.128 -13.015  1.00 78.72           O  
ANISOU 2843  OG  SER B  63     9701  11618   8592   -849   -743  -1008       O  
ATOM   2844  N   VAL B  64       5.439  16.635 -16.189  1.00 46.40           N  
ANISOU 2844  N   VAL B  64     5514   7166   4949   -569   -567   -796       N  
ATOM   2845  CA  VAL B  64       5.481  15.191 -16.404  1.00 52.14           C  
ANISOU 2845  CA  VAL B  64     6103   7972   5738   -466   -537   -635       C  
ATOM   2846  C   VAL B  64       5.197  14.756 -17.845  1.00 48.02           C  
ANISOU 2846  C   VAL B  64     5559   7302   5386   -404   -484   -572       C  
ATOM   2847  O   VAL B  64       5.221  13.565 -18.140  1.00 46.82           O  
ANISOU 2847  O   VAL B  64     5315   7184   5291   -320   -455   -446       O  
ATOM   2848  CB  VAL B  64       4.474  14.461 -15.477  1.00 40.73           C  
ANISOU 2848  CB  VAL B  64     4659   6588   4228   -353   -481   -599       C  
ATOM   2849  CG1 VAL B  64       4.670  14.885 -14.006  1.00 43.97           C  
ANISOU 2849  CG1 VAL B  64     5102   7152   4454   -408   -527   -665       C  
ATOM   2850  CG2 VAL B  64       3.041  14.718 -15.942  1.00 40.58           C  
ANISOU 2850  CG2 VAL B  64     4727   6411   4280   -266   -396   -660       C  
ATOM   2851  N   ALA B  65       4.935  15.709 -18.735  1.00 55.91           N  
ANISOU 2851  N   ALA B  65     6654   8132   6456   -444   -475   -659       N  
ATOM   2852  CA  ALA B  65       4.542  15.402 -20.119  1.00 55.15           C  
ANISOU 2852  CA  ALA B  65     6554   7892   6510   -387   -425   -613       C  
ATOM   2853  C   ALA B  65       5.519  14.485 -20.868  1.00 52.74           C  
ANISOU 2853  C   ALA B  65     6118   7646   6276   -391   -435   -489       C  
ATOM   2854  O   ALA B  65       5.107  13.660 -21.691  1.00 56.54           O  
ANISOU 2854  O   ALA B  65     6566   8059   6857   -304   -382   -414       O  
ATOM   2855  CB  ALA B  65       4.349  16.696 -20.900  1.00 49.78           C  
ANISOU 2855  CB  ALA B  65     6008   7036   5871   -448   -431   -722       C  
ATOM   2856  N   ASP B  66       6.806  14.622 -20.575  1.00 50.51           N  
ANISOU 2856  N   ASP B  66     5759   7499   5933   -489   -501   -472       N  
ATOM   2857  CA  ASP B  66       7.834  13.855 -21.269  1.00 54.38           C  
ANISOU 2857  CA  ASP B  66     6115   8069   6479   -484   -510   -364       C  
ATOM   2858  C   ASP B  66       7.918  12.407 -20.801  1.00 59.37           C  
ANISOU 2858  C   ASP B  66     6644   8814   7099   -353   -493   -233       C  
ATOM   2859  O   ASP B  66       8.488  11.566 -21.497  1.00 58.48           O  
ANISOU 2859  O   ASP B  66     6442   8727   7051   -292   -477   -137       O  
ATOM   2860  CB  ASP B  66       9.204  14.514 -21.083  1.00 73.44           C  
ANISOU 2860  CB  ASP B  66     8459  10624   8819   -638   -590   -390       C  
ATOM   2861  CG  ASP B  66       9.202  15.987 -21.440  1.00100.40           C  
ANISOU 2861  CG  ASP B  66    12005  13917  12226   -795   -612   -520       C  
ATOM   2862  OD1 ASP B  66       8.408  16.391 -22.316  1.00111.52           O  
ANISOU 2862  OD1 ASP B  66    13526  15122  13723   -767   -563   -559       O  
ATOM   2863  OD2 ASP B  66      10.002  16.744 -20.847  1.00109.17           O  
ANISOU 2863  OD2 ASP B  66    13113  15133  13234   -949   -681   -580       O  
ATOM   2864  N   ARG B  67       7.353  12.115 -19.629  1.00 52.07           N  
ANISOU 2864  N   ARG B  67     5745   7954   6086   -305   -492   -229       N  
ATOM   2865  CA  ARG B  67       7.597  10.837 -18.967  1.00 46.66           C  
ANISOU 2865  CA  ARG B  67     4978   7394   5356   -200   -492    -99       C  
ATOM   2866  C   ARG B  67       6.346  10.022 -18.639  1.00 42.97           C  
ANISOU 2866  C   ARG B  67     4574   6852   4899    -97   -419    -54       C  
ATOM   2867  O   ARG B  67       6.440   8.811 -18.427  1.00 41.88           O  
ANISOU 2867  O   ARG B  67     4399   6757   4757     -1   -400     71       O  
ATOM   2868  CB  ARG B  67       8.370  11.069 -17.655  1.00 53.58           C  
ANISOU 2868  CB  ARG B  67     5800   8484   6075   -255   -574   -103       C  
ATOM   2869  CG  ARG B  67       9.659  11.835 -17.794  1.00 61.08           C  
ANISOU 2869  CG  ARG B  67     6668   9555   6985   -385   -654   -144       C  
ATOM   2870  CD  ARG B  67      10.276  12.082 -16.414  1.00 60.97           C  
ANISOU 2870  CD  ARG B  67     6607   9760   6798   -449   -740   -159       C  
ATOM   2871  NE  ARG B  67       9.584  13.144 -15.684  1.00 57.09           N  
ANISOU 2871  NE  ARG B  67     6250   9217   6223   -544   -748   -301       N  
ATOM   2872  CZ  ARG B  67       9.155  13.021 -14.433  1.00 55.42           C  
ANISOU 2872  CZ  ARG B  67     6077   9096   5884   -519   -759   -311       C  
ATOM   2873  NH1 ARG B  67       9.345  11.881 -13.791  1.00 50.89           N1+
ANISOU 2873  NH1 ARG B  67     5422   8661   5254   -409   -767   -176       N1+
ATOM   2874  NH2 ARG B  67       8.546  14.033 -13.825  1.00 54.52           N  
ANISOU 2874  NH2 ARG B  67     6093   8931   5691   -597   -760   -454       N  
ATOM   2875  N   PHE B  68       5.200  10.691 -18.516  1.00 47.19           N  
ANISOU 2875  N   PHE B  68     5208   7290   5433   -116   -381   -154       N  
ATOM   2876  CA  PHE B  68       3.963  10.026 -18.103  1.00 42.10           C  
ANISOU 2876  CA  PHE B  68     4609   6610   4779    -43   -311   -122       C  
ATOM   2877  C   PHE B  68       3.017   9.878 -19.273  1.00 42.93           C  
ANISOU 2877  C   PHE B  68     4753   6544   5014     -7   -242   -134       C  
ATOM   2878  O   PHE B  68       2.957  10.745 -20.132  1.00 36.46           O  
ANISOU 2878  O   PHE B  68     3967   5622   4263    -45   -247   -217       O  
ATOM   2879  CB  PHE B  68       3.220  10.797 -17.009  1.00 41.70           C  
ANISOU 2879  CB  PHE B  68     4622   6610   4613    -70   -308   -225       C  
ATOM   2880  CG  PHE B  68       3.910  10.825 -15.649  1.00 39.46           C  
ANISOU 2880  CG  PHE B  68     4311   6513   4170   -103   -369   -213       C  
ATOM   2881  CD1 PHE B  68       5.245  10.508 -15.503  1.00 40.83           C  
ANISOU 2881  CD1 PHE B  68     4398   6806   4309   -124   -443   -139       C  
ATOM   2882  CD2 PHE B  68       3.181  11.178 -14.513  1.00 35.03           C  
ANISOU 2882  CD2 PHE B  68     3805   6021   3484   -107   -352   -278       C  
ATOM   2883  CE1 PHE B  68       5.850  10.560 -14.263  1.00 43.60           C  
ANISOU 2883  CE1 PHE B  68     4719   7345   4504   -156   -508   -128       C  
ATOM   2884  CE2 PHE B  68       3.785  11.235 -13.267  1.00 38.17           C  
ANISOU 2884  CE2 PHE B  68     4185   6596   3723   -142   -411   -273       C  
ATOM   2885  CZ  PHE B  68       5.116  10.923 -13.142  1.00 40.72           C  
ANISOU 2885  CZ  PHE B  68     4422   7038   4013   -170   -493   -196       C  
ATOM   2886  N   THR B  69       2.248   8.797 -19.280  1.00 39.89           N  
ANISOU 2886  N   THR B  69     4372   6131   4652     54   -179    -51       N  
ATOM   2887  CA  THR B  69       1.129   8.663 -20.196  1.00 41.38           C  
ANISOU 2887  CA  THR B  69     4596   6189   4938     75   -113    -72       C  
ATOM   2888  C   THR B  69      -0.109   8.188 -19.442  1.00 41.06           C  
ANISOU 2888  C   THR B  69     4575   6188   4837     95    -51    -58       C  
ATOM   2889  O   THR B  69      -0.018   7.469 -18.449  1.00 38.27           O  
ANISOU 2889  O   THR B  69     4215   5933   4394    105    -45     20       O  
ATOM   2890  CB  THR B  69       1.457   7.697 -21.350  1.00 46.12           C  
ANISOU 2890  CB  THR B  69     5179   6693   5649    106    -90     20       C  
ATOM   2891  OG1 THR B  69       1.959   6.476 -20.811  1.00 53.64           O  
ANISOU 2891  OG1 THR B  69     6114   7704   6562    150    -86    149       O  
ATOM   2892  CG2 THR B  69       2.534   8.295 -22.227  1.00 46.27           C  
ANISOU 2892  CG2 THR B  69     5171   6679   5729     79   -137     -9       C  
ATOM   2893  N   THR B  70      -1.273   8.631 -19.886  1.00 35.96           N  
ANISOU 2893  N   THR B  70     3950   5483   4231    100     -5   -133       N  
ATOM   2894  CA  THR B  70      -2.496   8.218 -19.231  1.00 36.13           C  
ANISOU 2894  CA  THR B  70     3969   5567   4192    109     61   -126       C  
ATOM   2895  C   THR B  70      -3.394   7.614 -20.292  1.00 36.79           C  
ANISOU 2895  C   THR B  70     4043   5561   4374    109    116    -97       C  
ATOM   2896  O   THR B  70      -3.302   7.952 -21.463  1.00 35.04           O  
ANISOU 2896  O   THR B  70     3827   5231   4254    115    102   -130       O  
ATOM   2897  CB  THR B  70      -3.209   9.389 -18.523  1.00 40.30           C  
ANISOU 2897  CB  THR B  70     4512   6162   4638    124     68   -258       C  
ATOM   2898  OG1 THR B  70      -4.261   8.873 -17.697  1.00 42.67           O  
ANISOU 2898  OG1 THR B  70     4790   6569   4854    129    137   -236       O  
ATOM   2899  CG2 THR B  70      -3.817  10.350 -19.532  1.00 38.80           C  
ANISOU 2899  CG2 THR B  70     4342   5869   4531    155     72   -363       C  
ATOM   2900  N   SER B  71      -4.227   6.673 -19.902  1.00 37.88           N  
ANISOU 2900  N   SER B  71     4171   5747   4476     89    179    -30       N  
ATOM   2901  CA  SER B  71      -5.191   6.149 -20.847  1.00 38.47           C  
ANISOU 2901  CA  SER B  71     4232   5757   4628     66    230    -16       C  
ATOM   2902  C   SER B  71      -6.405   5.752 -20.076  1.00 42.50           C  
ANISOU 2902  C   SER B  71     4711   6384   5053     33    300     -5       C  
ATOM   2903  O   SER B  71      -6.359   5.612 -18.848  1.00 31.40           O  
ANISOU 2903  O   SER B  71     3308   5089   3533     26    312     22       O  
ATOM   2904  CB  SER B  71      -4.640   4.959 -21.628  1.00 40.48           C  
ANISOU 2904  CB  SER B  71     4522   5899   4959     44    234     94       C  
ATOM   2905  OG  SER B  71      -4.554   3.813 -20.810  1.00 39.34           O  
ANISOU 2905  OG  SER B  71     4412   5791   4745     18    265    210       O  
ATOM   2906  N   ARG B  72      -7.494   5.578 -20.807  1.00 34.88           N  
ANISOU 2906  N   ARG B  72     3708   5410   4135      5    344    -26       N  
ATOM   2907  CA  ARG B  72      -8.737   5.184 -20.207  1.00 34.11           C  
ANISOU 2907  CA  ARG B  72     3557   5444   3959    -44    417    -17       C  
ATOM   2908  C   ARG B  72      -9.354   4.037 -20.995  1.00 41.81           C  
ANISOU 2908  C   ARG B  72     4532   6366   4987   -139    461     59       C  
ATOM   2909  O   ARG B  72      -9.475   4.109 -22.221  1.00 36.27           O  
ANISOU 2909  O   ARG B  72     3825   5570   4386   -139    443     33       O  
ATOM   2910  CB  ARG B  72      -9.693   6.369 -20.146  1.00 39.86           C  
ANISOU 2910  CB  ARG B  72     4210   6275   4660     21    431   -148       C  
ATOM   2911  CG  ARG B  72     -10.930   6.050 -19.392  1.00 43.34           C  
ANISOU 2911  CG  ARG B  72     4572   6895   5000    -21    511   -146       C  
ATOM   2912  CD  ARG B  72     -11.865   7.236 -19.234  1.00 46.10           C  
ANISOU 2912  CD  ARG B  72     4842   7367   5308     77    530   -280       C  
ATOM   2913  NE  ARG B  72     -13.048   6.771 -18.526  1.00 65.84           N  
ANISOU 2913  NE  ARG B  72     7246  10067   7705     24    618   -265       N  
ATOM   2914  CZ  ARG B  72     -14.167   6.391 -19.121  1.00 66.84           C  
ANISOU 2914  CZ  ARG B  72     7269  10277   7849    -28    664   -260       C  
ATOM   2915  NH1 ARG B  72     -14.280   6.468 -20.436  1.00 74.52           N1+
ANISOU 2915  NH1 ARG B  72     8229  11147   8938    -19    625   -275       N1+
ATOM   2916  NH2 ARG B  72     -15.178   5.956 -18.396  1.00 79.77           N  
ANISOU 2916  NH2 ARG B  72     8812  12119   9380    -95    747   -241       N  
ATOM   2917  N   ASP B  73      -9.725   2.984 -20.275  1.00 41.71           N  
ANISOU 2917  N   ASP B  73     4539   6410   4897   -229    517    155       N  
ATOM   2918  CA  ASP B  73     -10.416   1.842 -20.840  1.00 42.58           C  
ANISOU 2918  CA  ASP B  73     4667   6481   5032   -352    568    227       C  
ATOM   2919  C   ASP B  73     -11.910   2.094 -20.705  1.00 45.92           C  
ANISOU 2919  C   ASP B  73     4967   7082   5400   -410    628    168       C  
ATOM   2920  O   ASP B  73     -12.487   1.884 -19.645  1.00 40.55           O  
ANISOU 2920  O   ASP B  73     4250   6552   4603   -460    685    193       O  
ATOM   2921  CB  ASP B  73      -9.992   0.555 -20.121  1.00 47.95           C  
ANISOU 2921  CB  ASP B  73     5456   7112   5649   -426    598    371       C  
ATOM   2922  CG  ASP B  73     -10.648  -0.710 -20.703  1.00 53.39           C  
ANISOU 2922  CG  ASP B  73     6203   7725   6357   -576    652    450       C  
ATOM   2923  OD1 ASP B  73     -11.716  -0.621 -21.347  1.00 54.23           O  
ANISOU 2923  OD1 ASP B  73     6227   7892   6485   -653    681    394       O  
ATOM   2924  OD2 ASP B  73     -10.093  -1.808 -20.489  1.00 50.12           O  
ANISOU 2924  OD2 ASP B  73     5925   7191   5926   -617    664    569       O  
ATOM   2925  N   VAL B  74     -12.542   2.551 -21.779  1.00 41.06           N  
ANISOU 2925  N   VAL B  74     4277   6467   4858   -398    615     92       N  
ATOM   2926  CA  VAL B  74     -13.944   2.926 -21.701  1.00 40.51           C  
ANISOU 2926  CA  VAL B  74     4061   6595   4734   -422    664     26       C  
ATOM   2927  C   VAL B  74     -14.841   1.716 -21.461  1.00 49.55           C  
ANISOU 2927  C   VAL B  74     5183   7830   5814   -611    740    110       C  
ATOM   2928  O   VAL B  74     -15.938   1.860 -20.946  1.00 54.18           O  
ANISOU 2928  O   VAL B  74     5641   8632   6311   -652    799     80       O  
ATOM   2929  CB  VAL B  74     -14.391   3.665 -22.967  1.00 46.21           C  
ANISOU 2929  CB  VAL B  74     4710   7300   5546   -357    623    -65       C  
ATOM   2930  CG1 VAL B  74     -13.561   4.952 -23.141  1.00 38.29           C  
ANISOU 2930  CG1 VAL B  74     3745   6209   4595   -183    553   -149       C  
ATOM   2931  CG2 VAL B  74     -14.259   2.759 -24.199  1.00 48.25           C  
ANISOU 2931  CG2 VAL B  74     5030   7408   5895   -463    606    -10       C  
ATOM   2932  N   ALA B  75     -14.375   0.522 -21.807  1.00 49.17           N  
ANISOU 2932  N   ALA B  75     5263   7619   5799   -728    744    214       N  
ATOM   2933  CA  ALA B  75     -15.214  -0.676 -21.656  1.00 56.35           C  
ANISOU 2933  CA  ALA B  75     6182   8582   6645   -936    816    297       C  
ATOM   2934  C   ALA B  75     -15.365  -1.103 -20.196  1.00 57.64           C  
ANISOU 2934  C   ALA B  75     6365   8864   6670   -999    881    372       C  
ATOM   2935  O   ALA B  75     -16.438  -1.554 -19.780  1.00 52.92           O  
ANISOU 2935  O   ALA B  75     5691   8437   5981  -1150    955    397       O  
ATOM   2936  CB  ALA B  75     -14.651  -1.840 -22.485  1.00 54.57           C  
ANISOU 2936  CB  ALA B  75     6126   8116   6493  -1036    803    382       C  
ATOM   2937  N   ASN B  76     -14.306  -0.974 -19.408  1.00 59.21           N  
ANISOU 2937  N   ASN B  76     6660   8992   6844   -895    853    413       N  
ATOM   2938  CA  ASN B  76     -14.430  -1.317 -17.993  1.00 64.65           C  
ANISOU 2938  CA  ASN B  76     7371   9805   7389   -946    909    485       C  
ATOM   2939  C   ASN B  76     -14.117  -0.174 -17.035  1.00 59.51           C  
ANISOU 2939  C   ASN B  76     6655   9287   6671   -789    889    409       C  
ATOM   2940  O   ASN B  76     -13.851  -0.407 -15.856  1.00 61.99           O  
ANISOU 2940  O   ASN B  76     7017   9667   6868   -798    914    473       O  
ATOM   2941  CB  ASN B  76     -13.562  -2.525 -17.654  1.00 63.20           C  
ANISOU 2941  CB  ASN B  76     7389   9438   7187  -1006    908    639       C  
ATOM   2942  CG  ASN B  76     -12.252  -2.511 -18.367  1.00 77.91           C  
ANISOU 2942  CG  ASN B  76     9361  11073   9169   -878    825    649       C  
ATOM   2943  OD1 ASN B  76     -11.305  -1.868 -17.925  1.00 81.19           O  
ANISOU 2943  OD1 ASN B  76     9784  11482   9583   -730    769    629       O  
ATOM   2944  ND2 ASN B  76     -12.178  -3.230 -19.488  1.00 87.94           N  
ANISOU 2944  ND2 ASN B  76    10714  12163  10535   -941    818    677       N  
ATOM   2945  N  AASN B  77     -14.173   1.054 -17.542  0.43 52.68           N  
ANISOU 2945  N  AASN B  77     5691   8456   5869   -650    845    272       N  
ATOM   2946  N  BASN B  77     -14.149   1.053 -17.544  0.57 52.53           N  
ANISOU 2946  N  BASN B  77     5674   8433   5851   -648    844    273       N  
ATOM   2947  CA AASN B  77     -14.045   2.246 -16.712  0.43 50.62           C  
ANISOU 2947  CA AASN B  77     5372   8320   5540   -507    832    174       C  
ATOM   2948  CA BASN B  77     -14.056   2.236 -16.702  0.57 50.47           C  
ANISOU 2948  CA BASN B  77     5353   8304   5520   -509    834    175       C  
ATOM   2949  C  AASN B  77     -12.785   2.267 -15.853  0.43 47.67           C  
ANISOU 2949  C  AASN B  77     5117   7876   5121   -444    786    223       C  
ATOM   2950  C  BASN B  77     -12.784   2.274 -15.853  0.57 47.70           C  
ANISOU 2950  C  BASN B  77     5120   7880   5125   -443    786    223       C  
ATOM   2951  O  AASN B  77     -12.824   2.661 -14.688  0.43 46.79           O  
ANISOU 2951  O  AASN B  77     4988   7906   4882   -410    809    202       O  
ATOM   2952  O  BASN B  77     -12.813   2.686 -14.694  0.57 46.56           O  
ANISOU 2952  O  BASN B  77     4959   7877   4855   -407    807    199       O  
ATOM   2953  CB AASN B  77     -15.273   2.386 -15.812  0.43 56.56           C  
ANISOU 2953  CB AASN B  77     5999   9341   6152   -554    925    142       C  
ATOM   2954  CB BASN B  77     -15.287   2.314 -15.796  0.57 53.80           C  
ANISOU 2954  CB BASN B  77     5651   8991   5798   -564    928    149       C  
ATOM   2955  CG AASN B  77     -16.216   3.463 -16.286  0.43 65.63           C  
ANISOU 2955  CG AASN B  77     6989  10627   7320   -453    935     -3       C  
ATOM   2956  CG BASN B  77     -15.602   3.722 -15.368  0.57 59.50           C  
ANISOU 2956  CG BASN B  77     6276   9859   6473   -399    927     -1       C  
ATOM   2957  OD1AASN B  77     -17.189   3.194 -16.996  0.43 70.98           O  
ANISOU 2957  OD1AASN B  77     7559  11383   8027   -528    968    -11       O  
ATOM   2958  OD1BASN B  77     -15.166   4.683 -15.999  0.57 59.97           O  
ANISOU 2958  OD1BASN B  77     6344   9817   6623   -261    858    -96       O  
ATOM   2959  ND2AASN B  77     -15.935   4.697 -15.892  0.43 62.94           N  
ANISOU 2959  ND2AASN B  77     6637  10319   6958   -280    904   -118       N  
ATOM   2960  ND2BASN B  77     -16.373   3.857 -14.296  0.57 60.26           N  
ANISOU 2960  ND2BASN B  77     6289  10188   6419   -413   1007    -23       N  
ATOM   2961  N   THR B  78     -11.670   1.838 -16.428  1.00 46.00           N  
ANISOU 2961  N   THR B  78     5016   7458   5003   -425    721    288       N  
ATOM   2962  CA  THR B  78     -10.404   1.835 -15.711  1.00 43.43           C  
ANISOU 2962  CA  THR B  78     4784   7080   4638   -359    665    340       C  
ATOM   2963  C   THR B  78      -9.530   2.987 -16.206  1.00 43.29           C  
ANISOU 2963  C   THR B  78     4758   6986   4703   -228    578    234       C  
ATOM   2964  O   THR B  78      -9.424   3.227 -17.403  1.00 39.72           O  
ANISOU 2964  O   THR B  78     4297   6415   4379   -202    546    191       O  
ATOM   2965  CB  THR B  78      -9.663   0.485 -15.879  1.00 47.62           C  
ANISOU 2965  CB  THR B  78     5447   7450   5196   -415    654    500       C  
ATOM   2966  OG1 THR B  78     -10.524  -0.588 -15.468  1.00 47.56           O  
ANISOU 2966  OG1 THR B  78     5472   7491   5109   -561    739    600       O  
ATOM   2967  CG2 THR B  78      -8.370   0.449 -15.058  1.00 43.54           C  
ANISOU 2967  CG2 THR B  78     5007   6916   4621   -333    593    565       C  
ATOM   2968  N   LEU B  79      -8.925   3.713 -15.275  1.00 39.93           N  
ANISOU 2968  N   LEU B  79     4341   6637   4193   -158    541    190       N  
ATOM   2969  CA  LEU B  79      -7.990   4.784 -15.618  1.00 37.87           C  
ANISOU 2969  CA  LEU B  79     4091   6306   3992    -62    456     97       C  
ATOM   2970  C   LEU B  79      -6.570   4.312 -15.334  1.00 36.22           C  
ANISOU 2970  C   LEU B  79     3954   6031   3776    -47    388    193       C  
ATOM   2971  O   LEU B  79      -6.318   3.696 -14.295  1.00 36.86           O  
ANISOU 2971  O   LEU B  79     4070   6190   3743    -69    397    285       O  
ATOM   2972  CB  LEU B  79      -8.314   6.047 -14.813  1.00 35.88           C  
ANISOU 2972  CB  LEU B  79     3803   6187   3644      0    457    -41       C  
ATOM   2973  CG  LEU B  79      -7.390   7.256 -14.919  1.00 37.54           C  
ANISOU 2973  CG  LEU B  79     4047   6339   3880     74    373   -147       C  
ATOM   2974  CD1 LEU B  79      -7.457   7.859 -16.339  1.00 32.74           C  
ANISOU 2974  CD1 LEU B  79     3429   5587   3423    112    344   -218       C  
ATOM   2975  CD2 LEU B  79      -7.779   8.277 -13.852  1.00 40.05           C  
ANISOU 2975  CD2 LEU B  79     4360   6793   4063    121    389   -270       C  
ATOM   2976  N   TYR B  80      -5.650   4.599 -16.248  1.00 33.75           N  
ANISOU 2976  N   TYR B  80     3657   5590   3577     -5    321    176       N  
ATOM   2977  CA  TYR B  80      -4.253   4.225 -16.085  1.00 36.90           C  
ANISOU 2977  CA  TYR B  80     4097   5948   3975     26    253    258       C  
ATOM   2978  C   TYR B  80      -3.329   5.425 -16.088  1.00 38.12           C  
ANISOU 2978  C   TYR B  80     4233   6116   4135     69    172    158       C  
ATOM   2979  O   TYR B  80      -3.578   6.417 -16.777  1.00 39.63           O  
ANISOU 2979  O   TYR B  80     4406   6257   4395     81    161     39       O  
ATOM   2980  CB  TYR B  80      -3.793   3.292 -17.203  1.00 36.80           C  
ANISOU 2980  CB  TYR B  80     4120   5776   4085     30    250    349       C  
ATOM   2981  CG  TYR B  80      -4.530   1.983 -17.269  1.00 45.47           C  
ANISOU 2981  CG  TYR B  80     5272   6827   5180    -30    323    460       C  
ATOM   2982  CD1 TYR B  80      -4.183   0.927 -16.434  1.00 44.44           C  
ANISOU 2982  CD1 TYR B  80     5212   6713   4961    -35    334    601       C  
ATOM   2983  CD2 TYR B  80      -5.551   1.791 -18.187  1.00 39.67           C  
ANISOU 2983  CD2 TYR B  80     4523   6026   4522    -89    377    427       C  
ATOM   2984  CE1 TYR B  80      -4.853  -0.283 -16.504  1.00 47.11           C  
ANISOU 2984  CE1 TYR B  80     5626   6984   5290   -109    403    706       C  
ATOM   2985  CE2 TYR B  80      -6.224   0.582 -18.269  1.00 43.11           C  
ANISOU 2985  CE2 TYR B  80     5017   6414   4948   -174    442    525       C  
ATOM   2986  CZ  TYR B  80      -5.870  -0.448 -17.423  1.00 45.67           C  
ANISOU 2986  CZ  TYR B  80     5431   6737   5186   -189    458    663       C  
ATOM   2987  OH  TYR B  80      -6.538  -1.647 -17.499  1.00 50.93           O  
ANISOU 2987  OH  TYR B  80     6181   7335   5836   -291    525    762       O  
ATOM   2988  N   LEU B  81      -2.238   5.303 -15.347  1.00 36.71           N  
ANISOU 2988  N   LEU B  81     4063   6003   3881     87    112    212       N  
ATOM   2989  CA  LEU B  81      -1.149   6.262 -15.430  1.00 36.92           C  
ANISOU 2989  CA  LEU B  81     4070   6043   3915    101     26    139       C  
ATOM   2990  C   LEU B  81       0.152   5.482 -15.513  1.00 39.22           C  
ANISOU 2990  C   LEU B  81     4351   6332   4218    134    -30    262       C  
ATOM   2991  O   LEU B  81       0.532   4.779 -14.580  1.00 40.92           O  
ANISOU 2991  O   LEU B  81     4576   6641   4330    154    -45    366       O  
ATOM   2992  CB  LEU B  81      -1.147   7.217 -14.219  1.00 36.17           C  
ANISOU 2992  CB  LEU B  81     3978   6089   3675     84     -2     43       C  
ATOM   2993  CG  LEU B  81      -0.110   8.350 -14.271  1.00 39.64           C  
ANISOU 2993  CG  LEU B  81     4411   6541   4107     64    -91    -55       C  
ATOM   2994  CD1 LEU B  81      -0.425   9.334 -15.399  1.00 38.51           C  
ANISOU 2994  CD1 LEU B  81     4285   6262   4084     58    -87   -176       C  
ATOM   2995  CD2 LEU B  81       0.006   9.095 -12.936  1.00 39.37           C  
ANISOU 2995  CD2 LEU B  81     4398   6656   3906     36   -124   -135       C  
ATOM   2996  N   GLN B  82       0.824   5.584 -16.648  1.00 38.40           N  
ANISOU 2996  N   GLN B  82     4226   6128   4235    150    -59    256       N  
ATOM   2997  CA  GLN B  82       2.136   4.988 -16.792  1.00 39.87           C  
ANISOU 2997  CA  GLN B  82     4382   6335   4433    200   -114    355       C  
ATOM   2998  C   GLN B  82       3.160   6.071 -16.492  1.00 42.40           C  
ANISOU 2998  C   GLN B  82     4643   6762   4704    168   -202    276       C  
ATOM   2999  O   GLN B  82       3.152   7.143 -17.104  1.00 41.60           O  
ANISOU 2999  O   GLN B  82     4537   6610   4659    117   -217    155       O  
ATOM   3000  CB  GLN B  82       2.329   4.406 -18.201  1.00 43.84           C  
ANISOU 3000  CB  GLN B  82     4890   6684   5083    235    -87    397       C  
ATOM   3001  CG  GLN B  82       3.716   3.800 -18.472  1.00 41.32           C  
ANISOU 3001  CG  GLN B  82     4529   6391   4782    311   -135    493       C  
ATOM   3002  CD  GLN B  82       3.932   2.505 -17.716  1.00 44.57           C  
ANISOU 3002  CD  GLN B  82     4981   6836   5119    391   -127    649       C  
ATOM   3003  OE1 GLN B  82       3.026   1.676 -17.616  1.00 46.10           O  
ANISOU 3003  OE1 GLN B  82     5261   6943   5311    387    -60    709       O  
ATOM   3004  NE2 GLN B  82       5.128   2.330 -17.170  1.00 54.37           N  
ANISOU 3004  NE2 GLN B  82     6161   8208   6289    458   -197    718       N  
ATOM   3005  N   MET B  83       4.025   5.788 -15.529  1.00 43.81           N  
ANISOU 3005  N   MET B  83     4786   7091   4769    191   -261    346       N  
ATOM   3006  CA  MET B  83       5.032   6.734 -15.072  1.00 44.71           C  
ANISOU 3006  CA  MET B  83     4838   7343   4808    139   -353    278       C  
ATOM   3007  C   MET B  83       6.407   6.169 -15.382  1.00 50.41           C  
ANISOU 3007  C   MET B  83     5469   8138   5546    198   -412    379       C  
ATOM   3008  O   MET B  83       6.797   5.154 -14.827  1.00 52.09           O  
ANISOU 3008  O   MET B  83     5669   8426   5698    286   -425    515       O  
ATOM   3009  CB  MET B  83       4.882   7.001 -13.571  1.00 43.60           C  
ANISOU 3009  CB  MET B  83     4713   7361   4490    109   -383    259       C  
ATOM   3010  CG  MET B  83       3.566   7.668 -13.196  1.00 48.15           C  
ANISOU 3010  CG  MET B  83     5366   7894   5033     62   -321    143       C  
ATOM   3011  SD  MET B  83       3.435   7.985 -11.402  1.00 74.91           S  
ANISOU 3011  SD  MET B  83     8780  11487   8195     28   -351    112       S  
ATOM   3012  CE  MET B  83       3.368   6.325 -10.792  1.00 46.61           C  
ANISOU 3012  CE  MET B  83     5201   7958   4549    112   -320    325       C  
ATOM   3013  N   ASN B  84       7.131   6.819 -16.287  1.00 50.85           N  
ANISOU 3013  N   ASN B  84     5466   8175   5681    155   -445    319       N  
ATOM   3014  CA  ASN B  84       8.473   6.376 -16.658  1.00 48.37           C  
ANISOU 3014  CA  ASN B  84     5040   7958   5380    211   -497    403       C  
ATOM   3015  C   ASN B  84       9.521   7.316 -16.113  1.00 44.21           C  
ANISOU 3015  C   ASN B  84     4417   7628   4754    114   -596    340       C  
ATOM   3016  O   ASN B  84       9.203   8.456 -15.752  1.00 45.40           O  
ANISOU 3016  O   ASN B  84     4611   7782   4856    -13   -618    208       O  
ATOM   3017  CB  ASN B  84       8.608   6.290 -18.189  1.00 43.56           C  
ANISOU 3017  CB  ASN B  84     4419   7202   4929    230   -452    394       C  
ATOM   3018  CG  ASN B  84       7.623   5.319 -18.795  1.00 50.57           C  
ANISOU 3018  CG  ASN B  84     5404   7900   5912    311   -359    452       C  
ATOM   3019  OD1 ASN B  84       7.465   4.198 -18.311  1.00 53.44           O  
ANISOU 3019  OD1 ASN B  84     5804   8261   6239    408   -336    570       O  
ATOM   3020  ND2 ASN B  84       6.939   5.748 -19.847  1.00 62.16           N  
ANISOU 3020  ND2 ASN B  84     6922   9205   7491    262   -308    372       N  
ATOM   3021  N   SER B  85      10.769   6.847 -16.083  1.00 47.24           N  
ANISOU 3021  N   SER B  85     4670   8175   5103    175   -656    431       N  
ATOM   3022  CA  SER B  85      11.899   7.694 -15.716  1.00 58.24           C  
ANISOU 3022  CA  SER B  85     5942   9783   6405     65   -756    378       C  
ATOM   3023  C   SER B  85      11.627   8.487 -14.439  1.00 55.76           C  
ANISOU 3023  C   SER B  85     5674   9573   5940    -50   -811    291       C  
ATOM   3024  O   SER B  85      11.778   9.710 -14.398  1.00 52.41           O  
ANISOU 3024  O   SER B  85     5263   9168   5483   -215   -850    154       O  
ATOM   3025  CB  SER B  85      12.228   8.642 -16.869  1.00 69.17           C  
ANISOU 3025  CB  SER B  85     7300  11094   7889    -58   -750    273       C  
ATOM   3026  OG  SER B  85      12.461   7.906 -18.057  1.00 78.16           O  
ANISOU 3026  OG  SER B  85     8399  12142   9157     49   -694    347       O  
ATOM   3027  N   LEU B  86      11.207   7.784 -13.398  1.00 54.51           N  
ANISOU 3027  N   LEU B  86     5559   9471   5683     36   -809    370       N  
ATOM   3028  CA  LEU B  86      10.761   8.445 -12.178  1.00 50.29           C  
ANISOU 3028  CA  LEU B  86     5090   9018   4999    -58   -841    287       C  
ATOM   3029  C   LEU B  86      11.907   9.174 -11.479  1.00 51.38           C  
ANISOU 3029  C   LEU B  86     5121   9408   4994   -175   -963    238       C  
ATOM   3030  O   LEU B  86      13.011   8.645 -11.371  1.00 55.95           O  
ANISOU 3030  O   LEU B  86     5552  10178   5526   -117  -1033    343       O  
ATOM   3031  CB  LEU B  86      10.105   7.414 -11.255  1.00 47.21           C  
ANISOU 3031  CB  LEU B  86     4765   8647   4528     61   -808    403       C  
ATOM   3032  CG  LEU B  86       8.661   7.117 -11.693  1.00 48.70           C  
ANISOU 3032  CG  LEU B  86     5088   8597   4819     96   -686    388       C  
ATOM   3033  CD1 LEU B  86       8.185   5.726 -11.294  1.00 41.62           C  
ANISOU 3033  CD1 LEU B  86     4243   7671   3900    230   -634    552       C  
ATOM   3034  CD2 LEU B  86       7.711   8.179 -11.150  1.00 48.57           C  
ANISOU 3034  CD2 LEU B  86     5169   8544   4741    -15   -660    228       C  
ATOM   3035  N   LYS B  87      11.645  10.405 -11.037  1.00 53.55           N  
ANISOU 3035  N   LYS B  87     5470   9682   5196   -340   -989     75       N  
ATOM   3036  CA  LYS B  87      12.622  11.185 -10.268  1.00 57.03           C  
ANISOU 3036  CA  LYS B  87     5835  10355   5478   -489  -1106      6       C  
ATOM   3037  C   LYS B  87      12.154  11.351  -8.827  1.00 61.26           C  
ANISOU 3037  C   LYS B  87     6451  10995   5828   -515  -1133    -33       C  
ATOM   3038  O   LYS B  87      11.003  11.052  -8.511  1.00 58.89           O  
ANISOU 3038  O   LYS B  87     6274  10570   5534   -438  -1050    -32       O  
ATOM   3039  CB  LYS B  87      12.833  12.570 -10.881  1.00 56.47           C  
ANISOU 3039  CB  LYS B  87     5807  10200   5447   -690  -1123   -165       C  
ATOM   3040  CG  LYS B  87      12.907  12.612 -12.390  1.00 67.55           C  
ANISOU 3040  CG  LYS B  87     7191  11430   7043   -681  -1067   -159       C  
ATOM   3041  CD  LYS B  87      12.573  14.014 -12.888  1.00 73.24           C  
ANISOU 3041  CD  LYS B  87     8047  11977   7803   -858  -1052   -338       C  
ATOM   3042  CE  LYS B  87      12.786  14.149 -14.380  1.00 83.55           C  
ANISOU 3042  CE  LYS B  87     9329  13138   9280   -874  -1008   -332       C  
ATOM   3043  NZ  LYS B  87      12.349  15.488 -14.861  1.00 91.30           N1+
ANISOU 3043  NZ  LYS B  87    10475  13919  10297  -1028   -989   -493       N1+
ATOM   3044  N   HIS B  88      13.033  11.858  -7.963  1.00 61.43           N  
ANISOU 3044  N   HIS B  88     6402  11260   5678   -636  -1247    -75       N  
ATOM   3045  CA  HIS B  88      12.663  12.134  -6.577  1.00 63.27           C  
ANISOU 3045  CA  HIS B  88     6718  11610   5714   -682  -1280   -131       C  
ATOM   3046  C   HIS B  88      11.468  13.078  -6.485  1.00 63.16           C  
ANISOU 3046  C   HIS B  88     6905  11383   5709   -755  -1200   -309       C  
ATOM   3047  O   HIS B  88      10.646  12.969  -5.571  1.00 60.92           O  
ANISOU 3047  O   HIS B  88     6721  11107   5319   -713  -1162   -328       O  
ATOM   3048  CB  HIS B  88      13.831  12.746  -5.798  1.00 71.29           C  
ANISOU 3048  CB  HIS B  88     7632  12910   6543   -844  -1423   -183       C  
ATOM   3049  CG  HIS B  88      13.387  13.686  -4.721  1.00 87.28           C  
ANISOU 3049  CG  HIS B  88     9800  14968   8393   -984  -1447   -346       C  
ATOM   3050  ND1 HIS B  88      12.842  13.249  -3.532  1.00 97.07           N  
ANISOU 3050  ND1 HIS B  88    11101  16305   9476   -909  -1441   -309       N  
ATOM   3051  CD2 HIS B  88      13.354  15.039  -4.674  1.00 89.74           C  
ANISOU 3051  CD2 HIS B  88    10228  15211   8660  -1188  -1468   -552       C  
ATOM   3052  CE1 HIS B  88      12.512  14.291  -2.791  1.00 96.59           C  
ANISOU 3052  CE1 HIS B  88    11175  16248   9278  -1056  -1456   -490       C  
ATOM   3053  NE2 HIS B  88      12.813  15.390  -3.460  1.00 95.99           N  
ANISOU 3053  NE2 HIS B  88    11142  16062   9266  -1223  -1474   -642       N  
ATOM   3054  N   GLU B  89      11.378  14.012  -7.429  1.00 59.87           N  
ANISOU 3054  N   GLU B  89     6552  10783   5413   -858  -1174   -436       N  
ATOM   3055  CA  GLU B  89      10.301  14.996  -7.427  1.00 63.47           C  
ANISOU 3055  CA  GLU B  89     7205  11030   5882   -910  -1103   -610       C  
ATOM   3056  C   GLU B  89       8.940  14.348  -7.716  1.00 59.93           C  
ANISOU 3056  C   GLU B  89     6831  10398   5540   -736   -973   -560       C  
ATOM   3057  O   GLU B  89       7.898  14.983  -7.568  1.00 57.78           O  
ANISOU 3057  O   GLU B  89     6705   9986   5262   -731   -904   -685       O  
ATOM   3058  CB  GLU B  89      10.592  16.105  -8.442  1.00 77.71           C  
ANISOU 3058  CB  GLU B  89     9066  12670   7789  -1052  -1111   -737       C  
ATOM   3059  CG  GLU B  89      10.511  15.659  -9.892  1.00 98.24           C  
ANISOU 3059  CG  GLU B  89    11614  15103  10610   -969  -1048   -654       C  
ATOM   3060  CD  GLU B  89      11.034  16.709 -10.860  1.00113.82           C  
ANISOU 3060  CD  GLU B  89    13625  16960  12663  -1130  -1072   -755       C  
ATOM   3061  OE1 GLU B  89      11.810  17.588 -10.427  1.00119.12           O  
ANISOU 3061  OE1 GLU B  89    14311  17735  13215  -1324  -1159   -854       O  
ATOM   3062  OE2 GLU B  89      10.671  16.651 -12.055  1.00118.65           O1-
ANISOU 3062  OE2 GLU B  89    14257  17377  13446  -1075  -1005   -735       O1-
ATOM   3063  N   ASP B  90       8.960  13.079  -8.117  1.00 53.48           N  
ANISOU 3063  N   ASP B  90     5914   9592   4813   -593   -940   -380       N  
ATOM   3064  CA  ASP B  90       7.740  12.324  -8.368  1.00 47.39           C  
ANISOU 3064  CA  ASP B  90     5200   8675   4133   -450   -823   -315       C  
ATOM   3065  C   ASP B  90       7.260  11.599  -7.104  1.00 47.14           C  
ANISOU 3065  C   ASP B  90     5186   8781   3945   -380   -805   -237       C  
ATOM   3066  O   ASP B  90       6.180  11.015  -7.091  1.00 48.37           O  
ANISOU 3066  O   ASP B  90     5395   8846   4137   -289   -707   -192       O  
ATOM   3067  CB  ASP B  90       7.957  11.307  -9.491  1.00 45.03           C  
ANISOU 3067  CB  ASP B  90     4815   8288   4008   -344   -789   -165       C  
ATOM   3068  CG  ASP B  90       8.315  11.964 -10.837  1.00 52.96           C  
ANISOU 3068  CG  ASP B  90     5807   9147   5171   -407   -790   -234       C  
ATOM   3069  OD1 ASP B  90       7.690  12.980 -11.214  1.00 45.64           O  
ANISOU 3069  OD1 ASP B  90     4989   8065   4288   -472   -755   -380       O  
ATOM   3070  OD2 ASP B  90       9.220  11.448 -11.523  1.00 54.62           O1-
ANISOU 3070  OD2 ASP B  90     5901   9397   5455   -381   -822   -136       O1-
ATOM   3071  N   THR B  91       8.072  11.617  -6.054  1.00 50.21           N  
ANISOU 3071  N   THR B  91     5525   9399   4153   -431   -902   -217       N  
ATOM   3072  CA  THR B  91       7.664  11.024  -4.781  1.00 54.07           C  
ANISOU 3072  CA  THR B  91     6043  10033   4467   -379   -893   -148       C  
ATOM   3073  C   THR B  91       6.505  11.816  -4.178  1.00 58.65           C  
ANISOU 3073  C   THR B  91     6764  10554   4966   -417   -818   -309       C  
ATOM   3074  O   THR B  91       6.628  13.011  -3.908  1.00 57.23           O  
ANISOU 3074  O   THR B  91     6652  10381   4713   -532   -855   -488       O  
ATOM   3075  CB  THR B  91       8.832  10.966  -3.792  1.00 57.17           C  
ANISOU 3075  CB  THR B  91     6349  10704   4668   -431  -1025   -100       C  
ATOM   3076  OG1 THR B  91       9.740   9.942  -4.215  1.00 55.42           O  
ANISOU 3076  OG1 THR B  91     5991  10559   4507   -335  -1076     88       O  
ATOM   3077  CG2 THR B  91       8.340  10.667  -2.344  1.00 49.23           C  
ANISOU 3077  CG2 THR B  91     5407   9856   3445   -411  -1019    -73       C  
ATOM   3078  N   ALA B  92       5.386  11.132  -3.963  1.00 52.33           N  
ANISOU 3078  N   ALA B  92     6011   9700   4170   -322   -710   -246       N  
ATOM   3079  CA  ALA B  92       4.134  11.778  -3.594  1.00 49.80           C  
ANISOU 3079  CA  ALA B  92     5804   9314   3803   -325   -614   -389       C  
ATOM   3080  C   ALA B  92       3.073  10.733  -3.303  1.00 50.89           C  
ANISOU 3080  C   ALA B  92     5953   9451   3932   -230   -503   -268       C  
ATOM   3081  O   ALA B  92       3.233   9.553  -3.642  1.00 44.64           O  
ANISOU 3081  O   ALA B  92     5106   8643   3211   -164   -493    -82       O  
ATOM   3082  CB  ALA B  92       3.645  12.707  -4.743  1.00 44.51           C  
ANISOU 3082  CB  ALA B  92     5189   8416   3309   -338   -565   -536       C  
ATOM   3083  N   VAL B  93       1.970  11.177  -2.709  1.00 52.63           N  
ANISOU 3083  N   VAL B  93     6251   9685   4063   -224   -415   -377       N  
ATOM   3084  CA  VAL B  93       0.757  10.375  -2.706  1.00 50.67           C  
ANISOU 3084  CA  VAL B  93     6008   9404   3840   -155   -288   -295       C  
ATOM   3085  C   VAL B  93      -0.022  10.720  -3.974  1.00 46.75           C  
ANISOU 3085  C   VAL B  93     5515   8697   3551   -118   -212   -369       C  
ATOM   3086  O   VAL B  93      -0.311  11.881  -4.231  1.00 46.25           O  
ANISOU 3086  O   VAL B  93     5505   8556   3513   -128   -204   -550       O  
ATOM   3087  CB  VAL B  93      -0.123  10.627  -1.462  1.00 50.56           C  
ANISOU 3087  CB  VAL B  93     6053   9537   3620   -159   -217   -370       C  
ATOM   3088  CG1 VAL B  93      -1.351   9.738  -1.521  1.00 48.05           C  
ANISOU 3088  CG1 VAL B  93     5721   9203   3331   -109    -83   -272       C  
ATOM   3089  CG2 VAL B  93       0.669  10.397  -0.166  1.00 50.41           C  
ANISOU 3089  CG2 VAL B  93     6040   9739   3373   -203   -302   -310       C  
ATOM   3090  N   TYR B  94      -0.345   9.713  -4.775  1.00 45.04           N  
ANISOU 3090  N   TYR B  94     5253   8382   3478    -74   -162   -229       N  
ATOM   3091  CA  TYR B  94      -1.074   9.937  -6.009  1.00 42.59           C  
ANISOU 3091  CA  TYR B  94     4936   7887   3358    -41    -97   -283       C  
ATOM   3092  C   TYR B  94      -2.546   9.629  -5.791  1.00 48.86           C  
ANISOU 3092  C   TYR B  94     5733   8707   4126     -9     34   -288       C  
ATOM   3093  O   TYR B  94      -2.890   8.586  -5.235  1.00 48.45           O  
ANISOU 3093  O   TYR B  94     5668   8741   3999    -15     82   -150       O  
ATOM   3094  CB  TYR B  94      -0.491   9.081  -7.136  1.00 41.38           C  
ANISOU 3094  CB  TYR B  94     4733   7608   3381    -23   -124   -143       C  
ATOM   3095  CG  TYR B  94       0.800   9.646  -7.675  1.00 41.46           C  
ANISOU 3095  CG  TYR B  94     4721   7576   3455    -53   -235   -179       C  
ATOM   3096  CD1 TYR B  94       1.952   9.635  -6.901  1.00 43.49           C  
ANISOU 3096  CD1 TYR B  94     4955   7982   3588    -88   -337   -139       C  
ATOM   3097  CD2 TYR B  94       0.864  10.201  -8.953  1.00 42.46           C  
ANISOU 3097  CD2 TYR B  94     4844   7533   3755    -54   -239   -249       C  
ATOM   3098  CE1 TYR B  94       3.136  10.154  -7.371  1.00 49.97           C  
ANISOU 3098  CE1 TYR B  94     5736   8796   4454   -134   -437   -172       C  
ATOM   3099  CE2 TYR B  94       2.052  10.731  -9.438  1.00 42.28           C  
ANISOU 3099  CE2 TYR B  94     4798   7488   3780   -102   -335   -280       C  
ATOM   3100  CZ  TYR B  94       3.182  10.697  -8.637  1.00 46.55           C  
ANISOU 3100  CZ  TYR B  94     5302   8191   4194   -146   -431   -242       C  
ATOM   3101  OH  TYR B  94       4.362  11.216  -9.081  1.00 46.10           O  
ANISOU 3101  OH  TYR B  94     5201   8144   4170   -210   -525   -272       O  
ATOM   3102  N   TYR B  95      -3.407  10.550  -6.208  1.00 45.26           N  
ANISOU 3102  N   TYR B  95     5295   8183   3721     25     90   -445       N  
ATOM   3103  CA  TYR B  95      -4.844  10.365  -6.065  1.00 45.61           C  
ANISOU 3103  CA  TYR B  95     5313   8276   3739     62    216   -466       C  
ATOM   3104  C   TYR B  95      -5.528  10.264  -7.419  1.00 45.11           C  
ANISOU 3104  C   TYR B  95     5207   8061   3872     97    263   -466       C  
ATOM   3105  O   TYR B  95      -5.288  11.068  -8.327  1.00 44.87           O  
ANISOU 3105  O   TYR B  95     5197   7887   3964    126    222   -561       O  
ATOM   3106  CB  TYR B  95      -5.490  11.507  -5.276  1.00 46.04           C  
ANISOU 3106  CB  TYR B  95     5415   8423   3656    101    259   -655       C  
ATOM   3107  CG  TYR B  95      -4.865  11.837  -3.945  1.00 48.85           C  
ANISOU 3107  CG  TYR B  95     5829   8929   3801     62    210   -697       C  
ATOM   3108  CD1 TYR B  95      -3.801  12.721  -3.863  1.00 47.83           C  
ANISOU 3108  CD1 TYR B  95     5768   8756   3649     27    100   -795       C  
ATOM   3109  CD2 TYR B  95      -5.368  11.301  -2.760  1.00 45.31           C  
ANISOU 3109  CD2 TYR B  95     5372   8678   3166     48    274   -644       C  
ATOM   3110  CE1 TYR B  95      -3.240  13.053  -2.647  1.00 53.87           C  
ANISOU 3110  CE1 TYR B  95     6587   9670   4212    -22     48   -843       C  
ATOM   3111  CE2 TYR B  95      -4.808  11.626  -1.533  1.00 52.41           C  
ANISOU 3111  CE2 TYR B  95     6328   9726   3858     11    226   -687       C  
ATOM   3112  CZ  TYR B  95      -3.739  12.502  -1.487  1.00 56.05           C  
ANISOU 3112  CZ  TYR B  95     6853  10141   4301    -23    109   -790       C  
ATOM   3113  OH  TYR B  95      -3.170  12.839  -0.288  1.00 60.93           O  
ANISOU 3113  OH  TYR B  95     7528  10915   4707    -74     53   -840       O  
ATOM   3114  N   CYS B  96      -6.396   9.269  -7.527  1.00 45.69           N  
ANISOU 3114  N   CYS B  96     5225   8172   3963     84    350   -358       N  
ATOM   3115  CA  CYS B  96      -7.336   9.126  -8.629  1.00 47.91           C  
ANISOU 3115  CA  CYS B  96     5451   8364   4389    108    414   -365       C  
ATOM   3116  C   CYS B  96      -8.512  10.081  -8.409  1.00 44.59           C  
ANISOU 3116  C   CYS B  96     5003   8026   3912    181    491   -528       C  
ATOM   3117  O   CYS B  96      -9.032  10.170  -7.304  1.00 46.25           O  
ANISOU 3117  O   CYS B  96     5208   8410   3956    185    551   -563       O  
ATOM   3118  CB  CYS B  96      -7.811   7.666  -8.702  1.00 57.88           C  
ANISOU 3118  CB  CYS B  96     6674   9653   5664     40    477   -188       C  
ATOM   3119  SG  CYS B  96      -9.001   7.235 -10.017  1.00 81.51           S  
ANISOU 3119  SG  CYS B  96     9588  12566   8816     29    554   -173       S  
ATOM   3120  N   ALA B  97      -8.926  10.802  -9.444  1.00 48.51           N  
ANISOU 3120  N   ALA B  97     5486   8407   4538    249    491   -626       N  
ATOM   3121  CA  ALA B  97     -10.122  11.642  -9.350  1.00 48.12           C  
ANISOU 3121  CA  ALA B  97     5401   8437   4445    350    569   -770       C  
ATOM   3122  C   ALA B  97     -11.172  11.234 -10.398  1.00 45.61           C  
ANISOU 3122  C   ALA B  97     4977   8103   4248    369    629   -736       C  
ATOM   3123  O   ALA B  97     -10.824  10.935 -11.542  1.00 44.94           O  
ANISOU 3123  O   ALA B  97     4891   7862   4322    344    582   -678       O  
ATOM   3124  CB  ALA B  97      -9.758  13.108  -9.509  1.00 51.96           C  
ANISOU 3124  CB  ALA B  97     5986   8814   4943    442    513   -945       C  
ATOM   3125  N   ALA B  98     -12.444  11.225 -10.001  1.00 50.04           N  
ANISOU 3125  N   ALA B  98     5443   8844   4726    410    733   -776       N  
ATOM   3126  CA  ALA B  98     -13.542  10.773 -10.865  1.00 53.53           C  
ANISOU 3126  CA  ALA B  98     5758   9326   5253    410    795   -742       C  
ATOM   3127  C   ALA B  98     -14.689  11.775 -10.969  1.00 61.78           C  
ANISOU 3127  C   ALA B  98     6730  10475   6268    567    855   -894       C  
ATOM   3128  O   ALA B  98     -14.989  12.509 -10.011  1.00 61.54           O  
ANISOU 3128  O   ALA B  98     6718  10566   6097    659    899  -1008       O  
ATOM   3129  CB  ALA B  98     -14.093   9.429 -10.368  1.00 46.53           C  
ANISOU 3129  CB  ALA B  98     4789   8598   4293    270    875   -597       C  
ATOM   3130  N   ARG B  99     -15.338  11.772 -12.132  1.00 57.65           N  
ANISOU 3130  N   ARG B  99     6122   9911   5870    605    858   -894       N  
ATOM   3131  CA  ARG B  99     -16.572  12.525 -12.360  1.00 63.78           C  
ANISOU 3131  CA  ARG B  99     6792  10816   6625    761    919  -1011       C  
ATOM   3132  C   ARG B  99     -17.813  11.639 -12.271  1.00 65.53           C  
ANISOU 3132  C   ARG B  99     6819  11286   6793    688   1023   -943       C  
ATOM   3133  O   ARG B  99     -17.808  10.489 -12.730  1.00 64.05           O  
ANISOU 3133  O   ARG B  99     6584  11084   6667    520   1023   -804       O  
ATOM   3134  CB  ARG B  99     -16.560  13.203 -13.734  1.00 61.53           C  
ANISOU 3134  CB  ARG B  99     6530  10348   6498    865    850  -1061       C  
ATOM   3135  CG  ARG B  99     -15.350  14.072 -14.007  1.00 70.87           C  
ANISOU 3135  CG  ARG B  99     7906  11275   7747    911    747  -1121       C  
ATOM   3136  CD  ARG B  99     -15.682  15.184 -14.988  1.00 77.90           C  
ANISOU 3136  CD  ARG B  99     8832  12041   8724   1083    710  -1225       C  
ATOM   3137  NE  ARG B  99     -14.479  15.803 -15.540  1.00 91.61           N  
ANISOU 3137  NE  ARG B  99    10745  13510  10551   1072    607  -1246       N  
ATOM   3138  CZ  ARG B  99     -13.752  16.722 -14.913  1.00 97.52           C  
ANISOU 3138  CZ  ARG B  99    11658  14160  11238   1111    570  -1345       C  
ATOM   3139  NH1 ARG B  99     -14.099  17.132 -13.703  1.00 94.55           N  
ANISOU 3139  NH1 ARG B  99    11299  13920  10705   1179    628  -1438       N  
ATOM   3140  NH2 ARG B  99     -12.672  17.227 -15.497  1.00101.96           N  
ANISOU 3140  NH2 ARG B  99    12366  14492  11884   1071    477  -1354       N  
ATOM   3141  N   ALA B 100     -18.876  12.191 -11.691  1.00 59.69           N  
ANISOU 3141  N   ALA B 100     5971  10775   5934    814   1112  -1045       N  
ATOM   3142  CA  ALA B 100     -20.205  11.597 -11.780  1.00 62.60           C  
ANISOU 3142  CA  ALA B 100     6120  11407   6256    772   1210  -1009       C  
ATOM   3143  C   ALA B 100     -20.741  11.760 -13.202  1.00 71.50           C  
ANISOU 3143  C   ALA B 100     7156  12482   7530    834   1169  -1017       C  
ATOM   3144  O   ALA B 100     -20.423  12.741 -13.875  1.00 68.01           O  
ANISOU 3144  O   ALA B 100     6801  11862   7176    998   1096  -1105       O  
ATOM   3145  CB  ALA B 100     -21.142  12.239 -10.780  1.00 61.88           C  
ANISOU 3145  CB  ALA B 100     5930  11591   5992    917   1317  -1128       C  
ATOM   3146  N   PRO B 101     -21.555  10.800 -13.666  1.00 82.77           N  
ANISOU 3146  N   PRO B 101     8414  14063   8974    693   1215   -924       N  
ATOM   3147  CA  PRO B 101     -22.110  10.887 -15.023  1.00 92.81           C  
ANISOU 3147  CA  PRO B 101     9584  15311  10369    735   1172   -927       C  
ATOM   3148  C   PRO B 101     -22.985  12.127 -15.218  1.00 97.13           C  
ANISOU 3148  C   PRO B 101    10057  15947  10900   1000   1171  -1062       C  
ATOM   3149  O   PRO B 101     -23.115  12.606 -16.348  1.00100.81           O  
ANISOU 3149  O   PRO B 101    10515  16311  11476   1107   1104  -1091       O  
ATOM   3150  CB  PRO B 101     -22.938   9.604 -15.149  1.00 94.20           C  
ANISOU 3150  CB  PRO B 101     9587  15692  10515    507   1239   -811       C  
ATOM   3151  CG  PRO B 101     -22.374   8.676 -14.117  1.00 93.45           C  
ANISOU 3151  CG  PRO B 101     9582  15591  10334    310   1282   -707       C  
ATOM   3152  CD  PRO B 101     -21.963   9.562 -12.981  1.00 86.12           C  
ANISOU 3152  CD  PRO B 101     8748  14678   9297    466   1301   -805       C  
ATOM   3153  N   VAL B 102     -23.571  12.632 -14.132  1.00 96.21           N  
ANISOU 3153  N   VAL B 102     9925  15971  10660   1096   1223  -1127       N  
ATOM   3154  CA  VAL B 102     -24.334  13.876 -14.174  1.00 97.86           C  
ANISOU 3154  CA  VAL B 102    10124  16204  10855   1356   1205  -1244       C  
ATOM   3155  C   VAL B 102     -23.402  15.084 -14.220  1.00103.40           C  
ANISOU 3155  C   VAL B 102    11035  16666  11588   1557   1152  -1362       C  
ATOM   3156  O   VAL B 102     -23.039  15.562 -15.297  1.00108.84           O  
ANISOU 3156  O   VAL B 102    11791  17170  12394   1647   1077  -1385       O  
ATOM   3157  CB  VAL B 102     -25.276  14.020 -12.961  1.00 98.45           C  
ANISOU 3157  CB  VAL B 102    10113  16512  10781   1395   1284  -1277       C  
ATOM   3158  CG1 VAL B 102     -26.487  13.104 -13.104  1.00 98.10           C  
ANISOU 3158  CG1 VAL B 102     9849  16714  10710   1244   1322  -1185       C  
ATOM   3159  CG2 VAL B 102     -24.523  13.756 -11.659  1.00 93.59           C  
ANISOU 3159  CG2 VAL B 102     9602  15907  10049   1304   1340  -1278       C  
ATOM   3160  N   ASP B 110     -12.894  20.463 -12.401  1.00111.50           N  
ANISOU 3160  N   ASP B 110    13972  15735  12657   1395    544  -1840       N  
ATOM   3161  CA  ASP B 110     -13.069  20.044 -11.014  1.00113.04           C  
ANISOU 3161  CA  ASP B 110    14114  16153  12683   1357    610  -1855       C  
ATOM   3162  C   ASP B 110     -13.720  18.663 -10.957  1.00107.17           C  
ANISOU 3162  C   ASP B 110    13137  15636  11946   1284    678  -1706       C  
ATOM   3163  O   ASP B 110     -14.448  18.280 -11.871  1.00106.31           O  
ANISOU 3163  O   ASP B 110    12899  15553  11942   1327    701  -1644       O  
ATOM   3164  CB  ASP B 110     -13.904  21.071 -10.247  1.00117.00           C  
ANISOU 3164  CB  ASP B 110    14689  16725  13040   1563    685  -2037       C  
ATOM   3165  CG  ASP B 110     -13.770  20.928  -8.745  1.00123.32           C  
ANISOU 3165  CG  ASP B 110    15508  17704  13644   1509    732  -2085       C  
ATOM   3166  OD1 ASP B 110     -13.868  19.790  -8.243  1.00126.13           O  
ANISOU 3166  OD1 ASP B 110    15710  18261  13955   1388    772  -1962       O  
ATOM   3167  OD2 ASP B 110     -13.558  21.953  -8.063  1.00125.87           O  
ANISOU 3167  OD2 ASP B 110    16016  17959  13851   1581    729  -2247       O  
ATOM   3168  N   TYR B 111     -13.462  17.922  -9.882  1.00 97.47           N  
ANISOU 3168  N   TYR B 111    11866  14571  10599   1163    707  -1647       N  
ATOM   3169  CA  TYR B 111     -13.914  16.533  -9.788  1.00 82.64           C  
ANISOU 3169  CA  TYR B 111     9802  12876   8720   1052    764  -1488       C  
ATOM   3170  C   TYR B 111     -14.821  16.291  -8.596  1.00 79.50           C  
ANISOU 3170  C   TYR B 111     9310  12757   8138   1087    880  -1519       C  
ATOM   3171  O   TYR B 111     -14.736  16.984  -7.580  1.00 86.06           O  
ANISOU 3171  O   TYR B 111    10236  13645   8818   1148    902  -1640       O  
ATOM   3172  CB  TYR B 111     -12.716  15.582  -9.720  1.00 73.41           C  
ANISOU 3172  CB  TYR B 111     8660  11645   7589    852    690  -1338       C  
ATOM   3173  CG  TYR B 111     -11.879  15.601 -10.973  1.00 65.16           C  
ANISOU 3173  CG  TYR B 111     7669  10362   6729    803    591  -1283       C  
ATOM   3174  CD1 TYR B 111     -10.914  16.576 -11.164  1.00 67.06           C  
ANISOU 3174  CD1 TYR B 111     8070  10413   6997    811    501  -1371       C  
ATOM   3175  CD2 TYR B 111     -12.065  14.657 -11.973  1.00 66.00           C  
ANISOU 3175  CD2 TYR B 111     7670  10436   6972    740    590  -1149       C  
ATOM   3176  CE1 TYR B 111     -10.153  16.612 -12.306  1.00 68.41           C  
ANISOU 3176  CE1 TYR B 111     8283  10384   7325    760    418  -1320       C  
ATOM   3177  CE2 TYR B 111     -11.303  14.685 -13.127  1.00 68.19           C  
ANISOU 3177  CE2 TYR B 111     7996  10506   7408    701    506  -1105       C  
ATOM   3178  CZ  TYR B 111     -10.347  15.669 -13.285  1.00 68.76           C  
ANISOU 3178  CZ  TYR B 111     8216  10407   7503    713    423  -1188       C  
ATOM   3179  OH  TYR B 111      -9.576  15.716 -14.421  1.00 74.35           O  
ANISOU 3179  OH  TYR B 111     8968  10925   8357    666    346  -1144       O  
ATOM   3180  N   ASP B 112     -15.679  15.286  -8.719  1.00 69.18           N  
ANISOU 3180  N   ASP B 112     7821  11628   6837   1033    957  -1409       N  
ATOM   3181  CA  ASP B 112     -16.669  15.006  -7.686  1.00 72.45           C  
ANISOU 3181  CA  ASP B 112     8117  12335   7077   1056   1082  -1428       C  
ATOM   3182  C   ASP B 112     -16.191  13.988  -6.648  1.00 64.92           C  
ANISOU 3182  C   ASP B 112     7165  11500   6002    871   1100  -1304       C  
ATOM   3183  O   ASP B 112     -16.695  13.953  -5.527  1.00 70.28           O  
ANISOU 3183  O   ASP B 112     7805  12400   6496    882   1190  -1339       O  
ATOM   3184  CB  ASP B 112     -17.963  14.513  -8.336  1.00 76.95           C  
ANISOU 3184  CB  ASP B 112     8474  13067   7696   1084   1164  -1382       C  
ATOM   3185  CG  ASP B 112     -18.424  15.414  -9.468  1.00 79.86           C  
ANISOU 3185  CG  ASP B 112     8832  13321   8190   1269   1133  -1478       C  
ATOM   3186  OD1 ASP B 112     -19.016  16.474  -9.174  1.00 89.78           O  
ANISOU 3186  OD1 ASP B 112    10106  14637   9370   1480   1178  -1637       O  
ATOM   3187  OD2 ASP B 112     -18.200  15.062 -10.648  1.00 73.82           O1-
ANISOU 3187  OD2 ASP B 112     8049  12404   7594   1212   1066  -1395       O1-
ATOM   3188  N   TYR B 113     -15.231  13.152  -7.032  1.00 60.57           N  
ANISOU 3188  N   TYR B 113     6659  10808   5548    713   1018  -1154       N  
ATOM   3189  CA  TYR B 113     -14.783  12.059  -6.172  1.00 60.46           C  
ANISOU 3189  CA  TYR B 113     6651  10891   5432    546   1028  -1007       C  
ATOM   3190  C   TYR B 113     -13.273  11.875  -6.249  1.00 53.77           C  
ANISOU 3190  C   TYR B 113     5939   9850   4643    461    901   -936       C  
ATOM   3191  O   TYR B 113     -12.653  12.090  -7.302  1.00 53.45           O  
ANISOU 3191  O   TYR B 113     5943   9596   4771    470    814   -931       O  
ATOM   3192  CB  TYR B 113     -15.473  10.737  -6.543  1.00 63.51           C  
ANISOU 3192  CB  TYR B 113     6901  11371   5860    417   1094   -841       C  
ATOM   3193  CG  TYR B 113     -16.985  10.803  -6.657  1.00 66.02           C  
ANISOU 3193  CG  TYR B 113     7045  11900   6139    475   1214   -893       C  
ATOM   3194  CD1 TYR B 113     -17.789  10.905  -5.525  1.00 63.21           C  
ANISOU 3194  CD1 TYR B 113     6617  11817   5584    501   1329   -946       C  
ATOM   3195  CD2 TYR B 113     -17.608  10.737  -7.904  1.00 62.79           C  
ANISOU 3195  CD2 TYR B 113     6532  11441   5885    502   1213   -887       C  
ATOM   3196  CE1 TYR B 113     -19.179  10.958  -5.630  1.00 66.62           C  
ANISOU 3196  CE1 TYR B 113     6864  12477   5973    558   1443   -993       C  
ATOM   3197  CE2 TYR B 113     -18.987  10.790  -8.023  1.00 67.19           C  
ANISOU 3197  CE2 TYR B 113     6907  12222   6401    556   1317   -932       C  
ATOM   3198  CZ  TYR B 113     -19.767  10.900  -6.884  1.00 73.93           C  
ANISOU 3198  CZ  TYR B 113     7676  13356   7057    585   1433   -984       C  
ATOM   3199  OH  TYR B 113     -21.134  10.949  -7.007  1.00 78.79           O  
ANISOU 3199  OH  TYR B 113     8118  14151   7668    629   1502  -1009       O  
ATOM   3200  N   TRP B 114     -12.700  11.426  -5.137  1.00 50.57           N  
ANISOU 3200  N   TRP B 114     5586   9538   4088    376    893   -871       N  
ATOM   3201  CA  TRP B 114     -11.253  11.332  -4.961  1.00 56.40           C  
ANISOU 3201  CA  TRP B 114     6440  10153   4836    309    772   -815       C  
ATOM   3202  C   TRP B 114     -10.872  10.022  -4.292  1.00 55.86           C  
ANISOU 3202  C   TRP B 114     6367  10175   4684    178    775   -620       C  
ATOM   3203  O   TRP B 114     -11.519   9.606  -3.346  1.00 53.20           O  
ANISOU 3203  O   TRP B 114     5994  10036   4184    143    864   -585       O  
ATOM   3204  CB  TRP B 114     -10.751  12.503  -4.113  1.00 62.51           C  
ANISOU 3204  CB  TRP B 114     7325  10949   5475    370    731   -981       C  
ATOM   3205  CG  TRP B 114     -10.976  13.818  -4.756  1.00 68.50           C  
ANISOU 3205  CG  TRP B 114     8135  11578   6313    499    716  -1167       C  
ATOM   3206  CD1 TRP B 114     -12.121  14.561  -4.738  1.00 78.69           C  
ANISOU 3206  CD1 TRP B 114     9391  12940   7566    638    808  -1309       C  
ATOM   3207  CD2 TRP B 114     -10.036  14.547  -5.545  1.00 64.52           C  
ANISOU 3207  CD2 TRP B 114     7731  10847   5938    507    604  -1225       C  
ATOM   3208  NE1 TRP B 114     -11.948  15.714  -5.468  1.00 78.13           N  
ANISOU 3208  NE1 TRP B 114     9413  12678   7593    743    756  -1450       N  
ATOM   3209  CE2 TRP B 114     -10.675  15.727  -5.974  1.00 67.35           C  
ANISOU 3209  CE2 TRP B 114     8134  11125   6330    651    632  -1400       C  
ATOM   3210  CE3 TRP B 114      -8.713  14.316  -5.929  1.00 61.00           C  
ANISOU 3210  CE3 TRP B 114     7338  10266   5575    408    485  -1145       C  
ATOM   3211  CZ2 TRP B 114     -10.032  16.676  -6.756  1.00 68.72           C  
ANISOU 3211  CZ2 TRP B 114     8424  11072   6613    682    545  -1491       C  
ATOM   3212  CZ3 TRP B 114      -8.079  15.257  -6.703  1.00 63.20           C  
ANISOU 3212  CZ3 TRP B 114     7707  10344   5960    430    403  -1239       C  
ATOM   3213  CH2 TRP B 114      -8.737  16.423  -7.112  1.00 67.67           C  
ANISOU 3213  CH2 TRP B 114     8337  10818   6556    557    433  -1408       C  
ATOM   3214  N   GLY B 115      -9.819   9.372  -4.770  1.00 54.13           N  
ANISOU 3214  N   GLY B 115     6188   9812   4565    113    681   -489       N  
ATOM   3215  CA  GLY B 115      -9.320   8.193  -4.086  1.00 53.51           C  
ANISOU 3215  CA  GLY B 115     6135   9799   4397     15    670   -303       C  
ATOM   3216  C   GLY B 115      -8.661   8.576  -2.771  1.00 51.70           C  
ANISOU 3216  C   GLY B 115     5977   9701   3965     11    626   -339       C  
ATOM   3217  O   GLY B 115      -8.359   9.744  -2.532  1.00 51.87           O  
ANISOU 3217  O   GLY B 115     6043   9721   3944     69    583   -508       O  
ATOM   3218  N   GLN B 116      -8.438   7.596  -1.906  1.00 49.09           N  
ANISOU 3218  N   GLN B 116     5669   9481   3501    -62    635   -181       N  
ATOM   3219  CA  GLN B 116      -7.721   7.842  -0.667  1.00 56.18           C  
ANISOU 3219  CA  GLN B 116     6634  10514   4198    -74    580   -192       C  
ATOM   3220  C   GLN B 116      -6.235   8.037  -0.946  1.00 55.11           C  
ANISOU 3220  C   GLN B 116     6546  10265   4128    -69    426   -172       C  
ATOM   3221  O   GLN B 116      -5.501   8.546  -0.110  1.00 48.47           O  
ANISOU 3221  O   GLN B 116     5754   9518   3145    -76    352   -227       O  
ATOM   3222  CB  GLN B 116      -7.940   6.698   0.320  1.00 55.70           C  
ANISOU 3222  CB  GLN B 116     6589  10608   3967   -151    634    -12       C  
ATOM   3223  CG  GLN B 116      -9.347   6.676   0.885  1.00 61.77           C  
ANISOU 3223  CG  GLN B 116     7304  11555   4612   -172    788    -55       C  
ATOM   3224  CD  GLN B 116      -9.414   5.980   2.207  1.00 69.17           C  
ANISOU 3224  CD  GLN B 116     8283  12690   5310   -245    830     68       C  
ATOM   3225  OE1 GLN B 116      -8.867   6.460   3.203  1.00 70.32           O  
ANISOU 3225  OE1 GLN B 116     8485  12956   5279   -230    780     12       O  
ATOM   3226  NE2 GLN B 116     -10.067   4.828   2.231  1.00 78.05           N  
ANISOU 3226  NE2 GLN B 116     9392  13848   6417   -336    918    239       N  
ATOM   3227  N   GLY B 117      -5.805   7.645  -2.142  1.00 55.55           N  
ANISOU 3227  N   GLY B 117     6581  10133   4393    -62    379   -100       N  
ATOM   3228  CA  GLY B 117      -4.448   7.903  -2.579  1.00 58.79           C  
ANISOU 3228  CA  GLY B 117     7012  10442   4885    -53    243    -94       C  
ATOM   3229  C   GLY B 117      -3.526   6.706  -2.489  1.00 61.26           C  
ANISOU 3229  C   GLY B 117     7333  10746   5195    -71    177    122       C  
ATOM   3230  O   GLY B 117      -3.762   5.767  -1.734  1.00 63.54           O  
ANISOU 3230  O   GLY B 117     7646  11134   5362    -97    217    267       O  
ATOM   3231  N   THR B 118      -2.453   6.743  -3.266  1.00 54.54           N  
ANISOU 3231  N   THR B 118     6469   9780   4475    -51     76    147       N  
ATOM   3232  CA  THR B 118      -1.436   5.705  -3.187  1.00 57.83           C  
ANISOU 3232  CA  THR B 118     6890  10198   4886    -36      0    341       C  
ATOM   3233  C   THR B 118      -0.048   6.314  -3.093  1.00 53.23           C  
ANISOU 3233  C   THR B 118     6281   9663   4279    -30   -140    299       C  
ATOM   3234  O   THR B 118       0.299   7.224  -3.850  1.00 53.68           O  
ANISOU 3234  O   THR B 118     6313   9633   4450    -38   -182    166       O  
ATOM   3235  CB  THR B 118      -1.501   4.763  -4.399  1.00 71.78           C  
ANISOU 3235  CB  THR B 118     8649  11773   6851     -9     30    463       C  
ATOM   3236  OG1 THR B 118      -2.828   4.239  -4.512  1.00 83.22           O  
ANISOU 3236  OG1 THR B 118    10114  13189   8316    -43    158    493       O  
ATOM   3237  CG2 THR B 118      -0.528   3.612  -4.223  1.00 71.67           C  
ANISOU 3237  CG2 THR B 118     8660  11761   6813     34    -35    671       C  
ATOM   3238  N   GLN B 119       0.746   5.810  -2.158  1.00 52.69           N  
ANISOU 3238  N   GLN B 119     6220   9745   4056    -22   -214    416       N  
ATOM   3239  CA  GLN B 119       2.096   6.305  -1.972  1.00 53.10           C  
ANISOU 3239  CA  GLN B 119     6227   9889   4061    -27   -355    389       C  
ATOM   3240  C   GLN B 119       2.993   5.865  -3.128  1.00 55.15           C  
ANISOU 3240  C   GLN B 119     6426  10023   4506     26   -413    475       C  
ATOM   3241  O   GLN B 119       3.098   4.677  -3.445  1.00 53.79           O  
ANISOU 3241  O   GLN B 119     6262   9783   4393     96   -394    656       O  
ATOM   3242  CB  GLN B 119       2.665   5.823  -0.635  1.00 54.47           C  
ANISOU 3242  CB  GLN B 119     6412  10281   4002    -23   -422    504       C  
ATOM   3243  CG  GLN B 119       4.108   6.231  -0.400  1.00 59.03           C  
ANISOU 3243  CG  GLN B 119     6920  10994   4514    -32   -577    495       C  
ATOM   3244  CD  GLN B 119       4.296   7.733  -0.410  1.00 58.46           C  
ANISOU 3244  CD  GLN B 119     6841  10948   4424   -129   -622    256       C  
ATOM   3245  OE1 GLN B 119       5.127   8.261  -1.144  1.00 64.15           O  
ANISOU 3245  OE1 GLN B 119     7499  11624   5249   -156   -698    196       O  
ATOM   3246  NE2 GLN B 119       3.523   8.428   0.401  1.00 53.47           N  
ANISOU 3246  NE2 GLN B 119     6280  10384   3652   -183   -570    118       N  
ATOM   3247  N   VAL B 120       3.620   6.834  -3.780  1.00 48.47           N  
ANISOU 3247  N   VAL B 120     5531   9138   3749    -11   -477    342       N  
ATOM   3248  CA  VAL B 120       4.698   6.520  -4.703  1.00 50.97           C  
ANISOU 3248  CA  VAL B 120     5769   9398   4198     32   -550    417       C  
ATOM   3249  C   VAL B 120       6.002   7.064  -4.132  1.00 45.26           C  
ANISOU 3249  C   VAL B 120     4973   8872   3353    -11   -689    389       C  
ATOM   3250  O   VAL B 120       6.132   8.257  -3.880  1.00 54.35           O  
ANISOU 3250  O   VAL B 120     6131  10075   4445   -113   -730    216       O  
ATOM   3251  CB  VAL B 120       4.442   7.089  -6.095  1.00 49.41           C  
ANISOU 3251  CB  VAL B 120     5563   8997   4215     14   -510    310       C  
ATOM   3252  CG1 VAL B 120       5.719   7.049  -6.939  1.00 50.63           C  
ANISOU 3252  CG1 VAL B 120     5623   9141   4473     33   -596    351       C  
ATOM   3253  CG2 VAL B 120       3.323   6.319  -6.764  1.00 44.43           C  
ANISOU 3253  CG2 VAL B 120     4981   8192   3709     62   -388    373       C  
ATOM   3254  N   THR B 121       6.956   6.172  -3.901  1.00 50.42           N  
ANISOU 3254  N   THR B 121     5561   9638   3959     69   -764    561       N  
ATOM   3255  CA  THR B 121       8.226   6.553  -3.293  1.00 62.00           C  
ANISOU 3255  CA  THR B 121     6931  11336   5290     34   -906    558       C  
ATOM   3256  C   THR B 121       9.375   6.203  -4.221  1.00 58.04           C  
ANISOU 3256  C   THR B 121     6305  10837   4912     99   -973    640       C  
ATOM   3257  O   THR B 121       9.622   5.029  -4.508  1.00 56.56           O  
ANISOU 3257  O   THR B 121     6100  10613   4777    242   -961    821       O  
ATOM   3258  CB  THR B 121       8.437   5.860  -1.927  1.00 61.38           C  
ANISOU 3258  CB  THR B 121     6866  11470   4987     83   -956    695       C  
ATOM   3259  OG1 THR B 121       7.414   6.275  -1.012  1.00 64.84           O  
ANISOU 3259  OG1 THR B 121     7411  11935   5288     11   -892    603       O  
ATOM   3260  CG2 THR B 121       9.794   6.206  -1.340  1.00 59.42           C  
ANISOU 3260  CG2 THR B 121     6497  11487   4594     51  -1114    700       C  
ATOM   3261  N   VAL B 122      10.072   7.227  -4.695  1.00 55.50           N  
ANISOU 3261  N   VAL B 122     5903  10553   4630     -8  -1038    505       N  
ATOM   3262  CA  VAL B 122      11.238   7.017  -5.544  1.00 57.05           C  
ANISOU 3262  CA  VAL B 122     5958  10795   4924     35  -1104    568       C  
ATOM   3263  C   VAL B 122      12.516   7.094  -4.697  1.00 64.20           C  
ANISOU 3263  C   VAL B 122     6725  12019   5648     15  -1251    614       C  
ATOM   3264  O   VAL B 122      12.925   8.166  -4.243  1.00 70.66           O  
ANISOU 3264  O   VAL B 122     7512  12976   6360   -150  -1328    473       O  
ATOM   3265  CB  VAL B 122      11.293   8.038  -6.696  1.00 57.79           C  
ANISOU 3265  CB  VAL B 122     6036  10746   5176    -81  -1083    408       C  
ATOM   3266  CG1 VAL B 122      12.330   7.616  -7.713  1.00 56.54           C  
ANISOU 3266  CG1 VAL B 122     5736  10609   5138    -12  -1118    494       C  
ATOM   3267  CG2 VAL B 122       9.925   8.157  -7.359  1.00 53.07           C  
ANISOU 3267  CG2 VAL B 122     5578   9866   4720    -77   -949    337       C  
ATOM   3268  N   SER B 123      13.131   5.942  -4.470  1.00 58.60           N  
ANISOU 3268  N   SER B 123     5943  11425   4897    185  -1293    814       N  
ATOM   3269  CA  SER B 123      14.306   5.879  -3.617  1.00 61.92           C  
ANISOU 3269  CA  SER B 123     6220  12173   5132    196  -1437    884       C  
ATOM   3270  C   SER B 123      15.279   4.823  -4.099  1.00 64.27           C  
ANISOU 3270  C   SER B 123     6383  12555   5482    399  -1480   1074       C  
ATOM   3271  O   SER B 123      14.883   3.840  -4.731  1.00 67.12           O  
ANISOU 3271  O   SER B 123     6813  12715   5974    563  -1391   1193       O  
ATOM   3272  CB  SER B 123      13.911   5.594  -2.164  1.00 62.01           C  
ANISOU 3272  CB  SER B 123     6318  12322   4922    209  -1465    941       C  
ATOM   3273  OG  SER B 123      15.065   5.435  -1.350  1.00 56.93           O  
ANISOU 3273  OG  SER B 123     5552  11932   4146    234  -1577   1011       O  
ATOM   3274  N   SER B 124      16.552   5.047  -3.784  1.00 64.65           N  
ANISOU 3274  N   SER B 124     6268  12827   5469    375  -1575   1075       N  
ATOM   3275  CA  SER B 124      17.639   4.155  -4.156  1.00 68.83           C  
ANISOU 3275  CA  SER B 124     6667  13418   6066    563  -1591   1220       C  
ATOM   3276  C   SER B 124      17.699   2.925  -3.252  1.00 76.95           C  
ANISOU 3276  C   SER B 124     7756  14483   6998    770  -1597   1414       C  
ATOM   3277  O   SER B 124      18.314   1.922  -3.605  1.00 82.39           O  
ANISOU 3277  O   SER B 124     8398  15156   7751    980  -1586   1559       O  
ATOM   3278  CB  SER B 124      18.970   4.904  -4.103  1.00 65.09           C  
ANISOU 3278  CB  SER B 124     6008  13153   5570    440  -1666   1133       C  
ATOM   3279  OG  SER B 124      19.319   5.217  -2.756  1.00 69.04           O  
ANISOU 3279  OG  SER B 124     6499  13846   5888    356  -1741   1112       O  
ATOM   3280  N   ALA B 125      17.057   2.994  -2.088  1.00 76.18           N  
ANISOU 3280  N   ALA B 125     7777  14426   6743    712  -1610   1414       N  
ATOM   3281  CA  ALA B 125      17.026   1.850  -1.177  1.00 84.59           C  
ANISOU 3281  CA  ALA B 125     8925  15511   7705    889  -1613   1600       C  
ATOM   3282  C   ALA B 125      16.001   0.796  -1.615  1.00 94.29           C  
ANISOU 3282  C   ALA B 125    10330  16494   9003   1043  -1513   1740       C  
ATOM   3283  O   ALA B 125      15.520   0.010  -0.799  1.00 91.94           O  
ANISOU 3283  O   ALA B 125    10170  16158   8603   1127  -1491   1869       O  
ATOM   3284  CB  ALA B 125      16.738   2.314   0.253  1.00 80.15           C  
ANISOU 3284  CB  ALA B 125     8426  15088   6939    761  -1658   1548       C  
ATOM   3285  N   ALA B 126      15.690   0.771  -2.909  1.00108.28           N  
ANISOU 3285  N   ALA B 126    12100  18094  10945   1071  -1451   1717       N  
ATOM   3286  CA  ALA B 126      14.708  -0.157  -3.462  1.00113.72           C  
ANISOU 3286  CA  ALA B 126    12959  18536  11714   1194  -1350   1838       C  
ATOM   3287  C   ALA B 126      15.339  -1.132  -4.455  1.00122.20           C  
ANISOU 3287  C   ALA B 126    14004  19483  12945   1412  -1318   1958       C  
ATOM   3288  O   ALA B 126      16.529  -1.041  -4.758  1.00131.84           O  
ANISOU 3288  O   ALA B 126    15057  20824  14212   1468  -1370   1939       O  
ATOM   3289  CB  ALA B 126      13.580   0.613  -4.129  1.00107.52           C  
ANISOU 3289  CB  ALA B 126    12268  17509  11075   1005  -1233   1651       C  
ATOM   3290  N   ALA B 127      14.533  -2.064  -4.958  1.00117.39           N  
ANISOU 3290  N   ALA B 127    13576  18596  12431   1516  -1211   2059       N  
ATOM   3291  CA  ALA B 127      14.975  -2.996  -5.992  1.00112.09           C  
ANISOU 3291  CA  ALA B 127    12914  17772  11905   1726  -1169   2165       C  
ATOM   3292  C   ALA B 127      13.934  -3.107  -7.102  1.00110.93           C  
ANISOU 3292  C   ALA B 127    12912  17274  11964   1654  -1022   2085       C  
ATOM   3293  O   ALA B 127      14.236  -3.558  -8.208  1.00112.33           O  
ANISOU 3293  O   ALA B 127    13081  17309  12292   1770   -976   2104       O  
ATOM   3294  CB  ALA B 127      15.261  -4.363  -5.397  1.00113.01           C  
ANISOU 3294  CB  ALA B 127    13158  17822  11959   1944  -1163   2366       C  
TER    3295      ALA B 127                                                      
HETATM 3296  CAP 4VO A 401       2.367  15.479 -57.772  1.00 35.23           C  
ANISOU 3296  CAP 4VO A 401     5189   3647   4550   -685     82     83       C  
HETATM 3297  CAO 4VO A 401       1.926  15.561 -56.292  1.00 34.72           C  
ANISOU 3297  CAO 4VO A 401     5064   3550   4578   -614     39     52       C  
HETATM 3298  NBB 4VO A 401       1.131  16.797 -56.074  1.00 40.34           N  
ANISOU 3298  NBB 4VO A 401     5893   4154   5279   -575    -53     79       N  
HETATM 3299  CAB 4VO A 401       0.786  16.930 -54.635  1.00 40.31           C  
ANISOU 3299  CAB 4VO A 401     5836   4127   5354   -510    -85     43       C  
HETATM 3300  CAZ 4VO A 401      -0.092  16.803 -56.917  1.00 32.02           C  
ANISOU 3300  CAZ 4VO A 401     4901   3086   4179   -494   -117     90       C  
HETATM 3301  CAQ 4VO A 401      -1.026  15.576 -56.678  1.00 38.17           C  
ANISOU 3301  CAQ 4VO A 401     5561   3943   4998   -408   -126     33       C  
HETATM 3302  CAW 4VO A 401      -0.724  14.452 -57.486  1.00 39.43           C  
ANISOU 3302  CAW 4VO A 401     5676   4176   5128   -450    -64     11       C  
HETATM 3303  CAM 4VO A 401      -1.498  13.308 -57.318  1.00 36.65           C  
ANISOU 3303  CAM 4VO A 401     5241   3881   4804   -402    -66    -41       C  
HETATM 3304  CAL 4VO A 401      -1.271  12.157 -58.072  1.00 42.46           C  
ANISOU 3304  CAL 4VO A 401     5957   4669   5509   -439     -7    -74       C  
HETATM 3305  CAU 4VO A 401      -0.253  12.153 -59.015  1.00 42.95           C  
ANISOU 3305  CAU 4VO A 401     6067   4744   5508   -509     60    -55       C  
HETATM 3306  OAD 4VO A 401      -0.015  11.030 -59.759  1.00 37.44           O  
ANISOU 3306  OAD 4VO A 401     5363   4092   4772   -532    125    -97       O  
HETATM 3307  CAN 4VO A 401       0.522  13.294 -59.189  1.00 37.46           C  
ANISOU 3307  CAN 4VO A 401     5434   4015   4784   -562     65      2       C  
HETATM 3308  CAX 4VO A 401       0.299  14.464 -58.455  1.00 34.54           C  
ANISOU 3308  CAX 4VO A 401     5103   3576   4446   -543      1     38       C  
HETATM 3309  CBF 4VO A 401       1.130  15.605 -58.699  1.00 35.40           C  
ANISOU 3309  CBF 4VO A 401     5301   3635   4513   -625     10     97       C  
HETATM 3310  CBA 4VO A 401       1.563  15.719 -60.219  1.00 34.49           C  
ANISOU 3310  CBA 4VO A 401     5273   3547   4284   -706     46    138       C  
HETATM 3311  NAS 4VO A 401       2.911  16.322 -60.505  1.00 39.49           N  
ANISOU 3311  NAS 4VO A 401     5940   4191   4873   -838    116    183       N  
HETATM 3312  CBE 4VO A 401       0.706  16.804 -60.923  1.00 40.82           C  
ANISOU 3312  CBE 4VO A 401     6230   4269   5011   -681    -49    200       C  
HETATM 3313  OAT 4VO A 401       0.927  16.799 -62.358  1.00 44.54           O  
ANISOU 3313  OAT 4VO A 401     6783   4776   5365   -746    -25    237       O  
HETATM 3314  CAA 4VO A 401       0.532  15.553 -62.946  1.00 39.73           C  
ANISOU 3314  CAA 4VO A 401     6104   4259   4733   -716     -1    180       C  
HETATM 3315  CAF 4VO A 401      -0.663  16.745 -60.593  1.00 37.08           C  
ANISOU 3315  CAF 4VO A 401     5743   3780   4566   -555   -141    179       C  
HETATM 3316  CAE 4VO A 401      -0.898  16.796 -59.219  1.00 30.66           C  
ANISOU 3316  CAE 4VO A 401     4856   2938   3853   -493   -161    143       C  
HETATM 3317  CBD 4VO A 401       0.250  16.841 -58.401  1.00 31.49           C  
ANISOU 3317  CBD 4VO A 401     4914   3036   4014   -566    -93    133       C  
HETATM 3318  CAR 4VO A 401       0.902  18.153 -58.794  1.00 33.11           C  
ANISOU 3318  CAR 4VO A 401     5268   3153   4159   -657    -99    203       C  
HETATM 3319  CBC 4VO A 401       1.296  18.067 -60.278  1.00 42.05           C  
ANISOU 3319  CBC 4VO A 401     6468   4324   5184   -738    -61    246       C  
HETATM 3320  CAC 4VO A 401       0.833  19.327 -61.026  1.00 37.87           C  
ANISOU 3320  CAC 4VO A 401     6136   3686   4566   -738   -136    328       C  
HETATM 3321  CAY 4VO A 401       2.812  17.752 -60.186  1.00 47.24           C  
ANISOU 3321  CAY 4VO A 401     7048   5055   5845   -871     50    240       C  
HETATM 3322  CAV 4VO A 401       3.726  18.839 -60.183  1.00 39.64           C  
ANISOU 3322  CAV 4VO A 401     6176   4041   4844  -1006     70    297       C  
HETATM 3323  CAJ 4VO A 401       4.028  19.696 -61.223  1.00 47.10           C  
ANISOU 3323  CAJ 4VO A 401     7274   4939   5680  -1110     72    374       C  
HETATM 3324  CAH 4VO A 401       4.929  20.735 -61.003  1.00 51.14           C  
ANISOU 3324  CAH 4VO A 401     7872   5395   6165  -1263     92    423       C  
HETATM 3325  CAG 4VO A 401       5.538  20.923 -59.767  1.00 52.14           C  
ANISOU 3325  CAG 4VO A 401     7923   5522   6368  -1313    106    389       C  
HETATM 3326  CAI 4VO A 401       5.239  20.064 -58.718  1.00 46.24           C  
ANISOU 3326  CAI 4VO A 401     7015   4829   5727  -1194    100    313       C  
HETATM 3327  CAK 4VO A 401       4.337  19.032 -58.938  1.00 41.97           C  
ANISOU 3327  CAK 4VO A 401     6398   4333   5216  -1043     85    271       C  
HETATM 3328  C9  OLC A 402     -13.429   6.669 -51.867  1.00 66.26           C  
ANISOU 3328  C9  OLC A 402     7969   8579   8629   -413   -346   -384       C  
HETATM 3329  C8  OLC A 402     -14.187   7.499 -52.884  1.00 68.17           C  
ANISOU 3329  C8  OLC A 402     8172   8933   8796   -346   -444   -375       C  
HETATM 3330  C24 OLC A 402     -15.851   8.396 -66.387  1.00 91.21           C  
ANISOU 3330  C24 OLC A 402    11646  12396  10612   -687  -1057   -321       C  
HETATM 3331  C7  OLC A 402     -14.382   6.750 -54.186  1.00 76.79           C  
ANISOU 3331  C7  OLC A 402     9311  10054   9812   -480   -466   -399       C  
HETATM 3332  C6  OLC A 402     -14.903   7.632 -55.302  1.00 78.07           C  
ANISOU 3332  C6  OLC A 402     9463  10307   9892   -402   -565   -378       C  
HETATM 3333  C5  OLC A 402     -14.657   7.042 -56.677  1.00 72.39           C  
ANISOU 3333  C5  OLC A 402     8844   9564   9098   -522   -574   -398       C  
HETATM 3334  C4  OLC A 402     -15.508   7.698 -57.746  1.00 75.09           C  
ANISOU 3334  C4  OLC A 402     9141  10057   9333   -472   -688   -379       C  
HETATM 3335  C3  OLC A 402     -15.235   7.155 -59.136  1.00 80.57           C  
ANISOU 3335  C3  OLC A 402     9944  10729   9938   -592   -697   -401       C  
HETATM 3336  C2  OLC A 402     -15.842   8.030 -60.214  1.00 88.64           C  
ANISOU 3336  C2  OLC A 402    10951  11876  10854   -509   -812   -361       C  
HETATM 3337  C21 OLC A 402     -15.738   7.838 -63.965  1.00 93.01           C  
ANISOU 3337  C21 OLC A 402    11736  12518  11085   -673   -934   -365       C  
HETATM 3338  C1  OLC A 402     -15.382   7.676 -61.614  1.00 96.32           C  
ANISOU 3338  C1  OLC A 402    12058  12808  11732   -608   -816   -375       C  
HETATM 3339  C22 OLC A 402     -15.389   8.863 -65.027  1.00 91.47           C  
ANISOU 3339  C22 OLC A 402    11650  12298  10805   -570   -989   -292       C  
HETATM 3340  O19 OLC A 402     -14.664   6.712 -61.791  1.00106.86           O  
ANISOU 3340  O19 OLC A 402    13493  14029  13080   -740   -730   -425       O  
HETATM 3341  O25 OLC A 402     -15.194   9.179 -67.362  1.00 91.52           O  
ANISOU 3341  O25 OLC A 402    11833  12362  10578   -621  -1070   -256       O  
HETATM 3342  O23 OLC A 402     -16.022  10.088 -64.753  1.00 95.34           O  
ANISOU 3342  O23 OLC A 402    12065  12866  11294   -375  -1082   -214       O  
HETATM 3343  O20 OLC A 402     -15.780   8.473 -62.705  1.00 91.56           O  
ANISOU 3343  O20 OLC A 402    11472  12300  11018   -535   -918   -329       O  
HETATM 3344  C10 OLC A 403     -11.423   3.535 -55.787  1.00 71.83           C  
ANISOU 3344  C10 OLC A 403     9133   8968   9191   -816   -222   -487       C  
HETATM 3345  C9  OLC A 403     -12.278   3.288 -57.006  1.00 75.36           C  
ANISOU 3345  C9  OLC A 403     9582   9523   9528   -918   -289   -524       C  
HETATM 3346  C11 OLC A 403     -11.520   4.966 -55.312  1.00 77.13           C  
ANISOU 3346  C11 OLC A 403     9718   9692   9895   -661   -276   -434       C  
HETATM 3347  C8  OLC A 403     -12.057   4.344 -58.065  1.00 78.11           C  
ANISOU 3347  C8  OLC A 403     9961   9896   9821   -831   -347   -493       C  
HETATM 3348  C24 OLC A 403     -14.929   6.094 -69.010  1.00106.93           C  
ANISOU 3348  C24 OLC A 403    13942  14338  12347  -1113   -965   -497       C  
HETATM 3349  C7  OLC A 403     -11.926   3.754 -59.451  1.00 79.31           C  
ANISOU 3349  C7  OLC A 403    10225  10036   9874   -936   -347   -537       C  
HETATM 3350  C6  OLC A 403     -10.480   3.584 -59.864  1.00 76.23           C  
ANISOU 3350  C6  OLC A 403     9982   9479   9504   -908   -253   -539       C  
HETATM 3351  C5  OLC A 403     -10.274   3.828 -61.344  1.00 73.66           C  
ANISOU 3351  C5  OLC A 403     9746   9172   9068   -930   -279   -547       C  
HETATM 3352  C4  OLC A 403     -10.935   5.100 -61.832  1.00 68.84           C  
ANISOU 3352  C4  OLC A 403     9068   8687   8402   -851   -393   -489       C  
HETATM 3353  C3  OLC A 403     -11.920   4.860 -62.960  1.00 71.72           C  
ANISOU 3353  C3  OLC A 403     9427   9194   8631   -946   -481   -522       C  
HETATM 3354  C2  OLC A 403     -11.356   5.208 -64.320  1.00 74.64           C  
ANISOU 3354  C2  OLC A 403     9918   9546   8897   -946   -485   -510       C  
HETATM 3355  C21 OLC A 403     -13.172   6.151 -67.251  1.00 99.05           C  
ANISOU 3355  C21 OLC A 403    13011  13001  11624  -1000   -755   -477       C  
HETATM 3356  C1  OLC A 403     -12.327   4.883 -65.433  1.00 92.35           C  
ANISOU 3356  C1  OLC A 403    12157  11940  10992  -1052   -576   -549       C  
HETATM 3357  C22 OLC A 403     -13.510   5.695 -68.657  1.00105.72           C  
ANISOU 3357  C22 OLC A 403    13927  13947  12296  -1121   -805   -522       C  
HETATM 3358  O19 OLC A 403     -13.299   4.197 -65.187  1.00104.67           O  
ANISOU 3358  O19 OLC A 403    13634  13602  12532  -1153   -618   -598       O  
HETATM 3359  O25 OLC A 403     -15.174   5.765 -70.360  1.00103.63           O  
ANISOU 3359  O25 OLC A 403    13598  14020  11755  -1223  -1018   -533       O  
HETATM 3360  O23 OLC A 403     -12.617   6.270 -69.582  1.00103.43           O  
ANISOU 3360  O23 OLC A 403    13776  13585  11938  -1075   -775   -478       O  
HETATM 3361  O20 OLC A 403     -12.117   5.364 -66.741  1.00 94.53           O  
ANISOU 3361  O20 OLC A 403    12523  12251  11145  -1046   -614   -526       O  
HETATM 3362  C1  CLR A 404     -13.879  13.282 -67.313  1.00 93.60           C  
ANISOU 3362  C1  CLR A 404    12373  12302  10889   -116  -1130     57       C  
HETATM 3363  C2  CLR A 404     -13.368  13.502 -68.730  1.00 95.75           C  
ANISOU 3363  C2  CLR A 404    12805  12554  11022   -172  -1141    103       C  
HETATM 3364  C3  CLR A 404     -13.709  14.918 -69.173  1.00102.82           C  
ANISOU 3364  C3  CLR A 404    13785  13442  11841      5  -1246    228       C  
HETATM 3365  C4  CLR A 404     -13.213  15.908 -68.142  1.00 97.53           C  
ANISOU 3365  C4  CLR A 404    13173  12589  11295    132  -1208    279       C  
HETATM 3366  C5  CLR A 404     -13.238  15.639 -66.826  1.00 93.32           C  
ANISOU 3366  C5  CLR A 404    12530  12022  10907    153  -1156    222       C  
HETATM 3367  C6  CLR A 404     -13.280  16.671 -65.962  1.00 92.93           C  
ANISOU 3367  C6  CLR A 404    12507  11869  10932    313  -1172    270       C  
HETATM 3368  C7  CLR A 404     -13.606  16.499 -64.682  1.00 92.73           C  
ANISOU 3368  C7  CLR A 404    12354  11856  11026    366  -1148    218       C  
HETATM 3369  C8  CLR A 404     -13.302  15.183 -64.019  1.00 87.89           C  
ANISOU 3369  C8  CLR A 404    11624  11268  10503    207  -1050    115       C  
HETATM 3370  C9  CLR A 404     -13.816  14.101 -64.951  1.00 89.28           C  
ANISOU 3370  C9  CLR A 404    11729  11612  10580     74  -1079     65       C  
HETATM 3371  C10 CLR A 404     -13.169  14.208 -66.331  1.00 89.55           C  
ANISOU 3371  C10 CLR A 404    11925  11602  10499     -3  -1075    106       C  
HETATM 3372  C11 CLR A 404     -13.643  12.725 -64.309  1.00 86.60           C  
ANISOU 3372  C11 CLR A 404    11292  11292  10321    -82   -988    -38       C  
HETATM 3373  C12 CLR A 404     -14.331  12.627 -62.946  1.00 85.58           C  
ANISOU 3373  C12 CLR A 404    11002  11223  10291    -14   -990    -71       C  
HETATM 3374  C13 CLR A 404     -13.825  13.722 -62.016  1.00 81.53           C  
ANISOU 3374  C13 CLR A 404    10548  10559   9872    133   -965    -23       C  
HETATM 3375  C14 CLR A 404     -14.073  15.046 -62.716  1.00 86.96           C  
ANISOU 3375  C14 CLR A 404    11337  11226  10476    290  -1059     70       C  
HETATM 3376  C15 CLR A 404     -13.871  16.113 -61.650  1.00 87.20           C  
ANISOU 3376  C15 CLR A 404    11412  11126  10594    446  -1048    102       C  
HETATM 3377  C16 CLR A 404     -14.416  15.433 -60.393  1.00 84.25           C  
ANISOU 3377  C16 CLR A 404    10853  10847  10310    442  -1015     28       C  
HETATM 3378  C17 CLR A 404     -14.596  13.942 -60.715  1.00 76.87           C  
ANISOU 3378  C17 CLR A 404     9813  10036   9358    249   -982    -43       C  
HETATM 3379  C18 CLR A 404     -12.338  13.524 -61.729  1.00 67.09           C  
ANISOU 3379  C18 CLR A 404     8838   8532   8123     39   -842    -32       C  
HETATM 3380  C19 CLR A 404     -11.700  13.814 -66.239  1.00 83.56           C  
ANISOU 3380  C19 CLR A 404    11274  10671   9804   -129   -933     80       C  
HETATM 3381  C20 CLR A 404     -14.245  13.110 -59.480  1.00 69.98           C  
ANISOU 3381  C20 CLR A 404     8863   9125   8603    163   -883   -108       C  
HETATM 3382  C21 CLR A 404     -14.467  11.613 -59.644  1.00 73.28           C  
ANISOU 3382  C21 CLR A 404     9197   9638   9008    -25   -845   -179       C  
HETATM 3383  C22 CLR A 404     -15.101  13.638 -58.334  1.00 66.40           C  
ANISOU 3383  C22 CLR A 404     8282   8753   8194    314   -916   -112       C  
HETATM 3384  C23 CLR A 404     -14.969  12.877 -57.021  1.00 61.95           C  
ANISOU 3384  C23 CLR A 404     7623   8184   7730    246   -831   -170       C  
HETATM 3385  C24 CLR A 404     -15.971  13.471 -56.036  1.00 65.18           C  
ANISOU 3385  C24 CLR A 404     7897   8712   8156    408   -872   -174       C  
HETATM 3386  C25 CLR A 404     -15.699  13.085 -54.588  1.00 63.16           C  
ANISOU 3386  C25 CLR A 404     7583   8416   7998    382   -787   -215       C  
HETATM 3387  C26 CLR A 404     -16.598  13.898 -53.667  1.00 65.60           C  
ANISOU 3387  C26 CLR A 404     7785   8827   8312    573   -823   -217       C  
HETATM 3388  C27 CLR A 404     -15.890  11.591 -54.363  1.00 56.76           C  
ANISOU 3388  C27 CLR A 404     6671   7695   7200    185   -733   -266       C  
HETATM 3389  O1  CLR A 404     -13.108  15.192 -70.447  1.00109.14           O  
ANISOU 3389  O1  CLR A 404    14756  14204  12510    -55  -1244    284       O  
HETATM 3390  P   PO4 A 405      10.530   3.004 -74.324  1.00122.66           P  
ANISOU 3390  P   PO4 A 405    16646  15932  14028   -538   1746   -727       P  
HETATM 3391  O1  PO4 A 405      11.538   3.685 -75.220  1.00126.19           O  
ANISOU 3391  O1  PO4 A 405    17034  16581  14330   -609   1856   -679       O  
HETATM 3392  O2  PO4 A 405       9.192   3.692 -74.456  1.00118.42           O  
ANISOU 3392  O2  PO4 A 405    16212  15289  13493   -673   1571   -674       O  
HETATM 3393  O3  PO4 A 405      10.401   1.556 -74.734  1.00129.06           O  
ANISOU 3393  O3  PO4 A 405    17582  16667  14788   -411   1826   -876       O  
HETATM 3394  O4  PO4 A 405      10.993   3.076 -72.888  1.00115.57           O  
ANISOU 3394  O4  PO4 A 405    15584  15019  13308   -458   1734   -678       O  
HETATM 3395  O1  P6G A 406       4.117   0.359 -28.654  1.00 83.03           O  
ANISOU 3395  O1  P6G A 406    10054  10634  10860    506    169    509       O  
HETATM 3396  C2  P6G A 406       3.193  -0.679 -28.526  1.00 91.41           C  
ANISOU 3396  C2  P6G A 406    11238  11577  11916    492    220    556       C  
HETATM 3397  C3  P6G A 406       1.883  -0.339 -29.297  1.00 86.98           C  
ANISOU 3397  C3  P6G A 406    10714  10930  11403    370    249    473       C  
HETATM 3398  O4  P6G A 406       2.036  -0.656 -30.663  1.00 85.52           O  
ANISOU 3398  O4  P6G A 406    10573  10635  11286    382    280    448       O  
HETATM 3399  C5  P6G A 406       1.121   0.042 -31.539  1.00 86.11           C  
ANISOU 3399  C5  P6G A 406    10638  10676  11404    281    282    356       C  
HETATM 3400  C6  P6G A 406       1.075  -0.652 -32.922  1.00 88.70           C  
ANISOU 3400  C6  P6G A 406    11051  10866  11786    282    326    343       C  
HETATM 3401  O7  P6G A 406       1.250   0.321 -33.929  1.00 90.20           O  
ANISOU 3401  O7  P6G A 406    11183  11074  12017    257    305    267       O  
HETATM 3402  C8  P6G A 406       0.454   0.135 -35.118  1.00 85.91           C  
ANISOU 3402  C8  P6G A 406    10701  10434  11509    190    331    218       C  
HETATM 3403  C9  P6G A 406       1.296   0.493 -36.342  1.00 87.85           C  
ANISOU 3403  C9  P6G A 406    10930  10660  11790    224    334    184       C  
HETATM 3404  O10 P6G A 406       1.157   1.877 -36.680  1.00 90.04           O  
ANISOU 3404  O10 P6G A 406    11131  11002  12079    174    289    120       O  
HETATM 3405  C11 P6G A 406       1.489   2.808 -35.654  1.00 85.98           C  
ANISOU 3405  C11 P6G A 406    10533  10596  11540    179    242    119       C  
HETATM 3406  C12 P6G A 406       1.929   4.150 -36.270  1.00 78.04           C  
ANISOU 3406  C12 P6G A 406     9476   9628  10546    146    205     64       C  
HETATM 3407  O13 P6G A 406       1.005   4.535 -37.299  1.00 78.11           O  
ANISOU 3407  O13 P6G A 406     9526   9572  10578     91    203     12       O  
HETATM 3408  C14 P6G A 406       1.495   4.441 -38.617  1.00 74.70           C  
ANISOU 3408  C14 P6G A 406     9121   9092  10169     90    226      1       C  
HETATM 3409  C15 P6G A 406       0.670   5.368 -39.541  1.00 71.50           C  
ANISOU 3409  C15 P6G A 406     8739   8653   9773     31    197    -55       C  
HETATM 3410  O16 P6G A 406       0.503   4.779 -40.843  1.00 70.90           O  
ANISOU 3410  O16 P6G A 406     8721   8508   9709     17    230    -65       O  
HETATM 3411  C17 P6G A 406       1.205   5.416 -41.879  1.00 66.58           C  
ANISOU 3411  C17 P6G A 406     8176   7956   9163      3    229    -80       C  
HETATM 3412  C18 P6G A 406       1.997   4.369 -42.648  1.00 68.24           C  
ANISOU 3412  C18 P6G A 406     8417   8134   9375     41    291    -61       C  
HETATM 3413  O19 P6G A 406       1.326   4.088 -43.889  1.00 78.04           O  
ANISOU 3413  O19 P6G A 406     9732   9308  10613      3    305    -93       O  
HETATM 3414  O7  P6G A 407       0.927  33.949 -45.882  1.00 96.32           O  
ANISOU 3414  O7  P6G A 407    15411   9107  12079   -628   -543   -215       O  
HETATM 3415  C8  P6G A 407       2.087  34.803 -45.970  1.00 98.82           C  
ANISOU 3415  C8  P6G A 407    15857   9363  12327   -895   -524   -195       C  
HETATM 3416  C9  P6G A 407       2.601  35.067 -44.559  1.00 99.37           C  
ANISOU 3416  C9  P6G A 407    15920   9445  12391  -1000   -518   -299       C  
HETATM 3417  O10 P6G A 407       1.805  34.292 -43.664  1.00 98.65           O  
ANISOU 3417  O10 P6G A 407    15686   9430  12366   -805   -527   -378       O  
HETATM 3418  C11 P6G A 407       2.484  33.850 -42.498  1.00 98.92           C  
ANISOU 3418  C11 P6G A 407    15591   9577  12417   -943   -515   -460       C  
HETATM 3419  C12 P6G A 407       1.645  34.276 -41.281  1.00 98.20           C  
ANISOU 3419  C12 P6G A 407    15579   9414  12320   -750   -533   -568       C  
HETATM 3420  O13 P6G A 407       1.976  33.459 -40.145  1.00 92.60           O  
ANISOU 3420  O13 P6G A 407    14692   8851  11640   -811   -526   -651       O  
HETATM 3421  C14 P6G A 407       2.410  34.209 -39.037  1.00 83.13           C  
ANISOU 3421  C14 P6G A 407    13596   7605  10385   -912   -531   -738       C  
HETATM 3422  C15 P6G A 407       2.103  33.421 -37.750  1.00 71.50           C  
ANISOU 3422  C15 P6G A 407    11975   6254   8938   -829   -533   -842       C  
HETATM 3423  O16 P6G A 407       2.080  34.318 -36.624  1.00 79.37           O  
ANISOU 3423  O16 P6G A 407    13120   7167   9871   -831   -541   -942       O  
HETATM 3424  C17 P6G A 407       3.203  35.158 -36.490  1.00 76.02           C  
ANISOU 3424  C17 P6G A 407    12808   6696   9379  -1100   -544   -942       C  
HETATM 3425  C18 P6G A 407       3.068  35.948 -35.195  1.00 79.31           C  
ANISOU 3425  C18 P6G A 407    13367   7037   9731  -1080   -554  -1061       C  
HETATM 3426  O19 P6G A 407       4.181  36.855 -35.038  1.00 82.38           O  
ANISOU 3426  O19 P6G A 407    13885   7373  10044  -1358   -561  -1065       O  
HETATM 3427  O   HOH A 501       0.406   8.928 -29.923  1.00 51.77           O  
ANISOU 3427  O   HOH A 501     6021   6698   6952     59     -6   -134       O  
HETATM 3428  O   HOH A 502      -4.331  11.330 -51.623  1.00 42.07           O  
ANISOU 3428  O   HOH A 502     5511   4684   5791   -161   -121   -190       O  
HETATM 3429  O   HOH A 503      -9.840  -3.331 -32.424  1.00 55.82           O  
ANISOU 3429  O   HOH A 503     6949   6873   7388   -794    519    234       O  
HETATM 3430  O   HOH A 504       3.456  20.321 -25.568  1.00 52.54           O  
ANISOU 3430  O   HOH A 504     6859   6597   6505   -544   -410   -905       O  
HETATM 3431  O   HOH A 505       3.029  10.492 -60.044  1.00 38.35           O  
ANISOU 3431  O   HOH A 505     5407   4296   4868   -611    352    -92       O  
HETATM 3432  O   HOH A 506       0.940  24.727 -63.251  1.00 46.21           O  
ANISOU 3432  O   HOH A 506     8137   4153   5266   -913   -316    714       O  
HETATM 3433  O   HOH A 507       0.723   7.114 -67.921  1.00 52.53           O  
ANISOU 3433  O   HOH A 507     7726   6259   5975   -791    420   -335       O  
HETATM 3434  O   HOH A 508      16.900  25.758 -61.400  1.00 57.37           O  
ANISOU 3434  O   HOH A 508     8314   7134   6351  -3393    692    708       O  
HETATM 3435  O   HOH A 509      13.192  26.106 -67.091  1.00 58.31           O  
ANISOU 3435  O   HOH A 509     9348   6697   6110  -3099    658   1014       O  
HETATM 3436  O   HOH A 510       8.099   5.544 -25.637  1.00 46.12           O  
ANISOU 3436  O   HOH A 510     4842   6767   5914    303   -174    327       O  
HETATM 3437  O   HOH A 511      -7.780  16.103 -44.468  1.00 44.93           O  
ANISOU 3437  O   HOH A 511     5759   5092   6219    408   -310   -332       O  
HETATM 3438  O   HOH A 512      -2.251  18.629 -49.588  1.00 43.94           O  
ANISOU 3438  O   HOH A 512     6256   4452   5986   -109   -281   -106       O  
HETATM 3439  O   HOH A 513     -10.735   2.447 -24.093  1.00 35.02           O  
ANISOU 3439  O   HOH A 513     3667   5308   4330   -326    500    102       O  
HETATM 3440  O   HOH A 514      -9.755  -4.168 -29.500  1.00 75.44           O  
ANISOU 3440  O   HOH A 514     9488   9444   9731   -817    590    402       O  
HETATM 3441  O   HOH A 515      -1.816  21.055 -41.051  1.00 43.14           O  
ANISOU 3441  O   HOH A 515     6166   4293   5931      4   -314   -431       O  
HETATM 3442  O   HOH A 516      -2.872  24.454 -68.048  1.00 66.53           O  
ANISOU 3442  O   HOH A 516    10959   6932   7387   -470   -627    943       O  
HETATM 3443  O   HOH A 517      18.927  16.518 -64.966  1.00 74.64           O  
ANISOU 3443  O   HOH A 517     9117  10772   8473  -2302   1441    414       O  
HETATM 3444  O   HOH A 518       2.396   8.022 -30.704  1.00 58.83           O  
ANISOU 3444  O   HOH A 518     6861   7608   7884     66     -4    -39       O  
HETATM 3445  O   HOH A 519       4.348  11.243 -39.389  1.00 40.25           O  
ANISOU 3445  O   HOH A 519     4708   4853   5730   -213     31   -139       O  
HETATM 3446  O   HOH A 520      -8.658  14.259 -42.836  1.00 40.82           O  
ANISOU 3446  O   HOH A 520     4990   4796   5723    378   -240   -366       O  
HETATM 3447  O   HOH A 521      -2.156  10.603 -66.002  1.00 40.73           O  
ANISOU 3447  O   HOH A 521     6153   4687   4635   -694      4   -103       O  
HETATM 3448  O   HOH A 522      -8.512  16.783 -55.929  1.00 35.05           O  
ANISOU 3448  O   HOH A 522     5009   3766   4542    250   -579     -6       O  
HETATM 3449  O   HOH A 523       5.433  23.185 -67.885  1.00 63.23           O  
ANISOU 3449  O   HOH A 523    10187   6868   6970  -1698    148    859       O  
HETATM 3450  O   HOH A 524      -0.261  22.923 -61.559  1.00 38.79           O  
ANISOU 3450  O   HOH A 524     6802   3398   4538   -657   -341    525       O  
HETATM 3451  O   HOH A 525      -5.311  16.540 -27.705  1.00 53.38           O  
ANISOU 3451  O   HOH A 525     6598   6785   6900    397    -81   -760       O  
HETATM 3452  O   HOH A 526      -1.364   8.782 -59.332  1.00 32.56           O  
ANISOU 3452  O   HOH A 526     4674   3498   4201   -488    128   -211       O  
HETATM 3453  O   HOH A 527     -14.221  -1.679 -31.993  1.00 44.32           O  
ANISOU 3453  O   HOH A 527     4957   6105   5779  -1053    516     72       O  
HETATM 3454  O   HOH A 528      -3.415  11.950 -32.570  1.00 58.52           O  
ANISOU 3454  O   HOH A 528     7031   7320   7884    136    -32   -367       O  
HETATM 3455  O   HOH A 529      -0.525  14.667 -66.537  1.00 62.90           O  
ANISOU 3455  O   HOH A 529     9209   7348   7343   -764    -33    190       O  
HETATM 3456  O   HOH A 530     -29.867  10.391 -26.129  1.00 75.11           O  
ANISOU 3456  O   HOH A 530     6240  13691   8609    749    657   -787       O  
HETATM 3457  O   HOH A 531       7.196  17.266 -34.817  1.00 50.30           O  
ANISOU 3457  O   HOH A 531     6135   6266   6712   -767   -239   -363       O  
HETATM 3458  O   HOH A 532      -7.083  11.396 -39.339  1.00 37.58           O  
ANISOU 3458  O   HOH A 532     4402   4510   5365    180    -72   -345       O  
HETATM 3459  O   HOH A 533       2.645  18.406 -51.885  1.00 42.35           O  
ANISOU 3459  O   HOH A 533     6075   4327   5687   -657    -71     18       O  
HETATM 3460  O   HOH A 534      -2.841  16.391 -47.501  1.00 38.89           O  
ANISOU 3460  O   HOH A 534     5293   4031   5451    -39   -221   -190       O  
HETATM 3461  O   HOH A 535      16.283  12.370 -65.048  1.00 59.53           O  
ANISOU 3461  O   HOH A 535     7300   8531   6788  -1408   1413    146       O  
HETATM 3462  O   HOH A 536       8.395  17.216 -37.360  1.00 55.76           O  
ANISOU 3462  O   HOH A 536     6791   6953   7442   -894   -175   -277       O  
HETATM 3463  O   HOH A 537       0.219  23.643 -65.583  1.00 64.34           O  
ANISOU 3463  O   HOH A 537    10400   6657   7389   -863   -328    765       O  
HETATM 3464  O   HOH A 538      -3.751   8.947 -58.754  1.00 35.28           O  
ANISOU 3464  O   HOH A 538     4963   3881   4561   -445    -31   -225       O  
HETATM 3465  O   HOH A 539      -0.989  17.846 -26.167  1.00 47.28           O  
ANISOU 3465  O   HOH A 539     5996   5963   6004     19   -219   -802       O  
HETATM 3466  O   HOH A 540      -4.378   7.296 -24.234  1.00 40.88           O  
ANISOU 3466  O   HOH A 540     4564   5757   5212    102    151   -116       O  
HETATM 3467  O   HOH A 541      10.647   8.669 -69.500  1.00 52.15           O  
ANISOU 3467  O   HOH A 541     7234   6937   5642   -936   1290   -162       O  
HETATM 3468  O   HOH A 542      -0.982  11.199 -29.324  1.00 55.22           O  
ANISOU 3468  O   HOH A 542     6534   7116   7332     63    -48   -303       O  
HETATM 3469  O   HOH A 543       9.929   4.555 -27.570  1.00 50.65           O  
ANISOU 3469  O   HOH A 543     5292   7370   6581    445   -127    412       O  
HETATM 3470  O   HOH A 544       5.145   4.499 -21.651  1.00 50.15           O  
ANISOU 3470  O   HOH A 544     5555   7325   6174    320   -150    404       O  
HETATM 3471  O   HOH A 545       7.124  12.304 -41.282  1.00 35.33           O  
ANISOU 3471  O   HOH A 545     4027   4340   5058   -420     69   -102       O  
HETATM 3472  O   HOH A 546      -4.591  26.870 -43.595  1.00 51.86           O  
ANISOU 3472  O   HOH A 546     8304   4563   6838    500   -531   -420       O  
HETATM 3473  O   HOH A 547       6.835   3.446 -24.699  1.00 65.80           O  
ANISOU 3473  O   HOH A 547     7480   9141   8380    456   -101    475       O  
HETATM 3474  O   HOH A 548      -3.240  18.229 -55.980  1.00 39.04           O  
ANISOU 3474  O   HOH A 548     5874   3875   5085   -170   -343     85       O  
HETATM 3475  O   HOH A 549     -11.960  -0.044 -24.488  1.00 57.71           O  
ANISOU 3475  O   HOH A 549     6617   8141   7170   -628    604    250       O  
HETATM 3476  O   HOH A 550      12.359   9.389 -30.384  1.00 54.40           O  
ANISOU 3476  O   HOH A 550     5551   8042   7078   -153   -213    122       O  
HETATM 3477  O   HOH A 551       7.184   1.707 -27.174  1.00 65.51           O  
ANISOU 3477  O   HOH A 551     7527   8850   8513    612     17    547       O  
HETATM 3478  O   HOH A 552       8.508  -0.897 -75.723  1.00 71.17           O  
ANISOU 3478  O   HOH A 552    10684   9014   7341   -364   1787  -1162       O  
HETATM 3479  O   HOH A 553       0.903  11.905 -62.464  1.00 43.47           O  
ANISOU 3479  O   HOH A 553     6310   4897   5310   -664    173    -27       O  
HETATM 3480  O   HOH A 554       2.304  12.257 -25.134  1.00 41.98           O  
ANISOU 3480  O   HOH A 554     4789   5805   5357    -80   -192   -331       O  
HETATM 3481  O   HOH A 555       2.618  24.721 -68.321  1.00 77.29           O  
ANISOU 3481  O   HOH A 555    12368   8310   8689  -1353   -153    986       O  
HETATM 3482  O   HOH A 556      -1.419  20.501 -38.143  1.00 46.09           O  
ANISOU 3482  O   HOH A 556     6383   4839   6288    -13   -288   -529       O  
HETATM 3483  O   HOH A 557       8.812   9.907 -24.326  1.00 48.17           O  
ANISOU 3483  O   HOH A 557     5061   7240   6001   -129   -360     17       O  
HETATM 3484  O   HOH A 558      -0.235  13.640 -26.290  1.00 43.88           O  
ANISOU 3484  O   HOH A 558     5185   5816   5672     10   -141   -480       O  
HETATM 3485  O   HOH A 559      -0.557  21.326 -64.000  1.00 51.25           O  
ANISOU 3485  O   HOH A 559     8287   5230   5956   -688   -304    544       O  
HETATM 3486  O   HOH A 560      -1.485  11.620 -26.661  1.00 50.36           O  
ANISOU 3486  O   HOH A 560     5905   6675   6552     89    -54   -362       O  
HETATM 3487  O   HOH A 561      -1.793  18.474 -53.224  1.00 51.48           O  
ANISOU 3487  O   HOH A 561     7359   5397   6805   -240   -267     15       O  
HETATM 3488  O   HOH A 562     -12.118  -3.185 -32.075  1.00 70.78           O  
ANISOU 3488  O   HOH A 562     8658   9044   9192  -1016    543    189       O  
HETATM 3489  O   HOH A 563      -0.662  12.752 -64.805  1.00 51.07           O  
ANISOU 3489  O   HOH A 563     7477   5881   6047   -689     31     36       O  
HETATM 3490  O   HOH A 564      16.461  -0.292 -67.613  1.00 72.10           O  
ANISOU 3490  O   HOH A 564     9206   9909   8281    581   2177   -711       O  
HETATM 3491  O   HOH A 565       3.080  10.713 -62.703  1.00 47.35           O  
ANISOU 3491  O   HOH A 565     6712   5486   5790   -709    386    -73       O  
HETATM 3492  O   HOH A 566       0.173  17.650 -51.360  1.00 37.52           O  
ANISOU 3492  O   HOH A 566     5409   3713   5133   -386   -154    -37       O  
HETATM 3493  O   HOH A 567       9.547   7.155 -23.821  1.00 48.55           O  
ANISOU 3493  O   HOH A 567     4991   7424   6034    157   -326    266       O  
HETATM 3494  O   HOH A 568       9.605  16.500 -33.132  1.00 61.01           O  
ANISOU 3494  O   HOH A 568     7177   8042   7961   -894   -281   -315       O  
HETATM 3495  O   HOH B 201     -22.034   4.009   0.329  1.00 67.01           O  
ANISOU 3495  O   HOH B 201     6780  13474   5207   -683   1908    -60       O  
HETATM 3496  O   HOH B 202       3.228  12.373 -22.467  1.00 45.34           O  
ANISOU 3496  O   HOH B 202     5166   6499   5563   -128   -263   -341       O  
HETATM 3497  O   HOH B 203      -7.373  -0.353  -9.010  1.00 65.57           O  
ANISOU 3497  O   HOH B 203     7960  10280   6673   -346    613    868       O  
HETATM 3498  O   HOH B 204       3.074  -0.234 -10.746  1.00 62.46           O  
ANISOU 3498  O   HOH B 204     7490   9667   6576    445   -145   1147       O  
HETATM 3499  O   HOH B 205      -8.806  15.925 -19.407  1.00 55.05           O  
ANISOU 3499  O   HOH B 205     6562   7911   6443    651    191  -1013       O  
HETATM 3500  O   HOH B 206      -8.028  15.906 -21.713  1.00 56.00           O  
ANISOU 3500  O   HOH B 206     6723   7773   6781    594    112   -932       O  
HETATM 3501  O   HOH B 207       7.517  16.015 -11.681  1.00 98.22           O  
ANISOU 3501  O   HOH B 207    11901  14484  10935   -742   -786   -759       O  
HETATM 3502  O   HOH B 208      -0.418  10.398 -24.450  1.00 43.47           O  
ANISOU 3502  O   HOH B 208     4957   6019   5543     69    -63   -259       O  
HETATM 3503  O   HOH B 209       8.668  14.673  -3.894  1.00 61.63           O  
ANISOU 3503  O   HOH B 209     7165  11086   5166   -820  -1067   -670       O  
HETATM 3504  O   HOH B 210      -9.049   4.892  -2.607  1.00 62.68           O  
ANISOU 3504  O   HOH B 210     7368  11113   5333   -219    728    208       O  
HETATM 3505  O   HOH B 211     -14.755  13.876 -21.105  1.00 52.48           O  
ANISOU 3505  O   HOH B 211     5591   8193   6154    883    455   -926       O  
HETATM 3506  O   HOH B 212      -6.848   6.132 -23.753  1.00 36.38           O  
ANISOU 3506  O   HOH B 212     3928   5319   4577     41    270    -83       O  
HETATM 3507  O   HOH B 213      12.156  10.677  -3.162  1.00 65.11           O  
ANISOU 3507  O   HOH B 213     7000  12280   5460   -517  -1349     64       O  
HETATM 3508  O   HOH B 214       2.553  18.043  -4.449  1.00 63.16           O  
ANISOU 3508  O   HOH B 214     8080  10408   5509   -543   -549  -1369       O  
HETATM 3509  O   HOH B 215      11.531   4.331 -16.809  1.00 50.97           O  
ANISOU 3509  O   HOH B 215     5088   8617   5661    513   -605    716       O  
HETATM 3510  O   HOH B 216      -9.603  -2.781 -14.131  1.00 67.96           O  
ANISOU 3510  O   HOH B 216     8327   9954   7540   -651    765    914       O  
HETATM 3511  O   HOH B 217      -1.050  17.863 -22.290  1.00 61.09           O  
ANISOU 3511  O   HOH B 217     7723   8027   7461     20   -218   -921       O  
HETATM 3512  O   HOH B 218       7.971  16.709 -18.577  1.00 60.75           O  
ANISOU 3512  O   HOH B 218     7154   8978   6949   -780   -651   -680       O  
HETATM 3513  O   HOH B 219      -0.309  20.797 -12.417  1.00 63.13           O  
ANISOU 3513  O   HOH B 219     8384   9006   6597   -180   -316  -1549       O  
HETATM 3514  O   HOH B 220       3.769  21.265 -14.558  1.00 60.41           O  
ANISOU 3514  O   HOH B 220     7968   8554   6429   -702   -575  -1407       O  
HETATM 3515  O   HOH B 221      -1.141  -2.514  -5.955  1.00 70.11           O  
ANISOU 3515  O   HOH B 221     8851  10924   6863    111    168   1488       O  
HETATM 3516  O   HOH B 222      -1.684  22.006 -10.491  1.00 64.34           O  
ANISOU 3516  O   HOH B 222     8752   9220   6475    -36   -234  -1817       O  
HETATM 3517  O   HOH B 223      -1.486  15.703 -25.124  1.00 52.50           O  
ANISOU 3517  O   HOH B 223     6437   6865   6646     76   -155   -682       O  
HETATM 3518  O   HOH B 224       7.366   8.472 -21.621  1.00 63.27           O  
ANISOU 3518  O   HOH B 224     7041   9247   7751     29   -349    112       O  
HETATM 3519  O   HOH B 225       8.395  17.027  -4.127  1.00 90.35           O  
ANISOU 3519  O   HOH B 225    11048  14500   8782  -1041  -1070  -1032       O  
HETATM 3520  O   HOH B 226     -20.187   2.185   1.198  1.00 91.04           O  
ANISOU 3520  O   HOH B 226    10162  16311   8118   -940   1848    282       O  
CONECT   29   35                                                                
CONECT   35   29   36                                                           
CONECT   36   35   37   43                                                      
CONECT   37   36   38                                                           
CONECT   38   37   39                                                           
CONECT   39   38   40                                                           
CONECT   40   39   41   42                                                      
CONECT   41   40                                                                
CONECT   42   40                                                                
CONECT   43   36   44   45                                                      
CONECT   44   43                                                                
CONECT   45   43                                                                
CONECT  680 1290                                                                
CONECT 1290  680                                                                
CONECT 2528 3119                                                                
CONECT 3119 2528                                                                
CONECT 3296 3297 3309                                                           
CONECT 3297 3296 3298                                                           
CONECT 3298 3297 3299 3300                                                      
CONECT 3299 3298                                                                
CONECT 3300 3298 3301 3317                                                      
CONECT 3301 3300 3302                                                           
CONECT 3302 3301 3303 3308                                                      
CONECT 3303 3302 3304                                                           
CONECT 3304 3303 3305                                                           
CONECT 3305 3304 3306 3307                                                      
CONECT 3306 3305                                                                
CONECT 3307 3305 3308                                                           
CONECT 3308 3302 3307 3309                                                      
CONECT 3309 3296 3308 3310 3317                                                 
CONECT 3310 3309 3311 3312                                                      
CONECT 3311 3310 3321                                                           
CONECT 3312 3310 3313 3315 3319                                                 
CONECT 3313 3312 3314                                                           
CONECT 3314 3313                                                                
CONECT 3315 3312 3316                                                           
CONECT 3316 3315 3317                                                           
CONECT 3317 3300 3309 3316 3318                                                 
CONECT 3318 3317 3319                                                           
CONECT 3319 3312 3318 3320 3321                                                 
CONECT 3320 3319                                                                
CONECT 3321 3311 3319 3322                                                      
CONECT 3322 3321 3323 3327                                                      
CONECT 3323 3322 3324                                                           
CONECT 3324 3323 3325                                                           
CONECT 3325 3324 3326                                                           
CONECT 3326 3325 3327                                                           
CONECT 3327 3322 3326                                                           
CONECT 3328 3329                                                                
CONECT 3329 3328 3331                                                           
CONECT 3330 3339 3341                                                           
CONECT 3331 3329 3332                                                           
CONECT 3332 3331 3333                                                           
CONECT 3333 3332 3334                                                           
CONECT 3334 3333 3335                                                           
CONECT 3335 3334 3336                                                           
CONECT 3336 3335 3338                                                           
CONECT 3337 3339 3343                                                           
CONECT 3338 3336 3340 3343                                                      
CONECT 3339 3330 3337 3342                                                      
CONECT 3340 3338                                                                
CONECT 3341 3330                                                                
CONECT 3342 3339                                                                
CONECT 3343 3337 3338                                                           
CONECT 3344 3345 3346                                                           
CONECT 3345 3344 3347                                                           
CONECT 3346 3344                                                                
CONECT 3347 3345 3349                                                           
CONECT 3348 3357 3359                                                           
CONECT 3349 3347 3350                                                           
CONECT 3350 3349 3351                                                           
CONECT 3351 3350 3352                                                           
CONECT 3352 3351 3353                                                           
CONECT 3353 3352 3354                                                           
CONECT 3354 3353 3356                                                           
CONECT 3355 3357 3361                                                           
CONECT 3356 3354 3358 3361                                                      
CONECT 3357 3348 3355 3360                                                      
CONECT 3358 3356                                                                
CONECT 3359 3348                                                                
CONECT 3360 3357                                                                
CONECT 3361 3355 3356                                                           
CONECT 3362 3363 3371                                                           
CONECT 3363 3362 3364                                                           
CONECT 3364 3363 3365 3389                                                      
CONECT 3365 3364 3366                                                           
CONECT 3366 3365 3367 3371                                                      
CONECT 3367 3366 3368                                                           
CONECT 3368 3367 3369                                                           
CONECT 3369 3368 3370 3375                                                      
CONECT 3370 3369 3371 3372                                                      
CONECT 3371 3362 3366 3370 3380                                                 
CONECT 3372 3370 3373                                                           
CONECT 3373 3372 3374                                                           
CONECT 3374 3373 3375 3378 3379                                                 
CONECT 3375 3369 3374 3376                                                      
CONECT 3376 3375 3377                                                           
CONECT 3377 3376 3378                                                           
CONECT 3378 3374 3377 3381                                                      
CONECT 3379 3374                                                                
CONECT 3380 3371                                                                
CONECT 3381 3378 3382 3383                                                      
CONECT 3382 3381                                                                
CONECT 3383 3381 3384                                                           
CONECT 3384 3383 3385                                                           
CONECT 3385 3384 3386                                                           
CONECT 3386 3385 3387 3388                                                      
CONECT 3387 3386                                                                
CONECT 3388 3386                                                                
CONECT 3389 3364                                                                
CONECT 3390 3391 3392 3393 3394                                                 
CONECT 3391 3390                                                                
CONECT 3392 3390                                                                
CONECT 3393 3390                                                                
CONECT 3394 3390                                                                
CONECT 3395 3396                                                                
CONECT 3396 3395 3397                                                           
CONECT 3397 3396 3398                                                           
CONECT 3398 3397 3399                                                           
CONECT 3399 3398 3400                                                           
CONECT 3400 3399 3401                                                           
CONECT 3401 3400 3402                                                           
CONECT 3402 3401 3403                                                           
CONECT 3403 3402 3404                                                           
CONECT 3404 3403 3405                                                           
CONECT 3405 3404 3406                                                           
CONECT 3406 3405 3407                                                           
CONECT 3407 3406 3408                                                           
CONECT 3408 3407 3409                                                           
CONECT 3409 3408 3410                                                           
CONECT 3410 3409 3411                                                           
CONECT 3411 3410 3412                                                           
CONECT 3412 3411 3413                                                           
CONECT 3413 3412                                                                
CONECT 3414 3415                                                                
CONECT 3415 3414 3416                                                           
CONECT 3416 3415 3417                                                           
CONECT 3417 3416 3418                                                           
CONECT 3418 3417 3419                                                           
CONECT 3419 3418 3420                                                           
CONECT 3420 3419 3421                                                           
CONECT 3421 3420 3422                                                           
CONECT 3422 3421 3423                                                           
CONECT 3423 3422 3424                                                           
CONECT 3424 3423 3425                                                           
CONECT 3425 3424 3426                                                           
CONECT 3426 3425                                                                
MASTER      342    0    8   12   16    0   11    6 3484    2  147   33          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.