CNRS Nantes University UFIP UFIP
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***  TRANSCRIPTION 11-APR-12 4EM9  ***

elNémo ID: 22091318121888532

Job options:

ID        	=	 22091318121888532
JOBID     	=	 TRANSCRIPTION 11-APR-12 4EM9
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    TRANSCRIPTION                           11-APR-12   4EM9              
TITLE     HUMAN PPAR GAMMA IN COMPLEX WITH NONANOIC ACIDS                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA;          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: LIGAND BINDING DOMAIN, UNP RESIDUES 235-505;               
COMPND   5 SYNONYM: PPAR-GAMMA, NUCLEAR RECEPTOR SUBFAMILY 1 GROUP C MEMBER 3;  
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PPARG, NR1C3;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    NUCLEAR RECEPTOR, RETINOIC ACID RECEPTOR, NUCLEUS, TRANSCRIPTION      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.V.LIBERATO,A.S.NASCIMENTO,I.POLIKARPOV                              
REVDAT   1   06-MAR-13 4EM9    0                                                
JRNL        AUTH   M.V.LIBERATO,A.S.NASCIMENTO,S.D.AYERS,J.Z.LIN,A.CVORO,       
JRNL        AUTH 2 R.L.SILVEIRA,L.MARTINEZ,P.C.SOUZA,D.SAIDEMBERG,T.DENG,       
JRNL        AUTH 3 A.A.AMATO,M.TOGASHI,W.A.HSUEH,K.PHILLIPS,M.S.PALMA,          
JRNL        AUTH 4 F.A.NEVES,M.S.SKAF,P.WEBB,I.POLIKARPOV                       
JRNL        TITL   MEDIUM CHAIN FATTY ACIDS ARE SELECTIVE PEROXISOME            
JRNL        TITL 2 PROLIFERATOR ACTIVATED RECEPTOR (PPAR) GAMMA ACTIVATORS AND  
JRNL        TITL 3 PAN-PPAR PARTIAL AGONISTS                                    
JRNL        REF    PLOS ONE                      V.   7 36297 2012              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   22649490                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0036297                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.80                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 36859                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.205                           
REMARK   3   FREE R VALUE                     : 0.235                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.050                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1860                            
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 32.8000 -  4.9297    0.96     2808   164  0.2080 0.2464        
REMARK   3     2  4.9297 -  3.9149    0.99     2818   173  0.1678 0.1854        
REMARK   3     3  3.9149 -  3.4207    1.00     2850   154  0.1744 0.1877        
REMARK   3     4  3.4207 -  3.1082    1.00     2824   139  0.2006 0.2200        
REMARK   3     5  3.1082 -  2.8855    1.00     2872   155  0.2168 0.2265        
REMARK   3     6  2.8855 -  2.7155    0.99     2796   156  0.2146 0.2770        
REMARK   3     7  2.7155 -  2.5796    0.99     2784   137  0.2097 0.2393        
REMARK   3     8  2.5796 -  2.4673    0.98     2784   156  0.2112 0.2820        
REMARK   3     9  2.4673 -  2.3724    0.97     2779   127  0.2124 0.2720        
REMARK   3    10  2.3724 -  2.2905    0.97     2761   130  0.2322 0.2624        
REMARK   3    11  2.2905 -  2.2189    0.96     2662   157  0.2385 0.2991        
REMARK   3    12  2.2189 -  2.1555    0.89     2529   118  0.2649 0.3114        
REMARK   3    13  2.1555 -  2.1000    0.61     1732    94  0.2994 0.3522        
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              : 0.35                                          
REMARK   3   B_SOL              : 81.82                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.200           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.35830                                             
REMARK   3    B22 (A**2) : 2.22940                                              
REMARK   3    B33 (A**2) : -1.87110                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.41070                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           4135                                  
REMARK   3   ANGLE     :  0.764           5569                                  
REMARK   3   CHIRALITY :  0.044            644                                  
REMARK   3   PLANARITY :  0.003            704                                  
REMARK   3   DIHEDRAL  : 15.199           1555                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND (RESID 207:477 OR RESID 501:503 ) )       
REMARK   3    ORIGIN FOR THE GROUP (A):  13.3685  -0.5311  16.9623              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2739 T22:   0.3107                                     
REMARK   3      T33:   0.2108 T12:   0.1475                                     
REMARK   3      T13:  -0.0211 T23:   0.0154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9049 L22:   1.6142                                     
REMARK   3      L33:   2.1620 L12:   0.4198                                     
REMARK   3      L13:  -0.2332 L23:  -0.0079                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1813 S12:  -0.1631 S13:  -0.0690                       
REMARK   3      S21:   0.0815 S22:   0.2108 S23:  -0.1730                       
REMARK   3      S31:  -0.1340 S32:   0.2534 S33:  -0.0368                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN B AND (RESID 207:474 OR RESID 501:502 ) )       
REMARK   3    ORIGIN FOR THE GROUP (A):  30.0097 -23.4979  33.7397              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3202 T22:   0.2397                                     
REMARK   3      T33:   0.2577 T12:   0.1127                                     
REMARK   3      T13:   0.0269 T23:   0.0247                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3921 L22:   1.0948                                     
REMARK   3      L33:   2.6420 L12:   0.2000                                     
REMARK   3      L13:  -0.3545 L23:  -0.0319                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0281 S12:  -0.1960 S13:  -0.0085                       
REMARK   3      S21:   0.1231 S22:   0.0171 S23:   0.0823                       
REMARK   3      S31:  -0.1172 S32:   0.1700 S33:  -0.0505                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 601:771 ) OR (CHAIN B AND RESID     
REMARK   3               601:740 )                                              
REMARK   3    ORIGIN FOR THE GROUP (A):  19.2558 -12.7485  23.1014              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3116 T22:   0.3040                                     
REMARK   3      T33:   0.2939 T12:   0.0458                                     
REMARK   3      T13:   0.0206 T23:  -0.0039                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3292 L22:   0.3516                                     
REMARK   3      L33:   0.7289 L12:  -0.2189                                     
REMARK   3      L13:   0.4390 L23:  -0.3063                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0525 S12:   0.0012 S13:  -0.0024                       
REMARK   3      S21:   0.0028 S22:   0.0301 S23:   0.0254                       
REMARK   3      S31:  -0.0480 S32:   0.0185 S33:   0.0086                       
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 4EM9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAY-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB071795.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-FEB-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : LNLS                               
REMARK 200  BEAMLINE                       : W01B-MX2                           
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.46                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36859                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1ZEO                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.88                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL, 0.9M SODIUM CITRATE, PH   
REMARK 280  7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       46.36550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       31.12750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       46.36550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       31.12750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 44590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350   BIOMT1   2 -1.000000  0.000000  0.000000       92.73100            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000       46.36550            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000      -31.12750            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000       46.36550            
REMARK 350   BIOMT2   4  0.000000  1.000000  0.000000      -31.12750            
REMARK 350   BIOMT3   4  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 A   203                                                      
REMARK 465     SER A   204                                                      
REMARK 465     HIS A   205                                                      
REMARK 465     MET A   206                                                      
REMARK 465     ILE A   262                                                      
REMARK 465     LYS A   263                                                      
REMARK 465     PHE A   264                                                      
REMARK 465     LYS A   265                                                      
REMARK 465     HIS A   266                                                      
REMARK 465     ILE A   267                                                      
REMARK 465     THR A   268                                                      
REMARK 465     PRO A   269                                                      
REMARK 465     LEU A   270                                                      
REMARK 465     GLN A   271                                                      
REMARK 465     GLU A   272                                                      
REMARK 465     GLN A   273                                                      
REMARK 465     GLY B   203                                                      
REMARK 465     SER B   204                                                      
REMARK 465     HIS B   205                                                      
REMARK 465     MET B   206                                                      
REMARK 465     LYS B   240                                                      
REMARK 465     THR B   241                                                      
REMARK 465     THR B   242                                                      
REMARK 465     ASP B   243                                                      
REMARK 465     LYS B   244                                                      
REMARK 465     LYS B   261                                                      
REMARK 465     ILE B   262                                                      
REMARK 465     LYS B   263                                                      
REMARK 465     THR B   268                                                      
REMARK 465     PRO B   269                                                      
REMARK 465     LEU B   270                                                      
REMARK 465     GLN B   271                                                      
REMARK 465     GLU B   272                                                      
REMARK 465     GLN B   273                                                      
REMARK 465     SER B   274                                                      
REMARK 465     LYS B   275                                                      
REMARK 465     ILE B   456                                                      
REMARK 465     LYS B   457                                                      
REMARK 465     LYS B   458                                                      
REMARK 465     THR B   459                                                      
REMARK 465     GLU B   460                                                      
REMARK 465     THR B   461                                                      
REMARK 465     ASP B   462                                                      
REMARK 465     MET B   463                                                      
REMARK 465     SER B   464                                                      
REMARK 465     ASP B   475                                                      
REMARK 465     LEU B   476                                                      
REMARK 465     TYR B   477                                                      
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 240    CG   CD   CE   NZ                                   
REMARK 470     MET A 257    CG   SD   CE                                        
REMARK 470     ARG A 280    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 358    CG   CD   CE   NZ                                   
REMARK 470     LYS A 457    CG   CD   CE   NZ                                   
REMARK 470     GLU A 471    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 474    CG   CD   CE   NZ                                   
REMARK 470     GLN B 283    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 343    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 357    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 358    CG   CD   CE   NZ                                   
REMARK 470     LYS B 373    CG   CD   CE   NZ                                   
REMARK 470     GLN B 451    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 474    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CB   CYS B   285     O9   TCE B   502              2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NZ   LYS B   265     O    HOH A   771     3545     2.05            
REMARK 500   CD   LYS B   265     O    HOH A   758     3545     2.06            
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    THR B 238      -90.87   -110.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 666        DISTANCE =  5.43 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KNA A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KNA A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KNA A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE KNA B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TCE B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 504                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2VV1   RELATED DB: PDB                                   
REMARK 900 HPPARGAMMA LIGAND BINDING DOMAIN IN COMPLEX WITH 4-HDHA              
REMARK 900 RELATED ID: 1PRG   RELATED DB: PDB                                   
REMARK 900 LIGAND BINDING DOMAIN OF THE HUMAN PEROXISOME PROLIFERATOR           
REMARK 900 ACTIVATED RECEPTOR GAMMA                                             
REMARK 900 RELATED ID: 3GWX   RELATED DB: PDB                                   
REMARK 900 MOLECULAR RECOGNITION OF FATTY ACIDS BY PEROXISOME                   
REMARK 900 PROLIFERATOR-ACTIVATED RECEPTORS                                     
REMARK 900 RELATED ID: 1ZEO   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN PPAR-GAMMA LIGAND BINDING DOMAIN          
REMARK 900 COMPLEXED WITH AN ALPHA-ARYLOXYPHENYLACETIC ACID AGONIST             
REMARK 900 RELATED ID: 3DZU   RELATED DB: PDB                                   
REMARK 900 INTACT PPAR GAMMA - RXR ALPHA NUCLEAR RECEPTOR COMPLEX ON            
REMARK 900 DNA BOUND WITH BVT.13, 9-CIS RETINOIC ACID AND NCOA2 PEPTIDE         
REMARK 900 RELATED ID: 3DZY   RELATED DB: PDB                                   
REMARK 900 INTACT PPAR GAMMA - RXR ALPHA NUCLEAR RECEPTOR COMPLEX ON            
REMARK 900 DNA BOUND WITH ROSIGLITAZONE, 9-CIS RETINOIC ACID AND NCOA2          
REMARK 900 PEPTIDE                                                              
REMARK 900 RELATED ID: 4EMA   RELATED DB: PDB                                   
DBREF  4EM9 A  207   477  UNP    P37231   PPARG_HUMAN    235    505             
DBREF  4EM9 B  207   477  UNP    P37231   PPARG_HUMAN    235    505             
SEQADV 4EM9 GLY A  203  UNP  P37231              EXPRESSION TAG                 
SEQADV 4EM9 SER A  204  UNP  P37231              EXPRESSION TAG                 
SEQADV 4EM9 HIS A  205  UNP  P37231              EXPRESSION TAG                 
SEQADV 4EM9 MET A  206  UNP  P37231              EXPRESSION TAG                 
SEQADV 4EM9 GLY B  203  UNP  P37231              EXPRESSION TAG                 
SEQADV 4EM9 SER B  204  UNP  P37231              EXPRESSION TAG                 
SEQADV 4EM9 HIS B  205  UNP  P37231              EXPRESSION TAG                 
SEQADV 4EM9 MET B  206  UNP  P37231              EXPRESSION TAG                 
SEQRES   1 A  275  GLY SER HIS MET GLU SER ALA ASP LEU ARG ALA LEU ALA          
SEQRES   2 A  275  LYS HIS LEU TYR ASP SER TYR ILE LYS SER PHE PRO LEU          
SEQRES   3 A  275  THR LYS ALA LYS ALA ARG ALA ILE LEU THR GLY LYS THR          
SEQRES   4 A  275  THR ASP LYS SER PRO PHE VAL ILE TYR ASP MET ASN SER          
SEQRES   5 A  275  LEU MET MET GLY GLU ASP LYS ILE LYS PHE LYS HIS ILE          
SEQRES   6 A  275  THR PRO LEU GLN GLU GLN SER LYS GLU VAL ALA ILE ARG          
SEQRES   7 A  275  ILE PHE GLN GLY CYS GLN PHE ARG SER VAL GLU ALA VAL          
SEQRES   8 A  275  GLN GLU ILE THR GLU TYR ALA LYS SER ILE PRO GLY PHE          
SEQRES   9 A  275  VAL ASN LEU ASP LEU ASN ASP GLN VAL THR LEU LEU LYS          
SEQRES  10 A  275  TYR GLY VAL HIS GLU ILE ILE TYR THR MET LEU ALA SER          
SEQRES  11 A  275  LEU MET ASN LYS ASP GLY VAL LEU ILE SER GLU GLY GLN          
SEQRES  12 A  275  GLY PHE MET THR ARG GLU PHE LEU LYS SER LEU ARG LYS          
SEQRES  13 A  275  PRO PHE GLY ASP PHE MET GLU PRO LYS PHE GLU PHE ALA          
SEQRES  14 A  275  VAL LYS PHE ASN ALA LEU GLU LEU ASP ASP SER ASP LEU          
SEQRES  15 A  275  ALA ILE PHE ILE ALA VAL ILE ILE LEU SER GLY ASP ARG          
SEQRES  16 A  275  PRO GLY LEU LEU ASN VAL LYS PRO ILE GLU ASP ILE GLN          
SEQRES  17 A  275  ASP ASN LEU LEU GLN ALA LEU GLU LEU GLN LEU LYS LEU          
SEQRES  18 A  275  ASN HIS PRO GLU SER SER GLN LEU PHE ALA LYS LEU LEU          
SEQRES  19 A  275  GLN LYS MET THR ASP LEU ARG GLN ILE VAL THR GLU HIS          
SEQRES  20 A  275  VAL GLN LEU LEU GLN VAL ILE LYS LYS THR GLU THR ASP          
SEQRES  21 A  275  MET SER LEU HIS PRO LEU LEU GLN GLU ILE TYR LYS ASP          
SEQRES  22 A  275  LEU TYR                                                      
SEQRES   1 B  275  GLY SER HIS MET GLU SER ALA ASP LEU ARG ALA LEU ALA          
SEQRES   2 B  275  LYS HIS LEU TYR ASP SER TYR ILE LYS SER PHE PRO LEU          
SEQRES   3 B  275  THR LYS ALA LYS ALA ARG ALA ILE LEU THR GLY LYS THR          
SEQRES   4 B  275  THR ASP LYS SER PRO PHE VAL ILE TYR ASP MET ASN SER          
SEQRES   5 B  275  LEU MET MET GLY GLU ASP LYS ILE LYS PHE LYS HIS ILE          
SEQRES   6 B  275  THR PRO LEU GLN GLU GLN SER LYS GLU VAL ALA ILE ARG          
SEQRES   7 B  275  ILE PHE GLN GLY CYS GLN PHE ARG SER VAL GLU ALA VAL          
SEQRES   8 B  275  GLN GLU ILE THR GLU TYR ALA LYS SER ILE PRO GLY PHE          
SEQRES   9 B  275  VAL ASN LEU ASP LEU ASN ASP GLN VAL THR LEU LEU LYS          
SEQRES  10 B  275  TYR GLY VAL HIS GLU ILE ILE TYR THR MET LEU ALA SER          
SEQRES  11 B  275  LEU MET ASN LYS ASP GLY VAL LEU ILE SER GLU GLY GLN          
SEQRES  12 B  275  GLY PHE MET THR ARG GLU PHE LEU LYS SER LEU ARG LYS          
SEQRES  13 B  275  PRO PHE GLY ASP PHE MET GLU PRO LYS PHE GLU PHE ALA          
SEQRES  14 B  275  VAL LYS PHE ASN ALA LEU GLU LEU ASP ASP SER ASP LEU          
SEQRES  15 B  275  ALA ILE PHE ILE ALA VAL ILE ILE LEU SER GLY ASP ARG          
SEQRES  16 B  275  PRO GLY LEU LEU ASN VAL LYS PRO ILE GLU ASP ILE GLN          
SEQRES  17 B  275  ASP ASN LEU LEU GLN ALA LEU GLU LEU GLN LEU LYS LEU          
SEQRES  18 B  275  ASN HIS PRO GLU SER SER GLN LEU PHE ALA LYS LEU LEU          
SEQRES  19 B  275  GLN LYS MET THR ASP LEU ARG GLN ILE VAL THR GLU HIS          
SEQRES  20 B  275  VAL GLN LEU LEU GLN VAL ILE LYS LYS THR GLU THR ASP          
SEQRES  21 B  275  MET SER LEU HIS PRO LEU LEU GLN GLU ILE TYR LYS ASP          
SEQRES  22 B  275  LEU TYR                                                      
HET    KNA  A 501      11                                                       
HET    KNA  A 502      11                                                       
HET    KNA  A 503      11                                                       
HET    GOL  A 504       6                                                       
HET    KNA  B 501      11                                                       
HET    TCE  B 502      16                                                       
HET    GOL  B 503       6                                                       
HET    GOL  B 504       6                                                       
HETNAM     KNA NONANOIC ACID                                                    
HETNAM     GOL GLYCEROL                                                         
HETNAM     TCE 3,3',3''-PHOSPHANETRIYLTRIPROPANOIC ACID                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     TCE 3-[BIS(2-CARBOXYETHYL)PHOSPHANYL]PROPANOIC ACID                  
FORMUL   3  KNA    4(C9 H18 O2)                                                 
FORMUL   6  GOL    3(C3 H8 O3)                                                  
FORMUL   8  TCE    C9 H15 O6 P                                                  
FORMUL  11  HOH   *311(H2 O)                                                    
HELIX    1   1 GLU A  207  PHE A  226  1                                  20    
HELIX    2   2 THR A  229  THR A  238  1                                  10    
HELIX    3   3 ASP A  251  GLU A  259  1                                   9    
HELIX    4   4 GLU A  276  ILE A  303  1                                  28    
HELIX    5   5 GLY A  305  LEU A  309  5                                   5    
HELIX    6   6 ASP A  310  ALA A  331  1                                  22    
HELIX    7   7 SER A  342  GLY A  344  5                                   3    
HELIX    8   8 ARG A  350  SER A  355  1                                   6    
HELIX    9   9 PRO A  359  PHE A  363  5                                   5    
HELIX   10  10 MET A  364  ALA A  376  1                                  13    
HELIX   11  11 ASP A  380  LEU A  393  1                                  14    
HELIX   12  12 ASN A  402  HIS A  425  1                                  24    
HELIX   13  13 GLN A  430  GLU A  460  1                                  31    
HELIX   14  14 HIS A  466  LYS A  474  1                                   9    
HELIX   15  15 SER B  208  PHE B  226  1                                  19    
HELIX   16  16 THR B  229  THR B  238  1                                  10    
HELIX   17  17 ASP B  251  GLU B  259  1                                   9    
HELIX   18  18 VAL B  277  SER B  302  1                                  26    
HELIX   19  19 GLY B  305  LEU B  309  5                                   5    
HELIX   20  20 ASP B  310  LEU B  333  1                                  24    
HELIX   21  21 ARG B  350  SER B  355  1                                   6    
HELIX   22  22 PRO B  359  PHE B  363  5                                   5    
HELIX   23  23 MET B  364  ALA B  376  1                                  13    
HELIX   24  24 ASP B  380  LEU B  393  1                                  14    
HELIX   25  25 ASN B  402  HIS B  425  1                                  24    
HELIX   26  26 GLN B  430  LEU B  453  1                                  24    
HELIX   27  27 HIS B  466  TYR B  473  1                                   8    
SHEET    1   A 4 PHE A 247  ILE A 249  0                                        
SHEET    2   A 4 GLY A 346  THR A 349  1  O  PHE A 347   N  ILE A 249           
SHEET    3   A 4 GLY A 338  ILE A 341 -1  N  VAL A 339   O  MET A 348           
SHEET    4   A 4 MET A 334  ASN A 335 -1  N  ASN A 335   O  GLY A 338           
SHEET    1   B 4 PHE B 247  ILE B 249  0                                        
SHEET    2   B 4 GLY B 346  THR B 349  1  O  PHE B 347   N  ILE B 249           
SHEET    3   B 4 GLY B 338  ILE B 341 -1  N  VAL B 339   O  MET B 348           
SHEET    4   B 4 MET B 334  ASN B 335 -1  N  ASN B 335   O  GLY B 338           
CISPEP   1 LYS A  358    PRO A  359          0         0.56                     
CISPEP   2 LYS B  358    PRO B  359          0        -2.28                     
SITE     1 AC1  8 CYS A 285  ARG A 288  SER A 289  ILE A 326                    
SITE     2 AC1  8 LEU A 333  MET A 364  KNA A 503  GOL A 504                    
SITE     1 AC2  7 PHE A 282  CYS A 285  SER A 289  HIS A 323                    
SITE     2 AC2  7 PHE A 363  HIS A 449  TYR A 473                               
SITE     1 AC3  6 ARG A 288  LEU A 340  ILE A 341  SER A 342                    
SITE     2 AC3  6 KNA A 501  HOH A 733                                          
SITE     1 AC4  8 PHE A 226  LEU A 228  ARG A 288  GLU A 295                    
SITE     2 AC4  8 MET A 329  LEU A 333  KNA A 501  HOH A 637                    
SITE     1 AC5  9 CYS B 285  ARG B 288  SER B 289  ALA B 292                    
SITE     2 AC5  9 ILE B 326  TYR B 327  MET B 364  HIS B 449                    
SITE     3 AC5  9 GOL B 504                                                     
SITE     1 AC6  7 GLU B 259  PHE B 264  HIS B 266  CYS B 285                    
SITE     2 AC6  7 ILE B 341  SER B 342  HOH B 664                               
SITE     1 AC7  1 ASN B 312                                                     
SITE     1 AC8  8 PRO B 227  LEU B 228  ARG B 288  GLU B 295                    
SITE     2 AC8  8 MET B 329  LEU B 333  KNA B 501  HOH B 613                    
CRYST1   92.731   62.255  118.649  90.00 101.94  90.00 C 1 2 1       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      0.010784  0.000000  0.002280        0.00000                         
SCALE2      0.000000  0.016063  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008615        0.00000                         
ATOM      1  N   GLU A 207      -7.639 -22.023  27.198  1.00 74.26           N  
ANISOU    1  N   GLU A 207     9755   9224   9237    672   1441   2462       N  
ATOM      2  CA  GLU A 207      -6.436 -21.206  27.306  1.00 68.36           C  
ANISOU    2  CA  GLU A 207     9046   8506   8421    884   1334   2396       C  
ATOM      3  C   GLU A 207      -5.971 -20.713  25.940  1.00 60.97           C  
ANISOU    3  C   GLU A 207     8061   7532   7572    894   1230   2209       C  
ATOM      4  O   GLU A 207      -5.644 -19.538  25.775  1.00 61.74           O  
ANISOU    4  O   GLU A 207     8093   7759   7607   1008   1154   2109       O  
ATOM      5  CB  GLU A 207      -5.314 -21.987  27.997  1.00 73.42           C  
ANISOU    5  CB  GLU A 207     9859   8986   9050    994   1318   2516       C  
ATOM      6  CG  GLU A 207      -4.004 -21.219  28.133  1.00 75.79           C  
ANISOU    6  CG  GLU A 207    10190   9321   9285   1204   1201   2451       C  
ATOM      7  CD  GLU A 207      -4.142 -19.970  28.987  1.00 80.68           C  
ANISOU    7  CD  GLU A 207    10741  10183   9730   1312   1187   2440       C  
ATOM      8  OE1 GLU A 207      -3.186 -19.166  29.030  1.00 80.77           O  
ANISOU    8  OE1 GLU A 207    10756  10248   9684   1459   1088   2362       O  
ATOM      9  OE2 GLU A 207      -5.208 -19.791  29.614  1.00 84.75           O  
ANISOU    9  OE2 GLU A 207    11199  10834  10168   1245   1280   2502       O  
ATOM     10  N   SER A 208      -5.940 -21.617  24.965  1.00 58.36           N  
ANISOU   10  N   SER A 208     7773   7020   7380    768   1231   2162       N  
ATOM     11  CA  SER A 208      -5.552 -21.263  23.604  1.00 57.13           C  
ANISOU   11  CA  SER A 208     7580   6827   7297    751   1144   1986       C  
ATOM     12  C   SER A 208      -6.408 -20.120  23.073  1.00 53.55           C  
ANISOU   12  C   SER A 208     6960   6584   6803    711   1109   1889       C  
ATOM     13  O   SER A 208      -5.904 -19.203  22.428  1.00 52.26           O  
ANISOU   13  O   SER A 208     6756   6480   6620    793   1019   1771       O  
ATOM     14  CB  SER A 208      -5.665 -22.476  22.680  1.00 63.32           C  
ANISOU   14  CB  SER A 208     8433   7401   8226    582   1175   1947       C  
ATOM     15  OG  SER A 208      -4.706 -23.462  23.016  1.00 70.66           O  
ANISOU   15  OG  SER A 208     9523   8109   9215    651   1195   2017       O  
ATOM     16  N   ALA A 209      -7.706 -20.183  23.350  1.00 55.39           N  
ANISOU   16  N   ALA A 209     7090   6928   7026    587   1182   1948       N  
ATOM     17  CA  ALA A 209      -8.634 -19.140  22.929  1.00 55.33           C  
ANISOU   17  CA  ALA A 209     6907   7127   6990    561   1154   1876       C  
ATOM     18  C   ALA A 209      -8.264 -17.801  23.560  1.00 53.93           C  
ANISOU   18  C   ALA A 209     6693   7102   6695    765   1114   1857       C  
ATOM     19  O   ALA A 209      -8.344 -16.759  22.913  1.00 49.89           O  
ANISOU   19  O   ALA A 209     6093   6691   6173    814   1038   1755       O  
ATOM     20  CB  ALA A 209     -10.062 -19.524  23.285  1.00 57.18           C  
ANISOU   20  CB  ALA A 209     7027   7462   7236    403   1255   1959       C  
ATOM     21  N   ASP A 210      -7.855 -17.839  24.825  1.00 53.29           N  
ANISOU   21  N   ASP A 210     6690   7032   6524    878   1162   1958       N  
ATOM     22  CA  ASP A 210      -7.424 -16.637  25.529  1.00 53.02           C  
ANISOU   22  CA  ASP A 210     6646   7130   6370   1063   1128   1934       C  
ATOM     23  C   ASP A 210      -6.131 -16.088  24.926  1.00 56.24           C  
ANISOU   23  C   ASP A 210     7117   7466   6783   1177   1008   1825       C  
ATOM     24  O   ASP A 210      -5.946 -14.875  24.828  1.00 56.69           O  
ANISOU   24  O   ASP A 210     7126   7626   6788   1280    948   1740       O  
ATOM     25  CB  ASP A 210      -7.230 -16.931  27.019  1.00 55.90           C  
ANISOU   25  CB  ASP A 210     7096   7522   6620   1139   1203   2069       C  
ATOM     26  CG  ASP A 210      -8.527 -17.314  27.714  1.00 62.30           C  
ANISOU   26  CG  ASP A 210     7834   8435   7402   1032   1338   2177       C  
ATOM     27  OD1 ASP A 210      -9.554 -16.645  27.479  1.00 62.25           O  
ANISOU   27  OD1 ASP A 210     7672   8579   7400    996   1369   2127       O  
ATOM     28  OD2 ASP A 210      -8.519 -18.283  28.501  1.00 64.96           O  
ANISOU   28  OD2 ASP A 210     8265   8705   7713    985   1417   2318       O  
ATOM     29  N   LEU A 211      -5.240 -16.985  24.520  1.00 55.51           N  
ANISOU   29  N   LEU A 211     7133   7194   6763   1158    979   1827       N  
ATOM     30  CA  LEU A 211      -3.973 -16.578  23.922  1.00 54.47           C  
ANISOU   30  CA  LEU A 211     7052   6996   6646   1255    877   1726       C  
ATOM     31  C   LEU A 211      -4.179 -15.984  22.530  1.00 54.65           C  
ANISOU   31  C   LEU A 211     6996   7041   6728   1188    813   1586       C  
ATOM     32  O   LEU A 211      -3.502 -15.031  22.148  1.00 56.06           O  
ANISOU   32  O   LEU A 211     7165   7259   6876   1276    734   1495       O  
ATOM     33  CB  LEU A 211      -3.000 -17.758  23.865  1.00 49.00           C  
ANISOU   33  CB  LEU A 211     6486   6106   6027   1262    877   1766       C  
ATOM     34  CG  LEU A 211      -2.574 -18.334  25.218  1.00 49.15           C  
ANISOU   34  CG  LEU A 211     6600   6092   5981   1352    916   1918       C  
ATOM     35  CD1 LEU A 211      -1.743 -19.597  25.034  1.00 47.19           C  
ANISOU   35  CD1 LEU A 211     6470   5625   5837   1356    919   1966       C  
ATOM     36  CD2 LEU A 211      -1.811 -17.294  26.026  1.00 48.71           C  
ANISOU   36  CD2 LEU A 211     6547   6165   5795   1523    851   1908       C  
ATOM     37  N   ARG A 212      -5.113 -16.552  21.773  1.00 50.58           N  
ANISOU   37  N   ARG A 212     6427   6503   6290   1023    845   1575       N  
ATOM     38  CA  ARG A 212      -5.448 -16.016  20.460  1.00 46.99           C  
ANISOU   38  CA  ARG A 212     5890   6090   5872    945    779   1458       C  
ATOM     39  C   ARG A 212      -5.995 -14.602  20.602  1.00 43.93           C  
ANISOU   39  C   ARG A 212     5391   5887   5413   1027    742   1434       C  
ATOM     40  O   ARG A 212      -5.662 -13.715  19.818  1.00 49.73           O  
ANISOU   40  O   ARG A 212     6101   6655   6139   1064    659   1342       O  
ATOM     41  CB  ARG A 212      -6.479 -16.903  19.761  1.00 52.09           C  
ANISOU   41  CB  ARG A 212     6487   6704   6599    739    818   1460       C  
ATOM     42  CG  ARG A 212      -5.931 -18.215  19.228  1.00 58.24           C  
ANISOU   42  CG  ARG A 212     7386   7276   7469    639    841   1438       C  
ATOM     43  CD  ARG A 212      -5.149 -17.988  17.950  1.00 67.42           C  
ANISOU   43  CD  ARG A 212     8579   8381   8656    631    762   1295       C  
ATOM     44  NE  ARG A 212      -3.847 -17.392  18.221  1.00 70.18           N  
ANISOU   44  NE  ARG A 212     8990   8710   8964    812    717   1268       N  
ATOM     45  CZ  ARG A 212      -3.098 -16.779  17.313  1.00 64.06           C  
ANISOU   45  CZ  ARG A 212     8221   7941   8179    845    645   1154       C  
ATOM     46  NH1 ARG A 212      -3.522 -16.668  16.060  1.00 63.79           N  
ANISOU   46  NH1 ARG A 212     8145   7933   8161    716    606   1060       N  
ATOM     47  NH2 ARG A 212      -1.926 -16.272  17.664  1.00 57.52           N  
ANISOU   47  NH2 ARG A 212     7437   7102   7317    999    611   1137       N  
ATOM     48  N   ALA A 213      -6.838 -14.400  21.612  1.00 45.27           N  
ANISOU   48  N   ALA A 213     5498   6170   5535   1054    813   1518       N  
ATOM     49  CA  ALA A 213      -7.434 -13.094  21.867  1.00 47.09           C  
ANISOU   49  CA  ALA A 213     5621   6566   5706   1148    798   1496       C  
ATOM     50  C   ALA A 213      -6.367 -12.062  22.210  1.00 48.69           C  
ANISOU   50  C   ALA A 213     5893   6773   5835   1318    738   1440       C  
ATOM     51  O   ALA A 213      -6.429 -10.919  21.761  1.00 47.44           O  
ANISOU   51  O   ALA A 213     5683   6681   5663   1380    676   1369       O  
ATOM     52  CB  ALA A 213      -8.466 -13.188  22.985  1.00 46.28           C  
ANISOU   52  CB  ALA A 213     5445   6579   5559   1149    909   1592       C  
ATOM     53  N   LEU A 214      -5.385 -12.473  23.007  1.00 50.24           N  
ANISOU   53  N   LEU A 214     6206   6898   5986   1388    751   1477       N  
ATOM     54  CA  LEU A 214      -4.300 -11.584  23.399  1.00 47.16           C  
ANISOU   54  CA  LEU A 214     5881   6516   5523   1532    689   1424       C  
ATOM     55  C   LEU A 214      -3.456 -11.188  22.193  1.00 44.85           C  
ANISOU   55  C   LEU A 214     5607   6152   5280   1524    590   1317       C  
ATOM     56  O   LEU A 214      -3.103 -10.019  22.026  1.00 42.93           O  
ANISOU   56  O   LEU A 214     5356   5955   4999   1601    531   1244       O  
ATOM     57  CB  LEU A 214      -3.421 -12.249  24.458  1.00 45.55           C  
ANISOU   57  CB  LEU A 214     5787   6258   5263   1597    711   1498       C  
ATOM     58  CG  LEU A 214      -2.186 -11.474  24.927  1.00 41.89           C  
ANISOU   58  CG  LEU A 214     5389   5808   4720   1731    638   1446       C  
ATOM     59  CD1 LEU A 214      -2.563 -10.073  25.381  1.00 42.55           C  
ANISOU   59  CD1 LEU A 214     5429   6022   4716   1815    632   1388       C  
ATOM     60  CD2 LEU A 214      -1.472 -12.229  26.043  1.00 42.92           C  
ANISOU   60  CD2 LEU A 214     5612   5909   4788   1791    656   1545       C  
ATOM     61  N   ALA A 215      -3.132 -12.169  21.357  1.00 42.19           N  
ANISOU   61  N   ALA A 215     5304   5700   5026   1426    582   1305       N  
ATOM     62  CA  ALA A 215      -2.335 -11.924  20.161  1.00 41.50           C  
ANISOU   62  CA  ALA A 215     5238   5549   4980   1401    506   1202       C  
ATOM     63  C   ALA A 215      -3.032 -10.924  19.245  1.00 41.89           C  
ANISOU   63  C   ALA A 215     5203   5684   5031   1363    455   1141       C  
ATOM     64  O   ALA A 215      -2.391 -10.047  18.669  1.00 42.56           O  
ANISOU   64  O   ALA A 215     5301   5772   5097   1403    386   1066       O  
ATOM     65  CB  ALA A 215      -2.069 -13.229  19.422  1.00 39.86           C  
ANISOU   65  CB  ALA A 215     5078   5205   4861   1291    527   1192       C  
ATOM     66  N   LYS A 216      -4.349 -11.057  19.123  1.00 44.50           N  
ANISOU   66  N   LYS A 216     5442   6084   5383   1286    488   1181       N  
ATOM     67  CA  LYS A 216      -5.130 -10.181  18.253  1.00 45.29           C  
ANISOU   67  CA  LYS A 216     5445   6273   5490   1255    432   1144       C  
ATOM     68  C   LYS A 216      -5.244  -8.766  18.810  1.00 44.15           C  
ANISOU   68  C   LYS A 216     5269   6218   5287   1399    410   1136       C  
ATOM     69  O   LYS A 216      -5.189  -7.792  18.060  1.00 45.49           O  
ANISOU   69  O   LYS A 216     5419   6410   5453   1423    336   1085       O  
ATOM     70  CB  LYS A 216      -6.523 -10.766  18.009  1.00 50.18           C  
ANISOU   70  CB  LYS A 216     5953   6958   6155   1131    470   1193       C  
ATOM     71  CG  LYS A 216      -6.506 -12.102  17.283  0.80 56.55           C  
ANISOU   71  CG  LYS A 216     6796   7667   7025    962    485   1181       C  
ATOM     72  CD  LYS A 216      -7.898 -12.516  16.840  0.50 60.53           C  
ANISOU   72  CD  LYS A 216     7174   8254   7572    815    498   1211       C  
ATOM     73  CE  LYS A 216      -7.879 -13.896  16.205  0.50 63.03           C  
ANISOU   73  CE  LYS A 216     7544   8455   7949    633    522   1188       C  
ATOM     74  NZ  LYS A 216      -6.867 -13.988  15.117  0.50 62.55           N  
ANISOU   74  NZ  LYS A 216     7581   8294   7891    601    459   1084       N  
ATOM     75  N   HIS A 217      -5.414  -8.659  20.126  1.00 42.67           N  
ANISOU   75  N   HIS A 217     5085   6076   5051   1492    479   1185       N  
ATOM     76  CA  HIS A 217      -5.461  -7.362  20.788  1.00 41.32           C  
ANISOU   76  CA  HIS A 217     4905   5975   4820   1634    473   1161       C  
ATOM     77  C   HIS A 217      -4.179  -6.585  20.518  1.00 39.69           C  
ANISOU   77  C   HIS A 217     4793   5703   4583   1698    394   1083       C  
ATOM     78  O   HIS A 217      -4.216  -5.418  20.127  1.00 38.25           O  
ANISOU   78  O   HIS A 217     4598   5539   4395   1753    342   1034       O  
ATOM     79  CB  HIS A 217      -5.663  -7.532  22.296  1.00 48.33           C  
ANISOU   79  CB  HIS A 217     5809   6918   5637   1710    567   1217       C  
ATOM     80  CG  HIS A 217      -5.338  -6.305  23.090  1.00 52.91           C  
ANISOU   80  CG  HIS A 217     6426   7540   6136   1856    563   1168       C  
ATOM     81  ND1 HIS A 217      -6.216  -5.252  23.230  1.00 56.29           N  
ANISOU   81  ND1 HIS A 217     6777   8052   6560   1936    583   1144       N  
ATOM     82  CD2 HIS A 217      -4.227  -5.960  23.785  1.00 54.56           C  
ANISOU   82  CD2 HIS A 217     6742   7719   6268   1935    539   1130       C  
ATOM     83  CE1 HIS A 217      -5.662  -4.312  23.974  1.00 58.15           C  
ANISOU   83  CE1 HIS A 217     7084   8291   6718   2053    579   1085       C  
ATOM     84  NE2 HIS A 217      -4.455  -4.717  24.323  1.00 54.52           N  
ANISOU   84  NE2 HIS A 217     6736   7772   6209   2046    548   1075       N  
ATOM     85  N   LEU A 218      -3.045  -7.248  20.719  1.00 38.38           N  
ANISOU   85  N   LEU A 218     4718   5458   4405   1689    387   1075       N  
ATOM     86  CA  LEU A 218      -1.742  -6.614  20.552  1.00 36.23           C  
ANISOU   86  CA  LEU A 218     4523   5136   4105   1739    320   1002       C  
ATOM     87  C   LEU A 218      -1.472  -6.209  19.104  1.00 35.19           C  
ANISOU   87  C   LEU A 218     4386   4965   4021   1669    247    940       C  
ATOM     88  O   LEU A 218      -0.934  -5.131  18.849  1.00 38.09           O  
ANISOU   88  O   LEU A 218     4782   5326   4363   1712    192    882       O  
ATOM     89  CB  LEU A 218      -0.630  -7.531  21.067  1.00 35.18           C  
ANISOU   89  CB  LEU A 218     4465   4941   3962   1748    328   1019       C  
ATOM     90  CG  LEU A 218      -0.614  -7.771  22.578  1.00 33.65           C  
ANISOU   90  CG  LEU A 218     4303   4793   3689   1831    379   1083       C  
ATOM     91  CD1 LEU A 218       0.367  -8.877  22.939  1.00 29.03           C  
ANISOU   91  CD1 LEU A 218     3781   4137   3112   1835    380   1126       C  
ATOM     92  CD2 LEU A 218      -0.267  -6.481  23.296  1.00 35.31           C  
ANISOU   92  CD2 LEU A 218     4540   5066   3811   1934    349   1027       C  
ATOM     93  N   TYR A 219      -1.838  -7.070  18.160  1.00 36.53           N  
ANISOU   93  N   TYR A 219     4526   5105   4249   1552    250    950       N  
ATOM     94  CA  TYR A 219      -1.669  -6.748  16.746  1.00 38.21           C  
ANISOU   94  CA  TYR A 219     4736   5297   4486   1471    185    895       C  
ATOM     95  C   TYR A 219      -2.511  -5.529  16.391  1.00 40.20           C  
ANISOU   95  C   TYR A 219     4929   5618   4725   1504    139    901       C  
ATOM     96  O   TYR A 219      -2.081  -4.657  15.634  1.00 39.77           O  
ANISOU   96  O   TYR A 219     4904   5550   4659   1502     75    859       O  
ATOM     97  CB  TYR A 219      -2.055  -7.937  15.862  1.00 38.31           C  
ANISOU   97  CB  TYR A 219     4728   5276   4550   1328    201    898       C  
ATOM     98  CG  TYR A 219      -1.856  -7.688  14.382  1.00 43.31           C  
ANISOU   98  CG  TYR A 219     5369   5901   5187   1231    137    837       C  
ATOM     99  CD1 TYR A 219      -0.676  -7.140  13.906  1.00 44.45           C  
ANISOU   99  CD1 TYR A 219     5578   6005   5305   1249    100    771       C  
ATOM    100  CD2 TYR A 219      -2.842  -8.016  13.462  1.00 53.92           C  
ANISOU  100  CD2 TYR A 219     6651   7287   6548   1111    115    846       C  
ATOM    101  CE1 TYR A 219      -0.487  -6.915  12.558  1.00 50.08           C  
ANISOU  101  CE1 TYR A 219     6305   6718   6004   1152     51    721       C  
ATOM    102  CE2 TYR A 219      -2.660  -7.795  12.110  1.00 53.89           C  
ANISOU  102  CE2 TYR A 219     6664   7289   6525   1016     53    793       C  
ATOM    103  CZ  TYR A 219      -1.481  -7.244  11.665  1.00 50.82           C  
ANISOU  103  CZ  TYR A 219     6349   6857   6102   1038     26    733       C  
ATOM    104  OH  TYR A 219      -1.291  -7.017  10.322  1.00 53.30           O  
ANISOU  104  OH  TYR A 219     6686   7185   6381    935    -26    686       O  
ATOM    105  N   ASP A 220      -3.711  -5.476  16.957  1.00 42.24           N  
ANISOU  105  N   ASP A 220     5104   5952   4992   1537    178    958       N  
ATOM    106  CA  ASP A 220      -4.631  -4.366  16.737  1.00 44.15           C  
ANISOU  106  CA  ASP A 220     5273   6264   5238   1595    143    975       C  
ATOM    107  C   ASP A 220      -4.024  -3.054  17.236  1.00 39.10           C  
ANISOU  107  C   ASP A 220     4699   5597   4558   1724    121    933       C  
ATOM    108  O   ASP A 220      -4.086  -2.033  16.550  1.00 36.31           O  
ANISOU  108  O   ASP A 220     4350   5234   4212   1748     56    919       O  
ATOM    109  CB  ASP A 220      -5.958  -4.650  17.447  1.00 47.29           C  
ANISOU  109  CB  ASP A 220     5556   6756   5655   1620    212   1040       C  
ATOM    110  CG  ASP A 220      -7.014  -3.599  17.169  1.00 50.45           C  
ANISOU  110  CG  ASP A 220     5854   7236   6079   1691    179   1063       C  
ATOM    111  OD1 ASP A 220      -7.450  -3.475  16.006  1.00 54.24           O  
ANISOU  111  OD1 ASP A 220     6279   7742   6590   1620    102   1076       O  
ATOM    112  OD2 ASP A 220      -7.424  -2.908  18.124  1.00 50.77           O  
ANISOU  112  OD2 ASP A 220     5867   7317   6105   1822    231   1069       O  
ATOM    113  N   SER A 221      -3.430  -3.097  18.428  1.00 36.76           N  
ANISOU  113  N   SER A 221     4461   5287   4218   1799    172    916       N  
ATOM    114  CA  SER A 221      -2.836  -1.914  19.051  1.00 33.29           C  
ANISOU  114  CA  SER A 221     4092   4823   3732   1908    157    862       C  
ATOM    115  C   SER A 221      -1.557  -1.521  18.336  1.00 33.45           C  
ANISOU  115  C   SER A 221     4199   4765   3746   1864     86    802       C  
ATOM    116  O   SER A 221      -1.251  -0.340  18.189  1.00 35.62           O  
ANISOU  116  O   SER A 221     4521   5005   4009   1910     43    760       O  
ATOM    117  CB  SER A 221      -2.514  -2.183  20.522  1.00 34.15           C  
ANISOU  117  CB  SER A 221     4241   4957   3776   1980    223    860       C  
ATOM    118  OG  SER A 221      -3.584  -2.840  21.173  1.00 48.99           O  
ANISOU  118  OG  SER A 221     6045   6913   5656   1990    306    926       O  
ATOM    119  N   TYR A 222      -0.796  -2.530  17.933  1.00 35.87           N  
ANISOU  119  N   TYR A 222     4527   5039   4062   1776     81    795       N  
ATOM    120  CA  TYR A 222       0.414  -2.337  17.148  1.00 32.80           C  
ANISOU  120  CA  TYR A 222     4200   4592   3672   1717     29    738       C  
ATOM    121  C   TYR A 222       0.086  -1.532  15.891  1.00 35.92           C  
ANISOU  121  C   TYR A 222     4589   4975   4085   1667    -31    734       C  
ATOM    122  O   TYR A 222       0.706  -0.503  15.619  1.00 39.36           O  
ANISOU  122  O   TYR A 222     5082   5371   4503   1678    -75    695       O  
ATOM    123  CB  TYR A 222       0.984  -3.710  16.790  1.00 32.03           C  
ANISOU  123  CB  TYR A 222     4104   4466   3600   1634     51    737       C  
ATOM    124  CG  TYR A 222       2.189  -3.751  15.872  1.00 33.79           C  
ANISOU  124  CG  TYR A 222     4368   4639   3830   1563     17    674       C  
ATOM    125  CD1 TYR A 222       2.037  -3.757  14.490  1.00 37.72           C  
ANISOU  125  CD1 TYR A 222     4861   5129   4344   1459    -11    658       C  
ATOM    126  CD2 TYR A 222       3.477  -3.855  16.389  1.00 32.72           C  
ANISOU  126  CD2 TYR A 222     4270   4481   3680   1596     17    632       C  
ATOM    127  CE1 TYR A 222       3.138  -3.831  13.645  1.00 35.22           C  
ANISOU  127  CE1 TYR A 222     4579   4777   4024   1389    -24    596       C  
ATOM    128  CE2 TYR A 222       4.585  -3.929  15.554  1.00 32.29           C  
ANISOU  128  CE2 TYR A 222     4235   4395   3639   1532     -1    571       C  
ATOM    129  CZ  TYR A 222       4.410  -3.917  14.183  1.00 33.83           C  
ANISOU  129  CZ  TYR A 222     4429   4578   3846   1428    -13    551       C  
ATOM    130  OH  TYR A 222       5.509  -3.996  13.350  1.00 33.97           O  
ANISOU  130  OH  TYR A 222     4465   4576   3868   1360    -14    485       O  
ATOM    131  N   ILE A 223      -0.900  -2.001  15.131  1.00 34.05           N  
ANISOU  131  N   ILE A 223     4285   4774   3878   1604    -38    780       N  
ATOM    132  CA  ILE A 223      -1.327  -1.304  13.920  1.00 32.56           C  
ANISOU  132  CA  ILE A 223     4084   4591   3694   1556   -106    797       C  
ATOM    133  C   ILE A 223      -1.747   0.127  14.236  1.00 38.34           C  
ANISOU  133  C   ILE A 223     4827   5316   4426   1670   -135    812       C  
ATOM    134  O   ILE A 223      -1.452   1.053  13.485  1.00 34.33           O  
ANISOU  134  O   ILE A 223     4368   4766   3908   1656   -195    809       O  
ATOM    135  CB  ILE A 223      -2.499  -2.025  13.224  1.00 38.65           C  
ANISOU  135  CB  ILE A 223     4763   5430   4493   1478   -116    850       C  
ATOM    136  CG1 ILE A 223      -2.090  -3.436  12.806  1.00 46.33           C  
ANISOU  136  CG1 ILE A 223     5744   6386   5472   1353    -84    821       C  
ATOM    137  CG2 ILE A 223      -2.961  -1.239  12.007  1.00 43.69           C  
ANISOU  137  CG2 ILE A 223     5387   6091   5121   1438   -204    881       C  
ATOM    138  CD1 ILE A 223      -0.856  -3.472  11.945  1.00 52.74           C  
ANISOU  138  CD1 ILE A 223     6639   7142   6257   1275   -106    755       C  
ATOM    139  N   LYS A 224      -2.425   0.305  15.364  1.00 38.34           N  
ANISOU  139  N   LYS A 224     4786   5348   4435   1783    -85    829       N  
ATOM    140  CA  LYS A 224      -2.911   1.621  15.760  1.00 41.08           C  
ANISOU  140  CA  LYS A 224     5141   5677   4790   1909    -95    833       C  
ATOM    141  C   LYS A 224      -1.802   2.543  16.271  1.00 39.80           C  
ANISOU  141  C   LYS A 224     5099   5430   4595   1955   -102    759       C  
ATOM    142  O   LYS A 224      -1.940   3.765  16.237  1.00 39.01           O  
ANISOU  142  O   LYS A 224     5042   5272   4507   2028   -129    750       O  
ATOM    143  CB  LYS A 224      -4.030   1.479  16.795  1.00 46.13           C  
ANISOU  143  CB  LYS A 224     5691   6391   5446   2013    -23    863       C  
ATOM    144  CG  LYS A 224      -5.329   0.932  16.205  1.00 41.06           C  
ANISOU  144  CG  LYS A 224     4908   5841   4851   1976    -30    940       C  
ATOM    145  CD  LYS A 224      -6.282   0.420  17.276  1.00 40.97           C  
ANISOU  145  CD  LYS A 224     4798   5920   4849   2037     66    968       C  
ATOM    146  CE  LYS A 224      -7.610  -0.011  16.663  1.00 42.65           C  
ANISOU  146  CE  LYS A 224     4851   6236   5116   1994     52   1043       C  
ATOM    147  NZ  LYS A 224      -8.587  -0.474  17.692  1.00 43.58           N  
ANISOU  147  NZ  LYS A 224     4858   6454   5247   2044    157   1074       N  
ATOM    148  N   SER A 225      -0.698   1.958  16.726  1.00 39.36           N  
ANISOU  148  N   SER A 225     5094   5361   4501   1909    -81    708       N  
ATOM    149  CA  SER A 225       0.392   2.732  17.318  1.00 38.82           C  
ANISOU  149  CA  SER A 225     5124   5233   4395   1937    -91    631       C  
ATOM    150  C   SER A 225       1.526   3.061  16.341  1.00 39.62           C  
ANISOU  150  C   SER A 225     5289   5273   4493   1832   -148    597       C  
ATOM    151  O   SER A 225       2.191   4.088  16.480  1.00 36.92           O  
ANISOU  151  O   SER A 225     5026   4865   4135   1841   -173    545       O  
ATOM    152  CB  SER A 225       0.965   1.997  18.535  1.00 38.26           C  
ANISOU  152  CB  SER A 225     5060   5202   4276   1962    -43    599       C  
ATOM    153  OG  SER A 225      -0.001   1.859  19.560  1.00 37.80           O  
ANISOU  153  OG  SER A 225     4959   5202   4200   2059     21    625       O  
ATOM    154  N   PHE A 226       1.755   2.184  15.368  1.00 33.73           N  
ANISOU  154  N   PHE A 226     4511   4548   3758   1725   -160    619       N  
ATOM    155  CA  PHE A 226       2.905   2.312  14.475  1.00 35.08           C  
ANISOU  155  CA  PHE A 226     4732   4681   3917   1617   -193    580       C  
ATOM    156  C   PHE A 226       2.477   2.559  13.033  1.00 35.64           C  
ANISOU  156  C   PHE A 226     4804   4745   3994   1534   -238    628       C  
ATOM    157  O   PHE A 226       2.056   1.633  12.342  1.00 41.83           O  
ANISOU  157  O   PHE A 226     5535   5574   4783   1468   -234    657       O  
ATOM    158  CB  PHE A 226       3.795   1.067  14.566  1.00 29.58           C  
ANISOU  158  CB  PHE A 226     4011   4013   3216   1560   -160    546       C  
ATOM    159  CG  PHE A 226       4.239   0.742  15.966  1.00 31.74           C  
ANISOU  159  CG  PHE A 226     4283   4307   3472   1641   -130    518       C  
ATOM    160  CD1 PHE A 226       5.136   1.564  16.630  1.00 33.38           C  
ANISOU  160  CD1 PHE A 226     4541   4494   3647   1667   -150    457       C  
ATOM    161  CD2 PHE A 226       3.756  -0.383  16.621  1.00 32.17           C  
ANISOU  161  CD2 PHE A 226     4288   4402   3534   1680    -84    557       C  
ATOM    162  CE1 PHE A 226       5.545   1.273  17.923  1.00 34.68           C  
ANISOU  162  CE1 PHE A 226     4706   4696   3777   1735   -135    434       C  
ATOM    163  CE2 PHE A 226       4.165  -0.683  17.913  1.00 33.69           C  
ANISOU  163  CE2 PHE A 226     4487   4620   3692   1752    -62    547       C  
ATOM    164  CZ  PHE A 226       5.060   0.146  18.563  1.00 32.60           C  
ANISOU  164  CZ  PHE A 226     4397   4478   3512   1783    -92    485       C  
ATOM    165  N   PRO A 227       2.586   3.818  12.579  1.00 33.79           N  
ANISOU  165  N   PRO A 227     4636   4448   3754   1532   -283    637       N  
ATOM    166  CA  PRO A 227       2.127   4.259  11.257  1.00 39.90           C  
ANISOU  166  CA  PRO A 227     5425   5214   4521   1467   -338    703       C  
ATOM    167  C   PRO A 227       2.763   3.495  10.097  1.00 44.04           C  
ANISOU  167  C   PRO A 227     5950   5776   5008   1315   -340    688       C  
ATOM    168  O   PRO A 227       2.097   3.288   9.084  1.00 50.21           O  
ANISOU  168  O   PRO A 227     6709   6599   5770   1254   -378    745       O  
ATOM    169  CB  PRO A 227       2.553   5.733  11.209  1.00 40.46           C  
ANISOU  169  CB  PRO A 227     5598   5183   4591   1486   -372    700       C  
ATOM    170  CG  PRO A 227       2.689   6.139  12.631  1.00 40.63           C  
ANISOU  170  CG  PRO A 227     5639   5168   4631   1598   -336    640       C  
ATOM    171  CD  PRO A 227       3.178   4.922  13.352  1.00 32.17           C  
ANISOU  171  CD  PRO A 227     4508   4169   3544   1588   -285    586       C  
ATOM    172  N   LEU A 228       4.022   3.091  10.231  1.00 40.25           N  
ANISOU  172  N   LEU A 228     5490   5289   4514   1254   -301    610       N  
ATOM    173  CA  LEU A 228       4.711   2.404   9.140  1.00 39.58           C  
ANISOU  173  CA  LEU A 228     5406   5236   4394   1117   -285    579       C  
ATOM    174  C   LEU A 228       5.030   0.965   9.498  1.00 38.40           C  
ANISOU  174  C   LEU A 228     5197   5126   4268   1111   -225    526       C  
ATOM    175  O   LEU A 228       6.060   0.687  10.098  1.00 37.54           O  
ANISOU  175  O   LEU A 228     5083   5007   4173   1126   -188    464       O  
ATOM    176  CB  LEU A 228       6.003   3.131   8.759  1.00 42.42           C  
ANISOU  176  CB  LEU A 228     5832   5559   4726   1036   -281    532       C  
ATOM    177  CG  LEU A 228       6.811   2.446   7.648  1.00 46.50           C  
ANISOU  177  CG  LEU A 228     6347   6119   5203    896   -244    486       C  
ATOM    178  CD1 LEU A 228       5.940   2.189   6.426  1.00 45.96           C  
ANISOU  178  CD1 LEU A 228     6284   6093   5085    818   -275    543       C  
ATOM    179  CD2 LEU A 228       8.048   3.257   7.264  1.00 44.41           C  
ANISOU  179  CD2 LEU A 228     6135   5829   4909    806   -233    447       C  
ATOM    180  N   THR A 229       4.145   0.053   9.119  1.00 38.21           N  
ANISOU  180  N   THR A 229     5126   5142   4249   1087   -220    555       N  
ATOM    181  CA  THR A 229       4.293  -1.355   9.460  1.00 34.93           C  
ANISOU  181  CA  THR A 229     4666   4739   3867   1084   -160    516       C  
ATOM    182  C   THR A 229       5.374  -2.029   8.620  1.00 35.15           C  
ANISOU  182  C   THR A 229     4710   4765   3879    980   -116    438       C  
ATOM    183  O   THR A 229       5.871  -1.453   7.651  1.00 33.70           O  
ANISOU  183  O   THR A 229     4568   4591   3647    890   -131    419       O  
ATOM    184  CB  THR A 229       2.973  -2.106   9.235  1.00 34.26           C  
ANISOU  184  CB  THR A 229     4529   4692   3795   1065   -166    565       C  
ATOM    185  OG1 THR A 229       2.592  -1.990   7.857  1.00 32.88           O  
ANISOU  185  OG1 THR A 229     4368   4555   3570    948   -208    578       O  
ATOM    186  CG2 THR A 229       1.873  -1.525  10.111  1.00 36.43           C  
ANISOU  186  CG2 THR A 229     4765   4984   4094   1177   -192    638       C  
ATOM    187  N   LYS A 230       5.732  -3.255   8.988  1.00 32.27           N  
ANISOU  187  N   LYS A 230     4316   4386   3558    994    -56    394       N  
ATOM    188  CA  LYS A 230       6.643  -4.045   8.172  1.00 32.94           C  
ANISOU  188  CA  LYS A 230     4410   4464   3643    909      0    311       C  
ATOM    189  C   LYS A 230       5.994  -4.384   6.834  1.00 28.70           C  
ANISOU  189  C   LYS A 230     3893   3956   3055    777     -6    301       C  
ATOM    190  O   LYS A 230       6.661  -4.413   5.800  1.00 31.87           O  
ANISOU  190  O   LYS A 230     4324   4374   3409    677     22    238       O  
ATOM    191  CB  LYS A 230       7.055  -5.334   8.885  1.00 33.71           C  
ANISOU  191  CB  LYS A 230     4476   4519   3812    971     64    278       C  
ATOM    192  CG  LYS A 230       7.994  -6.192   8.053  1.00 35.54           C  
ANISOU  192  CG  LYS A 230     4713   4731   4058    903    135    181       C  
ATOM    193  CD  LYS A 230       8.509  -7.414   8.812  1.00 34.82           C  
ANISOU  193  CD  LYS A 230     4595   4579   4055    990    196    158       C  
ATOM    194  CE  LYS A 230       9.490  -8.211   7.954  1.00 36.01           C  
ANISOU  194  CE  LYS A 230     4747   4703   4232    939    277     49       C  
ATOM    195  NZ  LYS A 230      10.171  -9.317   8.694  1.00 38.26           N  
ANISOU  195  NZ  LYS A 230     5003   4917   4616   1048    334     31       N  
ATOM    196  N   ALA A 231       4.692  -4.649   6.866  1.00 29.71           N  
ANISOU  196  N   ALA A 231     4000   4102   3186    772    -40    361       N  
ATOM    197  CA  ALA A 231       3.943  -4.967   5.654  1.00 35.15           C  
ANISOU  197  CA  ALA A 231     4699   4836   3819    641    -65    357       C  
ATOM    198  C   ALA A 231       4.069  -3.846   4.616  1.00 37.14           C  
ANISOU  198  C   ALA A 231     4996   5138   3976    565   -123    379       C  
ATOM    199  O   ALA A 231       4.338  -4.097   3.442  1.00 37.14           O  
ANISOU  199  O   ALA A 231     5035   5172   3904    436   -110    327       O  
ATOM    200  CB  ALA A 231       2.477  -5.232   5.989  1.00 36.50           C  
ANISOU  200  CB  ALA A 231     4816   5037   4013    657   -107    433       C  
ATOM    201  N   LYS A 232       3.890  -2.606   5.057  1.00 32.29           N  
ANISOU  201  N   LYS A 232     4387   4522   3359    643   -182    457       N  
ATOM    202  CA  LYS A 232       4.009  -1.467   4.155  1.00 30.58           C  
ANISOU  202  CA  LYS A 232     4227   4332   3062    581   -240    499       C  
ATOM    203  C   LYS A 232       5.459  -1.256   3.736  1.00 31.79           C  
ANISOU  203  C   LYS A 232     4430   4467   3182    517   -182    423       C  
ATOM    204  O   LYS A 232       5.754  -1.018   2.563  1.00 33.82           O  
ANISOU  204  O   LYS A 232     4738   4764   3348    393   -185    412       O  
ATOM    205  CB  LYS A 232       3.452  -0.201   4.804  1.00 32.33           C  
ANISOU  205  CB  LYS A 232     4450   4528   3308    693   -309    596       C  
ATOM    206  CG  LYS A 232       3.592   1.036   3.928  1.00 41.95           C  
ANISOU  206  CG  LYS A 232     5741   5745   4452    638   -370    657       C  
ATOM    207  CD  LYS A 232       2.870   2.240   4.514  1.00 47.82           C  
ANISOU  207  CD  LYS A 232     6490   6445   5233    761   -440    756       C  
ATOM    208  CE  LYS A 232       3.002   3.451   3.598  1.00 51.38           C  
ANISOU  208  CE  LYS A 232     7030   6874   5617    705   -502    833       C  
ATOM    209  NZ  LYS A 232       2.339   4.660   4.153  1.00 48.40           N  
ANISOU  209  NZ  LYS A 232     6671   6428   5291    838   -564    925       N  
ATOM    210  N   ALA A 233       6.366  -1.355   4.702  1.00 31.50           N  
ANISOU  210  N   ALA A 233     4373   4384   3213    597   -128    372       N  
ATOM    211  CA  ALA A 233       7.786  -1.189   4.431  1.00 31.42           C  
ANISOU  211  CA  ALA A 233     4382   4370   3188    545    -69    296       C  
ATOM    212  C   ALA A 233       8.271  -2.145   3.339  1.00 36.97           C  
ANISOU  212  C   ALA A 233     5090   5110   3845    425      4    206       C  
ATOM    213  O   ALA A 233       9.046  -1.755   2.464  1.00 39.13           O  
ANISOU  213  O   ALA A 233     5400   5417   4051    321     36    170       O  
ATOM    214  CB  ALA A 233       8.592  -1.378   5.709  1.00 34.15           C  
ANISOU  214  CB  ALA A 233     4680   4678   3619    658    -33    254       C  
ATOM    215  N   ARG A 234       7.812  -3.393   3.388  1.00 34.28           N  
ANISOU  215  N   ARG A 234     4721   4762   3541    433     38    166       N  
ATOM    216  CA  ARG A 234       8.218  -4.382   2.393  1.00 36.91           C  
ANISOU  216  CA  ARG A 234     5071   5117   3838    326    117     61       C  
ATOM    217  C   ARG A 234       7.609  -4.058   1.032  1.00 41.40           C  
ANISOU  217  C   ARG A 234     5699   5757   4275    176     74     82       C  
ATOM    218  O   ARG A 234       8.263  -4.214   0.001  1.00 42.17           O  
ANISOU  218  O   ARG A 234     5835   5897   4292     59    135      4       O  
ATOM    219  CB  ARG A 234       7.833  -5.805   2.814  1.00 38.18           C  
ANISOU  219  CB  ARG A 234     5202   5227   4079    367    164     13       C  
ATOM    220  CG  ARG A 234       8.283  -6.218   4.212  1.00 45.18           C  
ANISOU  220  CG  ARG A 234     6034   6045   5087    522    193     18       C  
ATOM    221  CD  ARG A 234       9.592  -5.556   4.632  1.00 53.07           C  
ANISOU  221  CD  ARG A 234     7007   7050   6107    578    216     -6       C  
ATOM    222  NE  ARG A 234      10.744  -6.052   3.886  1.00 59.67           N  
ANISOU  222  NE  ARG A 234     7835   7898   6938    520    312   -121       N  
ATOM    223  CZ  ARG A 234      12.007  -5.754   4.180  1.00 64.28           C  
ANISOU  223  CZ  ARG A 234     8371   8497   7555    560    352   -164       C  
ATOM    224  NH1 ARG A 234      12.995  -6.248   3.443  1.00 69.26           N  
ANISOU  224  NH1 ARG A 234     8982   9150   8186    509    451   -274       N  
ATOM    225  NH2 ARG A 234      12.284  -4.964   5.211  1.00 49.15           N  
ANISOU  225  NH2 ARG A 234     6422   6583   5671    647    294   -105       N  
ATOM    226  N   ALA A 235       6.356  -3.609   1.035  1.00 36.34           N  
ANISOU  226  N   ALA A 235     5060   5140   3607    182    -29    188       N  
ATOM    227  CA  ALA A 235       5.676  -3.248  -0.205  1.00 38.51           C  
ANISOU  227  CA  ALA A 235     5384   5497   3750     50    -96    232       C  
ATOM    228  C   ALA A 235       6.420  -2.123  -0.916  1.00 43.13           C  
ANISOU  228  C   ALA A 235     6035   6112   4240    -20   -103    263       C  
ATOM    229  O   ALA A 235       6.470  -2.079  -2.144  1.00 48.72           O  
ANISOU  229  O   ALA A 235     6802   6894   4817   -163   -104    248       O  
ATOM    230  CB  ALA A 235       4.234  -2.848   0.066  1.00 31.42           C  
ANISOU  230  CB  ALA A 235     4453   4624   2862     99   -215    357       C  
ATOM    231  N   ILE A 236       6.997  -1.216  -0.136  1.00 41.05           N  
ANISOU  231  N   ILE A 236     5767   5793   4036     71   -106    304       N  
ATOM    232  CA  ILE A 236       7.771  -0.112  -0.689  1.00 41.68           C  
ANISOU  232  CA  ILE A 236     5911   5882   4043      0   -105    336       C  
ATOM    233  C   ILE A 236       9.124  -0.594  -1.214  1.00 40.10           C  
ANISOU  233  C   ILE A 236     5713   5711   3811    -93     22    207       C  
ATOM    234  O   ILE A 236       9.529  -0.250  -2.324  1.00 39.41           O  
ANISOU  234  O   ILE A 236     5689   5685   3601   -233     48    202       O  
ATOM    235  CB  ILE A 236       8.008   0.985   0.361  1.00 38.75           C  
ANISOU  235  CB  ILE A 236     5537   5433   3754    115   -142    402       C  
ATOM    236  CG1 ILE A 236       6.681   1.621   0.780  1.00 41.49           C  
ANISOU  236  CG1 ILE A 236     5887   5752   4127    211   -257    530       C  
ATOM    237  CG2 ILE A 236       8.973   2.037  -0.175  1.00 40.44           C  
ANISOU  237  CG2 ILE A 236     5818   5642   3904     20   -121    419       C  
ATOM    238  CD1 ILE A 236       6.818   2.617   1.916  1.00 37.04           C  
ANISOU  238  CD1 ILE A 236     5325   5098   3649    337   -285    575       C  
ATOM    239  N   LEU A 237       9.813  -1.396  -0.408  1.00 38.56           N  
ANISOU  239  N   LEU A 237     5447   5478   3726    -10    103    109       N  
ATOM    240  CA  LEU A 237      11.137  -1.904  -0.764  1.00 42.88           C  
ANISOU  240  CA  LEU A 237     5968   6051   4273    -65    230    -19       C  
ATOM    241  C   LEU A 237      11.128  -2.851  -1.966  1.00 47.34           C  
ANISOU  241  C   LEU A 237     6565   6676   4745   -189    305   -118       C  
ATOM    242  O   LEU A 237      12.069  -2.861  -2.756  1.00 52.95           O  
ANISOU  242  O   LEU A 237     7288   7442   5387   -291    401   -198       O  
ATOM    243  CB  LEU A 237      11.784  -2.604   0.437  1.00 35.82           C  
ANISOU  243  CB  LEU A 237     4981   5100   3528     78    283    -87       C  
ATOM    244  CG  LEU A 237      12.169  -1.729   1.630  1.00 40.62           C  
ANISOU  244  CG  LEU A 237     5551   5666   4215    184    235    -30       C  
ATOM    245  CD1 LEU A 237      12.452  -2.577   2.867  1.00 40.39           C  
ANISOU  245  CD1 LEU A 237     5439   5591   4317    336    258    -71       C  
ATOM    246  CD2 LEU A 237      13.361  -0.846   1.284  1.00 46.02           C  
ANISOU  246  CD2 LEU A 237     6236   6388   4864     99    277    -54       C  
ATOM    247  N   THR A 238      10.070  -3.643  -2.103  1.00 49.91           N  
ANISOU  247  N   THR A 238     6902   6997   5065   -190    267   -119       N  
ATOM    248  CA  THR A 238      10.034  -4.683  -3.130  1.00 54.63           C  
ANISOU  248  CA  THR A 238     7534   7637   5585   -306    342   -238       C  
ATOM    249  C   THR A 238       9.172  -4.337  -4.347  1.00 62.97           C  
ANISOU  249  C   THR A 238     8674   8787   6464   -462    267   -185       C  
ATOM    250  O   THR A 238       8.912  -5.194  -5.193  1.00 64.19           O  
ANISOU  250  O   THR A 238     8867   8985   6537   -570    306   -281       O  
ATOM    251  CB  THR A 238       9.548  -6.018  -2.548  1.00 55.15           C  
ANISOU  251  CB  THR A 238     7562   7628   5762   -230    369   -305       C  
ATOM    252  OG1 THR A 238       8.169  -5.901  -2.175  1.00 56.99           O  
ANISOU  252  OG1 THR A 238     7792   7855   6006   -203    245   -194       O  
ATOM    253  CG2 THR A 238      10.376  -6.396  -1.328  1.00 54.23           C  
ANISOU  253  CG2 THR A 238     7367   7425   5814    -68    431   -338       C  
ATOM    254  N   GLY A 239       8.827  -3.071  -4.534  1.00 64.66           N  
ANISOU  254  N   GLY A 239     8926   9037   6604   -485    164    -42       N  
ATOM    255  CA  GLY A 239       7.971  -2.639  -5.632  1.00 65.61           C  
ANISOU  255  CA  GLY A 239     9122   9252   6555   -616     68     41       C  
ATOM    256  C   GLY A 239       6.515  -3.081  -5.805  1.00 64.46           C  
ANISOU  256  C   GLY A 239     8968   9144   6381   -632    -47     91       C  
ATOM    257  O   GLY A 239       6.139  -3.530  -6.866  1.00 63.85           O  
ANISOU  257  O   GLY A 239     8939   9158   6162   -777    -59     47       O  
ATOM    258  N   LYS A 240       5.685  -2.942  -4.768  1.00 62.81           N  
ANISOU  258  N   LYS A 240     8690   8875   6299   -492   -132    181       N  
ATOM    259  CA  LYS A 240       4.290  -3.351  -4.854  1.00 62.51           C  
ANISOU  259  CA  LYS A 240     8618   8883   6250   -506   -239    233       C  
ATOM    260  C   LYS A 240       3.462  -2.162  -5.346  1.00 63.02           C  
ANISOU  260  C   LYS A 240     8706   9020   6218   -521   -392    410       C  
ATOM    261  O   LYS A 240       3.847  -1.009  -5.146  1.00 65.77           O  
ANISOU  261  O   LYS A 240     9086   9331   6573   -461   -417    508       O  
ATOM    262  CB  LYS A 240       3.783  -3.847  -3.494  1.00 58.89           C  
ANISOU  262  CB  LYS A 240     8065   8336   5974   -351   -240    241       C  
ATOM    263  N   THR A 241       2.341  -2.439  -6.002  1.00 62.23           N  
ANISOU  263  N   THR A 241     8592   9021   6030   -604   -497    452       N  
ATOM    264  CA  THR A 241       1.486  -1.375  -6.523  1.00 63.64           C  
ANISOU  264  CA  THR A 241     8783   9279   6118   -609   -657    632       C  
ATOM    265  C   THR A 241       0.583  -0.790  -5.437  1.00 61.73           C  
ANISOU  265  C   THR A 241     8446   8984   6027   -421   -747    762       C  
ATOM    266  O   THR A 241      -0.182   0.145  -5.681  1.00 62.93           O  
ANISOU  266  O   THR A 241     8589   9179   6142   -379   -880    923       O  
ATOM    267  CB  THR A 241       0.635  -1.871  -7.704  1.00 63.03           C  
ANISOU  267  CB  THR A 241     8717   9357   5873   -777   -751    631       C  
ATOM    268  OG1 THR A 241      -0.233  -2.922  -7.262  1.00 58.58           O  
ANISOU  268  OG1 THR A 241     8055   8807   5395   -772   -766    568       O  
ATOM    269  CG2 THR A 241       1.535  -2.404  -8.805  1.00 67.79           C  
ANISOU  269  CG2 THR A 241     9427  10020   6310   -965   -651    491       C  
ATOM    270  N   THR A 242       0.684  -1.346  -4.235  1.00 60.35           N  
ANISOU  270  N   THR A 242     8199   8713   6017   -304   -669    694       N  
ATOM    271  CA  THR A 242      -0.074  -0.852  -3.093  1.00 58.83           C  
ANISOU  271  CA  THR A 242     7917   8468   5968   -122   -723    794       C  
ATOM    272  C   THR A 242       0.592   0.394  -2.517  1.00 62.19           C  
ANISOU  272  C   THR A 242     8392   8791   6446      0   -711    864       C  
ATOM    273  O   THR A 242      -0.038   1.176  -1.808  1.00 58.66           O  
ANISOU  273  O   THR A 242     7901   8304   6083    146   -774    970       O  
ATOM    274  CB  THR A 242      -0.168  -1.918  -1.986  1.00 50.19           C  
ANISOU  274  CB  THR A 242     6741   7312   5015    -51   -636    700       C  
ATOM    275  OG1 THR A 242       1.152  -2.367  -1.650  1.00 48.08           O  
ANISOU  275  OG1 THR A 242     6525   6957   4785    -52   -499    575       O  
ATOM    276  CG2 THR A 242      -0.997  -3.102  -2.454  1.00 46.47           C  
ANISOU  276  CG2 THR A 242     6218   6925   4514   -171   -656    642       C  
ATOM    277  N   ASP A 243       1.870   0.576  -2.827  1.00 66.89           N  
ANISOU  277  N   ASP A 243     9077   9346   6994    -66   -625    797       N  
ATOM    278  CA  ASP A 243       2.626   1.702  -2.291  1.00 71.50           C  
ANISOU  278  CA  ASP A 243     9712   9828   7626     20   -604    843       C  
ATOM    279  C   ASP A 243       3.502   2.384  -3.336  1.00 72.80           C  
ANISOU  279  C   ASP A 243     9992  10009   7659   -112   -589    863       C  
ATOM    280  O   ASP A 243       3.507   2.000  -4.507  1.00 76.24           O  
ANISOU  280  O   ASP A 243    10472  10547   7950   -266   -595    843       O  
ATOM    281  CB  ASP A 243       3.462   1.259  -1.092  1.00 73.65           C  
ANISOU  281  CB  ASP A 243     9946  10009   8028    111   -490    732       C  
ATOM    282  CG  ASP A 243       2.641   1.155   0.174  1.00 80.34           C  
ANISOU  282  CG  ASP A 243    10704  10811   9009    277   -515    764       C  
ATOM    283  OD1 ASP A 243       1.839   2.075   0.432  1.00 81.45           O  
ANISOU  283  OD1 ASP A 243    10835  10936   9177    373   -604    883       O  
ATOM    284  OD2 ASP A 243       2.798   0.159   0.910  1.00 84.90           O  
ANISOU  284  OD2 ASP A 243    11224  11370   9664    316   -442    674       O  
ATOM    285  N   LYS A 244       4.243   3.398  -2.902  1.00 67.70           N  
ANISOU  285  N   LYS A 244     9399   9267   7057    -62   -565    898       N  
ATOM    286  CA  LYS A 244       5.014   4.226  -3.820  1.00 64.17           C  
ANISOU  286  CA  LYS A 244     9065   8824   6492   -186   -554    944       C  
ATOM    287  C   LYS A 244       6.521   4.071  -3.651  1.00 56.60           C  
ANISOU  287  C   LYS A 244     8123   7833   5549   -250   -413    817       C  
ATOM    288  O   LYS A 244       7.016   3.771  -2.564  1.00 51.17           O  
ANISOU  288  O   LYS A 244     7371   7080   4990   -153   -349    729       O  
ATOM    289  CB  LYS A 244       4.627   5.695  -3.664  1.00 68.08           C  
ANISOU  289  CB  LYS A 244     9627   9229   7012   -106   -651   1111       C  
ATOM    290  CG  LYS A 244       3.322   6.068  -4.338  1.00 73.23           C  
ANISOU  290  CG  LYS A 244    10287   9941   7596    -88   -799   1270       C  
ATOM    291  CD  LYS A 244       3.037   7.547  -4.153  1.00 79.99           C  
ANISOU  291  CD  LYS A 244    11219  10679   8495     10   -883   1434       C  
ATOM    292  CE  LYS A 244       4.290   8.376  -4.399  1.00 83.69           C  
ANISOU  292  CE  LYS A 244    11812  11060   8925    -88   -811   1436       C  
ATOM    293  NZ  LYS A 244       4.088   9.816  -4.079  1.00 85.33           N  
ANISOU  293  NZ  LYS A 244    12108  11113   9201     11   -878   1579       N  
ATOM    294  N   SER A 245       7.238   4.290  -4.746  1.00 52.32           N  
ANISOU  294  N   SER A 245     7662   7349   4867   -417   -367    812       N  
ATOM    295  CA  SER A 245       8.688   4.176  -4.773  1.00 51.05           C  
ANISOU  295  CA  SER A 245     7505   7186   4705   -499   -228    695       C  
ATOM    296  C   SER A 245       9.346   5.284  -3.966  1.00 48.57           C  
ANISOU  296  C   SER A 245     7213   6753   4487   -441   -221    736       C  
ATOM    297  O   SER A 245       8.903   6.432  -4.010  1.00 49.59           O  
ANISOU  297  O   SER A 245     7422   6813   4609   -419   -311    880       O  
ATOM    298  CB  SER A 245       9.181   4.238  -6.216  1.00 59.08           C  
ANISOU  298  CB  SER A 245     8610   8308   5531   -703   -180    695       C  
ATOM    299  OG  SER A 245       8.586   3.219  -7.000  1.00 61.46           O  
ANISOU  299  OG  SER A 245     8902   8722   5727   -773   -187    641       O  
ATOM    300  N   PRO A 246      10.418   4.943  -3.235  1.00 42.84           N  
ANISOU  300  N   PRO A 246     6417   6003   3855   -418   -117    608       N  
ATOM    301  CA  PRO A 246      11.153   5.912  -2.420  1.00 37.76           C  
ANISOU  301  CA  PRO A 246     5785   5261   3302   -383   -106    620       C  
ATOM    302  C   PRO A 246      12.145   6.702  -3.260  1.00 43.32           C  
ANISOU  302  C   PRO A 246     6567   5982   3911   -561    -46    643       C  
ATOM    303  O   PRO A 246      12.628   6.200  -4.276  1.00 44.11           O  
ANISOU  303  O   PRO A 246     6675   6191   3895   -701     35    591       O  
ATOM    304  CB  PRO A 246      11.933   5.027  -1.435  1.00 41.21           C  
ANISOU  304  CB  PRO A 246     6096   5705   3855   -304    -21    467       C  
ATOM    305  CG  PRO A 246      11.597   3.592  -1.792  1.00 42.21           C  
ANISOU  305  CG  PRO A 246     6161   5916   3960   -296     21    382       C  
ATOM    306  CD  PRO A 246      11.023   3.606  -3.162  1.00 39.71           C  
ANISOU  306  CD  PRO A 246     5928   5674   3486   -426     -6    443       C  
ATOM    307  N   PHE A 247      12.440   7.929  -2.847  1.00 47.88           N  
ANISOU  307  N   PHE A 247     7208   6450   4532   -564    -77    715       N  
ATOM    308  CA  PHE A 247      13.563   8.649  -3.424  1.00 50.76           C  
ANISOU  308  CA  PHE A 247     7630   6821   4835   -740     -1    719       C  
ATOM    309  C   PHE A 247      14.823   8.149  -2.732  1.00 48.01           C  
ANISOU  309  C   PHE A 247     7154   6512   4576   -747    109    555       C  
ATOM    310  O   PHE A 247      14.867   8.052  -1.508  1.00 44.73           O  
ANISOU  310  O   PHE A 247     6666   6038   4293   -611     83    500       O  
ATOM    311  CB  PHE A 247      13.416  10.159  -3.243  1.00 52.33           C  
ANISOU  311  CB  PHE A 247     7956   6870   5058   -753    -75    856       C  
ATOM    312  CG  PHE A 247      14.586  10.943  -3.771  1.00 55.24           C  
ANISOU  312  CG  PHE A 247     8385   7232   5371   -951      7    865       C  
ATOM    313  CD1 PHE A 247      15.643  11.277  -2.941  1.00 55.89           C  
ANISOU  313  CD1 PHE A 247     8409   7271   5555   -977     65    770       C  
ATOM    314  CD2 PHE A 247      14.635  11.332  -5.100  1.00 53.69           C  
ANISOU  314  CD2 PHE A 247     8302   7085   5013  -1123     25    970       C  
ATOM    315  CE1 PHE A 247      16.724  11.995  -3.426  1.00 57.46           C  
ANISOU  315  CE1 PHE A 247     8651   7472   5708  -1177    145    776       C  
ATOM    316  CE2 PHE A 247      15.713  12.049  -5.590  1.00 54.01           C  
ANISOU  316  CE2 PHE A 247     8397   7124   4998  -1321    112    984       C  
ATOM    317  CZ  PHE A 247      16.760  12.379  -4.752  1.00 56.18           C  
ANISOU  317  CZ  PHE A 247     8604   7353   5390  -1351    175    884       C  
ATOM    318  N   VAL A 248      15.843   7.820  -3.515  1.00 46.03           N  
ANISOU  318  N   VAL A 248     6870   6371   4248   -903    230    479       N  
ATOM    319  CA  VAL A 248      17.033   7.188  -2.962  1.00 44.91           C  
ANISOU  319  CA  VAL A 248     6579   6293   4192   -898    338    320       C  
ATOM    320  C   VAL A 248      18.181   8.166  -2.734  1.00 47.02           C  
ANISOU  320  C   VAL A 248     6839   6536   4491  -1017    385    311       C  
ATOM    321  O   VAL A 248      18.643   8.834  -3.662  1.00 49.17           O  
ANISOU  321  O   VAL A 248     7189   6835   4660  -1203    438    365       O  
ATOM    322  CB  VAL A 248      17.512   6.021  -3.844  1.00 42.44           C  
ANISOU  322  CB  VAL A 248     6196   6129   3802   -968    464    205       C  
ATOM    323  CG1 VAL A 248      18.822   5.456  -3.313  1.00 38.38           C  
ANISOU  323  CG1 VAL A 248     5516   5681   3386   -956    578     51       C  
ATOM    324  CG2 VAL A 248      16.440   4.940  -3.907  1.00 36.80           C  
ANISOU  324  CG2 VAL A 248     5475   5428   3079   -851    421    187       C  
ATOM    325  N   ILE A 249      18.630   8.238  -1.486  1.00 43.42           N  
ANISOU  325  N   ILE A 249     6290   6034   4173   -920    363    244       N  
ATOM    326  CA  ILE A 249      19.755   9.080  -1.106  1.00 45.73           C  
ANISOU  326  CA  ILE A 249     6550   6312   4512  -1031    399    212       C  
ATOM    327  C   ILE A 249      21.005   8.225  -0.960  1.00 42.33           C  
ANISOU  327  C   ILE A 249     5927   6026   4130  -1053    515     58       C  
ATOM    328  O   ILE A 249      21.056   7.324  -0.125  1.00 44.19           O  
ANISOU  328  O   ILE A 249     6038   6293   4460   -894    504    -29       O  
ATOM    329  CB  ILE A 249      19.476   9.824   0.216  1.00 46.99           C  
ANISOU  329  CB  ILE A 249     6737   6334   4784   -921    289    233       C  
ATOM    330  CG1 ILE A 249      18.321  10.812   0.030  1.00 50.71           C  
ANISOU  330  CG1 ILE A 249     7399   6649   5220   -899    186    387       C  
ATOM    331  CG2 ILE A 249      20.729  10.537   0.706  1.00 45.86           C  
ANISOU  331  CG2 ILE A 249     6534   6194   4697  -1042    325    169       C  
ATOM    332  CD1 ILE A 249      17.763  11.360   1.328  1.00 51.60           C  
ANISOU  332  CD1 ILE A 249     7545   6623   5439   -746     83    397       C  
ATOM    333  N   TYR A 250      22.011   8.509  -1.779  1.00 45.28           N  
ANISOU  333  N   TYR A 250     6273   6490   4441  -1248    628     31       N  
ATOM    334  CA  TYR A 250      23.213   7.687  -1.827  1.00 48.07           C  
ANISOU  334  CA  TYR A 250     6430   6999   4834  -1274    757   -115       C  
ATOM    335  C   TYR A 250      24.485   8.534  -1.846  1.00 50.29           C  
ANISOU  335  C   TYR A 250     6644   7332   5131  -1462    825   -144       C  
ATOM    336  O   TYR A 250      25.592   7.997  -1.882  1.00 50.11           O  
ANISOU  336  O   TYR A 250     6438   7451   5150  -1498    934   -261       O  
ATOM    337  CB  TYR A 250      23.178   6.782  -3.060  1.00 46.12           C  
ANISOU  337  CB  TYR A 250     6180   6867   4477  -1324    875   -157       C  
ATOM    338  CG  TYR A 250      23.210   7.547  -4.365  1.00 47.79           C  
ANISOU  338  CG  TYR A 250     6532   7105   4523  -1549    935    -69       C  
ATOM    339  CD1 TYR A 250      22.046   8.065  -4.919  1.00 49.96           C  
ANISOU  339  CD1 TYR A 250     7006   7288   4688  -1570    842     79       C  
ATOM    340  CD2 TYR A 250      24.405   7.754  -5.040  1.00 51.15           C  
ANISOU  340  CD2 TYR A 250     6883   7654   4897  -1741   1084   -125       C  
ATOM    341  CE1 TYR A 250      22.071   8.768  -6.112  1.00 50.38           C  
ANISOU  341  CE1 TYR A 250     7197   7368   4579  -1775    888    179       C  
ATOM    342  CE2 TYR A 250      24.441   8.456  -6.233  1.00 55.32           C  
ANISOU  342  CE2 TYR A 250     7549   8211   5259  -1957   1145    -32       C  
ATOM    343  CZ  TYR A 250      23.271   8.961  -6.764  1.00 52.40           C  
ANISOU  343  CZ  TYR A 250     7392   7743   4776  -1973   1042    125       C  
ATOM    344  OH  TYR A 250      23.307   9.661  -7.948  1.00 49.66           O  
ANISOU  344  OH  TYR A 250     7189   7426   4251  -2187   1094    234       O  
ATOM    345  N   ASP A 251      24.321   9.854  -1.838  1.00 53.52           N  
ANISOU  345  N   ASP A 251     7198   7623   5513  -1584    762    -36       N  
ATOM    346  CA  ASP A 251      25.458  10.774  -1.812  1.00 59.72           C  
ANISOU  346  CA  ASP A 251     7940   8434   6318  -1787    817    -53       C  
ATOM    347  C   ASP A 251      25.026  12.191  -1.433  1.00 66.50           C  
ANISOU  347  C   ASP A 251     8983   9097   7187  -1857    708     63       C  
ATOM    348  O   ASP A 251      23.883  12.411  -1.028  1.00 66.05           O  
ANISOU  348  O   ASP A 251     9060   8893   7142  -1714    588    143       O  
ATOM    349  CB  ASP A 251      26.215  10.767  -3.145  1.00 59.05           C  
ANISOU  349  CB  ASP A 251     7836   8487   6115  -2006    981    -60       C  
ATOM    350  CG  ASP A 251      25.397  11.331  -4.292  1.00 62.86           C  
ANISOU  350  CG  ASP A 251     8551   8897   6438  -2117    977     94       C  
ATOM    351  OD1 ASP A 251      24.289  11.851  -4.050  1.00 61.79           O  
ANISOU  351  OD1 ASP A 251     8587   8595   6297  -2030    841    213       O  
ATOM    352  OD2 ASP A 251      25.869  11.258  -5.446  1.00 70.06           O  
ANISOU  352  OD2 ASP A 251     9471   9927   7223  -2290   1110     98       O  
ATOM    353  N   MET A 252      25.939  13.148  -1.573  1.00 68.83           N  
ANISOU  353  N   MET A 252     9282   9387   7482  -2078    758     69       N  
ATOM    354  CA AMET A 252      25.674  14.522  -1.166  0.50 70.08           C  
ANISOU  354  CA AMET A 252     9616   9344   7668  -2160    667    161       C  
ATOM    355  CA BMET A 252      25.672  14.526  -1.167  0.50 70.08           C  
ANISOU  355  CA BMET A 252     9617   9343   7668  -2160    667    162       C  
ATOM    356  C   MET A 252      24.575  15.179  -2.001  1.00 68.64           C  
ANISOU  356  C   MET A 252     9691   9007   7383  -2182    621    343       C  
ATOM    357  O   MET A 252      23.613  15.720  -1.459  1.00 72.13           O  
ANISOU  357  O   MET A 252    10276   9263   7866  -2057    498    420       O  
ATOM    358  CB AMET A 252      26.959  15.351  -1.217  0.50 74.39           C  
ANISOU  358  CB AMET A 252    10105   9924   8234  -2422    744    123       C  
ATOM    359  CB BMET A 252      26.943  15.382  -1.217  0.50 74.40           C  
ANISOU  359  CB BMET A 252    10113   9920   8235  -2424    742    127       C  
ATOM    360  CG AMET A 252      28.109  14.751  -0.417  0.50 76.47           C  
ANISOU  360  CG AMET A 252    10092  10362   8599  -2409    780    -50       C  
ATOM    361  CG BMET A 252      27.985  15.039  -0.160  0.50 75.18           C  
ANISOU  361  CG BMET A 252     9969  10141   8454  -2405    742    -38       C  
ATOM    362  SD AMET A 252      27.673  14.423   1.303  0.50 70.69           S  
ANISOU  362  SD AMET A 252     9293   9564   8000  -2143    618   -135       S  
ATOM    363  SD BMET A 252      29.295  13.967  -0.779  0.50 82.04           S  
ANISOU  363  SD BMET A 252    10547  11315   9311  -2486    918   -167       S  
ATOM    364  CE AMET A 252      29.185  13.675   1.907  0.50249.32           C  
ANISOU  364  CE AMET A 252    31576  32440  30715  -2165    678   -312       C  
ATOM    365  CE BMET A 252      30.174  13.607   0.739  0.50251.23           C  
ANISOU  365  CE BMET A 252    31714  32845  30899  -2385    849   -329       C  
ATOM    366  N   ASN A 253      24.722  15.133  -3.320  1.00 64.82           N  
ANISOU  366  N   ASN A 253     9260   8607   6761  -2337    721    413       N  
ATOM    367  CA  ASN A 253      23.739  15.752  -4.204  1.00 69.15           C  
ANISOU  367  CA  ASN A 253    10048   9032   7194  -2371    672    602       C  
ATOM    368  C   ASN A 253      22.335  15.171  -4.042  1.00 68.29           C  
ANISOU  368  C   ASN A 253     9997   8869   7081  -2119    556    653       C  
ATOM    369  O   ASN A 253      21.367  15.910  -3.856  1.00 69.01           O  
ANISOU  369  O   ASN A 253    10257   8774   7188  -2036    438    781       O  
ATOM    370  CB  ASN A 253      24.185  15.658  -5.665  1.00 73.30           C  
ANISOU  370  CB  ASN A 253    10606   9696   7547  -2584    807    658       C  
ATOM    371  CG  ASN A 253      25.282  16.650  -6.008  1.00 76.87           C  
ANISOU  371  CG  ASN A 253    11088  10140   7980  -2871    904    686       C  
ATOM    372  OD1 ASN A 253      25.817  17.338  -5.137  1.00 74.29           O  
ANISOU  372  OD1 ASN A 253    10734   9715   7777  -2921    875    642       O  
ATOM    373  ND2 ASN A 253      25.622  16.726  -7.289  1.00 80.62           N  
ANISOU  373  ND2 ASN A 253    11622  10721   8290  -3074   1022    758       N  
ATOM    374  N   SER A 254      22.229  13.848  -4.118  1.00 63.32           N  
ANISOU  374  N   SER A 254     9223   8399   6436  -1998    593    550       N  
ATOM    375  CA  SER A 254      20.943  13.180  -3.963  1.00 61.44           C  
ANISOU  375  CA  SER A 254     9016   8132   6196  -1776    493    584       C  
ATOM    376  C   SER A 254      20.338  13.502  -2.597  1.00 63.00           C  
ANISOU  376  C   SER A 254     9223   8174   6541  -1582    366    577       C  
ATOM    377  O   SER A 254      19.118  13.522  -2.434  1.00 65.23           O  
ANISOU  377  O   SER A 254     9593   8364   6829  -1425    259    662       O  
ATOM    378  CB  SER A 254      21.088  11.668  -4.157  1.00 56.33           C  
ANISOU  378  CB  SER A 254     8203   7669   5529  -1693    569    450       C  
ATOM    379  OG  SER A 254      21.959  11.104  -3.193  1.00 56.04           O  
ANISOU  379  OG  SER A 254     7970   7699   5622  -1626    612    290       O  
ATOM    380  N   LEU A 255      21.199  13.762  -1.618  1.00 60.78           N  
ANISOU  380  N   LEU A 255     8845   7877   6373  -1598    378    472       N  
ATOM    381  CA  LEU A 255      20.742  14.184  -0.300  1.00 64.26           C  
ANISOU  381  CA  LEU A 255     9306   8173   6936  -1441    268    453       C  
ATOM    382  C   LEU A 255      20.108  15.568  -0.368  1.00 69.02           C  
ANISOU  382  C   LEU A 255    10131   8554   7539  -1478    189    598       C  
ATOM    383  O   LEU A 255      19.053  15.807   0.217  1.00 67.34           O  
ANISOU  383  O   LEU A 255     9999   8209   7377  -1300     87    649       O  
ATOM    384  CB  LEU A 255      21.899  14.194   0.698  1.00 65.05           C  
ANISOU  384  CB  LEU A 255     9255   8325   7136  -1480    296    306       C  
ATOM    385  CG  LEU A 255      21.618  14.920   2.016  1.00 67.96           C  
ANISOU  385  CG  LEU A 255     9677   8536   7609  -1382    191    281       C  
ATOM    386  CD1 LEU A 255      20.537  14.204   2.817  1.00 65.92           C  
ANISOU  386  CD1 LEU A 255     9396   8257   7395  -1113    108    269       C  
ATOM    387  CD2 LEU A 255      22.891  15.055   2.832  1.00 69.51           C  
ANISOU  387  CD2 LEU A 255     9730   8802   7877  -1477    216    143       C  
ATOM    388  N   MET A 256      20.760  16.476  -1.088  1.00 74.65           N  
ANISOU  388  N   MET A 256    10942   9222   8199  -1708    244    665       N  
ATOM    389  CA  MET A 256      20.277  17.847  -1.217  1.00 76.96           C  
ANISOU  389  CA  MET A 256    11460   9281   8498  -1761    180    811       C  
ATOM    390  C   MET A 256      18.978  17.906  -2.013  1.00 77.07           C  
ANISOU  390  C   MET A 256    11620   9233   8431  -1660    109    986       C  
ATOM    391  O   MET A 256      18.039  18.608  -1.635  1.00 78.68           O  
ANISOU  391  O   MET A 256    11959   9246   8691  -1529      7   1081       O  
ATOM    392  CB  MET A 256      21.336  18.725  -1.884  1.00 80.51           C  
ANISOU  392  CB  MET A 256    11980   9709   8902  -2055    269    851       C  
ATOM    393  CG  MET A 256      22.727  18.573  -1.295  1.00 81.41           C  
ANISOU  393  CG  MET A 256    11915   9938   9080  -2190    350    678       C  
ATOM    394  SD  MET A 256      22.812  18.970   0.461  1.00169.69           S  
ANISOU  394  SD  MET A 256    23055  20993  20427  -2066    257    543       S  
ATOM    395  CE  MET A 256      24.564  18.755   0.764  1.00 70.82           C  
ANISOU  395  CE  MET A 256    10304   8664   7941  -2279    359    371       C  
ATOM    396  N   MET A 257      18.930  17.169  -3.117  1.00 74.25           N  
ANISOU  396  N   MET A 257    11229   9044   7940  -1720    162   1025       N  
ATOM    397  CA  MET A 257      17.729  17.106  -3.939  1.00 76.29           C  
ANISOU  397  CA  MET A 257    11601   9286   8101  -1638     87   1186       C  
ATOM    398  C   MET A 257      16.584  16.475  -3.152  1.00 81.70           C  
ANISOU  398  C   MET A 257    12223   9953   8865  -1361    -15   1156       C  
ATOM    399  O   MET A 257      15.436  16.912  -3.244  1.00 83.72           O  
ANISOU  399  O   MET A 257    12592  10094   9125  -1235   -122   1294       O  
ATOM    400  CB  MET A 257      17.996  16.312  -5.218  1.00 75.90           C  
ANISOU  400  CB  MET A 257    11511   9448   7879  -1770    173   1195       C  
ATOM    401  N   GLY A 258      16.908  15.447  -2.375  1.00 81.62           N  
ANISOU  401  N   GLY A 258    12028  10060   8922  -1267     21    983       N  
ATOM    402  CA  GLY A 258      15.920  14.773  -1.555  1.00 82.71           C  
ANISOU  402  CA  GLY A 258    12095  10195   9136  -1021    -58    945       C  
ATOM    403  C   GLY A 258      15.612  15.541  -0.285  1.00 88.68           C  
ANISOU  403  C   GLY A 258    12893  10770  10030   -888   -129    928       C  
ATOM    404  O   GLY A 258      14.636  15.248   0.404  1.00 90.57           O  
ANISOU  404  O   GLY A 258    13107  10973  10332   -681   -201    927       O  
ATOM    405  N   GLU A 259      16.432  16.538  -0.011  1.00 95.45           N  
ANISOU  405  N   GLU A 259    13822  11516  10930  -1018   -103    913       N  
ATOM    406  CA  GLU A 259      16.264  17.309   1.184  1.00100.81           C  
ANISOU  406  CA  GLU A 259    14552  12020  11730   -918   -159    873       C  
ATOM    407  C   GLU A 259      15.144  18.293   0.965  1.00105.25           C  
ANISOU  407  C   GLU A 259    15303  12379  12309   -826   -246   1038       C  
ATOM    408  O   GLU A 259      15.301  19.470   1.225  1.00107.42           O  
ANISOU  408  O   GLU A 259    15720  12456  12640   -878   -263   1074       O  
ATOM    409  CB  GLU A 259      17.559  18.067   1.512  1.00103.10           C  
ANISOU  409  CB  GLU A 259    14858  12257  12058  -1115   -102    792       C  
ATOM    410  CG  GLU A 259      18.046  17.938   2.961  1.00103.81           C  
ANISOU  410  CG  GLU A 259    14842  12350  12250  -1043   -112    619       C  
ATOM    411  CD  GLU A 259      19.291  18.764   3.262  1.00107.49           C  
ANISOU  411  CD  GLU A 259    15324  12765  12752  -1257    -70    541       C  
ATOM    412  OE1 GLU A 259      20.212  18.256   3.922  1.00106.70           O  
ANISOU  412  OE1 GLU A 259    15059  12801  12681  -1296    -39    392       O  
ATOM    413  OE2 GLU A 259      19.348  19.932   2.848  1.00110.54           O  
ANISOU  413  OE2 GLU A 259    15888  12973  13139  -1389    -72    633       O  
ATOM    414  N   ASP A 260      13.998  17.774   0.526  1.00105.84           N  
ANISOU  414  N   ASP A 260    15370  12503  12343   -681   -304   1133       N  
ATOM    415  CA  ASP A 260      12.768  18.538   0.370  1.00106.20           C  
ANISOU  415  CA  ASP A 260    15553  12384  12414   -541   -401   1293       C  
ATOM    416  C   ASP A 260      11.643  17.854   1.138  1.00107.82           C  
ANISOU  416  C   ASP A 260    15656  12628  12682   -285   -461   1258       C  
ATOM    417  O   ASP A 260      10.763  18.512   1.692  1.00109.31           O  
ANISOU  417  O   ASP A 260    15917  12661  12957   -117   -526   1311       O  
ATOM    418  CB  ASP A 260      12.389  18.647  -1.108  1.00103.59           C  
ANISOU  418  CB  ASP A 260    15312  12096  11953   -634   -428   1478       C  
ATOM    419  CG  ASP A 260      13.514  19.195  -1.963  1.00103.46           C  
ANISOU  419  CG  ASP A 260    15387  12074  11850   -907   -351   1519       C  
ATOM    420  OD1 ASP A 260      13.311  19.341  -3.187  1.00104.61           O  
ANISOU  420  OD1 ASP A 260    15620  12259  11867  -1008   -365   1674       O  
ATOM    421  OD2 ASP A 260      14.601  19.482  -1.418  1.00102.52           O  
ANISOU  421  OD2 ASP A 260    15248  11921  11783  -1029   -279   1399       O  
ATOM    422  N   LYS A 261      11.685  16.526   1.163  1.00106.28           N  
ANISOU  422  N   LYS A 261    15294  12639  12447   -260   -430   1167       N  
ATOM    423  CA  LYS A 261      10.660  15.728   1.825  1.00103.30           C  
ANISOU  423  CA  LYS A 261    14807  12323  12118    -45   -473   1134       C  
ATOM    424  C   LYS A 261      10.595  16.034   3.317  1.00105.86           C  
ANISOU  424  C   LYS A 261    15113  12544  12564     98   -477   1027       C  
ATOM    425  O   LYS A 261      11.623  16.108   3.991  1.00107.28           O  
ANISOU  425  O   LYS A 261    15266  12719  12775     22   -425    899       O  
ATOM    426  CB  LYS A 261      10.928  14.237   1.608  1.00 97.19           C  
ANISOU  426  CB  LYS A 261    13871  11770  11285    -75   -422   1040       C  
ATOM    427  CG  LYS A 261      11.252  13.869   0.169  1.00 93.72           C  
ANISOU  427  CG  LYS A 261    13448  11452  10709   -250   -391   1101       C  
ATOM    428  CD  LYS A 261      11.373  12.361  -0.008  1.00 88.40           C  
ANISOU  428  CD  LYS A 261    12623  10973   9991   -254   -339    998       C  
ATOM    429  CE  LYS A 261      12.442  11.776   0.900  1.00 83.92           C  
ANISOU  429  CE  LYS A 261    11938  10457   9492   -261   -257    823       C  
ATOM    430  NZ  LYS A 261      13.788  12.347   0.623  1.00 82.65           N  
ANISOU  430  NZ  LYS A 261    11806  10289   9308   -449   -182    781       N  
ATOM    431  N   SER A 274      23.606  21.500  11.827  0.79120.83           N  
ANISOU  431  N   SER A 274    16786  14330  14792  -1527   -332   -533       N  
ATOM    432  CA  SER A 274      24.822  22.132  12.318  0.51123.08           C  
ANISOU  432  CA  SER A 274    17028  14646  15092  -1774   -348   -666       C  
ATOM    433  C   SER A 274      25.948  22.131  11.283  0.55120.99           C  
ANISOU  433  C   SER A 274    16647  14498  14825  -2035   -274   -631       C  
ATOM    434  O   SER A 274      27.072  21.743  11.570  0.89121.71           O  
ANISOU  434  O   SER A 274    16525  14805  14913  -2160   -278   -730       O  
ATOM    435  CB  SER A 274      25.276  21.525  13.659  1.00125.33           C  
ANISOU  435  CB  SER A 274    17142  15124  15355  -1696   -425   -824       C  
ATOM    436  OG  SER A 274      26.241  22.331  14.338  1.00127.78           O  
ANISOU  436  OG  SER A 274    17452  15424  15675  -1920   -467   -969       O  
ATOM    437  N   LYS A 275      25.609  22.543  10.070  1.00117.85           N  
ANISOU  437  N   LYS A 275    16384  13968  14424  -2109   -205   -482       N  
ATOM    438  CA  LYS A 275      26.559  22.733   8.980  1.00116.39           C  
ANISOU  438  CA  LYS A 275    16140  13855  14226  -2376   -116   -429       C  
ATOM    439  C   LYS A 275      27.480  21.610   8.589  1.00110.98           C  
ANISOU  439  C   LYS A 275    15164  13491  13514  -2420    -61   -462       C  
ATOM    440  O   LYS A 275      28.618  21.880   8.247  1.00115.80           O  
ANISOU  440  O   LYS A 275    15669  14200  14130  -2675     -6   -503       O  
ATOM    441  CB  LYS A 275      27.450  23.946   9.234  1.00119.94           C  
ANISOU  441  CB  LYS A 275    16671  14186  14715  -2675   -116   -508       C  
ATOM    442  CG  LYS A 275      28.490  24.170   8.131  1.00122.33           C  
ANISOU  442  CG  LYS A 275    16901  14576  15001  -2977    -11   -455       C  
ATOM    443  CD  LYS A 275      29.525  25.247   8.471  1.00126.37           C  
ANISOU  443  CD  LYS A 275    17443  15014  15556  -3300    -10   -555       C  
ATOM    444  CE  LYS A 275      30.937  24.660   8.663  1.00127.44           C  
ANISOU  444  CE  LYS A 275    17253  15476  15693  -3468     12   -680       C  
ATOM    445  NZ  LYS A 275      32.050  25.677   8.679  1.00129.85           N  
ANISOU  445  NZ  LYS A 275    17560  15744  16034  -3842     39   -753       N  
ATOM    446  N   GLU A 276      27.021  20.377   8.600  1.00 97.86           N  
ANISOU  446  N   GLU A 276    13370  11985  11828  -2183    -65   -444       N  
ATOM    447  CA  GLU A 276      27.866  19.280   8.193  1.00 87.45           C  
ANISOU  447  CA  GLU A 276    11782  10950  10493  -2203     -2   -477       C  
ATOM    448  C   GLU A 276      26.890  18.164   7.978  1.00 77.92           C  
ANISOU  448  C   GLU A 276    10553   9795   9259  -1928     -2   -410       C  
ATOM    449  O   GLU A 276      26.134  17.863   8.858  1.00 75.96           O  
ANISOU  449  O   GLU A 276    10336   9504   9023  -1713    -82   -433       O  
ATOM    450  CB  GLU A 276      28.851  18.927   9.280  1.00 86.69           C  
ANISOU  450  CB  GLU A 276    11461  11045  10433  -2223    -59   -635       C  
ATOM    451  CG  GLU A 276      29.770  17.858   8.858  1.00 87.81           C  
ANISOU  451  CG  GLU A 276    11319  11467  10577  -2237      9   -668       C  
ATOM    452  CD  GLU A 276      30.649  17.346   9.957  1.00 89.02           C  
ANISOU  452  CD  GLU A 276    11229  11828  10766  -2204    -64   -805       C  
ATOM    453  OE1 GLU A 276      30.652  17.894  11.061  1.00 89.57           O  
ANISOU  453  OE1 GLU A 276    11349  11837  10846  -2210   -171   -885       O  
ATOM    454  OE2 GLU A 276      31.357  16.380   9.698  1.00 89.12           O  
ANISOU  454  OE2 GLU A 276    10997  12072  10795  -2171    -14   -832       O  
ATOM    455  N   VAL A 277      26.879  17.560   6.806  1.00 70.72           N  
ANISOU  455  N   VAL A 277     9594   8973   8303  -1943     91   -329       N  
ATOM    456  CA  VAL A 277      25.873  16.534   6.552  1.00 68.25           C  
ANISOU  456  CA  VAL A 277     9281   8691   7962  -1699     88   -265       C  
ATOM    457  C   VAL A 277      25.805  15.458   7.637  1.00 61.06           C  
ANISOU  457  C   VAL A 277     8203   7911   7087  -1473     27   -356       C  
ATOM    458  O   VAL A 277      24.718  15.032   8.025  1.00 57.73           O  
ANISOU  458  O   VAL A 277     7849   7424   6660  -1254    -26   -318       O  
ATOM    459  CB  VAL A 277      26.095  15.876   5.171  1.00 69.26           C  
ANISOU  459  CB  VAL A 277     9342   8944   8029  -1767    206   -203       C  
ATOM    460  CG1 VAL A 277      27.582  15.680   4.910  1.00 71.96           C  
ANISOU  460  CG1 VAL A 277     9470   9487   8385  -1959    295   -293       C  
ATOM    461  CG2 VAL A 277      25.362  14.552   5.088  1.00 66.11           C  
ANISOU  461  CG2 VAL A 277     8870   8635   7614  -1526    206   -189       C  
ATOM    462  N   ALA A 278      26.962  15.022   8.125  1.00 58.86           N  
ANISOU  462  N   ALA A 278     7702   7821   6842  -1527     32   -467       N  
ATOM    463  CA  ALA A 278      27.017  13.988   9.154  1.00 54.30           C  
ANISOU  463  CA  ALA A 278     6958   7378   6294  -1320    -30   -541       C  
ATOM    464  C   ALA A 278      26.206  14.381  10.384  1.00 53.80           C  
ANISOU  464  C   ALA A 278     7022   7184   6235  -1179   -147   -559       C  
ATOM    465  O   ALA A 278      25.441  13.576  10.917  1.00 52.81           O  
ANISOU  465  O   ALA A 278     6887   7072   6107   -951   -187   -543       O  
ATOM    466  CB  ALA A 278      28.457  13.696   9.539  1.00 54.40           C  
ANISOU  466  CB  ALA A 278     6719   7605   6348  -1421    -24   -651       C  
ATOM    467  N   ILE A 279      26.383  15.621  10.832  1.00 56.10           N  
ANISOU  467  N   ILE A 279     7437   7347   6532  -1323   -193   -598       N  
ATOM    468  CA  ILE A 279      25.643  16.137  11.977  1.00 55.31           C  
ANISOU  468  CA  ILE A 279     7477   7110   6429  -1209   -289   -633       C  
ATOM    469  C   ILE A 279      24.158  16.233  11.654  1.00 55.30           C  
ANISOU  469  C   ILE A 279     7674   6924   6413  -1044   -285   -522       C  
ATOM    470  O   ILE A 279      23.312  15.814  12.443  1.00 56.08           O  
ANISOU  470  O   ILE A 279     7800   7003   6504   -832   -336   -525       O  
ATOM    471  CB  ILE A 279      26.147  17.535  12.398  1.00 56.41           C  
ANISOU  471  CB  ILE A 279     7733   7120   6581  -1422   -326   -707       C  
ATOM    472  CG1 ILE A 279      27.623  17.484  12.797  1.00 61.11           C  
ANISOU  472  CG1 ILE A 279     8113   7915   7191  -1598   -345   -825       C  
ATOM    473  CG2 ILE A 279      25.311  18.081  13.544  1.00 53.54           C  
ANISOU  473  CG2 ILE A 279     7533   6602   6208  -1294   -410   -755       C  
ATOM    474  CD1 ILE A 279      27.882  16.803  14.120  1.00 60.12           C  
ANISOU  474  CD1 ILE A 279     7836   7955   7054  -1456   -443   -923       C  
ATOM    475  N   ARG A 280      23.852  16.786  10.484  1.00 56.15           N  
ANISOU  475  N   ARG A 280     7914   6909   6513  -1147   -224   -419       N  
ATOM    476  CA  ARG A 280      22.471  16.993  10.058  1.00 54.56           C  
ANISOU  476  CA  ARG A 280     7896   6534   6299  -1009   -227   -299       C  
ATOM    477  C   ARG A 280      21.697  15.682   9.980  1.00 51.58           C  
ANISOU  477  C   ARG A 280     7427   6266   5904   -784   -223   -253       C  
ATOM    478  O   ARG A 280      20.534  15.612  10.378  1.00 48.53           O  
ANISOU  478  O   ARG A 280     7131   5788   5521   -597   -263   -210       O  
ATOM    479  CB  ARG A 280      22.431  17.711   8.708  1.00 56.95           C  
ANISOU  479  CB  ARG A 280     8332   6723   6583  -1175   -166   -182       C  
ATOM    480  N   ILE A 281      22.344  14.643   9.464  1.00 50.32           N  
ANISOU  480  N   ILE A 281     7088   6299   5733   -805   -168   -265       N  
ATOM    481  CA  ILE A 281      21.719  13.331   9.387  1.00 47.23           C  
ANISOU  481  CA  ILE A 281     6606   6008   5332   -611   -158   -234       C  
ATOM    482  C   ILE A 281      21.487  12.778  10.790  1.00 48.98           C  
ANISOU  482  C   ILE A 281     6757   6278   5574   -426   -228   -302       C  
ATOM    483  O   ILE A 281      20.422  12.236  11.087  1.00 47.08           O  
ANISOU  483  O   ILE A 281     6551   6008   5329   -239   -251   -257       O  
ATOM    484  CB  ILE A 281      22.572  12.347   8.569  1.00 49.48           C  
ANISOU  484  CB  ILE A 281     6714   6478   5607   -676    -73   -253       C  
ATOM    485  CG1 ILE A 281      22.729  12.847   7.131  1.00 49.13           C  
ANISOU  485  CG1 ILE A 281     6750   6399   5518   -861      7   -179       C  
ATOM    486  CG2 ILE A 281      21.950  10.959   8.586  1.00 49.58           C  
ANISOU  486  CG2 ILE A 281     6644   6574   5621   -476    -63   -236       C  
ATOM    487  CD1 ILE A 281      23.560  11.933   6.257  1.00 50.24           C  
ANISOU  487  CD1 ILE A 281     6728   6722   5640   -932    110   -210       C  
ATOM    488  N   PHE A 282      22.485  12.930  11.655  1.00 50.17           N  
ANISOU  488  N   PHE A 282     6808   6514   5742   -489   -265   -408       N  
ATOM    489  CA  PHE A 282      22.371  12.465  13.033  1.00 51.33           C  
ANISOU  489  CA  PHE A 282     6892   6723   5888   -332   -339   -471       C  
ATOM    490  C   PHE A 282      21.197  13.133  13.739  1.00 50.52           C  
ANISOU  490  C   PHE A 282     6973   6452   5771   -218   -389   -453       C  
ATOM    491  O   PHE A 282      20.374  12.462  14.357  1.00 49.38           O  
ANISOU  491  O   PHE A 282     6825   6323   5614    -25   -412   -431       O  
ATOM    492  CB  PHE A 282      23.662  12.729  13.810  1.00 49.80           C  
ANISOU  492  CB  PHE A 282     6574   6647   5702   -449   -386   -587       C  
ATOM    493  CG  PHE A 282      23.635  12.206  15.220  1.00 54.83           C  
ANISOU  493  CG  PHE A 282     7140   7374   6319   -296   -470   -645       C  
ATOM    494  CD1 PHE A 282      23.227  13.016  16.268  1.00 57.75           C  
ANISOU  494  CD1 PHE A 282     7640   7649   6655   -275   -540   -700       C  
ATOM    495  CD2 PHE A 282      24.009  10.900  15.496  1.00 54.12           C  
ANISOU  495  CD2 PHE A 282     6863   7461   6240   -171   -476   -642       C  
ATOM    496  CE1 PHE A 282      23.200  12.537  17.564  1.00 60.02           C  
ANISOU  496  CE1 PHE A 282     7871   8034   6901   -144   -616   -750       C  
ATOM    497  CE2 PHE A 282      23.984  10.413  16.789  1.00 54.99           C  
ANISOU  497  CE2 PHE A 282     6917   7657   6319    -33   -558   -676       C  
ATOM    498  CZ  PHE A 282      23.577  11.233  17.825  1.00 59.26           C  
ANISOU  498  CZ  PHE A 282     7588   8120   6807    -24   -629   -729       C  
ATOM    499  N   GLN A 283      21.130  14.457  13.650  1.00 51.30           N  
ANISOU  499  N   GLN A 283     7233   6385   5874   -340   -399   -464       N  
ATOM    500  CA  GLN A 283      20.044  15.209  14.267  1.00 52.17           C  
ANISOU  500  CA  GLN A 283     7526   6315   5981   -232   -434   -457       C  
ATOM    501  C   GLN A 283      18.694  14.714  13.763  1.00 48.57           C  
ANISOU  501  C   GLN A 283     7125   5803   5528    -55   -409   -338       C  
ATOM    502  O   GLN A 283      17.754  14.550  14.539  1.00 54.47           O  
ANISOU  502  O   GLN A 283     7913   6514   6267    123   -434   -336       O  
ATOM    503  CB  GLN A 283      20.196  16.706  13.987  1.00 59.68           C  
ANISOU  503  CB  GLN A 283     8654   7066   6953   -400   -432   -470       C  
ATOM    504  CG  GLN A 283      21.492  17.326  14.502  1.00 66.56           C  
ANISOU  504  CG  GLN A 283     9486   7980   7826   -604   -460   -597       C  
ATOM    505  CD  GLN A 283      21.473  17.591  15.999  1.00 71.79           C  
ANISOU  505  CD  GLN A 283    10174   8643   8461   -537   -531   -725       C  
ATOM    506  OE1 GLN A 283      22.034  18.581  16.472  1.00 74.29           O  
ANISOU  506  OE1 GLN A 283    10569   8879   8780   -690   -561   -826       O  
ATOM    507  NE2 GLN A 283      20.826  16.707  16.751  1.00 71.28           N  
ANISOU  507  NE2 GLN A 283    10049   8670   8364   -320   -556   -723       N  
ATOM    508  N   GLY A 284      18.604  14.475  12.458  1.00 47.82           N  
ANISOU  508  N   GLY A 284     7025   5710   5436   -114   -359   -240       N  
ATOM    509  CA  GLY A 284      17.387  13.961  11.859  1.00 48.61           C  
ANISOU  509  CA  GLY A 284     7159   5779   5531     27   -344   -127       C  
ATOM    510  C   GLY A 284      17.005  12.608  12.425  1.00 52.77           C  
ANISOU  510  C   GLY A 284     7554   6447   6050    201   -347   -136       C  
ATOM    511  O   GLY A 284      15.860  12.395  12.825  1.00 49.30           O  
ANISOU  511  O   GLY A 284     7155   5964   5612    367   -364    -94       O  
ATOM    512  N   CYS A 285      17.970  11.692  12.463  1.00 54.03           N  
ANISOU  512  N   CYS A 285     7551   6772   6206    163   -328   -188       N  
ATOM    513  CA  CYS A 285      17.746  10.357  13.007  1.00 52.52           C  
ANISOU  513  CA  CYS A 285     7235   6704   6014    318   -329   -193       C  
ATOM    514  C   CYS A 285      17.319  10.437  14.465  1.00 54.21           C  
ANISOU  514  C   CYS A 285     7473   6909   6217    453   -384   -238       C  
ATOM    515  O   CYS A 285      16.558   9.598  14.948  1.00 53.00           O  
ANISOU  515  O   CYS A 285     7288   6793   6057    612   -386   -205       O  
ATOM    516  CB  CYS A 285      19.015   9.511  12.897  1.00 57.19           C  
ANISOU  516  CB  CYS A 285     7650   7462   6618    256   -304   -250       C  
ATOM    517  SG  CYS A 285      19.706   9.400  11.234  1.00 82.67           S  
ANISOU  517  SG  CYS A 285    10835  10730   9846     81   -217   -224       S  
ATOM    518  N   GLN A 286      17.823  11.451  15.161  1.00 55.02           N  
ANISOU  518  N   GLN A 286     7635   6962   6309    378   -425   -318       N  
ATOM    519  CA  GLN A 286      17.511  11.647  16.570  1.00 58.11           C  
ANISOU  519  CA  GLN A 286     8062   7350   6668    484   -475   -381       C  
ATOM    520  C   GLN A 286      16.042  12.010  16.770  1.00 53.31           C  
ANISOU  520  C   GLN A 286     7587   6609   6060    626   -465   -328       C  
ATOM    521  O   GLN A 286      15.399  11.535  17.707  1.00 54.38           O  
ANISOU  521  O   GLN A 286     7711   6785   6166    777   -475   -333       O  
ATOM    522  CB  GLN A 286      18.415  12.724  17.170  1.00 64.97           C  
ANISOU  522  CB  GLN A 286     8977   8189   7522    343   -518   -494       C  
ATOM    523  CG  GLN A 286      18.099  13.060  18.612  1.00 73.68           C  
ANISOU  523  CG  GLN A 286    10142   9282   8573    434   -568   -577       C  
ATOM    524  CD  GLN A 286      19.071  14.060  19.206  1.00 80.25           C  
ANISOU  524  CD  GLN A 286    11012  10099   9382    272   -618   -705       C  
ATOM    525  OE1 GLN A 286      20.283  13.837  19.218  1.00 79.09           O  
ANISOU  525  OE1 GLN A 286    10734  10085   9231    148   -649   -755       O  
ATOM    526  NE2 GLN A 286      18.541  15.171  19.707  1.00 83.73           N  
ANISOU  526  NE2 GLN A 286    11628  10374   9810    272   -625   -766       N  
ATOM    527  N   PHE A 287      15.514  12.855  15.890  1.00 50.71           N  
ANISOU  527  N   PHE A 287     7378   6127   5762    580   -444   -270       N  
ATOM    528  CA APHE A 287      14.110  13.251  15.949  0.59 53.00           C  
ANISOU  528  CA APHE A 287     7778   6291   6067    721   -435   -209       C  
ATOM    529  CA BPHE A 287      14.114  13.248  15.970  0.41 53.02           C  
ANISOU  529  CA BPHE A 287     7781   6295   6070    722   -436   -210       C  
ATOM    530  C   PHE A 287      13.199  12.053  15.719  1.00 49.62           C  
ANISOU  530  C   PHE A 287     7262   5950   5639    861   -413   -119       C  
ATOM    531  O   PHE A 287      12.145  11.929  16.338  1.00 51.18           O  
ANISOU  531  O   PHE A 287     7482   6130   5835   1016   -408   -100       O  
ATOM    532  CB APHE A 287      13.806  14.335  14.912  0.59 56.31           C  
ANISOU  532  CB APHE A 287     8334   6536   6526    641   -427   -141       C  
ATOM    533  CB BPHE A 287      13.808  14.382  14.989  0.41 56.35           C  
ANISOU  533  CB BPHE A 287     8344   6537   6531    643   -428   -148       C  
ATOM    534  CG APHE A 287      12.338  14.599  14.726  0.59 59.31           C  
ANISOU  534  CG APHE A 287     8793   6806   6934    798   -421    -50       C  
ATOM    535  CG BPHE A 287      14.373  15.711  15.406  0.41 58.23           C  
ANISOU  535  CG BPHE A 287     8712   6634   6780    535   -446   -236       C  
ATOM    536  CD1APHE A 287      11.675  15.504  15.537  0.59 64.38           C  
ANISOU  536  CD1APHE A 287     9552   7311   7597    901   -426    -93       C  
ATOM    537  CD1BPHE A 287      13.881  16.366  16.522  0.41 60.38           C  
ANISOU  537  CD1BPHE A 287     9080   6811   7049    634   -458   -317       C  
ATOM    538  CD2APHE A 287      11.619  13.936  13.743  0.59 59.97           C  
ANISOU  538  CD2APHE A 287     8827   6933   7024    843   -410     72       C  
ATOM    539  CD2BPHE A 287      15.390  16.307  14.679  0.41 59.79           C  
ANISOU  539  CD2BPHE A 287     8939   6792   6988    324   -443   -244       C  
ATOM    540  CE1APHE A 287      10.324  15.747  15.369  0.59 66.51           C  
ANISOU  540  CE1APHE A 287     9875   7492   7905   1059   -418     -9       C  
ATOM    541  CE1BPHE A 287      14.397  17.590  16.910  0.41 64.07           C  
ANISOU  541  CE1BPHE A 287     9680   7134   7529    524   -472   -413       C  
ATOM    542  CE2APHE A 287      10.269  14.173  13.572  0.59 60.20           C  
ANISOU  542  CE2APHE A 287     8908   6883   7084    986   -415    160       C  
ATOM    543  CE2BPHE A 287      15.909  17.531  15.061  0.41 62.93           C  
ANISOU  543  CE2BPHE A 287     9463   7047   7402    205   -457   -329       C  
ATOM    544  CZ APHE A 287       9.621  15.079  14.386  0.59 62.96           C  
ANISOU  544  CZ APHE A 287     9358   7099   7465   1102   -418    124       C  
ATOM    545  CZ BPHE A 287      15.411  18.173  16.177  0.41 64.81           C  
ANISOU  545  CZ BPHE A 287     9805   7178   7640    305   -475   -417       C  
ATOM    546  N   ARG A 288      13.613  11.173  14.816  1.00 46.33           N  
ANISOU  546  N   ARG A 288     6746   5630   5226    798   -392    -72       N  
ATOM    547  CA  ARG A 288      12.845   9.972  14.525  1.00 45.78           C  
ANISOU  547  CA  ARG A 288     6596   5639   5159    903   -369      2       C  
ATOM    548  C   ARG A 288      12.839   9.036  15.735  1.00 43.55           C  
ANISOU  548  C   ARG A 288     6226   5466   4856   1021   -373    -38       C  
ATOM    549  O   ARG A 288      11.809   8.457  16.075  1.00 42.08           O  
ANISOU  549  O   ARG A 288     6025   5296   4669   1151   -359     11       O  
ATOM    550  CB  ARG A 288      13.399   9.269  13.282  1.00 48.24           C  
ANISOU  550  CB  ARG A 288     6833   6021   5474    796   -337     38       C  
ATOM    551  CG  ARG A 288      12.789   7.907  13.002  1.00 48.68           C  
ANISOU  551  CG  ARG A 288     6802   6162   5533    881   -310     91       C  
ATOM    552  CD  ARG A 288      11.267   7.936  13.065  1.00 50.98           C  
ANISOU  552  CD  ARG A 288     7140   6398   5831   1004   -319    169       C  
ATOM    553  NE  ARG A 288      10.719   6.601  13.290  1.00 48.50           N  
ANISOU  553  NE  ARG A 288     6736   6169   5522   1096   -296    196       N  
ATOM    554  CZ  ARG A 288       9.479   6.353  13.699  1.00 50.47           C  
ANISOU  554  CZ  ARG A 288     6986   6411   5780   1217   -296    248       C  
ATOM    555  NH1 ARG A 288       8.640   7.354  13.934  1.00 47.10           N  
ANISOU  555  NH1 ARG A 288     6637   5898   5360   1281   -317    275       N  
ATOM    556  NH2 ARG A 288       9.079   5.100  13.879  1.00 51.86           N  
ANISOU  556  NH2 ARG A 288     7082   6659   5963   1275   -270    272       N  
ATOM    557  N   SER A 289      13.990   8.901  16.388  1.00 42.52           N  
ANISOU  557  N   SER A 289     6035   5416   4705    969   -394   -121       N  
ATOM    558  CA  SER A 289      14.086   8.098  17.603  1.00 42.07           C  
ANISOU  558  CA  SER A 289     5905   5464   4614   1076   -411   -150       C  
ATOM    559  C   SER A 289      13.116   8.621  18.659  1.00 39.79           C  
ANISOU  559  C   SER A 289     5707   5122   4290   1193   -419   -164       C  
ATOM    560  O   SER A 289      12.403   7.851  19.298  1.00 41.71           O  
ANISOU  560  O   SER A 289     5918   5419   4511   1320   -403   -127       O  
ATOM    561  CB  SER A 289      15.514   8.109  18.152  1.00 47.47           C  
ANISOU  561  CB  SER A 289     6515   6245   5277    993   -453   -237       C  
ATOM    562  OG  SER A 289      16.391   7.381  17.313  1.00 58.60           O  
ANISOU  562  OG  SER A 289     7808   7732   6723    919   -432   -225       O  
ATOM    563  N   VAL A 290      13.098   9.937  18.836  1.00 40.54           N  
ANISOU  563  N   VAL A 290     5919   5106   4380   1147   -435   -222       N  
ATOM    564  CA  VAL A 290      12.165  10.574  19.757  1.00 42.09           C  
ANISOU  564  CA  VAL A 290     6213   5232   4548   1260   -428   -253       C  
ATOM    565  C   VAL A 290      10.730  10.247  19.375  1.00 41.85           C  
ANISOU  565  C   VAL A 290     6188   5162   4551   1387   -384   -152       C  
ATOM    566  O   VAL A 290       9.909   9.919  20.231  1.00 39.33           O  
ANISOU  566  O   VAL A 290     5863   4880   4201   1518   -359   -146       O  
ATOM    567  CB  VAL A 290      12.347  12.098  19.772  1.00 45.61           C  
ANISOU  567  CB  VAL A 290     6800   5524   5005   1183   -443   -329       C  
ATOM    568  CG1 VAL A 290      11.084  12.792  20.284  1.00 46.95           C  
ANISOU  568  CG1 VAL A 290     7079   5578   5180   1322   -411   -334       C  
ATOM    569  CG2 VAL A 290      13.557  12.468  20.616  1.00 43.92           C  
ANISOU  569  CG2 VAL A 290     6586   5364   4735   1079   -491   -456       C  
ATOM    570  N   GLU A 291      10.437  10.327  18.082  1.00 40.63           N  
ANISOU  570  N   GLU A 291     6038   4946   4453   1340   -374    -70       N  
ATOM    571  CA  GLU A 291       9.104  10.014  17.586  1.00 43.20           C  
ANISOU  571  CA  GLU A 291     6352   5250   4813   1443   -347     31       C  
ATOM    572  C   GLU A 291       8.756   8.554  17.866  1.00 43.00           C  
ANISOU  572  C   GLU A 291     6207   5358   4771   1513   -323     77       C  
ATOM    573  O   GLU A 291       7.632   8.238  18.262  1.00 45.00           O  
ANISOU  573  O   GLU A 291     6441   5629   5027   1632   -294    122       O  
ATOM    574  CB  GLU A 291       9.012  10.306  16.088  1.00 44.68           C  
ANISOU  574  CB  GLU A 291     6562   5371   5044   1355   -356    112       C  
ATOM    575  CG  GLU A 291       7.593  10.413  15.559  1.00 56.43           C  
ANISOU  575  CG  GLU A 291     8061   6810   6568   1455   -349    213       C  
ATOM    576  CD  GLU A 291       7.544  10.772  14.079  1.00 66.37           C  
ANISOU  576  CD  GLU A 291     9356   8012   7850   1360   -372    300       C  
ATOM    577  OE1 GLU A 291       8.421  10.309  13.314  1.00 63.36           O  
ANISOU  577  OE1 GLU A 291     8941   7686   7448   1226   -372    300       O  
ATOM    578  OE2 GLU A 291       6.621  11.517  13.680  1.00 70.48           O  
ANISOU  578  OE2 GLU A 291     9936   8437   8405   1425   -389    371       O  
ATOM    579  N   ALA A 292       9.729   7.669  17.662  1.00 35.51           N  
ANISOU  579  N   ALA A 292     5178   4501   3812   1438   -329     67       N  
ATOM    580  CA  ALA A 292       9.541   6.242  17.912  1.00 36.39           C  
ANISOU  580  CA  ALA A 292     5189   4718   3918   1496   -305    110       C  
ATOM    581  C   ALA A 292       9.257   5.957  19.388  1.00 36.71           C  
ANISOU  581  C   ALA A 292     5225   4819   3906   1608   -298     86       C  
ATOM    582  O   ALA A 292       8.385   5.156  19.721  1.00 38.55           O  
ANISOU  582  O   ALA A 292     5418   5094   4136   1695   -263    147       O  
ATOM    583  CB  ALA A 292      10.756   5.452  17.435  1.00 32.66           C  
ANISOU  583  CB  ALA A 292     4638   4315   3456   1405   -311     92       C  
ATOM    584  N   VAL A 293       9.994   6.614  20.274  1.00 35.24           N  
ANISOU  584  N   VAL A 293     5081   4641   3668   1593   -330     -2       N  
ATOM    585  CA  VAL A 293       9.779   6.428  21.704  1.00 35.61           C  
ANISOU  585  CA  VAL A 293     5136   4755   3637   1689   -326    -31       C  
ATOM    586  C   VAL A 293       8.342   6.786  22.075  1.00 36.70           C  
ANISOU  586  C   VAL A 293     5324   4849   3771   1802   -274     -5       C  
ATOM    587  O   VAL A 293       7.734   6.152  22.936  1.00 42.12           O  
ANISOU  587  O   VAL A 293     5984   5608   4410   1895   -239     25       O  
ATOM    588  CB  VAL A 293      10.755   7.271  22.535  1.00 42.78           C  
ANISOU  588  CB  VAL A 293     6098   5677   4481   1637   -378   -147       C  
ATOM    589  CG1 VAL A 293      10.412   7.180  24.021  1.00 45.57           C  
ANISOU  589  CG1 VAL A 293     6480   6104   4731   1735   -371   -182       C  
ATOM    590  CG2 VAL A 293      12.184   6.820  22.277  1.00 42.77           C  
ANISOU  590  CG2 VAL A 293     6014   5752   4485   1535   -430   -170       C  
ATOM    591  N   GLN A 294       7.802   7.797  21.406  1.00 37.82           N  
ANISOU  591  N   GLN A 294     5532   4872   3966   1796   -267     -9       N  
ATOM    592  CA  GLN A 294       6.426   8.221  21.632  1.00 40.15           C  
ANISOU  592  CA  GLN A 294     5858   5119   4277   1914   -217     18       C  
ATOM    593  C   GLN A 294       5.453   7.136  21.187  1.00 37.08           C  
ANISOU  593  C   GLN A 294     5371   4792   3926   1965   -180    133       C  
ATOM    594  O   GLN A 294       4.506   6.814  21.899  1.00 38.94           O  
ANISOU  594  O   GLN A 294     5578   5078   4139   2069   -127    158       O  
ATOM    595  CB  GLN A 294       6.145   9.535  20.899  1.00 39.50           C  
ANISOU  595  CB  GLN A 294     5867   4884   4259   1900   -229      5       C  
ATOM    596  CG  GLN A 294       7.036  10.680  21.356  1.00 47.70           C  
ANISOU  596  CG  GLN A 294     7018   5837   5268   1837   -260   -116       C  
ATOM    597  CD  GLN A 294       6.815  11.957  20.570  1.00 56.81           C  
ANISOU  597  CD  GLN A 294     8277   6815   6495   1814   -271   -115       C  
ATOM    598  OE1 GLN A 294       7.114  13.049  21.050  1.00 62.90           O  
ANISOU  598  OE1 GLN A 294     9164   7478   7257   1800   -275   -214       O  
ATOM    599  NE2 GLN A 294       6.286  11.829  19.358  1.00 59.03           N  
ANISOU  599  NE2 GLN A 294     8525   7060   6844   1807   -278     -2       N  
ATOM    600  N   GLU A 295       5.700   6.570  20.010  1.00 34.73           N  
ANISOU  600  N   GLU A 295     5021   4494   3680   1881   -202    195       N  
ATOM    601  CA  GLU A 295       4.878   5.478  19.495  1.00 34.45           C  
ANISOU  601  CA  GLU A 295     4896   4515   3679   1899   -174    292       C  
ATOM    602  C   GLU A 295       4.956   4.247  20.401  1.00 34.03           C  
ANISOU  602  C   GLU A 295     4783   4565   3582   1935   -141    310       C  
ATOM    603  O   GLU A 295       3.943   3.623  20.710  1.00 34.78           O  
ANISOU  603  O   GLU A 295     4827   4706   3680   1998    -93    371       O  
ATOM    604  CB  GLU A 295       5.308   5.112  18.071  1.00 35.62           C  
ANISOU  604  CB  GLU A 295     5017   4645   3872   1784   -204    331       C  
ATOM    605  CG  GLU A 295       5.060   6.208  17.043  1.00 38.93           C  
ANISOU  605  CG  GLU A 295     5494   4968   4329   1746   -236    349       C  
ATOM    606  CD  GLU A 295       5.896   6.033  15.788  1.00 44.40           C  
ANISOU  606  CD  GLU A 295     6187   5651   5033   1606   -264    359       C  
ATOM    607  OE1 GLU A 295       6.435   4.927  15.572  1.00 45.56           O  
ANISOU  607  OE1 GLU A 295     6271   5866   5175   1553   -250    357       O  
ATOM    608  OE2 GLU A 295       6.025   7.006  15.020  1.00 47.10           O  
ANISOU  608  OE2 GLU A 295     6596   5911   5387   1551   -295    368       O  
ATOM    609  N   ILE A 296       6.166   3.899  20.821  1.00 35.57           N  
ANISOU  609  N   ILE A 296     4979   4798   3737   1892   -169    266       N  
ATOM    610  CA  ILE A 296       6.367   2.736  21.680  1.00 34.50           C  
ANISOU  610  CA  ILE A 296     4798   4752   3559   1930   -150    297       C  
ATOM    611  C   ILE A 296       5.682   2.929  23.035  1.00 36.85           C  
ANISOU  611  C   ILE A 296     5124   5098   3778   2032   -111    290       C  
ATOM    612  O   ILE A 296       5.065   2.004  23.571  1.00 37.98           O  
ANISOU  612  O   ILE A 296     5229   5303   3901   2082    -63    359       O  
ATOM    613  CB  ILE A 296       7.862   2.458  21.874  1.00 36.34           C  
ANISOU  613  CB  ILE A 296     5018   5022   3768   1876   -202    252       C  
ATOM    614  CG1 ILE A 296       8.499   2.055  20.538  1.00 35.64           C  
ANISOU  614  CG1 ILE A 296     4885   4901   3756   1780   -216    262       C  
ATOM    615  CG2 ILE A 296       8.078   1.397  22.945  1.00 39.15           C  
ANISOU  615  CG2 ILE A 296     5340   5466   4067   1937   -194    294       C  
ATOM    616  CD1 ILE A 296      10.014   2.174  20.524  1.00 38.00           C  
ANISOU  616  CD1 ILE A 296     5163   5228   4047   1715   -266    196       C  
ATOM    617  N   THR A 297       5.786   4.136  23.583  1.00 37.14           N  
ANISOU  617  N   THR A 297     5238   5106   3769   2056   -124    202       N  
ATOM    618  CA  THR A 297       5.123   4.455  24.842  1.00 41.71           C  
ANISOU  618  CA  THR A 297     5856   5730   4262   2152    -75    173       C  
ATOM    619  C   THR A 297       3.614   4.240  24.724  1.00 41.76           C  
ANISOU  619  C   THR A 297     5817   5740   4309   2229      4    245       C  
ATOM    620  O   THR A 297       2.980   3.673  25.614  1.00 37.99           O  
ANISOU  620  O   THR A 297     5317   5346   3773   2293     66    282       O  
ATOM    621  CB  THR A 297       5.392   5.908  25.275  1.00 41.69           C  
ANISOU  621  CB  THR A 297     5956   5664   4220   2160    -94     48       C  
ATOM    622  OG1 THR A 297       6.787   6.080  25.558  1.00 42.58           O  
ANISOU  622  OG1 THR A 297     6098   5799   4281   2078   -169    -24       O  
ATOM    623  CG2 THR A 297       4.586   6.246  26.523  1.00 38.88           C  
ANISOU  623  CG2 THR A 297     5645   5355   3774   2267    -24      6       C  
ATOM    624  N   GLU A 298       3.045   4.692  23.612  1.00 38.63           N  
ANISOU  624  N   GLU A 298     5403   5264   4010   2217     -1    270       N  
ATOM    625  CA  GLU A 298       1.615   4.539  23.371  1.00 42.83           C  
ANISOU  625  CA  GLU A 298     5869   5811   4595   2283     60    341       C  
ATOM    626  C   GLU A 298       1.224   3.063  23.280  1.00 38.29           C  
ANISOU  626  C   GLU A 298     5200   5317   4031   2255     92    442       C  
ATOM    627  O   GLU A 298       0.215   2.640  23.842  1.00 35.75           O  
ANISOU  627  O   GLU A 298     4825   5062   3695   2315    165    490       O  
ATOM    628  CB  GLU A 298       1.212   5.282  22.098  1.00 49.00           C  
ANISOU  628  CB  GLU A 298     6647   6497   5473   2266     24    361       C  
ATOM    629  CG  GLU A 298      -0.282   5.384  21.884  1.00 59.72           C  
ANISOU  629  CG  GLU A 298     7929   7874   6889   2352     72    425       C  
ATOM    630  CD  GLU A 298      -0.635   6.204  20.660  1.00 69.16           C  
ANISOU  630  CD  GLU A 298     9129   8978   8172   2345     19    455       C  
ATOM    631  OE1 GLU A 298       0.203   7.021  20.226  1.00 71.68           O  
ANISOU  631  OE1 GLU A 298     9542   9198   8496   2297    -36    408       O  
ATOM    632  OE2 GLU A 298      -1.752   6.033  20.132  1.00 74.35           O  
ANISOU  632  OE2 GLU A 298     9693   9668   8887   2383     30    534       O  
ATOM    633  N   TYR A 299       2.032   2.282  22.570  1.00 36.80           N  
ANISOU  633  N   TYR A 299     4994   5118   3871   2160     46    470       N  
ATOM    634  CA  TYR A 299       1.792   0.848  22.448  1.00 34.55           C  
ANISOU  634  CA  TYR A 299     4640   4882   3606   2123     75    556       C  
ATOM    635  C   TYR A 299       1.849   0.147  23.803  1.00 35.58           C  
ANISOU  635  C   TYR A 299     4778   5090   3650   2173    122    582       C  
ATOM    636  O   TYR A 299       1.034  -0.726  24.095  1.00 40.42           O  
ANISOU  636  O   TYR A 299     5340   5751   4267   2183    185    661       O  
ATOM    637  CB  TYR A 299       2.806   0.207  21.497  1.00 32.78           C  
ANISOU  637  CB  TYR A 299     4409   4618   3426   2024     23    558       C  
ATOM    638  CG  TYR A 299       2.613  -1.284  21.337  1.00 36.03           C  
ANISOU  638  CG  TYR A 299     4768   5052   3870   1985     57    636       C  
ATOM    639  CD1 TYR A 299       1.454  -1.793  20.769  1.00 35.42           C  
ANISOU  639  CD1 TYR A 299     4628   4982   3846   1957     95    698       C  
ATOM    640  CD2 TYR A 299       3.586  -2.184  21.759  1.00 35.37           C  
ANISOU  640  CD2 TYR A 299     4694   4977   3768   1976     49    646       C  
ATOM    641  CE1 TYR A 299       1.264  -3.155  20.626  1.00 34.91           C  
ANISOU  641  CE1 TYR A 299     4527   4920   3815   1907    130    761       C  
ATOM    642  CE2 TYR A 299       3.407  -3.551  21.616  1.00 35.71           C  
ANISOU  642  CE2 TYR A 299     4704   5012   3851   1946     86    717       C  
ATOM    643  CZ  TYR A 299       2.244  -4.029  21.049  1.00 35.63           C  
ANISOU  643  CZ  TYR A 299     4647   4996   3894   1904    130    770       C  
ATOM    644  OH  TYR A 299       2.053  -5.383  20.894  1.00 38.56           O  
ANISOU  644  OH  TYR A 299     4998   5343   4311   1857    170    832       O  
ATOM    645  N   ALA A 300       2.822   0.527  24.623  1.00 34.97           N  
ANISOU  645  N   ALA A 300     4766   5031   3491   2194     88    519       N  
ATOM    646  CA  ALA A 300       3.031  -0.122  25.913  1.00 36.70           C  
ANISOU  646  CA  ALA A 300     5003   5334   3607   2237    115    550       C  
ATOM    647  C   ALA A 300       1.783  -0.053  26.785  1.00 38.44           C  
ANISOU  647  C   ALA A 300     5214   5620   3770   2310    210    579       C  
ATOM    648  O   ALA A 300       1.420  -1.025  27.444  1.00 39.82           O  
ANISOU  648  O   ALA A 300     5369   5860   3901   2321    265    665       O  
ATOM    649  CB  ALA A 300       4.220   0.496  26.636  1.00 34.51           C  
ANISOU  649  CB  ALA A 300     4794   5081   3237   2243     49    463       C  
ATOM    650  N   LYS A 301       1.125   1.099  26.779  1.00 40.80           N  
ANISOU  650  N   LYS A 301     5529   5900   4075   2361    237    511       N  
ATOM    651  CA  LYS A 301      -0.067   1.300  27.596  1.00 43.37           C  
ANISOU  651  CA  LYS A 301     5835   6294   4351   2443    341    520       C  
ATOM    652  C   LYS A 301      -1.192   0.333  27.226  1.00 43.63           C  
ANISOU  652  C   LYS A 301     5760   6363   4452   2426    410    636       C  
ATOM    653  O   LYS A 301      -2.089   0.079  28.030  1.00 45.66           O  
ANISOU  653  O   LYS A 301     5984   6707   4658   2472    509    673       O  
ATOM    654  CB  LYS A 301      -0.545   2.751  27.487  1.00 44.70           C  
ANISOU  654  CB  LYS A 301     6032   6407   4543   2514    355    421       C  
ATOM    655  CG  LYS A 301       0.505   3.764  27.921  1.00 51.77           C  
ANISOU  655  CG  LYS A 301     7044   7257   5368   2517    295    293       C  
ATOM    656  CD  LYS A 301       0.303   5.116  27.250  1.00 56.53           C  
ANISOU  656  CD  LYS A 301     7685   7740   6052   2548    274    213       C  
ATOM    657  CE  LYS A 301      -0.799   5.920  27.918  1.00 60.51           C  
ANISOU  657  CE  LYS A 301     8199   8254   6538   2673    374    158       C  
ATOM    658  NZ  LYS A 301      -0.945   7.270  27.302  1.00 61.33           N  
ANISOU  658  NZ  LYS A 301     8356   8216   6729   2718    351     84       N  
ATOM    659  N   SER A 302      -1.138  -0.209  26.013  1.00 39.42           N  
ANISOU  659  N   SER A 302     5175   5773   4031   2347    363    686       N  
ATOM    660  CA  SER A 302      -2.163  -1.134  25.537  1.00 39.02           C  
ANISOU  660  CA  SER A 302     5022   5750   4052   2303    415    785       C  
ATOM    661  C   SER A 302      -1.885  -2.568  25.987  1.00 39.76           C  
ANISOU  661  C   SER A 302     5119   5873   4117   2248    443    875       C  
ATOM    662  O   SER A 302      -2.770  -3.421  25.960  1.00 40.87           O  
ANISOU  662  O   SER A 302     5190   6048   4291   2208    509    960       O  
ATOM    663  CB  SER A 302      -2.263  -1.085  24.011  1.00 41.55           C  
ANISOU  663  CB  SER A 302     5294   6000   4493   2233    350    792       C  
ATOM    664  OG  SER A 302      -1.291  -1.933  23.418  1.00 45.33           O  
ANISOU  664  OG  SER A 302     5800   6426   4998   2142    294    809       O  
ATOM    665  N   ILE A 303      -0.650  -2.842  26.386  1.00 38.50           N  
ANISOU  665  N   ILE A 303     5038   5693   3900   2242    390    861       N  
ATOM    666  CA  ILE A 303      -0.311  -4.168  26.885  1.00 40.41           C  
ANISOU  666  CA  ILE A 303     5294   5946   4113   2211    410    956       C  
ATOM    667  C   ILE A 303      -1.002  -4.385  28.232  1.00 44.81           C  
ANISOU  667  C   ILE A 303     5863   6607   4556   2261    505   1013       C  
ATOM    668  O   ILE A 303      -0.729  -3.669  29.195  1.00 46.08           O  
ANISOU  668  O   ILE A 303     6082   6831   4596   2330    508    958       O  
ATOM    669  CB  ILE A 303       1.208  -4.345  27.034  1.00 37.34           C  
ANISOU  669  CB  ILE A 303     4972   5525   3691   2213    321    931       C  
ATOM    670  CG1 ILE A 303       1.919  -4.007  25.720  1.00 35.56           C  
ANISOU  670  CG1 ILE A 303     4734   5212   3567   2160    241    862       C  
ATOM    671  CG2 ILE A 303       1.535  -5.762  27.477  1.00 35.10           C  
ANISOU  671  CG2 ILE A 303     4704   5235   3398   2196    338   1046       C  
ATOM    672  CD1 ILE A 303       3.432  -3.994  25.835  1.00 35.65           C  
ANISOU  672  CD1 ILE A 303     4787   5208   3552   2165    156    820       C  
ATOM    673  N   PRO A 304      -1.912  -5.370  28.298  1.00 43.38           N  
ANISOU  673  N   PRO A 304     5628   6447   4406   2214    589   1119       N  
ATOM    674  CA  PRO A 304      -2.746  -5.561  29.490  1.00 44.59           C  
ANISOU  674  CA  PRO A 304     5777   6710   4455   2247    701   1181       C  
ATOM    675  C   PRO A 304      -1.894  -5.750  30.737  1.00 43.73           C  
ANISOU  675  C   PRO A 304     5773   6655   4189   2295    688   1206       C  
ATOM    676  O   PRO A 304      -1.008  -6.607  30.754  1.00 42.11           O  
ANISOU  676  O   PRO A 304     5615   6397   3987   2270    630   1272       O  
ATOM    677  CB  PRO A 304      -3.521  -6.844  29.173  1.00 45.54           C  
ANISOU  677  CB  PRO A 304     5837   6812   4655   2152    769   1304       C  
ATOM    678  CG  PRO A 304      -3.509  -6.938  27.679  1.00 46.30           C  
ANISOU  678  CG  PRO A 304     5877   6810   4906   2081    703   1271       C  
ATOM    679  CD  PRO A 304      -2.171  -6.394  27.273  1.00 41.72           C  
ANISOU  679  CD  PRO A 304     5365   6159   4326   2115    587   1184       C  
ATOM    680  N   GLY A 305      -2.156  -4.944  31.761  1.00 38.89           N  
ANISOU  680  N   GLY A 305     5193   6145   3437   2367    738   1152       N  
ATOM    681  CA  GLY A 305      -1.421  -5.030  33.007  1.00 38.86           C  
ANISOU  681  CA  GLY A 305     5290   6219   3256   2408    721   1169       C  
ATOM    682  C   GLY A 305      -0.343  -3.972  33.141  1.00 39.49           C  
ANISOU  682  C   GLY A 305     5438   6294   3273   2455    614   1033       C  
ATOM    683  O   GLY A 305       0.038  -3.612  34.250  1.00 42.86           O  
ANISOU  683  O   GLY A 305     5943   6815   3528   2497    609    999       O  
ATOM    684  N   PHE A 306       0.148  -3.461  32.015  1.00 38.72           N  
ANISOU  684  N   PHE A 306     5313   6092   3305   2436    527    952       N  
ATOM    685  CA  PHE A 306       1.232  -2.480  32.048  1.00 38.53           C  
ANISOU  685  CA  PHE A 306     5350   6053   3238   2456    423    824       C  
ATOM    686  C   PHE A 306       0.894  -1.221  32.856  1.00 40.63           C  
ANISOU  686  C   PHE A 306     5671   6384   3385   2518    466    696       C  
ATOM    687  O   PHE A 306       1.643  -0.834  33.754  1.00 40.68           O  
ANISOU  687  O   PHE A 306     5757   6455   3243   2537    418    636       O  
ATOM    688  CB  PHE A 306       1.677  -2.092  30.634  1.00 34.81           C  
ANISOU  688  CB  PHE A 306     4839   5459   2929   2413    344    764       C  
ATOM    689  CG  PHE A 306       2.823  -1.123  30.616  1.00 37.63           C  
ANISOU  689  CG  PHE A 306     5252   5794   3252   2412    240    639       C  
ATOM    690  CD1 PHE A 306       4.131  -1.576  30.681  1.00 42.24           C  
ANISOU  690  CD1 PHE A 306     5851   6383   3815   2386    139    653       C  
ATOM    691  CD2 PHE A 306       2.595   0.242  30.558  1.00 41.03           C  
ANISOU  691  CD2 PHE A 306     5716   6197   3675   2438    246    508       C  
ATOM    692  CE1 PHE A 306       5.190  -0.688  30.674  1.00 41.73           C  
ANISOU  692  CE1 PHE A 306     5823   6313   3721   2367     44    537       C  
ATOM    693  CE2 PHE A 306       3.648   1.136  30.546  1.00 41.96           C  
ANISOU  693  CE2 PHE A 306     5891   6286   3764   2417    154    392       C  
ATOM    694  CZ  PHE A 306       4.948   0.670  30.607  1.00 42.86           C  
ANISOU  694  CZ  PHE A 306     6009   6422   3853   2373     52    405       C  
ATOM    695  N   VAL A 307      -0.224  -0.577  32.530  1.00 38.24           N  
ANISOU  695  N   VAL A 307     5322   6063   3145   2552    553    651       N  
ATOM    696  CA  VAL A 307      -0.596   0.669  33.197  1.00 38.42           C  
ANISOU  696  CA  VAL A 307     5397   6121   3079   2625    607    515       C  
ATOM    697  C   VAL A 307      -1.000   0.446  34.651  1.00 41.67           C  
ANISOU  697  C   VAL A 307     5857   6680   3297   2665    706    532       C  
ATOM    698  O   VAL A 307      -1.131   1.400  35.415  1.00 44.71           O  
ANISOU  698  O   VAL A 307     6310   7110   3568   2722    752    406       O  
ATOM    699  CB  VAL A 307      -1.728   1.425  32.453  1.00 47.70           C  
ANISOU  699  CB  VAL A 307     6500   7236   4390   2674    676    470       C  
ATOM    700  CG1 VAL A 307      -1.261   1.850  31.070  1.00 47.10           C  
ANISOU  700  CG1 VAL A 307     6402   7019   4474   2634    571    441       C  
ATOM    701  CG2 VAL A 307      -2.990   0.575  32.366  1.00 42.15           C  
ANISOU  701  CG2 VAL A 307     5682   6595   3740   2673    789    593       C  
ATOM    702  N   ASN A 308      -1.186  -0.816  35.028  1.00 38.94           N  
ANISOU  702  N   ASN A 308     5484   6403   2907   2630    744    686       N  
ATOM    703  CA  ASN A 308      -1.576  -1.162  36.392  1.00 40.96           C  
ANISOU  703  CA  ASN A 308     5789   6808   2965   2653    844    732       C  
ATOM    704  C   ASN A 308      -0.351  -1.361  37.283  1.00 45.62           C  
ANISOU  704  C   ASN A 308     6490   7467   3378   2639    742    736       C  
ATOM    705  O   ASN A 308      -0.465  -1.486  38.504  1.00 40.49           O  
ANISOU  705  O   ASN A 308     5908   6953   2522   2657    800    755       O  
ATOM    706  CB  ASN A 308      -2.450  -2.421  36.399  1.00 42.41           C  
ANISOU  706  CB  ASN A 308     5896   7031   3186   2613    944    911       C  
ATOM    707  CG  ASN A 308      -3.659  -2.301  35.480  1.00 48.41           C  
ANISOU  707  CG  ASN A 308     6526   7743   4127   2613   1029    915       C  
ATOM    708  OD1 ASN A 308      -3.791  -3.045  34.506  1.00 45.78           O  
ANISOU  708  OD1 ASN A 308     6116   7328   3950   2549    997   1004       O  
ATOM    709  ND2 ASN A 308      -4.541  -1.353  35.781  1.00 46.73           N  
ANISOU  709  ND2 ASN A 308     6282   7584   3891   2688   1135    812       N  
ATOM    710  N   LEU A 309       0.821  -1.387  36.658  1.00 43.68           N  
ANISOU  710  N   LEU A 309     6254   7138   3205   2606    589    720       N  
ATOM    711  CA  LEU A 309       2.076  -1.567  37.374  1.00 46.52           C  
ANISOU  711  CA  LEU A 309     6691   7565   3419   2593    468    726       C  
ATOM    712  C   LEU A 309       2.473  -0.283  38.084  1.00 45.44           C  
ANISOU  712  C   LEU A 309     6644   7487   3134   2614    438    539       C  
ATOM    713  O   LEU A 309       2.024   0.805  37.720  1.00 44.10           O  
ANISOU  713  O   LEU A 309     6478   7252   3027   2637    483    394       O  
ATOM    714  CB  LEU A 309       3.188  -1.973  36.402  1.00 46.31           C  
ANISOU  714  CB  LEU A 309     6622   7434   3539   2552    324    758       C  
ATOM    715  CG  LEU A 309       3.040  -3.304  35.660  1.00 41.98           C  
ANISOU  715  CG  LEU A 309     6002   6808   3141   2525    333    928       C  
ATOM    716  CD1 LEU A 309       4.095  -3.438  34.560  1.00 40.37           C  
ANISOU  716  CD1 LEU A 309     5752   6492   3094   2492    209    909       C  
ATOM    717  CD2 LEU A 309       3.126  -4.468  36.637  1.00 45.91           C  
ANISOU  717  CD2 LEU A 309     6539   7394   3510   2535    347   1099       C  
ATOM    718  N   ASP A 310       3.328  -0.421  39.093  1.00 46.73           N  
ANISOU  718  N   ASP A 310     6884   7770   3099   2604    357    544       N  
ATOM    719  CA  ASP A 310       3.904   0.719  39.791  1.00 49.60           C  
ANISOU  719  CA  ASP A 310     7342   8196   3307   2600    302    359       C  
ATOM    720  C   ASP A 310       4.479   1.698  38.777  1.00 48.25           C  
ANISOU  720  C   ASP A 310     7152   7882   3299   2570    218    212       C  
ATOM    721  O   ASP A 310       5.158   1.298  37.832  1.00 47.99           O  
ANISOU  721  O   ASP A 310     7049   7762   3423   2534    121    270       O  
ATOM    722  CB  ASP A 310       4.996   0.243  40.752  1.00 54.91           C  
ANISOU  722  CB  ASP A 310     8070   9014   3779   2576    173    415       C  
ATOM    723  CG  ASP A 310       5.559   1.365  41.603  1.00 60.78           C  
ANISOU  723  CG  ASP A 310     8918   9848   4328   2553    115    220       C  
ATOM    724  OD1 ASP A 310       6.118   2.328  41.038  1.00 60.93           O  
ANISOU  724  OD1 ASP A 310     8940   9773   4436   2517     42     60       O  
ATOM    725  OD2 ASP A 310       5.454   1.276  42.845  1.00 66.68           O  
ANISOU  725  OD2 ASP A 310     9751  10762   4823   2561    142    225       O  
ATOM    726  N   LEU A 311       4.202   2.982  38.975  1.00 50.99           N  
ANISOU  726  N   LEU A 311     7568   8199   3608   2583    262     22       N  
ATOM    727  CA  LEU A 311       4.563   4.006  38.000  1.00 52.22           C  
ANISOU  727  CA  LEU A 311     7720   8195   3924   2554    208   -113       C  
ATOM    728  C   LEU A 311       6.072   4.061  37.769  1.00 51.87           C  
ANISOU  728  C   LEU A 311     7675   8150   3883   2470     27   -143       C  
ATOM    729  O   LEU A 311       6.529   4.311  36.653  1.00 48.23           O  
ANISOU  729  O   LEU A 311     7163   7561   3601   2427    -35   -160       O  
ATOM    730  CB  LEU A 311       4.049   5.374  38.451  1.00 56.81           C  
ANISOU  730  CB  LEU A 311     8401   8741   4442   2589    290   -315       C  
ATOM    731  CG  LEU A 311       3.395   6.254  37.383  1.00 58.26           C  
ANISOU  731  CG  LEU A 311     8563   8738   4837   2625    348   -388       C  
ATOM    732  CD1 LEU A 311       3.182   7.662  37.916  1.00 59.92           C  
ANISOU  732  CD1 LEU A 311     8896   8895   4977   2657    403   -607       C  
ATOM    733  CD2 LEU A 311       4.211   6.282  36.101  1.00 55.46           C  
ANISOU  733  CD2 LEU A 311     8152   8251   4668   2552    224   -359       C  
ATOM    734  N   ASN A 312       6.839   3.836  38.831  1.00 49.34           N  
ANISOU  734  N   ASN A 312     7405   7984   3359   2443    -56   -148       N  
ATOM    735  CA  ASN A 312       8.293   3.825  38.733  1.00 52.07           C  
ANISOU  735  CA  ASN A 312     7726   8364   3694   2366   -233   -170       C  
ATOM    736  C   ASN A 312       8.783   2.707  37.826  1.00 50.59           C  
ANISOU  736  C   ASN A 312     7414   8135   3673   2363   -297      2       C  
ATOM    737  O   ASN A 312       9.732   2.885  37.065  1.00 48.96           O  
ANISOU  737  O   ASN A 312     7150   7869   3583   2303   -401    -31       O  
ATOM    738  CB  ASN A 312       8.924   3.687  40.117  1.00 55.74           C  
ANISOU  738  CB  ASN A 312     8258   9031   3891   2348   -315   -185       C  
ATOM    739  CG  ASN A 312       8.476   4.775  41.070  1.00 63.72           C  
ANISOU  739  CG  ASN A 312     9405  10091   4714   2345   -246   -375       C  
ATOM    740  OD1 ASN A 312       8.565   5.962  40.763  1.00 67.24           O  
ANISOU  740  OD1 ASN A 312     9906  10429   5215   2303   -243   -563       O  
ATOM    741  ND2 ASN A 312       7.992   4.373  42.239  1.00 66.66           N  
ANISOU  741  ND2 ASN A 312     9842  10624   4863   2386   -183   -329       N  
ATOM    742  N   ASP A 313       8.127   1.554  37.911  1.00 49.07           N  
ANISOU  742  N   ASP A 313     7184   7969   3492   2422   -225    182       N  
ATOM    743  CA  ASP A 313       8.482   0.411  37.080  1.00 47.40           C  
ANISOU  743  CA  ASP A 313     6868   7701   3440   2426   -265    343       C  
ATOM    744  C   ASP A 313       8.062   0.616  35.624  1.00 47.08           C  
ANISOU  744  C   ASP A 313     6764   7483   3640   2408   -214    323       C  
ATOM    745  O   ASP A 313       8.784   0.226  34.709  1.00 45.36           O  
ANISOU  745  O   ASP A 313     6469   7199   3566   2376   -284    360       O  
ATOM    746  CB  ASP A 313       7.874  -0.874  37.644  1.00 43.20           C  
ANISOU  746  CB  ASP A 313     6333   7235   2847   2483   -198    539       C  
ATOM    747  CG  ASP A 313       8.547  -1.322  38.935  1.00 49.23           C  
ANISOU  747  CG  ASP A 313     7145   8176   3385   2499   -286    607       C  
ATOM    748  OD1 ASP A 313       9.546  -0.684  39.345  1.00 45.76           O  
ANISOU  748  OD1 ASP A 313     6725   7817   2844   2463   -412    499       O  
ATOM    749  OD2 ASP A 313       8.076  -2.315  39.535  1.00 49.80           O  
ANISOU  749  OD2 ASP A 313     7236   8308   3377   2541   -232    774       O  
ATOM    750  N   GLN A 314       6.897   1.222  35.411  1.00 45.39           N  
ANISOU  750  N   GLN A 314     6578   7202   3465   2431    -91    267       N  
ATOM    751  CA  GLN A 314       6.469   1.567  34.059  1.00 43.08           C  
ANISOU  751  CA  GLN A 314     6235   6755   3380   2413    -55    242       C  
ATOM    752  C   GLN A 314       7.558   2.385  33.369  1.00 45.76           C  
ANISOU  752  C   GLN A 314     6572   7023   3793   2341   -165    126       C  
ATOM    753  O   GLN A 314       7.958   2.087  32.243  1.00 42.22           O  
ANISOU  753  O   GLN A 314     6053   6489   3500   2300   -202    164       O  
ATOM    754  CB  GLN A 314       5.159   2.363  34.087  1.00 43.65           C  
ANISOU  754  CB  GLN A 314     6341   6781   3463   2461     73    174       C  
ATOM    755  CG  GLN A 314       3.944   1.585  34.581  1.00 43.13           C  
ANISOU  755  CG  GLN A 314     6251   6780   3355   2520    203    289       C  
ATOM    756  CD  GLN A 314       2.659   2.394  34.503  1.00 45.45           C  
ANISOU  756  CD  GLN A 314     6549   7034   3687   2578    330    219       C  
ATOM    757  OE1 GLN A 314       1.801   2.306  35.382  1.00 50.38           O  
ANISOU  757  OE1 GLN A 314     7191   7750   4201   2631    443    231       O  
ATOM    758  NE2 GLN A 314       2.523   3.191  33.450  1.00 37.17           N  
ANISOU  758  NE2 GLN A 314     5479   5850   2792   2572    316    149       N  
ATOM    759  N   VAL A 315       8.032   3.418  34.059  1.00 51.36           N  
ANISOU  759  N   VAL A 315     7362   7770   4383   2315   -209    -21       N  
ATOM    760  CA  VAL A 315       9.093   4.275  33.545  1.00 51.78           C  
ANISOU  760  CA  VAL A 315     7421   7765   4488   2226   -311   -142       C  
ATOM    761  C   VAL A 315      10.372   3.481  33.280  1.00 50.31           C  
ANISOU  761  C   VAL A 315     7144   7639   4333   2178   -431    -71       C  
ATOM    762  O   VAL A 315      11.000   3.631  32.233  1.00 48.30           O  
ANISOU  762  O   VAL A 315     6830   7304   4216   2114   -477    -89       O  
ATOM    763  CB  VAL A 315       9.408   5.424  34.526  1.00 53.38           C  
ANISOU  763  CB  VAL A 315     7736   8014   4532   2195   -341   -316       C  
ATOM    764  CG1 VAL A 315      10.643   6.192  34.071  1.00 57.70           C  
ANISOU  764  CG1 VAL A 315     8280   8518   5125   2078   -458   -431       C  
ATOM    765  CG2 VAL A 315       8.209   6.354  34.660  1.00 46.64           C  
ANISOU  765  CG2 VAL A 315     6972   7070   3677   2252   -215   -410       C  
ATOM    766  N   THR A 316      10.751   2.635  34.233  1.00 49.46           N  
ANISOU  766  N   THR A 316     7021   7677   4094   2214   -479     13       N  
ATOM    767  CA  THR A 316      11.961   1.829  34.100  1.00 47.65           C  
ANISOU  767  CA  THR A 316     6695   7516   3892   2195   -597     89       C  
ATOM    768  C   THR A 316      11.874   0.845  32.935  1.00 44.97           C  
ANISOU  768  C   THR A 316     6261   7080   3747   2215   -562    214       C  
ATOM    769  O   THR A 316      12.843   0.653  32.201  1.00 48.06           O  
ANISOU  769  O   THR A 316     6566   7451   4245   2173   -631    212       O  
ATOM    770  CB  THR A 316      12.270   1.067  35.399  1.00 49.24           C  
ANISOU  770  CB  THR A 316     6909   7892   3910   2249   -655    181       C  
ATOM    771  OG1 THR A 316      12.650   2.001  36.415  1.00 51.75           O  
ANISOU  771  OG1 THR A 316     7306   8320   4038   2205   -719     44       O  
ATOM    772  CG2 THR A 316      13.404   0.072  35.179  1.00 49.06           C  
ANISOU  772  CG2 THR A 316     6770   7923   3947   2262   -766    292       C  
ATOM    773  N   LEU A 317      10.712   0.228  32.764  1.00 44.68           N  
ANISOU  773  N   LEU A 317     6236   6987   3752   2272   -448    313       N  
ATOM    774  CA  LEU A 317      10.493  -0.692  31.651  1.00 48.11           C  
ANISOU  774  CA  LEU A 317     6595   7320   4363   2279   -405    416       C  
ATOM    775  C   LEU A 317      10.653   0.008  30.299  1.00 45.60           C  
ANISOU  775  C   LEU A 317     6247   6881   4199   2206   -402    327       C  
ATOM    776  O   LEU A 317      11.228  -0.548  29.361  1.00 42.67           O  
ANISOU  776  O   LEU A 317     5798   6459   3953   2179   -424    361       O  
ATOM    777  CB  LEU A 317       9.112  -1.342  31.759  1.00 45.52           C  
ANISOU  777  CB  LEU A 317     6291   6962   4043   2331   -281    521       C  
ATOM    778  CG  LEU A 317       8.936  -2.326  32.918  1.00 45.01           C  
ANISOU  778  CG  LEU A 317     6251   7000   3849   2394   -269    654       C  
ATOM    779  CD1 LEU A 317       7.587  -3.018  32.825  1.00 44.89           C  
ANISOU  779  CD1 LEU A 317     6242   6940   3874   2420   -137    761       C  
ATOM    780  CD2 LEU A 317      10.067  -3.351  32.931  1.00 44.29           C  
ANISOU  780  CD2 LEU A 317     6102   6936   3789   2416   -364    753       C  
ATOM    781  N   LEU A 318      10.151   1.233  30.207  1.00 44.10           N  
ANISOU  781  N   LEU A 318     6122   6641   3994   2177   -370    213       N  
ATOM    782  CA  LEU A 318      10.264   2.012  28.979  1.00 42.81           C  
ANISOU  782  CA  LEU A 318     5948   6359   3959   2104   -370    138       C  
ATOM    783  C   LEU A 318      11.697   2.498  28.772  1.00 42.50           C  
ANISOU  783  C   LEU A 318     5878   6344   3927   2019   -475     51       C  
ATOM    784  O   LEU A 318      12.207   2.506  27.655  1.00 45.29           O  
ANISOU  784  O   LEU A 318     6176   6633   4400   1954   -488     44       O  
ATOM    785  CB  LEU A 318       9.296   3.197  29.011  1.00 41.56           C  
ANISOU  785  CB  LEU A 318     5877   6128   3787   2114   -307     52       C  
ATOM    786  CG  LEU A 318       7.828   2.876  28.716  1.00 43.12           C  
ANISOU  786  CG  LEU A 318     6071   6277   4038   2179   -197    130       C  
ATOM    787  CD1 LEU A 318       6.931   4.051  29.074  1.00 40.22           C  
ANISOU  787  CD1 LEU A 318     5784   5864   3634   2221   -136     40       C  
ATOM    788  CD2 LEU A 318       7.646   2.484  27.255  1.00 38.77           C  
ANISOU  788  CD2 LEU A 318     5453   5631   3646   2138   -184    190       C  
ATOM    789  N   LYS A 319      12.342   2.895  29.863  1.00 44.31           N  
ANISOU  789  N   LYS A 319     6138   6678   4020   2010   -547    -16       N  
ATOM    790  CA  LYS A 319      13.705   3.413  29.817  1.00 48.53           C  
ANISOU  790  CA  LYS A 319     6633   7260   4547   1917   -654   -107       C  
ATOM    791  C   LYS A 319      14.674   2.440  29.145  1.00 47.84           C  
ANISOU  791  C   LYS A 319     6410   7207   4561   1906   -702    -31       C  
ATOM    792  O   LYS A 319      15.449   2.822  28.267  1.00 43.09           O  
ANISOU  792  O   LYS A 319     5752   6568   4052   1815   -730    -87       O  
ATOM    793  CB  LYS A 319      14.178   3.729  31.238  1.00 56.83           C  
ANISOU  793  CB  LYS A 319     7728   8453   5413   1918   -733   -170       C  
ATOM    794  CG  LYS A 319      15.572   4.327  31.332  1.00 62.23           C  
ANISOU  794  CG  LYS A 319     8364   9210   6072   1807   -855   -276       C  
ATOM    795  CD  LYS A 319      15.862   4.801  32.749  1.00 65.89           C  
ANISOU  795  CD  LYS A 319     8895   9809   6332   1795   -930   -359       C  
ATOM    796  CE  LYS A 319      17.153   5.600  32.823  1.00 66.63           C  
ANISOU  796  CE  LYS A 319     8949   9967   6401   1656  -1051   -492       C  
ATOM    797  NZ  LYS A 319      18.351   4.731  32.698  1.00 70.74           N  
ANISOU  797  NZ  LYS A 319     9299  10618   6960   1653  -1157   -413       N  
ATOM    798  N   TYR A 320      14.621   1.179  29.562  1.00 46.42           N  
ANISOU  798  N   TYR A 320     6182   7092   4365   2000   -703     98       N  
ATOM    799  CA  TYR A 320      15.548   0.167  29.072  1.00 46.34           C  
ANISOU  799  CA  TYR A 320     6045   7113   4450   2018   -745    173       C  
ATOM    800  C   TYR A 320      15.009  -0.577  27.855  1.00 48.67           C  
ANISOU  800  C   TYR A 320     6310   7283   4901   2033   -650    244       C  
ATOM    801  O   TYR A 320      15.762  -1.226  27.134  1.00 56.19           O  
ANISOU  801  O   TYR A 320     7163   8226   5960   2029   -662    270       O  
ATOM    802  CB  TYR A 320      15.867  -0.831  30.185  1.00 44.55           C  
ANISOU  802  CB  TYR A 320     5789   7010   4127   2118   -805    283       C  
ATOM    803  CG  TYR A 320      16.710  -0.253  31.296  1.00 49.27           C  
ANISOU  803  CG  TYR A 320     6384   7766   4570   2093   -929    217       C  
ATOM    804  CD1 TYR A 320      16.131   0.460  32.335  1.00 52.05           C  
ANISOU  804  CD1 TYR A 320     6855   8171   4750   2087   -929    159       C  
ATOM    805  CD2 TYR A 320      18.088  -0.420  31.304  1.00 57.04           C  
ANISOU  805  CD2 TYR A 320     7241   8854   5576   2072  -1045    203       C  
ATOM    806  CE1 TYR A 320      16.900   0.992  33.355  1.00 60.65           C  
ANISOU  806  CE1 TYR A 320     7951   9412   5682   2049  -1048     86       C  
ATOM    807  CE2 TYR A 320      18.867   0.106  32.319  1.00 62.66           C  
ANISOU  807  CE2 TYR A 320     7941   9728   6140   2036  -1172    140       C  
ATOM    808  CZ  TYR A 320      18.269   0.811  33.341  1.00 64.86           C  
ANISOU  808  CZ  TYR A 320     8353  10055   6237   2018  -1176     79       C  
ATOM    809  OH  TYR A 320      19.040   1.338  34.351  1.00 69.67           O  
ANISOU  809  OH  TYR A 320     8958  10831   6683   1968  -1307      3       O  
ATOM    810  N   GLY A 321      13.705  -0.477  27.624  1.00 45.55           N  
ANISOU  810  N   GLY A 321     5993   6798   4516   2049   -556    268       N  
ATOM    811  CA  GLY A 321      13.072  -1.233  26.560  1.00 40.47           C  
ANISOU  811  CA  GLY A 321     5326   6049   4001   2056   -472    338       C  
ATOM    812  C   GLY A 321      12.982  -0.553  25.205  1.00 40.59           C  
ANISOU  812  C   GLY A 321     5339   5965   4118   1963   -438    267       C  
ATOM    813  O   GLY A 321      13.008  -1.226  24.175  1.00 40.74           O  
ANISOU  813  O   GLY A 321     5310   5923   4245   1944   -399    302       O  
ATOM    814  N   VAL A 322      12.877   0.773  25.191  1.00 40.86           N  
ANISOU  814  N   VAL A 322     5434   5975   4114   1902   -452    170       N  
ATOM    815  CA  VAL A 322      12.600   1.486  23.943  1.00 43.20           C  
ANISOU  815  CA  VAL A 322     5752   6168   4496   1820   -417    126       C  
ATOM    816  C   VAL A 322      13.626   1.238  22.838  1.00 43.53           C  
ANISOU  816  C   VAL A 322     5711   6198   4630   1739   -431    105       C  
ATOM    817  O   VAL A 322      13.259   1.062  21.679  1.00 42.33           O  
ANISOU  817  O   VAL A 322     5554   5973   4558   1698   -380    126       O  
ATOM    818  CB  VAL A 322      12.434   3.008  24.156  1.00 43.58           C  
ANISOU  818  CB  VAL A 322     5890   6172   4494   1771   -434     25       C  
ATOM    819  CG1 VAL A 322      11.133   3.295  24.882  1.00 43.64           C  
ANISOU  819  CG1 VAL A 322     5978   6160   4441   1856   -383     42       C  
ATOM    820  CG2 VAL A 322      13.619   3.574  24.919  1.00 44.29           C  
ANISOU  820  CG2 VAL A 322     5973   6344   4511   1722   -520    -65       C  
ATOM    821  N   HIS A 323      14.906   1.221  23.188  1.00 41.53           N  
ANISOU  821  N   HIS A 323     5389   6030   4360   1713   -498     62       N  
ATOM    822  CA  HIS A 323      15.943   1.077  22.170  1.00 47.72           C  
ANISOU  822  CA  HIS A 323     6082   6819   5230   1632   -501     29       C  
ATOM    823  C   HIS A 323      16.046  -0.328  21.575  1.00 45.38           C  
ANISOU  823  C   HIS A 323     5706   6516   5021   1688   -453    102       C  
ATOM    824  O   HIS A 323      16.345  -0.480  20.391  1.00 46.23           O  
ANISOU  824  O   HIS A 323     5775   6584   5208   1622   -408     81       O  
ATOM    825  CB  HIS A 323      17.297   1.570  22.684  1.00 53.18           C  
ANISOU  825  CB  HIS A 323     6703   7616   5888   1577   -587    -48       C  
ATOM    826  CG  HIS A 323      17.442   3.058  22.639  1.00 59.18           C  
ANISOU  826  CG  HIS A 323     7535   8342   6609   1457   -614   -149       C  
ATOM    827  ND1 HIS A 323      17.312   3.854  23.757  1.00 65.22           N  
ANISOU  827  ND1 HIS A 323     8377   9135   7269   1460   -669   -205       N  
ATOM    828  CD2 HIS A 323      17.679   3.898  21.604  1.00 58.26           C  
ANISOU  828  CD2 HIS A 323     7440   8153   6544   1328   -588   -204       C  
ATOM    829  CE1 HIS A 323      17.474   5.119  23.414  1.00 67.50           C  
ANISOU  829  CE1 HIS A 323     8733   9356   7558   1338   -675   -295       C  
ATOM    830  NE2 HIS A 323      17.698   5.173  22.113  1.00 63.80           N  
ANISOU  830  NE2 HIS A 323     8232   8825   7183   1256   -629   -287       N  
ATOM    831  N   GLU A 324      15.794  -1.349  22.388  1.00 41.79           N  
ANISOU  831  N   GLU A 324     5238   6092   4546   1804   -458    185       N  
ATOM    832  CA  GLU A 324      15.785  -2.719  21.886  1.00 38.40           C  
ANISOU  832  CA  GLU A 324     4757   5627   4207   1864   -405    256       C  
ATOM    833  C   GLU A 324      14.642  -2.877  20.887  1.00 39.30           C  
ANISOU  833  C   GLU A 324     4933   5631   4370   1824   -318    277       C  
ATOM    834  O   GLU A 324      14.759  -3.588  19.890  1.00 39.08           O  
ANISOU  834  O   GLU A 324     4870   5552   4428   1802   -263    278       O  
ATOM    835  CB  GLU A 324      15.654  -3.724  23.038  1.00 37.72           C  
ANISOU  835  CB  GLU A 324     4668   5580   4084   1993   -428    358       C  
ATOM    836  CG  GLU A 324      16.842  -3.719  23.994  1.00 37.42           C  
ANISOU  836  CG  GLU A 324     4554   5670   3996   2041   -530    353       C  
ATOM    837  CD  GLU A 324      16.624  -4.585  25.226  1.00 43.44           C  
ANISOU  837  CD  GLU A 324     5335   6478   4692   2167   -563    471       C  
ATOM    838  OE1 GLU A 324      15.550  -5.209  25.341  1.00 48.56           O  
ANISOU  838  OE1 GLU A 324     6058   7053   5341   2210   -495    555       O  
ATOM    839  OE2 GLU A 324      17.530  -4.642  26.083  1.00 44.23           O  
ANISOU  839  OE2 GLU A 324     5375   6695   4736   2216   -659    485       O  
ATOM    840  N   ILE A 325      13.539  -2.192  21.160  1.00 36.07           N  
ANISOU  840  N   ILE A 325     4612   5191   3903   1816   -307    286       N  
ATOM    841  CA  ILE A 325      12.387  -2.213  20.272  1.00 37.64           C  
ANISOU  841  CA  ILE A 325     4859   5305   4138   1778   -242    310       C  
ATOM    842  C   ILE A 325      12.646  -1.385  19.013  1.00 34.32           C  
ANISOU  842  C   ILE A 325     4443   4846   3751   1662   -234    241       C  
ATOM    843  O   ILE A 325      12.267  -1.779  17.914  1.00 39.59           O  
ANISOU  843  O   ILE A 325     5109   5462   4470   1612   -186    252       O  
ATOM    844  CB  ILE A 325      11.127  -1.692  20.990  1.00 36.08           C  
ANISOU  844  CB  ILE A 325     4735   5099   3874   1821   -231    344       C  
ATOM    845  CG1 ILE A 325      10.722  -2.656  22.107  1.00 38.25           C  
ANISOU  845  CG1 ILE A 325     5011   5411   4111   1921   -216    430       C  
ATOM    846  CG2 ILE A 325       9.985  -1.503  20.004  1.00 29.55           C  
ANISOU  846  CG2 ILE A 325     3938   4202   3087   1775   -182    362       C  
ATOM    847  CD1 ILE A 325       9.608  -2.133  22.974  1.00 41.25           C  
ANISOU  847  CD1 ILE A 325     5452   5810   4411   1967   -196    453       C  
ATOM    848  N   ILE A 326      13.300  -0.241  19.181  1.00 31.80           N  
ANISOU  848  N   ILE A 326     4137   4552   3394   1609   -283    172       N  
ATOM    849  CA  ILE A 326      13.626   0.624  18.052  1.00 37.45           C  
ANISOU  849  CA  ILE A 326     4868   5229   4133   1489   -277    116       C  
ATOM    850  C   ILE A 326      14.455  -0.097  16.987  1.00 36.87           C  
ANISOU  850  C   ILE A 326     4717   5167   4124   1429   -239     96       C  
ATOM    851  O   ILE A 326      14.187   0.030  15.795  1.00 38.61           O  
ANISOU  851  O   ILE A 326     4960   5343   4368   1347   -198     92       O  
ATOM    852  CB  ILE A 326      14.366   1.898  18.515  1.00 40.33           C  
ANISOU  852  CB  ILE A 326     5257   5615   4452   1429   -335     40       C  
ATOM    853  CG1 ILE A 326      13.374   2.900  19.111  1.00 38.50           C  
ANISOU  853  CG1 ILE A 326     5133   5328   4166   1459   -349     39       C  
ATOM    854  CG2 ILE A 326      15.133   2.531  17.358  1.00 40.54           C  
ANISOU  854  CG2 ILE A 326     5271   5622   4511   1289   -324    -12       C  
ATOM    855  CD1 ILE A 326      14.023   4.158  19.635  1.00 42.50           C  
ANISOU  855  CD1 ILE A 326     5686   5834   4627   1397   -402    -47       C  
ATOM    856  N   TYR A 327      15.456  -0.857  17.415  1.00 35.47           N  
ANISOU  856  N   TYR A 327     4446   5056   3973   1476   -250     84       N  
ATOM    857  CA  TYR A 327      16.308  -1.569  16.466  1.00 40.25           C  
ANISOU  857  CA  TYR A 327     4967   5677   4650   1438   -202     52       C  
ATOM    858  C   TYR A 327      15.620  -2.816  15.921  1.00 40.32           C  
ANISOU  858  C   TYR A 327     4985   5625   4710   1483   -133     99       C  
ATOM    859  O   TYR A 327      15.931  -3.274  14.825  1.00 40.86           O  
ANISOU  859  O   TYR A 327     5024   5675   4825   1427    -70     63       O  
ATOM    860  CB  TYR A 327      17.648  -1.939  17.102  1.00 43.70           C  
ANISOU  860  CB  TYR A 327     5284   6208   5111   1487   -240     23       C  
ATOM    861  CG  TYR A 327      18.345  -0.773  17.758  1.00 52.60           C  
ANISOU  861  CG  TYR A 327     6397   7407   6183   1431   -319    -30       C  
ATOM    862  CD1 TYR A 327      18.488   0.440  17.093  1.00 54.29           C  
ANISOU  862  CD1 TYR A 327     6654   7600   6375   1289   -316    -89       C  
ATOM    863  CD2 TYR A 327      18.870  -0.885  19.038  1.00 60.29           C  
ANISOU  863  CD2 TYR A 327     7320   8468   7120   1512   -400    -21       C  
ATOM    864  CE1 TYR A 327      19.125   1.513  17.693  1.00 57.59           C  
ANISOU  864  CE1 TYR A 327     7068   8067   6746   1221   -385   -148       C  
ATOM    865  CE2 TYR A 327      19.511   0.180  19.645  1.00 63.24           C  
ANISOU  865  CE2 TYR A 327     7682   8911   7434   1444   -477    -84       C  
ATOM    866  CZ  TYR A 327      19.638   1.376  18.968  1.00 64.10           C  
ANISOU  866  CZ  TYR A 327     7838   8984   7533   1295   -466   -153       C  
ATOM    867  OH  TYR A 327      20.277   2.437  19.569  1.00 69.58           O  
ANISOU  867  OH  TYR A 327     8531   9733   8174   1211   -539   -224       O  
ATOM    868  N   THR A 328      14.689  -3.364  16.694  1.00 38.28           N  
ANISOU  868  N   THR A 328     4770   5337   4439   1576   -138    174       N  
ATOM    869  CA  THR A 328      13.902  -4.505  16.249  1.00 36.70           C  
ANISOU  869  CA  THR A 328     4590   5068   4285   1601    -75    221       C  
ATOM    870  C   THR A 328      13.005  -4.090  15.090  1.00 38.32           C  
ANISOU  870  C   THR A 328     4856   5225   4478   1495    -41    209       C  
ATOM    871  O   THR A 328      12.922  -4.776  14.070  1.00 41.12           O  
ANISOU  871  O   THR A 328     5207   5542   4873   1444     17    188       O  
ATOM    872  CB  THR A 328      13.020  -5.052  17.387  1.00 37.31           C  
ANISOU  872  CB  THR A 328     4705   5131   4341   1703    -86    312       C  
ATOM    873  OG1 THR A 328      13.841  -5.714  18.360  1.00 37.73           O  
ANISOU  873  OG1 THR A 328     4705   5224   4407   1808   -116    343       O  
ATOM    874  CG2 THR A 328      11.995  -6.031  16.842  1.00 32.29           C  
ANISOU  874  CG2 THR A 328     4103   4416   3749   1692    -21    358       C  
ATOM    875  N   MET A 329      12.336  -2.955  15.254  1.00 35.88           N  
ANISOU  875  N   MET A 329     4604   4918   4111   1467    -80    222       N  
ATOM    876  CA  MET A 329      11.408  -2.459  14.247  1.00 36.46           C  
ANISOU  876  CA  MET A 329     4732   4954   4167   1383    -67    232       C  
ATOM    877  C   MET A 329      12.137  -1.780  13.091  1.00 33.53           C  
ANISOU  877  C   MET A 329     4364   4591   3786   1262    -60    172       C  
ATOM    878  O   MET A 329      11.649  -1.776  11.966  1.00 35.69           O  
ANISOU  878  O   MET A 329     4668   4843   4049   1178    -36    175       O  
ATOM    879  CB  MET A 329      10.386  -1.518  14.885  1.00 37.34           C  
ANISOU  879  CB  MET A 329     4900   5055   4232   1420   -107    277       C  
ATOM    880  CG  MET A 329       9.698  -2.134  16.091  1.00 37.04           C  
ANISOU  880  CG  MET A 329     4857   5027   4189   1532   -102    335       C  
ATOM    881  SD  MET A 329       8.294  -1.183  16.687  1.00 42.78           S  
ANISOU  881  SD  MET A 329     5637   5747   4871   1582   -120    381       S  
ATOM    882  CE  MET A 329       7.235  -1.223  15.247  1.00 45.36           C  
ANISOU  882  CE  MET A 329     5970   6040   5226   1499   -104    415       C  
ATOM    883  N   LEU A 330      13.311  -1.222  13.371  1.00 39.16           N  
ANISOU  883  N   LEU A 330     5041   5342   4494   1243    -81    119       N  
ATOM    884  CA  LEU A 330      14.143  -0.641  12.321  1.00 39.63           C  
ANISOU  884  CA  LEU A 330     5093   5420   4546   1117    -61     61       C  
ATOM    885  C   LEU A 330      14.510  -1.694  11.278  1.00 38.41           C  
ANISOU  885  C   LEU A 330     4894   5274   4426   1074     17     25       C  
ATOM    886  O   LEU A 330      14.665  -1.384  10.096  1.00 36.30           O  
ANISOU  886  O   LEU A 330     4650   5012   4132    956     52     -3       O  
ATOM    887  CB  LEU A 330      15.414  -0.031  12.912  1.00 39.60           C  
ANISOU  887  CB  LEU A 330     5033   5471   4543   1102    -93      6       C  
ATOM    888  CG  LEU A 330      16.295   0.774  11.952  1.00 41.50           C  
ANISOU  888  CG  LEU A 330     5266   5735   4769    954    -71    -49       C  
ATOM    889  CD1 LEU A 330      15.513   1.931  11.343  1.00 41.85           C  
ANISOU  889  CD1 LEU A 330     5428   5712   4762    867    -91    -12       C  
ATOM    890  CD2 LEU A 330      17.526   1.285  12.677  1.00 45.00           C  
ANISOU  890  CD2 LEU A 330     5633   6245   5220    937   -109   -106       C  
ATOM    891  N   ALA A 331      14.648  -2.939  11.726  1.00 35.59           N  
ANISOU  891  N   ALA A 331     4483   4914   4125   1170     46     26       N  
ATOM    892  CA  ALA A 331      14.925  -4.053  10.827  1.00 35.64           C  
ANISOU  892  CA  ALA A 331     4459   4907   4176   1148    129    -18       C  
ATOM    893  C   ALA A 331      13.845  -4.157   9.754  1.00 35.15           C  
ANISOU  893  C   ALA A 331     4476   4805   4075   1058    156     -4       C  
ATOM    894  O   ALA A 331      14.130  -4.475   8.599  1.00 34.45           O  
ANISOU  894  O   ALA A 331     4390   4723   3975    967    220    -64       O  
ATOM    895  CB  ALA A 331      15.025  -5.357  11.607  1.00 34.30           C  
ANISOU  895  CB  ALA A 331     4245   4708   4082   1281    148      2       C  
ATOM    896  N   SER A 332      12.603  -3.880  10.140  1.00 33.61           N  
ANISOU  896  N   SER A 332     4339   4579   3851   1082    106     72       N  
ATOM    897  CA  SER A 332      11.490  -3.929   9.198  1.00 35.42           C  
ANISOU  897  CA  SER A 332     4629   4788   4041   1000    110     97       C  
ATOM    898  C   SER A 332      11.676  -2.939   8.054  1.00 35.96           C  
ANISOU  898  C   SER A 332     4739   4887   4038    868    103     78       C  
ATOM    899  O   SER A 332      11.122  -3.124   6.971  1.00 33.90           O  
ANISOU  899  O   SER A 332     4517   4631   3731    774    119     76       O  
ATOM    900  CB  SER A 332      10.171  -3.629   9.907  1.00 35.19           C  
ANISOU  900  CB  SER A 332     4631   4739   3999   1060     53    187       C  
ATOM    901  OG  SER A 332       9.955  -4.529  10.973  1.00 35.70           O  
ANISOU  901  OG  SER A 332     4667   4780   4116   1169     65    217       O  
ATOM    902  N   LEU A 333      12.455  -1.890   8.305  1.00 33.07           N  
ANISOU  902  N   LEU A 333     4368   4542   3655    852     77     68       N  
ATOM    903  CA  LEU A 333      12.642  -0.812   7.338  1.00 37.48           C  
ANISOU  903  CA  LEU A 333     4979   5116   4144    724     66     70       C  
ATOM    904  C   LEU A 333      13.939  -0.987   6.559  1.00 38.22           C  
ANISOU  904  C   LEU A 333     5029   5260   4231    630    142    -17       C  
ATOM    905  O   LEU A 333      14.284  -0.164   5.707  1.00 36.06           O  
ANISOU  905  O   LEU A 333     4796   5009   3895    507    152    -20       O  
ATOM    906  CB  LEU A 333      12.648   0.542   8.053  1.00 38.97           C  
ANISOU  906  CB  LEU A 333     5205   5280   4321    745     -3    111       C  
ATOM    907  CG  LEU A 333      11.292   1.162   8.408  1.00 46.13           C  
ANISOU  907  CG  LEU A 333     6177   6138   5213    803    -72    199       C  
ATOM    908  CD1 LEU A 333      10.325   0.130   8.966  1.00 46.00           C  
ANISOU  908  CD1 LEU A 333     6129   6119   5232    905    -70    230       C  
ATOM    909  CD2 LEU A 333      11.474   2.319   9.385  1.00 45.43           C  
ANISOU  909  CD2 LEU A 333     6119   6012   5131    852   -123    209       C  
ATOM    910  N   MET A 334      14.653  -2.067   6.856  1.00 35.73           N  
ANISOU  910  N   MET A 334     4631   4963   3983    693    202    -83       N  
ATOM    911  CA  MET A 334      15.968  -2.293   6.278  1.00 35.90           C  
ANISOU  911  CA  MET A 334     4581   5042   4017    633    284   -175       C  
ATOM    912  C   MET A 334      16.021  -3.487   5.331  1.00 35.94           C  
ANISOU  912  C   MET A 334     4577   5049   4028    603    383   -246       C  
ATOM    913  O   MET A 334      15.331  -4.486   5.522  1.00 39.69           O  
ANISOU  913  O   MET A 334     5067   5471   4541    674    391   -239       O  
ATOM    914  CB  MET A 334      16.994  -2.508   7.389  1.00 36.10           C  
ANISOU  914  CB  MET A 334     4496   5095   4125    740    277   -206       C  
ATOM    915  CG  MET A 334      17.316  -1.281   8.214  1.00 35.34           C  
ANISOU  915  CG  MET A 334     4398   5017   4014    735    195   -175       C  
ATOM    916  SD  MET A 334      18.502  -1.685   9.514  1.00 42.52           S  
ANISOU  916  SD  MET A 334     5163   5985   5006    860    171   -212       S  
ATOM    917  CE  MET A 334      19.226  -0.079   9.834  1.00 41.94           C  
ANISOU  917  CE  MET A 334     5086   5958   4892    752    110   -226       C  
ATOM    918  N   ASN A 335      16.841  -3.368   4.297  1.00 41.31           N  
ANISOU  918  N   ASN A 335     5239   5789   4667    488    465   -321       N  
ATOM    919  CA  ASN A 335      17.329  -4.542   3.592  1.00 42.86           C  
ANISOU  919  CA  ASN A 335     5395   5997   4891    484    583   -426       C  
ATOM    920  C   ASN A 335      18.850  -4.480   3.581  1.00 45.27           C  
ANISOU  920  C   ASN A 335     5576   6379   5245    484    659   -509       C  
ATOM    921  O   ASN A 335      19.441  -3.640   4.260  1.00 44.16           O  
ANISOU  921  O   ASN A 335     5379   6278   5123    493    605   -479       O  
ATOM    922  CB  ASN A 335      16.740  -4.664   2.183  1.00 38.04           C  
ANISOU  922  CB  ASN A 335     4882   5402   4169    338    632   -456       C  
ATOM    923  CG  ASN A 335      17.137  -3.519   1.274  1.00 40.05           C  
ANISOU  923  CG  ASN A 335     5175   5735   4309    173    645   -447       C  
ATOM    924  OD1 ASN A 335      18.155  -2.860   1.483  1.00 43.23           O  
ANISOU  924  OD1 ASN A 335     5509   6188   4730    150    664   -462       O  
ATOM    925  ND2 ASN A 335      16.330  -3.281   0.248  1.00 38.22           N  
ANISOU  925  ND2 ASN A 335     5053   5517   3953     49    632   -417       N  
ATOM    926  N   LYS A 336      19.480  -5.367   2.824  1.00 46.44           N  
ANISOU  926  N   LYS A 336     5678   6552   5416    471    787   -620       N  
ATOM    927  CA  LYS A 336      20.936  -5.424   2.772  1.00 54.10           C  
ANISOU  927  CA  LYS A 336     6504   7607   6445    483    874   -707       C  
ATOM    928  C   LYS A 336      21.556  -4.094   2.338  1.00 48.20           C  
ANISOU  928  C   LYS A 336     5742   6958   5614    325    873   -697       C  
ATOM    929  O   LYS A 336      22.683  -3.773   2.714  1.00 46.92           O  
ANISOU  929  O   LYS A 336     5446   6874   5508    336    892   -730       O  
ATOM    930  CB  LYS A 336      21.379  -6.538   1.819  1.00 62.37           C  
ANISOU  930  CB  LYS A 336     7524   8661   7512    479   1031   -841       C  
ATOM    931  CG  LYS A 336      22.878  -6.636   1.610  1.00 72.06           C  
ANISOU  931  CG  LYS A 336     8588   9991   8801    490   1144   -943       C  
ATOM    932  CD  LYS A 336      23.243  -7.759   0.639  1.00 79.80           C  
ANISOU  932  CD  LYS A 336     9553  10966   9800    496   1315  -1089       C  
ATOM    933  CE  LYS A 336      22.777  -7.465  -0.785  1.00 80.38           C  
ANISOU  933  CE  LYS A 336     9759  11079   9702    291   1389  -1136       C  
ATOM    934  NZ  LYS A 336      21.314  -7.677  -0.971  1.00 78.15           N  
ANISOU  934  NZ  LYS A 336     9650  10699   9344    254   1309  -1076       N  
ATOM    935  N   ASP A 337      20.807  -3.318   1.559  1.00 44.03           N  
ANISOU  935  N   ASP A 337     5349   6425   4954    176    846   -644       N  
ATOM    936  CA  ASP A 337      21.363  -2.163   0.855  1.00 41.12           C  
ANISOU  936  CA  ASP A 337     4996   6137   4491     -3    874   -635       C  
ATOM    937  C   ASP A 337      21.095  -0.795   1.489  1.00 41.70           C  
ANISOU  937  C   ASP A 337     5123   6180   4539    -45    746   -523       C  
ATOM    938  O   ASP A 337      21.748   0.187   1.133  1.00 44.83           O  
ANISOU  938  O   ASP A 337     5514   6631   4887   -184    767   -515       O  
ATOM    939  CB  ASP A 337      20.876  -2.157  -0.596  1.00 42.01           C  
ANISOU  939  CB  ASP A 337     5230   6276   4457   -161    942   -650       C  
ATOM    940  CG  ASP A 337      21.379  -3.352  -1.383  1.00 54.38           C  
ANISOU  940  CG  ASP A 337     6745   7887   6029   -157   1099   -793       C  
ATOM    941  OD1 ASP A 337      22.508  -3.814  -1.110  1.00 54.54           O  
ANISOU  941  OD1 ASP A 337     6613   7959   6151    -88   1188   -886       O  
ATOM    942  OD2 ASP A 337      20.645  -3.830  -2.273  1.00 61.43           O  
ANISOU  942  OD2 ASP A 337     7746   8767   6827   -222   1131   -818       O  
ATOM    943  N   GLY A 338      20.140  -0.719   2.409  1.00 36.24           N  
ANISOU  943  N   GLY A 338     4489   5399   3881     67    625   -440       N  
ATOM    944  CA  GLY A 338      19.826   0.552   3.039  1.00 35.49           C  
ANISOU  944  CA  GLY A 338     4456   5259   3768     43    512   -347       C  
ATOM    945  C   GLY A 338      18.564   0.548   3.877  1.00 37.51           C  
ANISOU  945  C   GLY A 338     4789   5419   4044    167    398   -261       C  
ATOM    946  O   GLY A 338      17.980  -0.507   4.133  1.00 39.88           O  
ANISOU  946  O   GLY A 338     5078   5689   4384    279    401   -268       O  
ATOM    947  N   VAL A 339      18.140   1.737   4.298  1.00 34.74           N  
ANISOU  947  N   VAL A 339     4518   5015   3668    142    307   -181       N  
ATOM    948  CA  VAL A 339      17.019   1.872   5.222  1.00 35.38           C  
ANISOU  948  CA  VAL A 339     4657   5013   3772    267    206   -106       C  
ATOM    949  C   VAL A 339      15.991   2.917   4.775  1.00 37.18           C  
ANISOU  949  C   VAL A 339     5026   5172   3929    209    140     -4       C  
ATOM    950  O   VAL A 339      16.346   4.023   4.369  1.00 38.14           O  
ANISOU  950  O   VAL A 339     5207   5278   4007     92    132     23       O  
ATOM    951  CB  VAL A 339      17.514   2.235   6.638  1.00 34.41           C  
ANISOU  951  CB  VAL A 339     4474   4882   3718    359    148   -120       C  
ATOM    952  CG1 VAL A 339      18.288   3.547   6.611  1.00 35.69           C  
ANISOU  952  CG1 VAL A 339     4655   5047   3857    234    131   -127       C  
ATOM    953  CG2 VAL A 339      16.347   2.308   7.622  1.00 30.36           C  
ANISOU  953  CG2 VAL A 339     4019   4295   3221    493     62    -52       C  
ATOM    954  N   LEU A 340      14.716   2.551   4.857  1.00 35.74           N  
ANISOU  954  N   LEU A 340     4892   4948   3741    291     93     57       N  
ATOM    955  CA  LEU A 340      13.620   3.487   4.622  1.00 33.96           C  
ANISOU  955  CA  LEU A 340     4779   4656   3468    281     15    164       C  
ATOM    956  C   LEU A 340      13.695   4.653   5.603  1.00 38.95           C  
ANISOU  956  C   LEU A 340     5448   5214   4136    327    -48    192       C  
ATOM    957  O   LEU A 340      14.010   4.463   6.777  1.00 38.42           O  
ANISOU  957  O   LEU A 340     5321   5145   4132    425    -60    147       O  
ATOM    958  CB  LEU A 340      12.281   2.770   4.803  1.00 36.85           C  
ANISOU  958  CB  LEU A 340     5149   5007   3846    386    -24    212       C  
ATOM    959  CG  LEU A 340      11.427   2.395   3.592  1.00 48.10           C  
ANISOU  959  CG  LEU A 340     6619   6463   5194    313    -29    256       C  
ATOM    960  CD1 LEU A 340      12.238   2.313   2.306  1.00 48.98           C  
ANISOU  960  CD1 LEU A 340     6751   6639   5221    149     43    209       C  
ATOM    961  CD2 LEU A 340      10.665   1.102   3.863  1.00 43.71           C  
ANISOU  961  CD2 LEU A 340     6010   5922   4675    394    -20    236       C  
ATOM    962  N   ILE A 341      13.399   5.856   5.122  1.00 39.71           N  
ANISOU  962  N   ILE A 341     5653   5246   4190    255    -89    267       N  
ATOM    963  CA  ILE A 341      13.344   7.030   5.986  1.00 39.68           C  
ANISOU  963  CA  ILE A 341     5710   5144   4222    297   -146    290       C  
ATOM    964  C   ILE A 341      12.144   7.897   5.636  1.00 40.92           C  
ANISOU  964  C   ILE A 341     5984   5206   4356    328   -214    408       C  
ATOM    965  O   ILE A 341      11.502   7.700   4.602  1.00 35.92           O  
ANISOU  965  O   ILE A 341     5384   4599   3666    287   -224    480       O  
ATOM    966  CB  ILE A 341      14.618   7.898   5.875  1.00 43.93           C  
ANISOU  966  CB  ILE A 341     6267   5671   4755    155   -118    245       C  
ATOM    967  CG1 ILE A 341      14.759   8.462   4.461  1.00 46.32           C  
ANISOU  967  CG1 ILE A 341     6655   5968   4977    -12    -93    310       C  
ATOM    968  CG2 ILE A 341      15.858   7.105   6.273  1.00 46.42           C  
ANISOU  968  CG2 ILE A 341     6443   6093   5103    135    -58    130       C  
ATOM    969  CD1 ILE A 341      15.877   9.469   4.320  1.00 47.00           C  
ANISOU  969  CD1 ILE A 341     6777   6024   5057   -170    -65    287       C  
ATOM    970  N   SER A 342      11.846   8.856   6.507  1.00 42.66           N  
ANISOU  970  N   SER A 342     6267   5322   4622    404   -263    425       N  
ATOM    971  CA  SER A 342      10.785   9.824   6.255  1.00 46.68           C  
ANISOU  971  CA  SER A 342     6886   5720   5129    453   -326    537       C  
ATOM    972  C   SER A 342       9.462   9.136   5.931  1.00 44.18           C  
ANISOU  972  C   SER A 342     6534   5449   4802    552   -359    611       C  
ATOM    973  O   SER A 342       8.843   9.407   4.900  1.00 44.90           O  
ANISOU  973  O   SER A 342     6681   5536   4844    510   -396    714       O  
ATOM    974  CB  SER A 342      11.191  10.765   5.119  1.00 54.15           C  
ANISOU  974  CB  SER A 342     7944   6611   6021    293   -328    608       C  
ATOM    975  OG  SER A 342      10.301  11.861   5.022  1.00 63.53           O  
ANISOU  975  OG  SER A 342     9251   7663   7226    354   -394    719       O  
ATOM    976  N   GLU A 343       9.037   8.241   6.817  1.00 42.73           N  
ANISOU  976  N   GLU A 343     6258   5317   4660    675   -350    564       N  
ATOM    977  CA  GLU A 343       7.799   7.494   6.627  1.00 49.67           C  
ANISOU  977  CA  GLU A 343     7085   6251   5538    759   -374    622       C  
ATOM    978  C   GLU A 343       7.786   6.730   5.304  1.00 46.82           C  
ANISOU  978  C   GLU A 343     6704   5981   5104    639   -362    645       C  
ATOM    979  O   GLU A 343       6.730   6.536   4.703  1.00 46.46           O  
ANISOU  979  O   GLU A 343     6653   5968   5032    656   -408    725       O  
ATOM    980  CB  GLU A 343       6.590   8.429   6.699  1.00 60.17           C  
ANISOU  980  CB  GLU A 343     8471   7498   6893    864   -443    727       C  
ATOM    981  CG  GLU A 343       6.596   9.367   7.895  1.00 69.09           C  
ANISOU  981  CG  GLU A 343     9649   8517   8086    974   -448    695       C  
ATOM    982  CD  GLU A 343       5.369  10.256   7.940  1.00 78.47           C  
ANISOU  982  CD  GLU A 343    10885   9617   9312   1100   -505    794       C  
ATOM    983  OE1 GLU A 343       4.259   9.755   7.659  1.00 81.76           O  
ANISOU  983  OE1 GLU A 343    11233  10100   9732   1169   -535    864       O  
ATOM    984  OE2 GLU A 343       5.514  11.456   8.259  1.00 81.00           O  
ANISOU  984  OE2 GLU A 343    11309   9802   9666   1129   -519    799       O  
ATOM    985  N   GLY A 344       8.960   6.304   4.850  1.00 41.18           N  
ANISOU  985  N   GLY A 344     5974   5316   4355    516   -298    569       N  
ATOM    986  CA  GLY A 344       9.052   5.470   3.666  1.00 38.54           C  
ANISOU  986  CA  GLY A 344     5621   5075   3947    401   -265    559       C  
ATOM    987  C   GLY A 344       9.141   6.217   2.348  1.00 41.06           C  
ANISOU  987  C   GLY A 344     6037   5398   4168    259   -285    635       C  
ATOM    988  O   GLY A 344       9.218   5.595   1.288  1.00 46.38           O  
ANISOU  988  O   GLY A 344     6709   6158   4757    149   -256    624       O  
ATOM    989  N   GLN A 345       9.139   7.546   2.403  1.00 39.60           N  
ANISOU  989  N   GLN A 345     5945   5114   3988    257   -331    712       N  
ATOM    990  CA  GLN A 345       9.237   8.354   1.188  1.00 44.94           C  
ANISOU  990  CA  GLN A 345     6730   5779   4568    121   -354    808       C  
ATOM    991  C   GLN A 345      10.673   8.401   0.680  1.00 43.18           C  
ANISOU  991  C   GLN A 345     6519   5593   4294    -49   -262    734       C  
ATOM    992  O   GLN A 345      10.919   8.631  -0.502  1.00 44.51           O  
ANISOU  992  O   GLN A 345     6755   5805   4353   -197   -246    785       O  
ATOM    993  CB  GLN A 345       8.727   9.775   1.431  1.00 49.61           C  
ANISOU  993  CB  GLN A 345     7428   6226   5195    184   -431    924       C  
ATOM    994  CG  GLN A 345       7.284   9.842   1.891  1.00 58.26           C  
ANISOU  994  CG  GLN A 345     8500   7289   6345    362   -517   1003       C  
ATOM    995  CD  GLN A 345       6.828  11.259   2.171  1.00 71.62           C  
ANISOU  995  CD  GLN A 345    10300   8822   8091    445   -582   1106       C  
ATOM    996  OE1 GLN A 345       7.202  12.197   1.465  1.00 76.67           O  
ANISOU  996  OE1 GLN A 345    11059   9386   8684    344   -598   1187       O  
ATOM    997  NE2 GLN A 345       6.012  11.423   3.205  1.00 77.22           N  
ANISOU  997  NE2 GLN A 345    10971   9471   8897    629   -612   1104       N  
ATOM    998  N   GLY A 346      11.622   8.188   1.583  1.00 38.18           N  
ANISOU  998  N   GLY A 346     5815   4955   3736    -29   -202    617       N  
ATOM    999  CA  GLY A 346      13.021   8.176   1.208  1.00 38.91           C  
ANISOU  999  CA  GLY A 346     5884   5100   3799   -180   -109    536       C  
ATOM   1000  C   GLY A 346      13.678   6.840   1.489  1.00 38.94           C  
ANISOU 1000  C   GLY A 346     5749   5212   3835   -157    -27    399       C  
ATOM   1001  O   GLY A 346      13.129   5.998   2.201  1.00 37.78           O  
ANISOU 1001  O   GLY A 346     5533   5075   3749    -18    -45    365       O  
ATOM   1002  N   PHE A 347      14.863   6.650   0.924  1.00 39.77           N  
ANISOU 1002  N   PHE A 347     5813   5395   3904   -292     69    324       N  
ATOM   1003  CA  PHE A 347      15.648   5.447   1.156  1.00 38.61           C  
ANISOU 1003  CA  PHE A 347     5528   5341   3800   -265    157    191       C  
ATOM   1004  C   PHE A 347      17.125   5.817   1.156  1.00 40.80           C  
ANISOU 1004  C   PHE A 347     5743   5665   4092   -379    236    115       C  
ATOM   1005  O   PHE A 347      17.681   6.185   0.122  1.00 45.77           O  
ANISOU 1005  O   PHE A 347     6411   6345   4637   -546    302    122       O  
ATOM   1006  CB  PHE A 347      15.359   4.394   0.081  1.00 34.86           C  
ANISOU 1006  CB  PHE A 347     5046   4954   3245   -313    216    160       C  
ATOM   1007  CG  PHE A 347      16.131   3.110   0.258  1.00 37.15           C  
ANISOU 1007  CG  PHE A 347     5206   5319   3591   -272    316     20       C  
ATOM   1008  CD1 PHE A 347      15.701   2.143   1.153  1.00 40.05           C  
ANISOU 1008  CD1 PHE A 347     5503   5661   4052   -109    294    -16       C  
ATOM   1009  CD2 PHE A 347      17.284   2.869  -0.476  1.00 41.71           C  
ANISOU 1009  CD2 PHE A 347     5730   5988   4130   -393    438    -69       C  
ATOM   1010  CE1 PHE A 347      16.409   0.962   1.318  1.00 40.58           C  
ANISOU 1010  CE1 PHE A 347     5460   5777   4181    -57    384   -133       C  
ATOM   1011  CE2 PHE A 347      17.996   1.689  -0.317  1.00 42.26           C  
ANISOU 1011  CE2 PHE A 347     5674   6116   4266   -334    533   -198       C  
ATOM   1012  CZ  PHE A 347      17.556   0.734   0.580  1.00 43.60           C  
ANISOU 1012  CZ  PHE A 347     5786   6244   4537   -161    502   -226       C  
ATOM   1013  N   MET A 348      17.754   5.730   2.321  1.00 39.45           N  
ANISOU 1013  N   MET A 348     5474   5491   4025   -294    229     46       N  
ATOM   1014  CA  MET A 348      19.163   6.076   2.458  1.00 40.61           C  
ANISOU 1014  CA  MET A 348     5533   5696   4200   -396    290    -30       C  
ATOM   1015  C   MET A 348      20.021   4.820   2.433  1.00 40.07           C  
ANISOU 1015  C   MET A 348     5300   5748   4175   -358    387   -149       C  
ATOM   1016  O   MET A 348      19.798   3.894   3.210  1.00 40.26           O  
ANISOU 1016  O   MET A 348     5250   5775   4273   -196    366   -186       O  
ATOM   1017  CB  MET A 348      19.391   6.847   3.756  1.00 44.10           C  
ANISOU 1017  CB  MET A 348     5965   6070   4720   -340    211    -35       C  
ATOM   1018  CG  MET A 348      20.807   7.364   3.936  1.00 50.42           C  
ANISOU 1018  CG  MET A 348     6677   6933   5550   -467    255   -107       C  
ATOM   1019  SD  MET A 348      20.906   8.631   5.217  1.00 60.81           S  
ANISOU 1019  SD  MET A 348     8047   8140   6920   -462    149   -101       S  
ATOM   1020  CE  MET A 348      20.032   9.985   4.430  1.00 54.01           C  
ANISOU 1020  CE  MET A 348     7418   7117   5988   -570    113     33       C  
ATOM   1021  N   THR A 349      21.004   4.790   1.538  1.00 42.31           N  
ANISOU 1021  N   THR A 349     5530   6129   4417   -505    498   -205       N  
ATOM   1022  CA  THR A 349      21.810   3.591   1.341  1.00 42.45           C  
ANISOU 1022  CA  THR A 349     5394   6260   4477   -466    609   -324       C  
ATOM   1023  C   THR A 349      22.754   3.321   2.511  1.00 44.68           C  
ANISOU 1023  C   THR A 349     5505   6588   4884   -366    595   -397       C  
ATOM   1024  O   THR A 349      23.165   4.237   3.223  1.00 44.42           O  
ANISOU 1024  O   THR A 349     5458   6539   4882   -404    531   -381       O  
ATOM   1025  CB  THR A 349      22.625   3.659   0.036  1.00 45.69           C  
ANISOU 1025  CB  THR A 349     5785   6776   4800   -652    749   -372       C  
ATOM   1026  OG1 THR A 349      23.661   4.639   0.168  1.00 43.38           O  
ANISOU 1026  OG1 THR A 349     5437   6525   4520   -788    769   -380       O  
ATOM   1027  CG2 THR A 349      21.724   4.019  -1.140  1.00 45.90           C  
ANISOU 1027  CG2 THR A 349     5990   6771   4679   -767    748   -285       C  
ATOM   1028  N   ARG A 350      23.086   2.048   2.690  1.00 46.03           N  
ANISOU 1028  N   ARG A 350     5550   6813   5125   -239    652   -478       N  
ATOM   1029  CA  ARG A 350      23.983   1.598   3.745  1.00 47.82           C  
ANISOU 1029  CA  ARG A 350     5600   7099   5471   -120    637   -540       C  
ATOM   1030  C   ARG A 350      25.396   2.137   3.529  1.00 48.76           C  
ANISOU 1030  C   ARG A 350     5579   7341   5606   -256    706   -606       C  
ATOM   1031  O   ARG A 350      26.067   2.546   4.478  1.00 50.89           O  
ANISOU 1031  O   ARG A 350     5745   7651   5939   -238    640   -620       O  
ATOM   1032  CB  ARG A 350      23.993   0.069   3.772  1.00 50.36           C  
ANISOU 1032  CB  ARG A 350     5836   7436   5863     42    699   -603       C  
ATOM   1033  CG  ARG A 350      24.926  -0.573   4.782  1.00 49.77           C  
ANISOU 1033  CG  ARG A 350     5570   7426   5915    190    686   -656       C  
ATOM   1034  CD  ARG A 350      24.738  -2.081   4.754  1.00 45.86           C  
ANISOU 1034  CD  ARG A 350     5034   6901   5492    358    746   -697       C  
ATOM   1035  NE  ARG A 350      25.606  -2.789   5.690  1.00 48.50           N  
ANISOU 1035  NE  ARG A 350     5186   7289   5952    522    730   -732       N  
ATOM   1036  CZ  ARG A 350      25.506  -4.089   5.947  1.00 49.65           C  
ANISOU 1036  CZ  ARG A 350     5291   7388   6186    700    761   -751       C  
ATOM   1037  NH1 ARG A 350      24.573  -4.810   5.340  1.00 50.02           N  
ANISOU 1037  NH1 ARG A 350     5467   7333   6206    718    812   -752       N  
ATOM   1038  NH2 ARG A 350      26.331  -4.670   6.808  1.00 48.53           N  
ANISOU 1038  NH2 ARG A 350     4984   7298   6159    855    735   -764       N  
ATOM   1039  N   GLU A 351      25.839   2.137   2.274  1.00 50.27           N  
ANISOU 1039  N   GLU A 351     5766   7603   5732   -402    839   -649       N  
ATOM   1040  CA AGLU A 351      27.172   2.623   1.934  0.50 50.95           C  
ANISOU 1040  CA AGLU A 351     5711   7821   5827   -552    928   -712       C  
ATOM   1041  CA BGLU A 351      27.170   2.626   1.926  0.50 50.96           C  
ANISOU 1041  CA BGLU A 351     5713   7821   5827   -553    929   -712       C  
ATOM   1042  C   GLU A 351      27.316   4.112   2.238  1.00 51.68           C  
ANISOU 1042  C   GLU A 351     5873   7880   5885   -714    848   -648       C  
ATOM   1043  O   GLU A 351      28.347   4.553   2.745  1.00 50.89           O  
ANISOU 1043  O   GLU A 351     5628   7865   5844   -776    842   -692       O  
ATOM   1044  CB AGLU A 351      27.491   2.346   0.463  0.50 52.95           C  
ANISOU 1044  CB AGLU A 351     5971   8155   5993   -688   1100   -766       C  
ATOM   1045  CB BGLU A 351      27.466   2.374   0.446  0.50 52.23           C  
ANISOU 1045  CB BGLU A 351     5886   8060   5897   -692   1099   -763       C  
ATOM   1046  CG AGLU A 351      27.799   0.888   0.149  0.50 57.02           C  
ANISOU 1046  CG AGLU A 351     6367   8731   6567   -549   1217   -876       C  
ATOM   1047  CG BGLU A 351      28.806   2.922  -0.019  0.50 52.64           C  
ANISOU 1047  CG BGLU A 351     5795   8259   5946   -872   1212   -824       C  
ATOM   1048  CD AGLU A 351      29.171   0.457   0.640  0.50 61.83           C  
ANISOU 1048  CD AGLU A 351     6711   9474   7307   -481   1279   -975       C  
ATOM   1049  CD BGLU A 351      29.023   2.758  -1.513  0.50 54.05           C  
ANISOU 1049  CD BGLU A 351     6010   8519   6006  -1026   1388   -867       C  
ATOM   1050  OE1AGLU A 351      29.848   1.262   1.315  0.50 59.06           O  
ANISOU 1050  OE1AGLU A 351     6263   9178   7001   -542   1213   -958       O  
ATOM   1051  OE1BGLU A 351      28.075   2.348  -2.215  0.50 50.39           O  
ANISOU 1051  OE1BGLU A 351     5707   7991   5448  -1011   1404   -841       O  
ATOM   1052  OE2AGLU A 351      29.576  -0.688   0.346  0.50 66.53           O  
ANISOU 1052  OE2AGLU A 351     7194  10120   7966   -365   1392  -1073       O  
ATOM   1053  OE2BGLU A 351      30.143   3.044  -1.986  0.50 55.82           O  
ANISOU 1053  OE2BGLU A 351     6101   8884   6227  -1170   1512   -929       O  
ATOM   1054  N   PHE A 352      26.280   4.885   1.929  1.00 49.87           N  
ANISOU 1054  N   PHE A 352     5862   7522   5565   -782    785   -544       N  
ATOM   1055  CA  PHE A 352      26.315   6.318   2.190  1.00 50.50           C  
ANISOU 1055  CA  PHE A 352     6039   7532   5618   -928    712   -478       C  
ATOM   1056  C   PHE A 352      26.450   6.582   3.685  1.00 51.52           C  
ANISOU 1056  C   PHE A 352     6106   7628   5841   -821    582   -493       C  
ATOM   1057  O   PHE A 352      27.249   7.415   4.110  1.00 51.52           O  
ANISOU 1057  O   PHE A 352     6050   7658   5868   -941    558   -519       O  
ATOM   1058  CB  PHE A 352      25.062   7.000   1.643  1.00 46.53           C  
ANISOU 1058  CB  PHE A 352     5783   6881   5014   -973    657   -354       C  
ATOM   1059  CG  PHE A 352      25.021   8.481   1.892  1.00 46.87           C  
ANISOU 1059  CG  PHE A 352     5953   6817   5041  -1108    585   -281       C  
ATOM   1060  CD1 PHE A 352      25.989   9.313   1.356  1.00 51.12           C  
ANISOU 1060  CD1 PHE A 352     6471   7403   5548  -1339    658   -288       C  
ATOM   1061  CD2 PHE A 352      24.008   9.042   2.651  1.00 48.32           C  
ANISOU 1061  CD2 PHE A 352     6276   6842   5240  -1008    452   -207       C  
ATOM   1062  CE1 PHE A 352      25.953  10.678   1.580  1.00 53.54           C  
ANISOU 1062  CE1 PHE A 352     6910   7587   5847  -1472    595   -222       C  
ATOM   1063  CE2 PHE A 352      23.966  10.406   2.880  1.00 50.99           C  
ANISOU 1063  CE2 PHE A 352     6744   7058   5572  -1124    393   -148       C  
ATOM   1064  CZ  PHE A 352      24.941  11.225   2.343  1.00 52.52           C  
ANISOU 1064  CZ  PHE A 352     6930   7283   5740  -1359    461   -155       C  
ATOM   1065  N   LEU A 353      25.664   5.862   4.477  1.00 53.75           N  
ANISOU 1065  N   LEU A 353     6404   7854   6165   -606    502   -479       N  
ATOM   1066  CA  LEU A 353      25.717   5.990   5.926  1.00 55.03           C  
ANISOU 1066  CA  LEU A 353     6515   7997   6396   -489    380   -493       C  
ATOM   1067  C   LEU A 353      27.078   5.561   6.467  1.00 59.58           C  
ANISOU 1067  C   LEU A 353     6848   8734   7055   -475    400   -589       C  
ATOM   1068  O   LEU A 353      27.619   6.188   7.377  1.00 62.32           O  
ANISOU 1068  O   LEU A 353     7137   9108   7433   -510    317   -615       O  
ATOM   1069  CB  LEU A 353      24.596   5.174   6.576  1.00 49.16           C  
ANISOU 1069  CB  LEU A 353     5830   7176   5671   -265    311   -452       C  
ATOM   1070  CG  LEU A 353      23.194   5.779   6.468  1.00 44.55           C  
ANISOU 1070  CG  LEU A 353     5466   6436   5026   -251    248   -353       C  
ATOM   1071  CD1 LEU A 353      22.122   4.714   6.632  1.00 41.22           C  
ANISOU 1071  CD1 LEU A 353     5077   5972   4613    -66    231   -319       C  
ATOM   1072  CD2 LEU A 353      23.011   6.894   7.489  1.00 44.18           C  
ANISOU 1072  CD2 LEU A 353     5498   6304   4986   -261    138   -333       C  
ATOM   1073  N   LYS A 354      27.634   4.498   5.895  1.00 59.23           N  
ANISOU 1073  N   LYS A 354     6659   8798   7046   -424    508   -646       N  
ATOM   1074  CA  LYS A 354      28.922   3.977   6.339  1.00 61.40           C  
ANISOU 1074  CA  LYS A 354     6681   9237   7413   -383    533   -732       C  
ATOM   1075  C   LYS A 354      30.070   4.919   5.980  1.00 61.58           C  
ANISOU 1075  C   LYS A 354     6601   9368   7430   -615    583   -779       C  
ATOM   1076  O   LYS A 354      31.135   4.881   6.598  1.00 61.63           O  
ANISOU 1076  O   LYS A 354     6397   9510   7508   -615    558   -841       O  
ATOM   1077  CB  LYS A 354      29.165   2.581   5.754  1.00 63.17           C  
ANISOU 1077  CB  LYS A 354     6787   9528   7686   -254    652   -785       C  
ATOM   1078  CG  LYS A 354      30.471   1.936   6.192  1.00 67.98           C  
ANISOU 1078  CG  LYS A 354     7118  10304   8408   -174    681   -868       C  
ATOM   1079  CD  LYS A 354      30.434   0.424   6.015  1.00 72.56           C  
ANISOU 1079  CD  LYS A 354     7617  10891   9061     36    757   -904       C  
ATOM   1080  CE  LYS A 354      30.388   0.025   4.549  1.00 77.93           C  
ANISOU 1080  CE  LYS A 354     8340  11576   9693    -46    937   -955       C  
ATOM   1081  NZ  LYS A 354      31.703   0.203   3.868  1.00 83.34           N  
ANISOU 1081  NZ  LYS A 354     8830  12433  10402   -177   1072  -1046       N  
ATOM   1082  N   SER A 355      29.844   5.776   4.990  1.00 61.20           N  
ANISOU 1082  N   SER A 355     6698   9263   7292   -817    648   -742       N  
ATOM   1083  CA  SER A 355      30.892   6.666   4.500  1.00 65.01           C  
ANISOU 1083  CA  SER A 355     7101   9840   7760  -1066    718   -777       C  
ATOM   1084  C   SER A 355      31.002   7.950   5.316  1.00 65.64           C  
ANISOU 1084  C   SER A 355     7247   9853   7839  -1192    596   -756       C  
ATOM   1085  O   SER A 355      31.934   8.730   5.126  1.00 65.52           O  
ANISOU 1085  O   SER A 355     7153   9915   7828  -1407    634   -790       O  
ATOM   1086  CB  SER A 355      30.660   7.008   3.027  1.00 67.36           C  
ANISOU 1086  CB  SER A 355     7533  10109   7950  -1243    852   -738       C  
ATOM   1087  OG  SER A 355      29.558   7.887   2.875  1.00 67.60           O  
ANISOU 1087  OG  SER A 355     7833   9954   7899  -1301    778   -628       O  
ATOM   1088  N   LEU A 356      30.051   8.169   6.219  1.00 62.02           N  
ANISOU 1088  N   LEU A 356     6936   9252   7376  -1067    458   -706       N  
ATOM   1089  CA  LEU A 356      30.046   9.380   7.034  1.00 62.94           C  
ANISOU 1089  CA  LEU A 356     7144   9281   7488  -1173    343   -699       C  
ATOM   1090  C   LEU A 356      31.266   9.437   7.948  1.00 63.99           C  
ANISOU 1090  C   LEU A 356     7046   9575   7691  -1212    287   -793       C  
ATOM   1091  O   LEU A 356      31.708   8.414   8.470  1.00 66.57           O  
ANISOU 1091  O   LEU A 356     7175  10039   8080  -1045    269   -839       O  
ATOM   1092  CB  LEU A 356      28.759   9.473   7.856  1.00 61.74           C  
ANISOU 1092  CB  LEU A 356     7181   8961   7318  -1002    220   -640       C  
ATOM   1093  CG  LEU A 356      27.471   9.634   7.046  1.00 61.85           C  
ANISOU 1093  CG  LEU A 356     7429   8808   7263   -977    247   -537       C  
ATOM   1094  CD1 LEU A 356      26.248   9.595   7.954  1.00 60.02           C  
ANISOU 1094  CD1 LEU A 356     7336   8441   7029   -785    133   -491       C  
ATOM   1095  CD2 LEU A 356      27.504  10.919   6.228  1.00 63.69           C  
ANISOU 1095  CD2 LEU A 356     7819   8940   7441  -1218    287   -485       C  
ATOM   1096  N   ARG A 357      31.805  10.638   8.140  1.00 63.27           N  
ANISOU 1096  N   ARG A 357     6982   9466   7593  -1435    255   -818       N  
ATOM   1097  CA  ARG A 357      33.007  10.818   8.949  1.00 67.83           C  
ANISOU 1097  CA  ARG A 357     7335  10209   8227  -1516    195   -912       C  
ATOM   1098  C   ARG A 357      32.815  10.299  10.372  1.00 70.22           C  
ANISOU 1098  C   ARG A 357     7576  10547   8558  -1298     42   -940       C  
ATOM   1099  O   ARG A 357      31.747  10.460  10.966  1.00 67.65           O  
ANISOU 1099  O   ARG A 357     7448  10063   8194  -1178    -44   -896       O  
ATOM   1100  CB  ARG A 357      33.445  12.288   8.947  1.00 69.52           C  
ANISOU 1100  CB  ARG A 357     7636  10356   8421  -1810    176   -932       C  
ATOM   1101  CG  ARG A 357      32.646  13.210   9.855  1.00 69.31           C  
ANISOU 1101  CG  ARG A 357     7844  10130   8363  -1806     42   -919       C  
ATOM   1102  CD  ARG A 357      33.466  13.621  11.070  1.00 73.46           C  
ANISOU 1102  CD  ARG A 357     8236  10758   8918  -1879    -83  -1023       C  
ATOM   1103  NE  ARG A 357      32.968  14.849  11.684  1.00 74.38           N  
ANISOU 1103  NE  ARG A 357     8589  10673   9001  -1985   -172  -1036       N  
ATOM   1104  CZ  ARG A 357      32.529  14.937  12.935  1.00 75.40           C  
ANISOU 1104  CZ  ARG A 357     8783  10756   9110  -1859   -309  -1078       C  
ATOM   1105  NH1 ARG A 357      32.534  13.866  13.717  1.00 76.03           N  
ANISOU 1105  NH1 ARG A 357     8710  10984   9196  -1628   -380  -1095       N  
ATOM   1106  NH2 ARG A 357      32.096  16.098  13.409  1.00 72.94           N  
ANISOU 1106  NH2 ARG A 357     8696  10249   8770  -1965   -370  -1103       N  
ATOM   1107  N   LYS A 358      33.856   9.668  10.907  1.00 73.06           N  
ANISOU 1107  N   LYS A 358     7655  11124   8981  -1245     10  -1007       N  
ATOM   1108  CA  LYS A 358      33.791   9.050  12.227  1.00 73.81           C  
ANISOU 1108  CA  LYS A 358     7666  11283   9094  -1033   -134  -1022       C  
ATOM   1109  C   LYS A 358      33.440  10.064  13.310  1.00 74.28           C  
ANISOU 1109  C   LYS A 358     7879  11245   9098  -1101   -281  -1044       C  
ATOM   1110  O   LYS A 358      33.845  11.225  13.233  1.00 75.34           O  
ANISOU 1110  O   LYS A 358     8066  11345   9215  -1349   -289  -1089       O  
ATOM   1111  CB  LYS A 358      35.116   8.361  12.562  1.00 74.64           C  
ANISOU 1111  CB  LYS A 358     7426  11653   9279   -996   -151  -1086       C  
ATOM   1112  N   PRO A 359      32.686   9.623  14.328  1.00 73.72           N  
ANISOU 1112  N   PRO A 359     7887  11127   8997   -886   -391  -1017       N  
ATOM   1113  CA  PRO A 359      32.202   8.249  14.460  1.00 70.50           C  
ANISOU 1113  CA  PRO A 359     7427  10747   8614   -605   -381   -958       C  
ATOM   1114  C   PRO A 359      30.776   8.073  13.939  1.00 64.00           C  
ANISOU 1114  C   PRO A 359     6851   9712   7753   -498   -321   -873       C  
ATOM   1115  O   PRO A 359      30.145   7.054  14.218  1.00 62.83           O  
ANISOU 1115  O   PRO A 359     6712   9548   7612   -272   -330   -820       O  
ATOM   1116  CB  PRO A 359      32.221   8.057  15.969  1.00 71.55           C  
ANISOU 1116  CB  PRO A 359     7517  10952   8715   -474   -547   -974       C  
ATOM   1117  CG  PRO A 359      31.747   9.396  16.476  1.00 73.76           C  
ANISOU 1117  CG  PRO A 359     8014  11092   8919   -625   -617  -1010       C  
ATOM   1118  CD  PRO A 359      32.278  10.438  15.487  1.00 75.16           C  
ANISOU 1118  CD  PRO A 359     8216  11227   9115   -910   -529  -1050       C  
ATOM   1119  N   PHE A 360      30.277   9.052  13.192  1.00 59.98           N  
ANISOU 1119  N   PHE A 360     6538   9047   7207   -660   -263   -854       N  
ATOM   1120  CA  PHE A 360      28.907   8.998  12.689  1.00 57.03           C  
ANISOU 1120  CA  PHE A 360     6392   8482   6795   -570   -220   -769       C  
ATOM   1121  C   PHE A 360      28.686   7.857  11.697  1.00 55.58           C  
ANISOU 1121  C   PHE A 360     6153   8327   6638   -462   -105   -723       C  
ATOM   1122  O   PHE A 360      27.578   7.332  11.581  1.00 56.10           O  
ANISOU 1122  O   PHE A 360     6344   8288   6685   -314    -96   -657       O  
ATOM   1123  CB  PHE A 360      28.509  10.339  12.068  1.00 54.12           C  
ANISOU 1123  CB  PHE A 360     6235   7944   6386   -769   -190   -747       C  
ATOM   1124  CG  PHE A 360      28.466  11.468  13.057  1.00 57.33           C  
ANISOU 1124  CG  PHE A 360     6752   8267   6765   -854   -298   -795       C  
ATOM   1125  CD1 PHE A 360      27.410  11.585  13.946  1.00 56.85           C  
ANISOU 1125  CD1 PHE A 360     6847   8085   6668   -700   -379   -774       C  
ATOM   1126  CD2 PHE A 360      29.483  12.407  13.105  1.00 58.92           C  
ANISOU 1126  CD2 PHE A 360     6899   8511   6975  -1093   -311   -869       C  
ATOM   1127  CE1 PHE A 360      27.367  12.618  14.861  1.00 55.80           C  
ANISOU 1127  CE1 PHE A 360     6825   7871   6504   -775   -467   -836       C  
ATOM   1128  CE2 PHE A 360      29.444  13.443  14.016  1.00 59.77           C  
ANISOU 1128  CE2 PHE A 360     7121   8531   7057  -1180   -407   -929       C  
ATOM   1129  CZ  PHE A 360      28.385  13.548  14.896  1.00 58.42           C  
ANISOU 1129  CZ  PHE A 360     7116   8235   6846  -1016   -484   -917       C  
ATOM   1130  N   GLY A 361      29.744   7.470  10.992  1.00 54.08           N  
ANISOU 1130  N   GLY A 361     5772   8283   6493   -542    -14   -767       N  
ATOM   1131  CA  GLY A 361      29.662   6.387  10.029  1.00 56.04           C  
ANISOU 1131  CA  GLY A 361     5960   8565   6766   -453    109   -750       C  
ATOM   1132  C   GLY A 361      29.630   5.009  10.668  1.00 59.91           C  
ANISOU 1132  C   GLY A 361     6325   9123   7315   -197     79   -748       C  
ATOM   1133  O   GLY A 361      29.442   4.006   9.981  1.00 61.52           O  
ANISOU 1133  O   GLY A 361     6499   9329   7546    -96    175   -739       O  
ATOM   1134  N   ASP A 362      29.807   4.961  11.986  1.00 59.86           N  
ANISOU 1134  N   ASP A 362     6255   9165   7322    -97    -54   -755       N  
ATOM   1135  CA  ASP A 362      29.846   3.693  12.712  1.00 61.38           C  
ANISOU 1135  CA  ASP A 362     6329   9423   7570    145    -97   -737       C  
ATOM   1136  C   ASP A 362      28.512   3.343  13.369  1.00 55.12           C  
ANISOU 1136  C   ASP A 362     5720   8490   6734    312   -162   -660       C  
ATOM   1137  O   ASP A 362      28.326   2.231  13.864  1.00 56.54           O  
ANISOU 1137  O   ASP A 362     5845   8684   6951    514   -182   -623       O  
ATOM   1138  CB  ASP A 362      30.950   3.719  13.775  1.00 65.89           C  
ANISOU 1138  CB  ASP A 362     6690  10170   8175    164   -208   -782       C  
ATOM   1139  CG  ASP A 362      32.340   3.745  13.172  1.00 71.61           C  
ANISOU 1139  CG  ASP A 362     7171  11070   8969     44   -136   -856       C  
ATOM   1140  OD1 ASP A 362      32.457   3.579  11.940  1.00 74.55           O  
ANISOU 1140  OD1 ASP A 362     7533  11429   9361    -29     15   -874       O  
ATOM   1141  OD2 ASP A 362      33.315   3.930  13.931  1.00 74.96           O  
ANISOU 1141  OD2 ASP A 362     7406  11655   9419     17   -229   -899       O  
ATOM   1142  N   PHE A 363      27.586   4.294  13.370  1.00 47.98           N  
ANISOU 1142  N   PHE A 363     5030   7444   5755    229   -189   -632       N  
ATOM   1143  CA  PHE A 363      26.318   4.115  14.068  1.00 48.83           C  
ANISOU 1143  CA  PHE A 363     5301   7431   5819    372   -250   -565       C  
ATOM   1144  C   PHE A 363      25.420   3.027  13.475  1.00 50.37           C  
ANISOU 1144  C   PHE A 363     5556   7549   6035    509   -173   -503       C  
ATOM   1145  O   PHE A 363      24.943   2.153  14.196  1.00 48.80           O  
ANISOU 1145  O   PHE A 363     5356   7339   5848    688   -211   -458       O  
ATOM   1146  CB  PHE A 363      25.555   5.443  14.149  1.00 52.18           C  
ANISOU 1146  CB  PHE A 363     5933   7721   6173    257   -287   -556       C  
ATOM   1147  CG  PHE A 363      25.939   6.293  15.328  1.00 58.00           C  
ANISOU 1147  CG  PHE A 363     6672   8493   6871    208   -403   -606       C  
ATOM   1148  CD1 PHE A 363      25.411   6.036  16.583  1.00 60.57           C  
ANISOU 1148  CD1 PHE A 363     7039   8818   7157    358   -497   -587       C  
ATOM   1149  CD2 PHE A 363      26.825   7.348  15.185  1.00 62.36           C  
ANISOU 1149  CD2 PHE A 363     7191   9083   7420     -1   -416   -676       C  
ATOM   1150  CE1 PHE A 363      25.762   6.811  17.672  1.00 61.94           C  
ANISOU 1150  CE1 PHE A 363     7223   9033   7278    306   -604   -646       C  
ATOM   1151  CE2 PHE A 363      27.179   8.128  16.271  1.00 62.62           C  
ANISOU 1151  CE2 PHE A 363     7232   9146   7412    -62   -526   -738       C  
ATOM   1152  CZ  PHE A 363      26.646   7.859  17.515  1.00 61.94           C  
ANISOU 1152  CZ  PHE A 363     7191   9064   7277     94   -622   -728       C  
ATOM   1153  N   MET A 364      25.192   3.079  12.167  1.00 53.34           N  
ANISOU 1153  N   MET A 364     5988   7871   6407    414    -65   -501       N  
ATOM   1154  CA  MET A 364      24.156   2.252  11.551  1.00 48.95           C  
ANISOU 1154  CA  MET A 364     5527   7223   5850    507     -2   -449       C  
ATOM   1155  C   MET A 364      24.605   0.854  11.123  1.00 47.68           C  
ANISOU 1155  C   MET A 364     5234   7120   5762    613     82   -472       C  
ATOM   1156  O   MET A 364      23.790  -0.065  11.056  1.00 47.33           O  
ANISOU 1156  O   MET A 364     5248   7004   5731    734    106   -431       O  
ATOM   1157  CB  MET A 364      23.518   2.985  10.368  1.00 48.49           C  
ANISOU 1157  CB  MET A 364     5619   7073   5732    359     58   -425       C  
ATOM   1158  CG  MET A 364      22.794   4.267  10.758  1.00 51.57           C  
ANISOU 1158  CG  MET A 364     6172   7358   6062    294    -20   -385       C  
ATOM   1159  SD  MET A 364      21.493   4.001  11.981  1.00 54.68           S  
ANISOU 1159  SD  MET A 364     6668   7665   6442    487   -112   -321       S  
ATOM   1160  CE  MET A 364      20.360   2.985  11.041  1.00 43.06           C  
ANISOU 1160  CE  MET A 364     5263   6129   4970    560    -40   -259       C  
ATOM   1161  N   GLU A 365      25.893   0.690  10.840  1.00 43.77           N  
ANISOU 1161  N   GLU A 365     4559   6751   5319    568    131   -542       N  
ATOM   1162  CA  GLU A 365      26.389  -0.580  10.312  1.00 47.84           C  
ANISOU 1162  CA  GLU A 365     4948   7313   5914    667    232   -579       C  
ATOM   1163  C   GLU A 365      25.988  -1.807  11.148  1.00 48.30           C  
ANISOU 1163  C   GLU A 365     4989   7331   6033    898    191   -531       C  
ATOM   1164  O   GLU A 365      25.498  -2.795  10.602  1.00 51.21           O  
ANISOU 1164  O   GLU A 365     5399   7625   6432    977    270   -526       O  
ATOM   1165  CB  GLU A 365      27.906  -0.532  10.098  1.00 52.86           C  
ANISOU 1165  CB  GLU A 365     5361   8111   6611    608    280   -661       C  
ATOM   1166  CG  GLU A 365      28.477  -1.762   9.404  1.00 54.52           C  
ANISOU 1166  CG  GLU A 365     5439   8366   6910    705    410   -717       C  
ATOM   1167  CD  GLU A 365      27.969  -1.933   7.983  1.00 59.56           C  
ANISOU 1167  CD  GLU A 365     6193   8937   7500    607    552   -748       C  
ATOM   1168  OE1 GLU A 365      28.394  -2.897   7.314  1.00 64.26           O  
ANISOU 1168  OE1 GLU A 365     6700   9558   8156    671    676   -812       O  
ATOM   1169  OE2 GLU A 365      27.148  -1.105   7.531  1.00 56.74           O  
ANISOU 1169  OE2 GLU A 365     6015   8502   7041    471    539   -709       O  
ATOM   1170  N   PRO A 366      26.199  -1.753  12.472  1.00 48.59           N  
ANISOU 1170  N   PRO A 366     4971   7413   6078    997     66   -494       N  
ATOM   1171  CA  PRO A 366      25.797  -2.883  13.320  1.00 51.87           C  
ANISOU 1171  CA  PRO A 366     5384   7785   6538   1210     23   -427       C  
ATOM   1172  C   PRO A 366      24.289  -3.160  13.270  1.00 50.05           C  
ANISOU 1172  C   PRO A 366     5355   7400   6261   1249     31   -358       C  
ATOM   1173  O   PRO A 366      23.878  -4.316  13.393  1.00 45.95           O  
ANISOU 1173  O   PRO A 366     4850   6813   5794   1390     60   -317       O  
ATOM   1174  CB  PRO A 366      26.216  -2.425  14.726  1.00 56.41           C  
ANISOU 1174  CB  PRO A 366     5897   8452   7086   1257   -126   -398       C  
ATOM   1175  CG  PRO A 366      26.368  -0.925  14.605  1.00 54.81           C  
ANISOU 1175  CG  PRO A 366     5740   8282   6805   1054   -162   -445       C  
ATOM   1176  CD  PRO A 366      26.945  -0.750  13.247  1.00 49.67           C  
ANISOU 1176  CD  PRO A 366     5029   7656   6185    916    -37   -517       C  
ATOM   1177  N   LYS A 367      23.480  -2.119  13.094  1.00 46.55           N  
ANISOU 1177  N   LYS A 367     5059   6899   5729   1128      6   -343       N  
ATOM   1178  CA  LYS A 367      22.036  -2.297  12.971  1.00 43.77           C  
ANISOU 1178  CA  LYS A 367     4877   6419   5336   1154     15   -280       C  
ATOM   1179  C   LYS A 367      21.688  -3.049  11.688  1.00 43.15           C  
ANISOU 1179  C   LYS A 367     4832   6279   5284   1125    134   -303       C  
ATOM   1180  O   LYS A 367      20.777  -3.876  11.673  1.00 44.83           O  
ANISOU 1180  O   LYS A 367     5120   6404   5510   1204    156   -259       O  
ATOM   1181  CB  LYS A 367      21.305  -0.952  13.006  1.00 38.45           C  
ANISOU 1181  CB  LYS A 367     4340   5699   4572   1039    -37   -260       C  
ATOM   1182  CG  LYS A 367      21.199  -0.327  14.388  1.00 38.04           C  
ANISOU 1182  CG  LYS A 367     4309   5667   4475   1089   -152   -234       C  
ATOM   1183  CD  LYS A 367      22.529   0.247  14.843  1.00 47.70           C  
ANISOU 1183  CD  LYS A 367     5406   7012   5705   1031   -204   -296       C  
ATOM   1184  CE  LYS A 367      22.398   0.944  16.187  1.00 48.52           C  
ANISOU 1184  CE  LYS A 367     5551   7139   5745   1058   -321   -286       C  
ATOM   1185  NZ  LYS A 367      23.689   1.546  16.629  1.00 49.64           N  
ANISOU 1185  NZ  LYS A 367     5567   7409   5887    979   -384   -355       N  
ATOM   1186  N   PHE A 368      22.415  -2.754  10.615  1.00 39.60           N  
ANISOU 1186  N   PHE A 368     4330   5881   4835   1000    215   -378       N  
ATOM   1187  CA  PHE A 368      22.222  -3.453   9.348  1.00 40.77           C  
ANISOU 1187  CA  PHE A 368     4507   5992   4993    959    337   -421       C  
ATOM   1188  C   PHE A 368      22.592  -4.924   9.479  1.00 45.23           C  
ANISOU 1188  C   PHE A 368     4982   6541   5662   1115    396   -446       C  
ATOM   1189  O   PHE A 368      21.886  -5.799   8.974  1.00 47.25           O  
ANISOU 1189  O   PHE A 368     5314   6707   5932   1148    458   -447       O  
ATOM   1190  CB  PHE A 368      23.049  -2.807   8.235  1.00 42.27           C  
ANISOU 1190  CB  PHE A 368     4650   6261   5151    788    420   -498       C  
ATOM   1191  CG  PHE A 368      22.415  -1.585   7.639  1.00 39.25           C  
ANISOU 1191  CG  PHE A 368     4406   5846   4660    619    398   -464       C  
ATOM   1192  CD1 PHE A 368      21.282  -1.695   6.848  1.00 39.24           C  
ANISOU 1192  CD1 PHE A 368     4551   5764   4595    573    422   -429       C  
ATOM   1193  CD2 PHE A 368      22.951  -0.327   7.862  1.00 41.26           C  
ANISOU 1193  CD2 PHE A 368     4648   6148   4879    504    348   -463       C  
ATOM   1194  CE1 PHE A 368      20.694  -0.573   6.293  1.00 40.01           C  
ANISOU 1194  CE1 PHE A 368     4774   5830   4597    434    393   -382       C  
ATOM   1195  CE2 PHE A 368      22.368   0.800   7.309  1.00 39.09           C  
ANISOU 1195  CE2 PHE A 368     4515   5823   4516    359    329   -421       C  
ATOM   1196  CZ  PHE A 368      21.237   0.676   6.525  1.00 39.50           C  
ANISOU 1196  CZ  PHE A 368     4707   5796   4507    333    349   -373       C  
ATOM   1197  N   GLU A 369      23.703  -5.191  10.160  1.00 47.39           N  
ANISOU 1197  N   GLU A 369     5093   6899   6013   1211    373   -466       N  
ATOM   1198  CA  GLU A 369      24.164  -6.560  10.360  1.00 48.45           C  
ANISOU 1198  CA  GLU A 369     5133   7013   6264   1384    423   -480       C  
ATOM   1199  C   GLU A 369      23.114  -7.361  11.116  1.00 44.19           C  
ANISOU 1199  C   GLU A 369     4701   6349   5740   1517    374   -386       C  
ATOM   1200  O   GLU A 369      22.807  -8.495  10.758  1.00 45.19           O  
ANISOU 1200  O   GLU A 369     4862   6377   5931   1594    451   -396       O  
ATOM   1201  CB  GLU A 369      25.495  -6.580  11.116  1.00 52.08           C  
ANISOU 1201  CB  GLU A 369     5389   7601   6798   1475    375   -493       C  
ATOM   1202  CG  GLU A 369      26.639  -5.911  10.375  1.00 58.24           C  
ANISOU 1202  CG  GLU A 369     6030   8517   7580   1344    439   -591       C  
ATOM   1203  CD  GLU A 369      27.958  -6.012  11.120  1.00 69.40           C  
ANISOU 1203  CD  GLU A 369     7215  10075   9078   1439    386   -605       C  
ATOM   1204  OE1 GLU A 369      27.932  -6.167  12.359  1.00 71.41           O  
ANISOU 1204  OE1 GLU A 369     7444  10342   9346   1566    257   -525       O  
ATOM   1205  OE2 GLU A 369      29.020  -5.937  10.465  1.00 74.31           O  
ANISOU 1205  OE2 GLU A 369     7678  10809   9749   1385    473   -695       O  
ATOM   1206  N   PHE A 370      22.558  -6.760  12.162  1.00 43.71           N  
ANISOU 1206  N   PHE A 370     4699   6291   5617   1535    252   -299       N  
ATOM   1207  CA  PHE A 370      21.505  -7.407  12.935  1.00 43.90           C  
ANISOU 1207  CA  PHE A 370     4827   6213   5640   1642    208   -201       C  
ATOM   1208  C   PHE A 370      20.243  -7.607  12.099  1.00 40.92           C  
ANISOU 1208  C   PHE A 370     4601   5723   5225   1561    270   -198       C  
ATOM   1209  O   PHE A 370      19.632  -8.676  12.118  1.00 41.55           O  
ANISOU 1209  O   PHE A 370     4736   5698   5353   1636    310   -166       O  
ATOM   1210  CB  PHE A 370      21.177  -6.583  14.179  1.00 42.24           C  
ANISOU 1210  CB  PHE A 370     4650   6048   5352   1660     78   -125       C  
ATOM   1211  CG  PHE A 370      19.860  -6.935  14.809  1.00 45.16           C  
ANISOU 1211  CG  PHE A 370     5151   6322   5685   1718     48    -29       C  
ATOM   1212  CD1 PHE A 370      19.762  -7.995  15.694  1.00 48.48           C  
ANISOU 1212  CD1 PHE A 370     5564   6701   6155   1875     27     53       C  
ATOM   1213  CD2 PHE A 370      18.720  -6.205  14.518  1.00 47.65           C  
ANISOU 1213  CD2 PHE A 370     5593   6593   5921   1617     43    -13       C  
ATOM   1214  CE1 PHE A 370      18.551  -8.319  16.279  1.00 48.92           C  
ANISOU 1214  CE1 PHE A 370     5736   6679   6175   1913     10    144       C  
ATOM   1215  CE2 PHE A 370      17.506  -6.524  15.099  1.00 47.45           C  
ANISOU 1215  CE2 PHE A 370     5668   6496   5867   1667     23     72       C  
ATOM   1216  CZ  PHE A 370      17.422  -7.584  15.979  1.00 47.84           C  
ANISOU 1216  CZ  PHE A 370     5707   6510   5959   1807     12    148       C  
ATOM   1217  N   ALA A 371      19.859  -6.569  11.367  1.00 35.63           N  
ANISOU 1217  N   ALA A 371     3996   5073   4468   1403    274   -227       N  
ATOM   1218  CA  ALA A 371      18.632  -6.601  10.581  1.00 38.12           C  
ANISOU 1218  CA  ALA A 371     4446   5307   4732   1316    309   -215       C  
ATOM   1219  C   ALA A 371      18.654  -7.703   9.520  1.00 41.09           C  
ANISOU 1219  C   ALA A 371     4830   5624   5157   1302    428   -285       C  
ATOM   1220  O   ALA A 371      17.673  -8.424   9.347  1.00 45.08           O  
ANISOU 1220  O   ALA A 371     5422   6037   5669   1310    450   -260       O  
ATOM   1221  CB  ALA A 371      18.380  -5.246   9.945  1.00 37.22           C  
ANISOU 1221  CB  ALA A 371     4390   5233   4519   1157    286   -226       C  
ATOM   1222  N   VAL A 372      19.772  -7.835   8.816  1.00 44.19           N  
ANISOU 1222  N   VAL A 372     5131   6075   5586   1273    509   -382       N  
ATOM   1223  CA  VAL A 372      19.907  -8.879   7.804  1.00 49.16           C  
ANISOU 1223  CA  VAL A 372     5766   6650   6261   1264    637   -473       C  
ATOM   1224  C   VAL A 372      19.653 -10.261   8.404  1.00 46.21           C  
ANISOU 1224  C   VAL A 372     5403   6159   5997   1424    655   -443       C  
ATOM   1225  O   VAL A 372      18.993 -11.104   7.797  1.00 47.33           O  
ANISOU 1225  O   VAL A 372     5631   6199   6153   1401    724   -476       O  
ATOM   1226  CB  VAL A 372      21.293  -8.847   7.132  1.00 54.24           C  
ANISOU 1226  CB  VAL A 372     6281   7388   6942   1239    732   -586       C  
ATOM   1227  CG1 VAL A 372      21.542 -10.135   6.365  1.00 57.35           C  
ANISOU 1227  CG1 VAL A 372     6668   7710   7413   1287    870   -687       C  
ATOM   1228  CG2 VAL A 372      21.404  -7.644   6.210  1.00 52.67           C  
ANISOU 1228  CG2 VAL A 372     6108   7281   6624   1043    748   -622       C  
ATOM   1229  N   LYS A 373      20.171 -10.480   9.608  1.00 45.52           N  
ANISOU 1229  N   LYS A 373     5232   6083   5980   1579    589   -376       N  
ATOM   1230  CA  LYS A 373      19.972 -11.743  10.309  1.00 50.25           C  
ANISOU 1230  CA  LYS A 373     5846   6565   6682   1741    595   -319       C  
ATOM   1231  C   LYS A 373      18.552 -11.862  10.867  1.00 47.18           C  
ANISOU 1231  C   LYS A 373     5591   6089   6245   1729    536   -213       C  
ATOM   1232  O   LYS A 373      17.899 -12.896  10.714  1.00 49.30           O  
ANISOU 1232  O   LYS A 373     5940   6228   6566   1754    589   -203       O  
ATOM   1233  CB  LYS A 373      21.003 -11.895  11.430  1.00 55.23           C  
ANISOU 1233  CB  LYS A 373     6342   7256   7389   1909    530   -265       C  
ATOM   1234  CG  LYS A 373      22.445 -11.865  10.939  1.00 66.02           C  
ANISOU 1234  CG  LYS A 373     7544   8720   8821   1936    592   -367       C  
ATOM   1235  CD  LYS A 373      23.432 -12.043  12.081  1.00 72.93           C  
ANISOU 1235  CD  LYS A 373     8270   9670   9772   2109    508   -303       C  
ATOM   1236  CE  LYS A 373      24.867 -11.880  11.602  1.00 79.87           C  
ANISOU 1236  CE  LYS A 373     8956  10677  10716   2123    563   -406       C  
ATOM   1237  NZ  LYS A 373      25.853 -12.117  12.694  1.00 84.84           N  
ANISOU 1237  NZ  LYS A 373     9419  11392  11424   2299    471   -340       N  
ATOM   1238  N   PHE A 374      18.076 -10.801  11.508  1.00 40.63           N  
ANISOU 1238  N   PHE A 374     4784   5332   5322   1687    433   -140       N  
ATOM   1239  CA  PHE A 374      16.735 -10.802  12.083  1.00 41.93           C  
ANISOU 1239  CA  PHE A 374     5057   5439   5438   1679    381    -40       C  
ATOM   1240  C   PHE A 374      15.687 -10.984  10.988  1.00 41.10           C  
ANISOU 1240  C   PHE A 374     5052   5268   5296   1545    439    -80       C  
ATOM   1241  O   PHE A 374      14.719 -11.725  11.156  1.00 39.59           O  
ANISOU 1241  O   PHE A 374     4934   4982   5124   1552    453    -30       O  
ATOM   1242  CB  PHE A 374      16.484  -9.508  12.865  1.00 41.20           C  
ANISOU 1242  CB  PHE A 374     4966   5440   5248   1656    274     20       C  
ATOM   1243  CG  PHE A 374      15.235  -9.534  13.705  1.00 40.69           C  
ANISOU 1243  CG  PHE A 374     4985   5335   5141   1683    225    127       C  
ATOM   1244  CD1 PHE A 374      15.226 -10.172  14.936  1.00 38.16           C  
ANISOU 1244  CD1 PHE A 374     4658   4991   4849   1819    189    221       C  
ATOM   1245  CD2 PHE A 374      14.075  -8.914  13.268  1.00 36.44           C  
ANISOU 1245  CD2 PHE A 374     4526   4790   4531   1576    215    140       C  
ATOM   1246  CE1 PHE A 374      14.085 -10.197  15.714  1.00 37.66           C  
ANISOU 1246  CE1 PHE A 374     4667   4902   4739   1836    159    318       C  
ATOM   1247  CE2 PHE A 374      12.927  -8.937  14.038  1.00 34.02           C  
ANISOU 1247  CE2 PHE A 374     4276   4458   4190   1605    181    233       C  
ATOM   1248  CZ  PHE A 374      12.931  -9.579  15.263  1.00 36.20           C  
ANISOU 1248  CZ  PHE A 374     4547   4716   4492   1729    160    319       C  
ATOM   1249  N   ASN A 375      15.894 -10.312   9.861  1.00 44.02           N  
ANISOU 1249  N   ASN A 375     5422   5696   5607   1412    472   -167       N  
ATOM   1250  CA  ASN A 375      14.958 -10.380   8.744  1.00 43.70           C  
ANISOU 1250  CA  ASN A 375     5472   5622   5510   1271    512   -206       C  
ATOM   1251  C   ASN A 375      14.858 -11.776   8.137  1.00 45.33           C  
ANISOU 1251  C   ASN A 375     5716   5717   5790   1275    614   -275       C  
ATOM   1252  O   ASN A 375      13.854 -12.113   7.511  1.00 44.30           O  
ANISOU 1252  O   ASN A 375     5670   5538   5624   1175    632   -287       O  
ATOM   1253  CB  ASN A 375      15.320  -9.351   7.668  1.00 39.64           C  
ANISOU 1253  CB  ASN A 375     4955   5202   4904   1129    525   -275       C  
ATOM   1254  CG  ASN A 375      14.946  -7.933   8.071  1.00 41.60           C  
ANISOU 1254  CG  ASN A 375     5218   5520   5067   1087    423   -200       C  
ATOM   1255  OD1 ASN A 375      14.191  -7.728   9.020  1.00 36.79           O  
ANISOU 1255  OD1 ASN A 375     4633   4891   4453   1149    350   -107       O  
ATOM   1256  ND2 ASN A 375      15.470  -6.950   7.348  1.00 35.85           N  
ANISOU 1256  ND2 ASN A 375     4481   4869   4272    980    427   -241       N  
ATOM   1257  N   ALA A 376      15.897 -12.585   8.329  1.00 48.49           N  
ANISOU 1257  N   ALA A 376     6052   6076   6298   1391    677   -323       N  
ATOM   1258  CA  ALA A 376      15.904 -13.957   7.828  1.00 53.19           C  
ANISOU 1258  CA  ALA A 376     6689   6539   6984   1416    784   -397       C  
ATOM   1259  C   ALA A 376      14.838 -14.808   8.519  1.00 51.98           C  
ANISOU 1259  C   ALA A 376     6619   6255   6877   1456    761   -303       C  
ATOM   1260  O   ALA A 376      14.414 -15.836   7.991  1.00 52.19           O  
ANISOU 1260  O   ALA A 376     6721   6157   6954   1419    839   -359       O  
ATOM   1261  CB  ALA A 376      17.286 -14.583   7.994  1.00 55.76           C  
ANISOU 1261  CB  ALA A 376     6913   6845   7430   1563    852   -455       C  
ATOM   1262  N   LEU A 377      14.408 -14.373   9.700  1.00 48.68           N  
ANISOU 1262  N   LEU A 377     6190   5867   6438   1522    662   -166       N  
ATOM   1263  CA  LEU A 377      13.354 -15.064  10.435  1.00 46.53           C  
ANISOU 1263  CA  LEU A 377     5991   5494   6196   1549    642    -61       C  
ATOM   1264  C   LEU A 377      11.996 -14.876   9.761  1.00 45.98           C  
ANISOU 1264  C   LEU A 377     6000   5425   6046   1380    635    -67       C  
ATOM   1265  O   LEU A 377      11.047 -15.607  10.040  1.00 47.35           O  
ANISOU 1265  O   LEU A 377     6236   5505   6249   1357    645    -12       O  
ATOM   1266  CB  LEU A 377      13.299 -14.567  11.881  1.00 45.12           C  
ANISOU 1266  CB  LEU A 377     5777   5372   5994   1660    544     81       C  
ATOM   1267  CG  LEU A 377      14.209 -15.248  12.908  1.00 49.68           C  
ANISOU 1267  CG  LEU A 377     6305   5905   6666   1847    536    147       C  
ATOM   1268  CD1 LEU A 377      15.603 -15.506  12.359  1.00 51.93           C  
ANISOU 1268  CD1 LEU A 377     6506   6197   7029   1915    592     42       C  
ATOM   1269  CD2 LEU A 377      14.267 -14.427  14.195  1.00 46.58           C  
ANISOU 1269  CD2 LEU A 377     5871   5624   6203   1925    427    261       C  
ATOM   1270  N   GLU A 378      11.913 -13.887   8.877  1.00 42.32           N  
ANISOU 1270  N   GLU A 378     5528   5070   5481   1258    614   -127       N  
ATOM   1271  CA  GLU A 378      10.694 -13.628   8.112  1.00 42.09           C  
ANISOU 1271  CA  GLU A 378     5559   5066   5368   1098    594   -134       C  
ATOM   1272  C   GLU A 378       9.454 -13.458   8.995  1.00 41.70           C  
ANISOU 1272  C   GLU A 378     5525   5020   5299   1105    523     -3       C  
ATOM   1273  O   GLU A 378       8.391 -14.006   8.708  1.00 43.02           O  
ANISOU 1273  O   GLU A 378     5739   5142   5466   1014    533      7       O  
ATOM   1274  CB  GLU A 378      10.477 -14.735   7.075  1.00 45.01           C  
ANISOU 1274  CB  GLU A 378     5996   5338   5770    999    686   -247       C  
ATOM   1275  CG  GLU A 378      11.628 -14.864   6.079  1.00 53.48           C  
ANISOU 1275  CG  GLU A 378     7055   6421   6845    978    774   -394       C  
ATOM   1276  CD  GLU A 378      11.499 -16.080   5.179  1.00 64.19           C  
ANISOU 1276  CD  GLU A 378     8488   7658   8244    901    880   -522       C  
ATOM   1277  OE1 GLU A 378      10.382 -16.631   5.074  1.00 65.19           O  
ANISOU 1277  OE1 GLU A 378     8684   7720   8366    810    870   -505       O  
ATOM   1278  OE2 GLU A 378      12.516 -16.489   4.578  1.00 70.66           O  
ANISOU 1278  OE2 GLU A 378     9295   8450   9102    927    979   -648       O  
ATOM   1279  N   LEU A 379       9.594 -12.693  10.071  1.00 41.37           N  
ANISOU 1279  N   LEU A 379     5440   5041   5239   1207    456     90       N  
ATOM   1280  CA  LEU A 379       8.460 -12.404  10.938  1.00 39.23           C  
ANISOU 1280  CA  LEU A 379     5175   4793   4937   1221    400    208       C  
ATOM   1281  C   LEU A 379       7.558 -11.372  10.276  1.00 41.41           C  
ANISOU 1281  C   LEU A 379     5452   5162   5119   1109    344    211       C  
ATOM   1282  O   LEU A 379       8.024 -10.552   9.488  1.00 41.05           O  
ANISOU 1282  O   LEU A 379     5400   5180   5016   1054    325    153       O  
ATOM   1283  CB  LEU A 379       8.940 -11.868  12.287  1.00 38.78           C  
ANISOU 1283  CB  LEU A 379     5079   4781   4875   1364    349    290       C  
ATOM   1284  CG  LEU A 379       9.893 -12.745  13.098  1.00 42.28           C  
ANISOU 1284  CG  LEU A 379     5508   5157   5401   1500    378    315       C  
ATOM   1285  CD1 LEU A 379      10.245 -12.053  14.398  1.00 41.02           C  
ANISOU 1285  CD1 LEU A 379     5311   5074   5199   1616    308    396       C  
ATOM   1286  CD2 LEU A 379       9.284 -14.113  13.366  1.00 43.24           C  
ANISOU 1286  CD2 LEU A 379     5683   5147   5601   1509    435    365       C  
ATOM   1287  N   ASP A 380       6.268 -11.407  10.590  1.00 39.19           N  
ANISOU 1287  N   ASP A 380     5176   4893   4823   1076    319    287       N  
ATOM   1288  CA  ASP A 380       5.377 -10.346  10.136  1.00 39.57           C  
ANISOU 1288  CA  ASP A 380     5209   5036   4791   1004    253    313       C  
ATOM   1289  C   ASP A 380       4.889  -9.502  11.309  1.00 34.32           C  
ANISOU 1289  C   ASP A 380     4512   4425   4102   1105    202    412       C  
ATOM   1290  O   ASP A 380       5.195  -9.794  12.465  1.00 36.43           O  
ANISOU 1290  O   ASP A 380     4774   4666   4400   1214    218    460       O  
ATOM   1291  CB  ASP A 380       4.218 -10.891   9.291  1.00 42.16           C  
ANISOU 1291  CB  ASP A 380     5547   5364   5109    865    256    304       C  
ATOM   1292  CG  ASP A 380       3.285 -11.788  10.076  1.00 47.77           C  
ANISOU 1292  CG  ASP A 380     6248   6026   5876    873    283    376       C  
ATOM   1293  OD1 ASP A 380       3.198 -11.631  11.311  1.00 48.77           O  
ANISOU 1293  OD1 ASP A 380     6354   6157   6020    987    281    461       O  
ATOM   1294  OD2 ASP A 380       2.628 -12.649   9.449  1.00 52.39           O  
ANISOU 1294  OD2 ASP A 380     6851   6574   6481    753    310    344       O  
ATOM   1295  N   ASP A 381       4.149  -8.445  11.003  1.00 30.72           N  
ANISOU 1295  N   ASP A 381     4038   4045   3587   1073    143    441       N  
ATOM   1296  CA  ASP A 381       3.715  -7.493  12.019  1.00 30.59           C  
ANISOU 1296  CA  ASP A 381     3998   4079   3545   1171    102    514       C  
ATOM   1297  C   ASP A 381       3.002  -8.139  13.206  1.00 36.45           C  
ANISOU 1297  C   ASP A 381     4719   4811   4319   1239    136    591       C  
ATOM   1298  O   ASP A 381       3.193  -7.721  14.346  1.00 36.59           O  
ANISOU 1298  O   ASP A 381     4735   4849   4321   1348    131    630       O  
ATOM   1299  CB  ASP A 381       2.815  -6.432  11.392  1.00 33.01           C  
ANISOU 1299  CB  ASP A 381     4288   4453   3803   1128     40    541       C  
ATOM   1300  CG  ASP A 381       3.562  -5.529  10.445  1.00 32.60           C  
ANISOU 1300  CG  ASP A 381     4270   4414   3704   1078      2    490       C  
ATOM   1301  OD1 ASP A 381       4.542  -4.893  10.883  1.00 33.92           O  
ANISOU 1301  OD1 ASP A 381     4457   4570   3862   1138     -4    465       O  
ATOM   1302  OD2 ASP A 381       3.163  -5.448   9.266  1.00 37.33           O  
ANISOU 1302  OD2 ASP A 381     4876   5040   4268    970    -25    477       O  
ATOM   1303  N   SER A 382       2.174  -9.144  12.935  1.00 36.71           N  
ANISOU 1303  N   SER A 382     4740   4819   4388   1161    171    611       N  
ATOM   1304  CA  SER A 382       1.427  -9.818  13.993  1.00 39.63           C  
ANISOU 1304  CA  SER A 382     5091   5180   4787   1200    214    694       C  
ATOM   1305  C   SER A 382       2.352 -10.577  14.949  1.00 38.60           C  
ANISOU 1305  C   SER A 382     5002   4976   4689   1291    258    713       C  
ATOM   1306  O   SER A 382       2.067 -10.687  16.142  1.00 38.79           O  
ANISOU 1306  O   SER A 382     5021   5016   4701   1370    279    793       O  
ATOM   1307  CB  SER A 382       0.365 -10.751  13.403  1.00 40.01           C  
ANISOU 1307  CB  SER A 382     5117   5212   4872   1070    242    706       C  
ATOM   1308  OG  SER A 382       0.956 -11.822  12.691  1.00 46.36           O  
ANISOU 1308  OG  SER A 382     5975   5915   5723    991    282    637       O  
ATOM   1309  N   ASP A 383       3.457 -11.098  14.421  1.00 35.60           N  
ANISOU 1309  N   ASP A 383     4658   4522   4345   1283    274    645       N  
ATOM   1310  CA  ASP A 383       4.480 -11.725  15.251  1.00 36.36           C  
ANISOU 1310  CA  ASP A 383     4782   4557   4477   1388    300    665       C  
ATOM   1311  C   ASP A 383       5.191 -10.659  16.069  1.00 38.11           C  
ANISOU 1311  C   ASP A 383     4987   4855   4638   1500    247    674       C  
ATOM   1312  O   ASP A 383       5.311 -10.765  17.292  1.00 37.96           O  
ANISOU 1312  O   ASP A 383     4974   4852   4599   1598    246    747       O  
ATOM   1313  CB  ASP A 383       5.511 -12.453  14.382  1.00 39.24           C  
ANISOU 1313  CB  ASP A 383     5173   4833   4904   1362    333    575       C  
ATOM   1314  CG  ASP A 383       4.897 -13.540  13.523  1.00 41.11           C  
ANISOU 1314  CG  ASP A 383     5443   4980   5199   1240    389    540       C  
ATOM   1315  OD1 ASP A 383       3.939 -14.195  13.981  1.00 44.41           O  
ANISOU 1315  OD1 ASP A 383     5871   5361   5640   1207    418    613       O  
ATOM   1316  OD2 ASP A 383       5.385 -13.744  12.390  1.00 38.07           O  
ANISOU 1316  OD2 ASP A 383     5075   4562   4830   1168    410    433       O  
ATOM   1317  N   LEU A 384       5.669  -9.633  15.373  1.00 36.62           N  
ANISOU 1317  N   LEU A 384     4784   4715   4413   1474    203    601       N  
ATOM   1318  CA  LEU A 384       6.423  -8.551  15.991  1.00 36.99           C  
ANISOU 1318  CA  LEU A 384     4821   4826   4406   1552    151    587       C  
ATOM   1319  C   LEU A 384       5.657  -7.896  17.138  1.00 36.64           C  
ANISOU 1319  C   LEU A 384     4776   4843   4301   1620    131    656       C  
ATOM   1320  O   LEU A 384       6.240  -7.549  18.163  1.00 37.15           O  
ANISOU 1320  O   LEU A 384     4846   4945   4324   1710    105    671       O  
ATOM   1321  CB  LEU A 384       6.808  -7.509  14.935  1.00 29.00           C  
ANISOU 1321  CB  LEU A 384     3806   3847   3367   1482    114    507       C  
ATOM   1322  CG  LEU A 384       7.790  -8.005  13.866  1.00 34.46           C  
ANISOU 1322  CG  LEU A 384     4495   4500   4100   1421    143    423       C  
ATOM   1323  CD1 LEU A 384       7.888  -7.026  12.692  1.00 29.78           C  
ANISOU 1323  CD1 LEU A 384     3910   3942   3462   1321    117    362       C  
ATOM   1324  CD2 LEU A 384       9.165  -8.258  14.474  1.00 33.33           C  
ANISOU 1324  CD2 LEU A 384     4325   4354   3985   1510    143    400       C  
ATOM   1325  N   ALA A 385       4.349  -7.734  16.964  1.00 34.26           N  
ANISOU 1325  N   ALA A 385     4462   4563   3991   1577    143    694       N  
ATOM   1326  CA  ALA A 385       3.529  -7.085  17.979  1.00 35.08           C  
ANISOU 1326  CA  ALA A 385     4557   4732   4041   1644    141    748       C  
ATOM   1327  C   ALA A 385       3.680  -7.778  19.331  1.00 36.26           C  
ANISOU 1327  C   ALA A 385     4723   4886   4168   1728    174    818       C  
ATOM   1328  O   ALA A 385       3.838  -7.121  20.359  1.00 38.61           O  
ANISOU 1328  O   ALA A 385     5034   5241   4394   1811    156    829       O  
ATOM   1329  CB  ALA A 385       2.063  -7.043  17.546  1.00 30.30           C  
ANISOU 1329  CB  ALA A 385     3911   4153   3448   1585    161    785       C  
ATOM   1330  N   ILE A 386       3.638  -9.106  19.330  1.00 32.00           N  
ANISOU 1330  N   ILE A 386     4193   4281   3683   1703    221    866       N  
ATOM   1331  CA  ILE A 386       3.793  -9.856  20.569  1.00 33.43           C  
ANISOU 1331  CA  ILE A 386     4402   4457   3843   1779    250    955       C  
ATOM   1332  C   ILE A 386       5.240  -9.843  21.061  1.00 37.46           C  
ANISOU 1332  C   ILE A 386     4932   4966   4336   1866    202    936       C  
ATOM   1333  O   ILE A 386       5.493  -9.716  22.259  1.00 40.65           O  
ANISOU 1333  O   ILE A 386     5354   5426   4666   1952    185    989       O  
ATOM   1334  CB  ILE A 386       3.321 -11.310  20.430  1.00 34.98           C  
ANISOU 1334  CB  ILE A 386     4616   4561   4115   1723    316   1022       C  
ATOM   1335  CG1 ILE A 386       1.973 -11.369  19.707  1.00 39.06           C  
ANISOU 1335  CG1 ILE A 386     5095   5085   4661   1608    351   1022       C  
ATOM   1336  CG2 ILE A 386       3.211 -11.949  21.803  1.00 33.71           C  
ANISOU 1336  CG2 ILE A 386     4489   4405   3913   1796    351   1142       C  
ATOM   1337  CD1 ILE A 386       1.368 -12.760  19.651  1.00 37.27           C  
ANISOU 1337  CD1 ILE A 386     4888   4768   4504   1529    422   1087       C  
ATOM   1338  N   PHE A 387       6.184  -9.972  20.133  1.00 33.32           N  
ANISOU 1338  N   PHE A 387     4397   4392   3874   1840    181    860       N  
ATOM   1339  CA  PHE A 387       7.600  -9.990  20.487  1.00 32.03           C  
ANISOU 1339  CA  PHE A 387     4224   4238   3709   1919    135    837       C  
ATOM   1340  C   PHE A 387       8.018  -8.710  21.206  1.00 33.29           C  
ANISOU 1340  C   PHE A 387     4375   4506   3769   1967     67    805       C  
ATOM   1341  O   PHE A 387       8.723  -8.763  22.210  1.00 37.54           O  
ANISOU 1341  O   PHE A 387     4914   5092   4258   2052     26    840       O  
ATOM   1342  CB  PHE A 387       8.474 -10.216  19.249  1.00 36.07           C  
ANISOU 1342  CB  PHE A 387     4710   4692   4303   1872    138    744       C  
ATOM   1343  CG  PHE A 387       9.952 -10.179  19.532  1.00 41.36           C  
ANISOU 1343  CG  PHE A 387     5342   5390   4984   1950     92    713       C  
ATOM   1344  CD1 PHE A 387      10.510 -11.022  20.481  1.00 40.32           C  
ANISOU 1344  CD1 PHE A 387     5209   5243   4868   2060     81    795       C  
ATOM   1345  CD2 PHE A 387      10.784  -9.309  18.844  1.00 43.76           C  
ANISOU 1345  CD2 PHE A 387     5603   5740   5283   1911     58    609       C  
ATOM   1346  CE1 PHE A 387      11.869 -10.991  20.747  1.00 41.36           C  
ANISOU 1346  CE1 PHE A 387     5285   5418   5014   2139     28    772       C  
ATOM   1347  CE2 PHE A 387      12.145  -9.276  19.103  1.00 40.22           C  
ANISOU 1347  CE2 PHE A 387     5098   5334   4850   1974     16    578       C  
ATOM   1348  CZ  PHE A 387      12.687 -10.118  20.056  1.00 43.23           C  
ANISOU 1348  CZ  PHE A 387     5463   5712   5251   2093     -3    658       C  
ATOM   1349  N   ILE A 388       7.582  -7.560  20.702  1.00 33.85           N  
ANISOU 1349  N   ILE A 388     4442   4611   3808   1911     51    739       N  
ATOM   1350  CA  ILE A 388       7.959  -6.292  21.323  1.00 37.81           C  
ANISOU 1350  CA  ILE A 388     4951   5192   4224   1944     -6    692       C  
ATOM   1351  C   ILE A 388       7.302  -6.105  22.691  1.00 35.25           C  
ANISOU 1351  C   ILE A 388     4659   4933   3804   2015      1    754       C  
ATOM   1352  O   ILE A 388       7.871  -5.462  23.571  1.00 34.94           O  
ANISOU 1352  O   ILE A 388     4634   4962   3680   2064    -48    729       O  
ATOM   1353  CB  ILE A 388       7.671  -5.076  20.416  1.00 42.94           C  
ANISOU 1353  CB  ILE A 388     5604   5839   4872   1872    -23    613       C  
ATOM   1354  CG1 ILE A 388       6.181  -4.972  20.102  1.00 48.18           C  
ANISOU 1354  CG1 ILE A 388     6273   6490   5543   1842     20    651       C  
ATOM   1355  CG2 ILE A 388       8.490  -5.158  19.128  1.00 44.71           C  
ANISOU 1355  CG2 ILE A 388     5802   6021   5163   1795    -31    546       C  
ATOM   1356  CD1 ILE A 388       5.835  -3.778  19.234  1.00 47.27           C  
ANISOU 1356  CD1 ILE A 388     6164   6367   5427   1789     -5    595       C  
ATOM   1357  N   ALA A 389       6.112  -6.673  22.864  1.00 35.67           N  
ANISOU 1357  N   ALA A 389     4719   4970   3864   2009     67    830       N  
ATOM   1358  CA  ALA A 389       5.445  -6.666  24.161  1.00 34.25           C  
ANISOU 1358  CA  ALA A 389     4566   4857   3589   2071     96    898       C  
ATOM   1359  C   ALA A 389       6.282  -7.459  25.154  1.00 38.18           C  
ANISOU 1359  C   ALA A 389     5087   5379   4042   2141     72    969       C  
ATOM   1360  O   ALA A 389       6.454  -7.049  26.303  1.00 40.54           O  
ANISOU 1360  O   ALA A 389     5415   5765   4223   2201     47    982       O  
ATOM   1361  CB  ALA A 389       4.042  -7.257  24.051  1.00 27.91           C  
ANISOU 1361  CB  ALA A 389     3750   4037   2818   2034    181    972       C  
ATOM   1362  N   VAL A 390       6.806  -8.593  24.696  1.00 36.25           N  
ANISOU 1362  N   VAL A 390     4831   5055   3890   2135     77   1013       N  
ATOM   1363  CA  VAL A 390       7.670  -9.429  25.521  1.00 36.12           C  
ANISOU 1363  CA  VAL A 390     4829   5044   3852   2216     45   1094       C  
ATOM   1364  C   VAL A 390       8.889  -8.644  25.989  1.00 37.92           C  
ANISOU 1364  C   VAL A 390     5037   5362   4011   2266    -54   1030       C  
ATOM   1365  O   VAL A 390       9.280  -8.722  27.153  1.00 40.99           O  
ANISOU 1365  O   VAL A 390     5447   5831   4297   2338    -99   1089       O  
ATOM   1366  CB  VAL A 390       8.136 -10.694  24.765  1.00 38.43           C  
ANISOU 1366  CB  VAL A 390     5108   5210   4282   2211     68   1128       C  
ATOM   1367  CG1 VAL A 390       9.300 -11.369  25.501  1.00 36.13           C  
ANISOU 1367  CG1 VAL A 390     4815   4928   3986   2317     11   1198       C  
ATOM   1368  CG2 VAL A 390       6.975 -11.659  24.576  1.00 34.72           C  
ANISOU 1368  CG2 VAL A 390     4672   4652   3869   2157    162   1211       C  
ATOM   1369  N   ILE A 391       9.481  -7.883  25.074  1.00 40.28           N  
ANISOU 1369  N   ILE A 391     5295   5653   4357   2217    -89    910       N  
ATOM   1370  CA  ILE A 391      10.661  -7.078  25.378  1.00 40.77           C  
ANISOU 1370  CA  ILE A 391     5326   5799   4367   2237   -182    834       C  
ATOM   1371  C   ILE A 391      10.375  -6.019  26.446  1.00 42.09           C  
ANISOU 1371  C   ILE A 391     5538   6070   4384   2252   -215    805       C  
ATOM   1372  O   ILE A 391      11.145  -5.855  27.389  1.00 41.21           O  
ANISOU 1372  O   ILE A 391     5424   6053   4179   2299   -290    809       O  
ATOM   1373  CB  ILE A 391      11.217  -6.390  24.110  1.00 40.94           C  
ANISOU 1373  CB  ILE A 391     5301   5786   4467   2156   -195    712       C  
ATOM   1374  CG1 ILE A 391      11.793  -7.429  23.143  1.00 42.81           C  
ANISOU 1374  CG1 ILE A 391     5489   5941   4837   2150   -166    718       C  
ATOM   1375  CG2 ILE A 391      12.272  -5.356  24.480  1.00 40.55           C  
ANISOU 1375  CG2 ILE A 391     5225   5830   4354   2148   -284    624       C  
ATOM   1376  CD1 ILE A 391      12.345  -6.835  21.859  1.00 38.00           C  
ANISOU 1376  CD1 ILE A 391     4837   5309   4293   2062   -164    604       C  
ATOM   1377  N   ILE A 392       9.270  -5.298  26.293  1.00 41.55           N  
ANISOU 1377  N   ILE A 392     5508   5987   4291   2213   -161    770       N  
ATOM   1378  CA  ILE A 392       8.912  -4.254  27.249  1.00 40.26           C  
ANISOU 1378  CA  ILE A 392     5396   5907   3994   2232   -174    723       C  
ATOM   1379  C   ILE A 392       8.779  -4.807  28.666  1.00 38.95           C  
ANISOU 1379  C   ILE A 392     5270   5830   3700   2305   -173    818       C  
ATOM   1380  O   ILE A 392       9.287  -4.223  29.623  1.00 42.59           O  
ANISOU 1380  O   ILE A 392     5760   6391   4031   2331   -234    778       O  
ATOM   1381  CB  ILE A 392       7.594  -3.564  26.862  1.00 42.30           C  
ANISOU 1381  CB  ILE A 392     5681   6127   4266   2204    -99    692       C  
ATOM   1382  CG1 ILE A 392       7.733  -2.873  25.508  1.00 41.03           C  
ANISOU 1382  CG1 ILE A 392     5495   5887   4206   2131   -112    606       C  
ATOM   1383  CG2 ILE A 392       7.183  -2.564  27.936  1.00 46.38           C  
ANISOU 1383  CG2 ILE A 392     6256   6720   4645   2242    -93    638       C  
ATOM   1384  CD1 ILE A 392       6.452  -2.254  25.005  1.00 41.08           C  
ANISOU 1384  CD1 ILE A 392     5513   5853   4243   2114    -52    592       C  
ATOM   1385  N   LEU A 393       8.097  -5.939  28.792  1.00 33.82           N  
ANISOU 1385  N   LEU A 393     4626   5146   3079   2328   -105    944       N  
ATOM   1386  CA  LEU A 393       7.845  -6.537  30.097  1.00 38.18           C  
ANISOU 1386  CA  LEU A 393     5225   5776   3505   2388    -89   1057       C  
ATOM   1387  C   LEU A 393       9.005  -7.425  30.547  1.00 42.39           C  
ANISOU 1387  C   LEU A 393     5745   6333   4030   2446   -172   1144       C  
ATOM   1388  O   LEU A 393       8.819  -8.602  30.847  1.00 44.74           O  
ANISOU 1388  O   LEU A 393     6061   6592   4346   2482   -139   1286       O  
ATOM   1389  CB  LEU A 393       6.531  -7.326  30.072  1.00 32.10           C  
ANISOU 1389  CB  LEU A 393     4470   4957   2769   2373     29   1163       C  
ATOM   1390  CG  LEU A 393       5.234  -6.511  30.213  1.00 37.79           C  
ANISOU 1390  CG  LEU A 393     5202   5714   3441   2351    116   1114       C  
ATOM   1391  CD1 LEU A 393       5.066  -5.990  31.633  1.00 39.53           C  
ANISOU 1391  CD1 LEU A 393     5483   6069   3466   2401    125   1113       C  
ATOM   1392  CD2 LEU A 393       5.156  -5.358  29.211  1.00 35.40           C  
ANISOU 1392  CD2 LEU A 393     4869   5368   3213   2311     98    972       C  
ATOM   1393  N   SER A 394      10.204  -6.853  30.589  1.00 45.62           N  
ANISOU 1393  N   SER A 394     6119   6800   4415   2455   -280   1062       N  
ATOM   1394  CA  SER A 394      11.390  -7.589  31.021  1.00 50.10           C  
ANISOU 1394  CA  SER A 394     6649   7410   4976   2522   -375   1138       C  
ATOM   1395  C   SER A 394      11.670  -7.342  32.497  1.00 50.82           C  
ANISOU 1395  C   SER A 394     6787   7660   4861   2570   -448   1179       C  
ATOM   1396  O   SER A 394      11.982  -6.223  32.899  1.00 50.72           O  
ANISOU 1396  O   SER A 394     6785   7747   4739   2538   -506   1059       O  
ATOM   1397  CB  SER A 394      12.609  -7.186  30.189  1.00 51.70           C  
ANISOU 1397  CB  SER A 394     6761   7606   5278   2498   -455   1029       C  
ATOM   1398  OG  SER A 394      12.447  -7.550  28.831  1.00 54.22           O  
ANISOU 1398  OG  SER A 394     7041   7787   5774   2456   -388   1001       O  
ATOM   1399  N   GLY A 395      11.563  -8.393  33.302  1.00 50.46           N  
ANISOU 1399  N   GLY A 395     6780   7636   4757   2641   -446   1348       N  
ATOM   1400  CA  GLY A 395      11.732  -8.266  34.737  1.00 50.87           C  
ANISOU 1400  CA  GLY A 395     6889   7849   4589   2683   -510   1409       C  
ATOM   1401  C   GLY A 395      13.175  -8.176  35.201  1.00 53.78           C  
ANISOU 1401  C   GLY A 395     7198   8337   4900   2730   -676   1403       C  
ATOM   1402  O   GLY A 395      13.440  -8.152  36.404  1.00 57.39           O  
ANISOU 1402  O   GLY A 395     7698   8943   5163   2767   -752   1464       O  
ATOM   1403  N   ASP A 396      14.110  -8.121  34.257  1.00 54.62           N  
ANISOU 1403  N   ASP A 396     7197   8391   5164   2725   -733   1330       N  
ATOM   1404  CA AASP A 396      15.536  -8.063  34.566  0.46 60.11           C  
ANISOU 1404  CA AASP A 396     7799   9205   5835   2767   -890   1320       C  
ATOM   1405  CA BASP A 396      15.521  -8.056  34.623  0.54 59.47           C  
ANISOU 1405  CA BASP A 396     7722   9129   5745   2768   -892   1322       C  
ATOM   1406  C   ASP A 396      16.066  -6.634  34.539  1.00 57.84           C  
ANISOU 1406  C   ASP A 396     7479   9020   5478   2673   -962   1122       C  
ATOM   1407  O   ASP A 396      17.246  -6.398  34.790  1.00 59.75           O  
ANISOU 1407  O   ASP A 396     7631   9381   5690   2680  -1098   1085       O  
ATOM   1408  CB AASP A 396      16.336  -8.899  33.565  0.46 63.31           C  
ANISOU 1408  CB AASP A 396     8090   9502   6462   2821   -902   1355       C  
ATOM   1409  CB BASP A 396      16.359  -9.010  33.767  0.54 62.83           C  
ANISOU 1409  CB BASP A 396     8035   9457   6379   2836   -914   1382       C  
ATOM   1410  CG AASP A 396      15.817 -10.316  33.433  0.46 66.95           C  
ANISOU 1410  CG AASP A 396     8593   9819   7025   2902   -820   1532       C  
ATOM   1411  CG BASP A 396      16.466  -8.561  32.325  0.54 60.36           C  
ANISOU 1411  CG BASP A 396     7655   9031   6249   2758   -852   1233       C  
ATOM   1412  OD1AASP A 396      14.901 -10.697  34.191  0.46 69.45           O  
ANISOU 1412  OD1AASP A 396     9021  10134   7233   2915   -764   1648       O  
ATOM   1413  OD1BASP A 396      17.502  -8.851  31.692  0.54 61.01           O  
ANISOU 1413  OD1BASP A 396     7617   9101   6464   2789   -900   1209       O  
ATOM   1414  OD2AASP A 396      16.331 -11.051  32.563  0.46 70.18           O  
ANISOU 1414  OD2AASP A 396     8928  10112   7625   2948   -803   1551       O  
ATOM   1415  OD2BASP A 396      15.520  -7.917  31.827  0.54 55.12           O  
ANISOU 1415  OD2BASP A 396     7054   8298   5593   2668   -753   1143       O  
ATOM   1416  N   ARG A 397      15.201  -5.683  34.205  1.00 50.28           N  
ANISOU 1416  N   ARG A 397     6589   8011   4506   2585   -871    994       N  
ATOM   1417  CA  ARG A 397      15.618  -4.288  34.134  1.00 52.30           C  
ANISOU 1417  CA  ARG A 397     6836   8327   4707   2488   -924    804       C  
ATOM   1418  C   ARG A 397      16.101  -3.796  35.498  1.00 60.62           C  
ANISOU 1418  C   ARG A 397     7927   9575   5530   2486  -1042    778       C  
ATOM   1419  O   ARG A 397      15.465  -4.056  36.521  1.00 61.16           O  
ANISOU 1419  O   ARG A 397     8091   9714   5433   2528  -1019    860       O  
ATOM   1420  CB  ARG A 397      14.479  -3.404  33.625  1.00 49.48           C  
ANISOU 1420  CB  ARG A 397     6562   7865   4373   2416   -800    694       C  
ATOM   1421  CG  ARG A 397      13.847  -3.871  32.324  1.00 48.50           C  
ANISOU 1421  CG  ARG A 397     6412   7566   4449   2408   -687    723       C  
ATOM   1422  CD  ARG A 397      14.875  -4.056  31.220  1.00 46.07           C  
ANISOU 1422  CD  ARG A 397     5988   7206   4310   2382   -730    686       C  
ATOM   1423  NE  ARG A 397      14.232  -4.077  29.909  1.00 43.87           N  
ANISOU 1423  NE  ARG A 397     5706   6773   4190   2336   -625    658       N  
ATOM   1424  CZ  ARG A 397      14.858  -4.345  28.769  1.00 41.91           C  
ANISOU 1424  CZ  ARG A 397     5372   6455   4096   2308   -621    630       C  
ATOM   1425  NH1 ARG A 397      16.153  -4.623  28.774  1.00 40.04           N  
ANISOU 1425  NH1 ARG A 397     5032   6287   3894   2330   -710    627       N  
ATOM   1426  NH2 ARG A 397      14.187  -4.339  27.625  1.00 39.65           N  
ANISOU 1426  NH2 ARG A 397     5097   6043   3925   2258   -528    606       N  
ATOM   1427  N   PRO A 398      17.238  -3.085  35.516  1.00 63.23           N  
ANISOU 1427  N   PRO A 398     8182  10004   5841   2424  -1167    662       N  
ATOM   1428  CA  PRO A 398      17.791  -2.548  36.764  1.00 62.99           C  
ANISOU 1428  CA  PRO A 398     8178  10171   5584   2400  -1297    615       C  
ATOM   1429  C   PRO A 398      16.826  -1.590  37.461  1.00 60.45           C  
ANISOU 1429  C   PRO A 398     8014   9866   5086   2345  -1226    506       C  
ATOM   1430  O   PRO A 398      16.211  -0.745  36.808  1.00 53.86           O  
ANISOU 1430  O   PRO A 398     7231   8907   4327   2279  -1128    378       O  
ATOM   1431  CB  PRO A 398      19.036  -1.787  36.295  1.00 61.35           C  
ANISOU 1431  CB  PRO A 398     7851  10019   5440   2305  -1411    472       C  
ATOM   1432  CG  PRO A 398      19.400  -2.417  34.992  1.00 59.76           C  
ANISOU 1432  CG  PRO A 398     7526   9689   5489   2332  -1367    517       C  
ATOM   1433  CD  PRO A 398      18.101  -2.799  34.357  1.00 59.00           C  
ANISOU 1433  CD  PRO A 398     7521   9409   5489   2365  -1195    572       C  
ATOM   1434  N   GLY A 399      16.693  -1.734  38.777  1.00 64.83           N  
ANISOU 1434  N   GLY A 399     8649  10577   5408   2378  -1274    560       N  
ATOM   1435  CA  GLY A 399      15.914  -0.804  39.574  1.00 66.10           C  
ANISOU 1435  CA  GLY A 399     8956  10783   5375   2329  -1214    438       C  
ATOM   1436  C   GLY A 399      14.421  -1.070  39.636  1.00 63.96           C  
ANISOU 1436  C   GLY A 399     8790  10417   5096   2381  -1029    500       C  
ATOM   1437  O   GLY A 399      13.660  -0.220  40.100  1.00 62.54           O  
ANISOU 1437  O   GLY A 399     8723  10244   4797   2348   -946    379       O  
ATOM   1438  N   LEU A 400      13.995  -2.240  39.171  1.00 62.68           N  
ANISOU 1438  N   LEU A 400     8588  10165   5063   2459   -960    683       N  
ATOM   1439  CA  LEU A 400      12.582  -2.606  39.239  1.00 59.58           C  
ANISOU 1439  CA  LEU A 400     8274   9696   4667   2498   -787    759       C  
ATOM   1440  C   LEU A 400      12.170  -2.885  40.681  1.00 59.28           C  
ANISOU 1440  C   LEU A 400     8341   9822   4362   2533   -775    843       C  
ATOM   1441  O   LEU A 400      12.837  -3.635  41.389  1.00 61.19           O  
ANISOU 1441  O   LEU A 400     8572  10186   4493   2577   -885    981       O  
ATOM   1442  CB  LEU A 400      12.287  -3.821  38.355  1.00 54.17           C  
ANISOU 1442  CB  LEU A 400     7522   8869   4191   2552   -723    927       C  
ATOM   1443  CG  LEU A 400      12.164  -3.553  36.853  1.00 48.03           C  
ANISOU 1443  CG  LEU A 400     6673   7911   3666   2512   -667    846       C  
ATOM   1444  CD1 LEU A 400      11.895  -4.845  36.107  1.00 47.51           C  
ANISOU 1444  CD1 LEU A 400     6555   7720   3778   2560   -608   1008       C  
ATOM   1445  CD2 LEU A 400      11.071  -2.534  36.568  1.00 45.58           C  
ANISOU 1445  CD2 LEU A 400     6426   7529   3363   2467   -543    711       C  
ATOM   1446  N   LEU A 401      11.069  -2.276  41.110  1.00 57.47           N  
ANISOU 1446  N   LEU A 401     8211   9599   4026   2518   -640    762       N  
ATOM   1447  CA  LEU A 401      10.605  -2.407  42.486  1.00 59.39           C  
ANISOU 1447  CA  LEU A 401     8564  10008   3994   2538   -605    815       C  
ATOM   1448  C   LEU A 401       9.836  -3.707  42.705  1.00 59.59           C  
ANISOU 1448  C   LEU A 401     8603  10018   4022   2599   -504   1053       C  
ATOM   1449  O   LEU A 401      10.074  -4.417  43.678  1.00 61.10           O  
ANISOU 1449  O   LEU A 401     8841  10344   4031   2631   -557   1206       O  
ATOM   1450  CB  LEU A 401       9.737  -1.207  42.872  1.00 61.62           C  
ANISOU 1450  CB  LEU A 401     8944  10305   4163   2503   -483    618       C  
ATOM   1451  CG  LEU A 401      10.383   0.174  42.741  1.00 62.99           C  
ANISOU 1451  CG  LEU A 401     9136  10475   4322   2431   -563    368       C  
ATOM   1452  CD1 LEU A 401       9.340   1.278  42.855  1.00 65.56           C  
ANISOU 1452  CD1 LEU A 401     9553  10746   4611   2421   -408    184       C  
ATOM   1453  CD2 LEU A 401      11.473   0.351  43.785  1.00 64.11           C  
ANISOU 1453  CD2 LEU A 401     9314  10819   4225   2392   -736    331       C  
ATOM   1454  N   ASN A 402       8.911  -4.008  41.799  1.00 61.64           N  
ANISOU 1454  N   ASN A 402     8824  10112   4483   2606   -363   1088       N  
ATOM   1455  CA  ASN A 402       8.098  -5.215  41.901  1.00 61.00           C  
ANISOU 1455  CA  ASN A 402     8754   9993   4431   2641   -253   1302       C  
ATOM   1456  C   ASN A 402       8.281  -6.104  40.678  1.00 54.89           C  
ANISOU 1456  C   ASN A 402     7883   9036   3936   2655   -261   1405       C  
ATOM   1457  O   ASN A 402       7.548  -5.978  39.697  1.00 51.67           O  
ANISOU 1457  O   ASN A 402     7430   8488   3714   2630   -158   1355       O  
ATOM   1458  CB  ASN A 402       6.617  -4.855  42.048  1.00 64.69           C  
ANISOU 1458  CB  ASN A 402     9264  10450   4864   2625    -51   1256       C  
ATOM   1459  CG  ASN A 402       6.369  -3.805  43.110  1.00 67.92           C  
ANISOU 1459  CG  ASN A 402     9769  11017   5020   2613    -17   1104       C  
ATOM   1460  OD1 ASN A 402       7.074  -3.742  44.117  1.00 70.58           O  
ANISOU 1460  OD1 ASN A 402    10172  11514   5130   2613   -120   1111       O  
ATOM   1461  ND2 ASN A 402       5.354  -2.974  42.892  1.00 66.42           N  
ANISOU 1461  ND2 ASN A 402     9586  10785   4865   2607    129    962       N  
ATOM   1462  N   VAL A 403       9.258  -7.004  40.740  1.00 53.78           N  
ANISOU 1462  N   VAL A 403     7711   8900   3824   2699   -386   1547       N  
ATOM   1463  CA  VAL A 403       9.577  -7.875  39.611  1.00 53.39           C  
ANISOU 1463  CA  VAL A 403     7576   8676   4035   2720   -399   1631       C  
ATOM   1464  C   VAL A 403       8.449  -8.851  39.275  1.00 50.50           C  
ANISOU 1464  C   VAL A 403     7229   8183   3777   2714   -244   1775       C  
ATOM   1465  O   VAL A 403       8.104  -9.032  38.109  1.00 53.81           O  
ANISOU 1465  O   VAL A 403     7587   8442   4414   2685   -182   1742       O  
ATOM   1466  CB  VAL A 403      10.879  -8.668  39.861  1.00 61.36           C  
ANISOU 1466  CB  VAL A 403     8545   9722   5046   2790   -563   1760       C  
ATOM   1467  CG1 VAL A 403      11.064  -9.743  38.800  1.00 63.03           C  
ANISOU 1467  CG1 VAL A 403     8687   9741   5519   2826   -544   1864       C  
ATOM   1468  CG2 VAL A 403      12.074  -7.731  39.890  1.00 63.45           C  
ANISOU 1468  CG2 VAL A 403     8750  10093   5265   2778   -723   1603       C  
ATOM   1469  N   LYS A 404       7.872  -9.468  40.300  1.00 51.33           N  
ANISOU 1469  N   LYS A 404     7418   8366   3717   2728   -181   1932       N  
ATOM   1470  CA  LYS A 404       6.873 -10.522  40.115  1.00 55.67           C  
ANISOU 1470  CA  LYS A 404     7992   8804   4357   2709    -40   2095       C  
ATOM   1471  C   LYS A 404       5.717 -10.166  39.166  1.00 54.78           C  
ANISOU 1471  C   LYS A 404     7830   8584   4401   2640    109   1990       C  
ATOM   1472  O   LYS A 404       5.422 -10.924  38.242  1.00 53.61           O  
ANISOU 1472  O   LYS A 404     7639   8272   4458   2615    158   2050       O  
ATOM   1473  CB  LYS A 404       6.332 -10.989  41.470  1.00 63.02           C  
ANISOU 1473  CB  LYS A 404     9030   9868   5047   2713     22   2258       C  
ATOM   1474  CG  LYS A 404       5.232 -12.036  41.387  1.00 73.59           C  
ANISOU 1474  CG  LYS A 404    10398  11104   6459   2671    182   2429       C  
ATOM   1475  CD  LYS A 404       5.728 -13.328  40.755  1.00 83.30           C  
ANISOU 1475  CD  LYS A 404    11613  12145   7891   2701    137   2592       C  
ATOM   1476  CE  LYS A 404       4.672 -14.422  40.838  1.00 90.27           C  
ANISOU 1476  CE  LYS A 404    12548  12930   8822   2643    291   2777       C  
ATOM   1477  NZ  LYS A 404       5.069 -15.641  40.078  1.00 94.17           N  
ANISOU 1477  NZ  LYS A 404    13035  13201   9545   2663    265   2905       N  
ATOM   1478  N   PRO A 405       5.054  -9.021  39.394  1.00 55.98           N  
ANISOU 1478  N   PRO A 405     7987   8826   4456   2612    178   1833       N  
ATOM   1479  CA  PRO A 405       3.929  -8.640  38.528  1.00 51.56           C  
ANISOU 1479  CA  PRO A 405     7369   8180   4042   2561    309   1743       C  
ATOM   1480  C   PRO A 405       4.347  -8.522  37.063  1.00 48.87           C  
ANISOU 1480  C   PRO A 405     6941   7681   3947   2542    252   1653       C  
ATOM   1481  O   PRO A 405       3.583  -8.876  36.164  1.00 51.12           O  
ANISOU 1481  O   PRO A 405     7173   7851   4398   2497    336   1667       O  
ATOM   1482  CB  PRO A 405       3.517  -7.267  39.070  1.00 48.01           C  
ANISOU 1482  CB  PRO A 405     6944   7855   3442   2566    351   1566       C  
ATOM   1483  CG  PRO A 405       4.016  -7.243  40.473  1.00 53.12           C  
ANISOU 1483  CG  PRO A 405     7686   8674   3821   2597    300   1613       C  
ATOM   1484  CD  PRO A 405       5.281  -8.041  40.470  1.00 54.93           C  
ANISOU 1484  CD  PRO A 405     7918   8878   4076   2629    141   1730       C  
ATOM   1485  N   ILE A 406       5.554  -8.022  36.831  1.00 49.10           N  
ANISOU 1485  N   ILE A 406     6953   7715   3989   2568    110   1560       N  
ATOM   1486  CA  ILE A 406       6.077  -7.884  35.478  1.00 43.60           C  
ANISOU 1486  CA  ILE A 406     6178   6884   3504   2547     55   1473       C  
ATOM   1487  C   ILE A 406       6.290  -9.250  34.828  1.00 45.75           C  
ANISOU 1487  C   ILE A 406     6423   7021   3941   2548     56   1614       C  
ATOM   1488  O   ILE A 406       5.941  -9.463  33.666  1.00 43.27           O  
ANISOU 1488  O   ILE A 406     6056   6576   3809   2503    101   1583       O  
ATOM   1489  CB  ILE A 406       7.403  -7.104  35.478  1.00 44.41           C  
ANISOU 1489  CB  ILE A 406     6263   7040   3572   2565    -94   1353       C  
ATOM   1490  CG1 ILE A 406       7.164  -5.666  35.950  1.00 47.48           C  
ANISOU 1490  CG1 ILE A 406     6688   7525   3826   2548    -87   1183       C  
ATOM   1491  CG2 ILE A 406       8.047  -7.141  34.096  1.00 42.66           C  
ANISOU 1491  CG2 ILE A 406     5958   6687   3564   2540   -144   1288       C  
ATOM   1492  CD1 ILE A 406       8.428  -4.850  36.128  1.00 47.39           C  
ANISOU 1492  CD1 ILE A 406     6672   7583   3752   2544   -233   1060       C  
ATOM   1493  N   GLU A 407       6.862 -10.174  35.588  1.00 47.12           N  
ANISOU 1493  N   GLU A 407     6637   7221   4044   2602      5   1770       N  
ATOM   1494  CA  GLU A 407       7.141 -11.516  35.087  1.00 49.12           C  
ANISOU 1494  CA  GLU A 407     6881   7328   4452   2621      6   1910       C  
ATOM   1495  C   GLU A 407       5.865 -12.297  34.789  1.00 48.33           C  
ANISOU 1495  C   GLU A 407     6802   7125   4435   2556    155   2003       C  
ATOM   1496  O   GLU A 407       5.813 -13.070  33.835  1.00 46.21           O  
ANISOU 1496  O   GLU A 407     6508   6696   4355   2527    185   2030       O  
ATOM   1497  CB  GLU A 407       8.016 -12.285  36.077  1.00 49.63           C  
ANISOU 1497  CB  GLU A 407     6993   7450   4415   2709    -88   2073       C  
ATOM   1498  CG  GLU A 407       9.461 -11.816  36.114  1.00 57.01           C  
ANISOU 1498  CG  GLU A 407     7873   8459   5331   2772   -254   1998       C  
ATOM   1499  CD  GLU A 407      10.310 -12.614  37.085  1.00 65.22           C  
ANISOU 1499  CD  GLU A 407     8945   9563   6271   2871   -361   2175       C  
ATOM   1500  OE1 GLU A 407       9.819 -12.942  38.185  1.00 65.69           O  
ANISOU 1500  OE1 GLU A 407     9097   9708   6154   2883   -331   2313       O  
ATOM   1501  OE2 GLU A 407      11.475 -12.909  36.750  1.00 72.60           O  
ANISOU 1501  OE2 GLU A 407     9809  10472   7302   2941   -474   2181       O  
ATOM   1502  N   ASP A 408       4.836 -12.095  35.606  1.00 49.68           N  
ANISOU 1502  N   ASP A 408     7018   7394   4463   2525    253   2045       N  
ATOM   1503  CA  ASP A 408       3.551 -12.744  35.373  1.00 49.38           C  
ANISOU 1503  CA  ASP A 408     6983   7284   4496   2446    401   2126       C  
ATOM   1504  C   ASP A 408       2.960 -12.320  34.031  1.00 47.13           C  
ANISOU 1504  C   ASP A 408     6610   6908   4388   2375    446   1988       C  
ATOM   1505  O   ASP A 408       2.413 -13.139  33.291  1.00 48.05           O  
ANISOU 1505  O   ASP A 408     6706   6895   4654   2307    512   2040       O  
ATOM   1506  CB  ASP A 408       2.576 -12.438  36.510  1.00 52.90           C  
ANISOU 1506  CB  ASP A 408     7473   7883   4743   2428    505   2174       C  
ATOM   1507  CG  ASP A 408       2.975 -13.106  37.813  1.00 58.83           C  
ANISOU 1507  CG  ASP A 408     8325   8715   5313   2476    480   2354       C  
ATOM   1508  OD1 ASP A 408       3.701 -14.122  37.763  1.00 63.31           O  
ANISOU 1508  OD1 ASP A 408     8927   9178   5949   2513    414   2490       O  
ATOM   1509  OD2 ASP A 408       2.564 -12.618  38.886  1.00 58.53           O  
ANISOU 1509  OD2 ASP A 408     8335   8846   5060   2482    527   2361       O  
ATOM   1510  N   ILE A 409       3.078 -11.035  33.718  1.00 44.60           N  
ANISOU 1510  N   ILE A 409     6245   6654   4047   2386    406   1813       N  
ATOM   1511  CA  ILE A 409       2.604 -10.523  32.438  1.00 43.55           C  
ANISOU 1511  CA  ILE A 409     6033   6445   4067   2327    429   1687       C  
ATOM   1512  C   ILE A 409       3.432 -11.078  31.278  1.00 42.46           C  
ANISOU 1512  C   ILE A 409     5867   6161   4106   2312    360   1666       C  
ATOM   1513  O   ILE A 409       2.881 -11.519  30.269  1.00 43.79           O  
ANISOU 1513  O   ILE A 409     5996   6223   4420   2239    410   1658       O  
ATOM   1514  CB  ILE A 409       2.618  -8.987  32.401  1.00 41.82           C  
ANISOU 1514  CB  ILE A 409     5790   6314   3784   2351    398   1515       C  
ATOM   1515  CG1 ILE A 409       1.681  -8.425  33.479  1.00 44.81           C  
ANISOU 1515  CG1 ILE A 409     6195   6831   4000   2369    490   1516       C  
ATOM   1516  CG2 ILE A 409       2.224  -8.490  31.009  1.00 39.29           C  
ANISOU 1516  CG2 ILE A 409     5395   5907   3625   2296    404   1406       C  
ATOM   1517  CD1 ILE A 409       1.732  -6.911  33.635  1.00 40.81           C  
ANISOU 1517  CD1 ILE A 409     5690   6401   3416   2407    465   1345       C  
ATOM   1518  N   GLN A 410       4.753 -11.064  31.426  1.00 46.26           N  
ANISOU 1518  N   GLN A 410     6362   6646   4570   2379    248   1652       N  
ATOM   1519  CA  GLN A 410       5.633 -11.576  30.378  1.00 44.19           C  
ANISOU 1519  CA  GLN A 410     6064   6256   4469   2378    192   1623       C  
ATOM   1520  C   GLN A 410       5.379 -13.058  30.128  1.00 45.31           C  
ANISOU 1520  C   GLN A 410     6234   6255   4725   2356    252   1758       C  
ATOM   1521  O   GLN A 410       5.463 -13.523  28.992  1.00 46.29           O  
ANISOU 1521  O   GLN A 410     6330   6249   5009   2310    267   1715       O  
ATOM   1522  CB  GLN A 410       7.109 -11.347  30.718  1.00 38.75           C  
ANISOU 1522  CB  GLN A 410     5367   5618   3738   2461     64   1597       C  
ATOM   1523  CG  GLN A 410       8.012 -11.317  29.483  1.00 38.36           C  
ANISOU 1523  CG  GLN A 410     5251   5479   3843   2451     11   1494       C  
ATOM   1524  CD  GLN A 410       9.485 -11.450  29.817  1.00 36.44           C  
ANISOU 1524  CD  GLN A 410     4979   5277   3589   2539   -105   1504       C  
ATOM   1525  OE1 GLN A 410       9.870 -12.239  30.677  1.00 41.64           O  
ANISOU 1525  OE1 GLN A 410     5671   5951   4199   2619   -138   1641       O  
ATOM   1526  NE2 GLN A 410      10.319 -10.682  29.127  1.00 36.52           N  
ANISOU 1526  NE2 GLN A 410     4923   5309   3645   2524   -169   1365       N  
ATOM   1527  N   ASP A 411       5.073 -13.793  31.194  1.00 45.44           N  
ANISOU 1527  N   ASP A 411     6318   6293   4653   2383    290   1919       N  
ATOM   1528  CA  ASP A 411       4.726 -15.208  31.085  1.00 50.27           C  
ANISOU 1528  CA  ASP A 411     6977   6756   5366   2353    359   2063       C  
ATOM   1529  C   ASP A 411       3.591 -15.421  30.085  1.00 49.87           C  
ANISOU 1529  C   ASP A 411     6893   6615   5440   2224    461   2015       C  
ATOM   1530  O   ASP A 411       3.687 -16.260  29.191  1.00 51.08           O  
ANISOU 1530  O   ASP A 411     7049   6606   5752   2180    482   2014       O  
ATOM   1531  CB  ASP A 411       4.320 -15.765  32.451  1.00 60.55           C  
ANISOU 1531  CB  ASP A 411     8363   8119   6525   2377    402   2248       C  
ATOM   1532  CG  ASP A 411       3.780 -17.181  32.367  1.00 72.97           C  
ANISOU 1532  CG  ASP A 411     9997   9527   8201   2321    493   2404       C  
ATOM   1533  OD1 ASP A 411       2.803 -17.490  33.080  1.00 81.66           O  
ANISOU 1533  OD1 ASP A 411    11142  10669   9217   2262    590   2518       O  
ATOM   1534  OD2 ASP A 411       4.329 -17.985  31.587  1.00 77.45           O  
ANISOU 1534  OD2 ASP A 411    10572   9918   8936   2332    474   2409       O  
ATOM   1535  N   ASN A 412       2.512 -14.663  30.254  1.00 48.09           N  
ANISOU 1535  N   ASN A 412     6632   6500   5140   2165    524   1971       N  
ATOM   1536  CA  ASN A 412       1.377 -14.735  29.343  1.00 49.52           C  
ANISOU 1536  CA  ASN A 412     6757   6633   5425   2042    606   1924       C  
ATOM   1537  C   ASN A 412       1.767 -14.339  27.922  1.00 45.04           C  
ANISOU 1537  C   ASN A 412     6132   5995   4987   2009    552   1771       C  
ATOM   1538  O   ASN A 412       1.396 -15.007  26.957  1.00 48.29           O  
ANISOU 1538  O   ASN A 412     6530   6289   5531   1916    589   1756       O  
ATOM   1539  CB  ASN A 412       0.236 -13.844  29.838  1.00 53.91           C  
ANISOU 1539  CB  ASN A 412     7265   7344   5874   2015    674   1898       C  
ATOM   1540  CG  ASN A 412      -0.322 -14.296  31.174  1.00 64.36           C  
ANISOU 1540  CG  ASN A 412     8643   8746   7064   2021    756   2049       C  
ATOM   1541  OD1 ASN A 412      -0.954 -13.519  31.889  1.00 69.94           O  
ANISOU 1541  OD1 ASN A 412     9328   9604   7643   2039    805   2029       O  
ATOM   1542  ND2 ASN A 412      -0.092 -15.559  31.518  1.00 67.71           N  
ANISOU 1542  ND2 ASN A 412     9144   9064   7517   2008    778   2202       N  
ATOM   1543  N   LEU A 413       2.513 -13.247  27.799  1.00 37.73           N  
ANISOU 1543  N   LEU A 413     5178   5143   4013   2075    467   1656       N  
ATOM   1544  CA  LEU A 413       2.965 -12.778  26.494  1.00 39.19           C  
ANISOU 1544  CA  LEU A 413     5314   5276   4299   2043    415   1517       C  
ATOM   1545  C   LEU A 413       3.806 -13.844  25.793  1.00 38.70           C  
ANISOU 1545  C   LEU A 413     5275   5061   4367   2040    399   1527       C  
ATOM   1546  O   LEU A 413       3.656 -14.078  24.593  1.00 38.23           O  
ANISOU 1546  O   LEU A 413     5192   4915   4420   1958    415   1453       O  
ATOM   1547  CB  LEU A 413       3.760 -11.476  26.635  1.00 37.98           C  
ANISOU 1547  CB  LEU A 413     5141   5221   4067   2111    328   1408       C  
ATOM   1548  CG  LEU A 413       2.981 -10.267  27.161  1.00 39.03           C  
ANISOU 1548  CG  LEU A 413     5256   5483   4089   2121    346   1361       C  
ATOM   1549  CD1 LEU A 413       3.918  -9.118  27.512  1.00 34.68           C  
ANISOU 1549  CD1 LEU A 413     4714   5012   3452   2188    257   1265       C  
ATOM   1550  CD2 LEU A 413       1.933  -9.832  26.137  1.00 39.20           C  
ANISOU 1550  CD2 LEU A 413     5217   5490   4187   2037    387   1298       C  
ATOM   1551  N   LEU A 414       4.687 -14.490  26.551  1.00 39.48           N  
ANISOU 1551  N   LEU A 414     5423   5131   4447   2133    366   1617       N  
ATOM   1552  CA  LEU A 414       5.522 -15.559  26.014  1.00 40.15           C  
ANISOU 1552  CA  LEU A 414     5531   5062   4662   2160    358   1637       C  
ATOM   1553  C   LEU A 414       4.663 -16.724  25.534  1.00 43.45           C  
ANISOU 1553  C   LEU A 414     5991   5328   5190   2060    455   1695       C  
ATOM   1554  O   LEU A 414       4.902 -17.280  24.464  1.00 42.01           O  
ANISOU 1554  O   LEU A 414     5808   5014   5139   2013    474   1625       O  
ATOM   1555  CB  LEU A 414       6.536 -16.037  27.056  1.00 40.80           C  
ANISOU 1555  CB  LEU A 414     5652   5152   4697   2297    299   1750       C  
ATOM   1556  CG  LEU A 414       7.693 -15.079  27.353  1.00 39.42           C  
ANISOU 1556  CG  LEU A 414     5427   5106   4446   2390    186   1676       C  
ATOM   1557  CD1 LEU A 414       8.457 -15.524  28.590  1.00 38.86           C  
ANISOU 1557  CD1 LEU A 414     5391   5082   4293   2516    121   1814       C  
ATOM   1558  CD2 LEU A 414       8.621 -14.957  26.149  1.00 40.21           C  
ANISOU 1558  CD2 LEU A 414     5463   5144   4670   2389    152   1540       C  
ATOM   1559  N   GLN A 415       3.664 -17.096  26.330  1.00 42.15           N  
ANISOU 1559  N   GLN A 415     5864   5184   4968   2018    523   1818       N  
ATOM   1560  CA  GLN A 415       2.707 -18.115  25.912  1.00 44.17           C  
ANISOU 1560  CA  GLN A 415     6152   5310   5320   1892    619   1871       C  
ATOM   1561  C   GLN A 415       2.021 -17.709  24.610  1.00 43.27           C  
ANISOU 1561  C   GLN A 415     5969   5194   5275   1761    638   1727       C  
ATOM   1562  O   GLN A 415       1.869 -18.524  23.699  1.00 44.17           O  
ANISOU 1562  O   GLN A 415     6106   5164   5514   1668    677   1691       O  
ATOM   1563  CB  GLN A 415       1.646 -18.343  26.989  1.00 50.56           C  
ANISOU 1563  CB  GLN A 415     6990   6186   6036   1850    695   2015       C  
ATOM   1564  CG  GLN A 415       2.101 -19.186  28.166  1.00 54.85           C  
ANISOU 1564  CG  GLN A 415     7631   6680   6530   1937    701   2198       C  
ATOM   1565  CD  GLN A 415       0.950 -19.553  29.084  1.00 58.48           C  
ANISOU 1565  CD  GLN A 415     8125   7189   6907   1861    800   2344       C  
ATOM   1566  OE1 GLN A 415       0.061 -20.319  28.710  1.00 54.68           O  
ANISOU 1566  OE1 GLN A 415     7656   6606   6513   1724    891   2384       O  
ATOM   1567  NE2 GLN A 415       0.962 -19.007  30.294  1.00 62.85           N  
ANISOU 1567  NE2 GLN A 415     8692   7906   7283   1937    788   2420       N  
ATOM   1568  N   ALA A 416       1.603 -16.449  24.536  1.00 35.67           N  
ANISOU 1568  N   ALA A 416     4931   4391   4230   1754    609   1648       N  
ATOM   1569  CA  ALA A 416       0.915 -15.929  23.358  1.00 41.92           C  
ANISOU 1569  CA  ALA A 416     5652   5208   5069   1642    610   1529       C  
ATOM   1570  C   ALA A 416       1.827 -15.951  22.132  1.00 45.08           C  
ANISOU 1570  C   ALA A 416     6051   5521   5555   1633    562   1403       C  
ATOM   1571  O   ALA A 416       1.403 -16.324  21.038  1.00 43.87           O  
ANISOU 1571  O   ALA A 416     5887   5299   5483   1514    585   1335       O  
ATOM   1572  CB  ALA A 416       0.399 -14.513  23.622  1.00 39.12           C  
ANISOU 1572  CB  ALA A 416     5225   5030   4609   1670    583   1482       C  
ATOM   1573  N   LEU A 417       3.080 -15.551  22.327  1.00 46.35           N  
ANISOU 1573  N   LEU A 417     6222   5697   5693   1752    496   1368       N  
ATOM   1574  CA  LEU A 417       4.059 -15.533  21.246  1.00 42.41           C  
ANISOU 1574  CA  LEU A 417     5713   5133   5267   1753    460   1248       C  
ATOM   1575  C   LEU A 417       4.324 -16.947  20.751  1.00 41.82           C  
ANISOU 1575  C   LEU A 417     5698   4872   5320   1721    515   1260       C  
ATOM   1576  O   LEU A 417       4.364 -17.194  19.548  1.00 44.61           O  
ANISOU 1576  O   LEU A 417     6049   5153   5748   1634    533   1153       O  
ATOM   1577  CB  LEU A 417       5.368 -14.890  21.714  1.00 41.01           C  
ANISOU 1577  CB  LEU A 417     5520   5020   5040   1887    383   1223       C  
ATOM   1578  CG  LEU A 417       6.491 -14.764  20.680  1.00 39.31           C  
ANISOU 1578  CG  LEU A 417     5278   4764   4893   1896    351   1099       C  
ATOM   1579  CD1 LEU A 417       6.031 -13.971  19.457  1.00 31.34           C  
ANISOU 1579  CD1 LEU A 417     4231   3795   3881   1779    347    977       C  
ATOM   1580  CD2 LEU A 417       7.719 -14.119  21.304  1.00 38.08           C  
ANISOU 1580  CD2 LEU A 417     5090   4696   4684   2018    273   1088       C  
ATOM   1581  N   GLU A 418       4.497 -17.874  21.686  1.00 42.77           N  
ANISOU 1581  N   GLU A 418     5879   4910   5460   1791    543   1391       N  
ATOM   1582  CA  GLU A 418       4.761 -19.268  21.343  1.00 46.20           C  
ANISOU 1582  CA  GLU A 418     6388   5139   6027   1778    601   1417       C  
ATOM   1583  C   GLU A 418       3.678 -19.850  20.437  1.00 47.57           C  
ANISOU 1583  C   GLU A 418     6582   5222   6271   1594    674   1368       C  
ATOM   1584  O   GLU A 418       3.979 -20.455  19.410  1.00 45.78           O  
ANISOU 1584  O   GLU A 418     6384   4864   6146   1539    704   1268       O  
ATOM   1585  CB  GLU A 418       4.895 -20.121  22.606  1.00 45.83           C  
ANISOU 1585  CB  GLU A 418     6415   5021   5977   1872    620   1600       C  
ATOM   1586  CG  GLU A 418       5.271 -21.572  22.333  1.00 50.24           C  
ANISOU 1586  CG  GLU A 418     7065   5339   6687   1885    679   1638       C  
ATOM   1587  CD  GLU A 418       5.437 -22.380  23.603  1.00 55.34           C  
ANISOU 1587  CD  GLU A 418     7792   5911   7325   1988    688   1842       C  
ATOM   1588  OE1 GLU A 418       4.894 -21.963  24.647  1.00 59.56           O  
ANISOU 1588  OE1 GLU A 418     8324   6579   7728   1994    677   1958       O  
ATOM   1589  OE2 GLU A 418       6.109 -23.431  23.561  1.00 60.90           O  
ANISOU 1589  OE2 GLU A 418     8566   6422   8149   2068    710   1889       O  
ATOM   1590  N   LEU A 419       2.419 -19.671  20.823  1.00 47.40           N  
ANISOU 1590  N   LEU A 419     6540   5278   6192   1496    704   1434       N  
ATOM   1591  CA  LEU A 419       1.300 -20.183  20.038  1.00 47.76           C  
ANISOU 1591  CA  LEU A 419     6585   5267   6295   1307    762   1395       C  
ATOM   1592  C   LEU A 419       1.178 -19.460  18.696  1.00 44.16           C  
ANISOU 1592  C   LEU A 419     6063   4880   5835   1217    722   1228       C  
ATOM   1593  O   LEU A 419       0.895 -20.081  17.673  1.00 49.44           O  
ANISOU 1593  O   LEU A 419     6756   5451   6577   1084    754   1142       O  
ATOM   1594  CB  LEU A 419      -0.007 -20.065  20.824  1.00 51.53           C  
ANISOU 1594  CB  LEU A 419     7027   5844   6706   1232    802   1508       C  
ATOM   1595  CG  LEU A 419      -1.250 -20.638  20.140  1.00 51.97           C  
ANISOU 1595  CG  LEU A 419     7064   5861   6821   1022    860   1486       C  
ATOM   1596  CD1 LEU A 419      -1.029 -22.097  19.769  1.00 53.86           C  
ANISOU 1596  CD1 LEU A 419     7418   5856   7192    947    924   1490       C  
ATOM   1597  CD2 LEU A 419      -2.474 -20.483  21.030  1.00 52.12           C  
ANISOU 1597  CD2 LEU A 419     7027   6001   6774    963    908   1606       C  
ATOM   1598  N   GLN A 420       1.391 -18.148  18.708  1.00 39.57           N  
ANISOU 1598  N   GLN A 420     5408   4465   5162   1283    652   1185       N  
ATOM   1599  CA  GLN A 420       1.346 -17.346  17.486  1.00 39.31           C  
ANISOU 1599  CA  GLN A 420     5319   4507   5111   1211    605   1047       C  
ATOM   1600  C   GLN A 420       2.346 -17.844  16.447  1.00 45.38           C  
ANISOU 1600  C   GLN A 420     6134   5155   5952   1200    612    926       C  
ATOM   1601  O   GLN A 420       2.012 -17.997  15.273  1.00 46.54           O  
ANISOU 1601  O   GLN A 420     6281   5281   6123   1067    619    823       O  
ATOM   1602  CB  GLN A 420       1.612 -15.872  17.802  1.00 39.80           C  
ANISOU 1602  CB  GLN A 420     5318   4735   5072   1307    532   1032       C  
ATOM   1603  CG  GLN A 420       1.969 -15.022  16.590  1.00 37.24           C  
ANISOU 1603  CG  GLN A 420     4958   4463   4728   1265    477    900       C  
ATOM   1604  CD  GLN A 420       0.786 -14.768  15.671  1.00 42.40           C  
ANISOU 1604  CD  GLN A 420     5562   5177   5370   1116    467    862       C  
ATOM   1605  OE1 GLN A 420      -0.361 -15.054  16.016  1.00 40.91           O  
ANISOU 1605  OE1 GLN A 420     5342   5018   5185   1050    496    932       O  
ATOM   1606  NE2 GLN A 420       1.062 -14.222  14.492  1.00 39.16           N  
ANISOU 1606  NE2 GLN A 420     5139   4798   4942   1058    424    757       N  
ATOM   1607  N   LEU A 421       3.575 -18.097  16.883  1.00 46.75           N  
ANISOU 1607  N   LEU A 421     6342   5264   6157   1342    609    937       N  
ATOM   1608  CA  LEU A 421       4.615 -18.569  15.977  1.00 47.02           C  
ANISOU 1608  CA  LEU A 421     6408   5191   6267   1357    629    821       C  
ATOM   1609  C   LEU A 421       4.317 -19.975  15.461  1.00 46.23           C  
ANISOU 1609  C   LEU A 421     6391   4895   6279   1261    713    794       C  
ATOM   1610  O   LEU A 421       4.508 -20.263  14.281  1.00 42.68           O  
ANISOU 1610  O   LEU A 421     5963   4384   5868   1173    742    656       O  
ATOM   1611  CB  LEU A 421       5.986 -18.508  16.654  1.00 46.43           C  
ANISOU 1611  CB  LEU A 421     6326   5107   6208   1544    602    850       C  
ATOM   1612  CG  LEU A 421       6.446 -17.088  17.000  1.00 43.40           C  
ANISOU 1612  CG  LEU A 421     5867   4907   5718   1618    517    839       C  
ATOM   1613  CD1 LEU A 421       7.796 -17.107  17.697  1.00 42.51           C  
ANISOU 1613  CD1 LEU A 421     5735   4796   5621   1789    483    869       C  
ATOM   1614  CD2 LEU A 421       6.505 -16.224  15.746  1.00 40.47           C  
ANISOU 1614  CD2 LEU A 421     5453   4613   5310   1522    495    699       C  
ATOM   1615  N   LYS A 422       3.838 -20.845  16.343  1.00 50.86           N  
ANISOU 1615  N   LYS A 422     7034   5380   6911   1270    757    924       N  
ATOM   1616  CA  LYS A 422       3.439 -22.188  15.940  1.00 55.51           C  
ANISOU 1616  CA  LYS A 422     7717   5764   7612   1162    841    909       C  
ATOM   1617  C   LYS A 422       2.357 -22.149  14.859  1.00 55.72           C  
ANISOU 1617  C   LYS A 422     7725   5826   7619    939    852    806       C  
ATOM   1618  O   LYS A 422       2.435 -22.869  13.861  1.00 57.70           O  
ANISOU 1618  O   LYS A 422     8036   5948   7939    836    900    682       O  
ATOM   1619  CB  LYS A 422       2.946 -22.988  17.149  1.00 60.68           C  
ANISOU 1619  CB  LYS A 422     8432   6325   8299   1187    883   1091       C  
ATOM   1620  CG  LYS A 422       4.047 -23.714  17.910  1.00 67.09           C  
ANISOU 1620  CG  LYS A 422     9314   6991   9187   1375    899   1181       C  
ATOM   1621  CD  LYS A 422       3.504 -24.363  19.177  1.00 71.47           C  
ANISOU 1621  CD  LYS A 422     9932   7481   9742   1395    931   1387       C  
ATOM   1622  CE  LYS A 422       4.434 -25.455  19.697  1.00 73.01           C  
ANISOU 1622  CE  LYS A 422    10230   7461  10051   1547    962   1480       C  
ATOM   1623  NZ  LYS A 422       5.819 -24.962  19.930  1.00 72.96           N  
ANISOU 1623  NZ  LYS A 422    10169   7520  10031   1762    891   1465       N  
ATOM   1624  N   LEU A 423       1.351 -21.306  15.065  1.00 49.08           N  
ANISOU 1624  N   LEU A 423     6799   5164   6683    868    806    854       N  
ATOM   1625  CA  LEU A 423       0.233 -21.200  14.133  1.00 53.49           C  
ANISOU 1625  CA  LEU A 423     7317   5789   7216    662    798    779       C  
ATOM   1626  C   LEU A 423       0.625 -20.504  12.831  1.00 50.86           C  
ANISOU 1626  C   LEU A 423     6953   5538   6833    616    748    619       C  
ATOM   1627  O   LEU A 423       0.270 -20.961  11.746  1.00 51.83           O  
ANISOU 1627  O   LEU A 423     7104   5618   6972    454    764    506       O  
ATOM   1628  CB  LEU A 423      -0.940 -20.458  14.780  1.00 53.39           C  
ANISOU 1628  CB  LEU A 423     7204   5956   7125    627    763    885       C  
ATOM   1629  CG  LEU A 423      -1.602 -21.107  15.998  1.00 54.65           C  
ANISOU 1629  CG  LEU A 423     7383   6070   7311    625    824   1046       C  
ATOM   1630  CD1 LEU A 423      -2.754 -20.250  16.494  1.00 51.72           C  
ANISOU 1630  CD1 LEU A 423     6892   5904   6857    592    798   1123       C  
ATOM   1631  CD2 LEU A 423      -2.082 -22.510  15.669  1.00 56.32           C  
ANISOU 1631  CD2 LEU A 423     7680   6092   7629    461    903   1038       C  
ATOM   1632  N   ASN A 424       1.357 -19.399  12.947  1.00 45.44           N  
ANISOU 1632  N   ASN A 424     6215   4973   6078    748    688    611       N  
ATOM   1633  CA  ASN A 424       1.699 -18.579  11.788  1.00 44.50           C  
ANISOU 1633  CA  ASN A 424     6063   4952   5894    703    638    484       C  
ATOM   1634  C   ASN A 424       2.867 -19.141  10.977  1.00 51.79           C  
ANISOU 1634  C   ASN A 424     7055   5755   6869    721    687    350       C  
ATOM   1635  O   ASN A 424       2.978 -18.886   9.778  1.00 55.44           O  
ANISOU 1635  O   ASN A 424     7519   6259   7286    621    676    224       O  
ATOM   1636  CB  ASN A 424       1.999 -17.142  12.225  1.00 47.67           C  
ANISOU 1636  CB  ASN A 424     6388   5519   6206    822    561    528       C  
ATOM   1637  CG  ASN A 424       1.854 -16.140  11.091  1.00 48.90           C  
ANISOU 1637  CG  ASN A 424     6501   5804   6276    739    497    441       C  
ATOM   1638  OD1 ASN A 424       1.072 -16.341  10.160  1.00 48.89           O  
ANISOU 1638  OD1 ASN A 424     6496   5826   6254    579    487    387       O  
ATOM   1639  ND2 ASN A 424       2.606 -15.049  11.171  1.00 47.95           N  
ANISOU 1639  ND2 ASN A 424     6350   5769   6099    840    448    433       N  
ATOM   1640  N   HIS A 425       3.736 -19.902  11.635  1.00 51.81           N  
ANISOU 1640  N   HIS A 425     7109   5612   6962    853    742    382       N  
ATOM   1641  CA  HIS A 425       4.895 -20.489  10.969  1.00 49.21           C  
ANISOU 1641  CA  HIS A 425     6834   5163   6703    900    801    258       C  
ATOM   1642  C   HIS A 425       5.047 -21.975  11.292  1.00 52.64           C  
ANISOU 1642  C   HIS A 425     7367   5357   7275    927    892    275       C  
ATOM   1643  O   HIS A 425       6.081 -22.393  11.812  1.00 56.64           O  
ANISOU 1643  O   HIS A 425     7894   5766   7862   1096    922    303       O  
ATOM   1644  CB  HIS A 425       6.173 -19.757  11.383  1.00 48.25           C  
ANISOU 1644  CB  HIS A 425     6655   5112   6564   1084    768    268       C  
ATOM   1645  CG  HIS A 425       6.126 -18.277  11.162  1.00 45.16           C  
ANISOU 1645  CG  HIS A 425     6181   4929   6048   1069    683    260       C  
ATOM   1646  ND1 HIS A 425       6.597 -17.682  10.012  1.00 48.38           N  
ANISOU 1646  ND1 HIS A 425     6571   5413   6400   1004    677    130       N  
ATOM   1647  CD2 HIS A 425       5.679 -17.272  11.950  1.00 43.71           C  
ANISOU 1647  CD2 HIS A 425     5938   4883   5787   1112    607    365       C  
ATOM   1648  CE1 HIS A 425       6.434 -16.374  10.097  1.00 48.69           C  
ANISOU 1648  CE1 HIS A 425     6547   5615   6338   1006    595    166       C  
ATOM   1649  NE2 HIS A 425       5.881 -16.099  11.264  1.00 44.42           N  
ANISOU 1649  NE2 HIS A 425     5980   5110   5787   1076    553    301       N  
ATOM   1650  N   PRO A 426       4.021 -22.782  10.975  1.00 53.69           N  
ANISOU 1650  N   PRO A 426     7563   5393   7442    757    934    261       N  
ATOM   1651  CA  PRO A 426       3.999 -24.205  11.341  1.00 58.28           C  
ANISOU 1651  CA  PRO A 426     8257   5726   8162    760   1023    293       C  
ATOM   1652  C   PRO A 426       5.185 -24.991  10.788  1.00 59.34           C  
ANISOU 1652  C   PRO A 426     8466   5677   8404    851   1104    167       C  
ATOM   1653  O   PRO A 426       5.444 -26.105  11.239  1.00 64.77           O  
ANISOU 1653  O   PRO A 426     9247   6140   9224    919   1176    212       O  
ATOM   1654  CB  PRO A 426       2.696 -24.705  10.697  1.00 57.42           C  
ANISOU 1654  CB  PRO A 426     8186   5586   8044    507   1044    241       C  
ATOM   1655  CG  PRO A 426       2.410 -23.698   9.615  1.00 58.04           C  
ANISOU 1655  CG  PRO A 426     8188   5871   7994    390    977    123       C  
ATOM   1656  CD  PRO A 426       2.799 -22.404  10.249  1.00 54.53           C  
ANISOU 1656  CD  PRO A 426     7637   5620   7464    544    894    217       C  
ATOM   1657  N   GLU A 427       5.897 -24.415   9.826  1.00 59.33           N  
ANISOU 1657  N   GLU A 427     8424   5768   8350    855   1100     15       N  
ATOM   1658  CA  GLU A 427       7.001 -25.110   9.174  1.00 63.92           C  
ANISOU 1658  CA  GLU A 427     9061   6197   9028    933   1192   -130       C  
ATOM   1659  C   GLU A 427       8.361 -24.673   9.713  1.00 62.30           C  
ANISOU 1659  C   GLU A 427     8777   6041   8853   1176   1175    -90       C  
ATOM   1660  O   GLU A 427       9.374 -25.322   9.455  1.00 60.90           O  
ANISOU 1660  O   GLU A 427     8627   5728   8783   1294   1254   -174       O  
ATOM   1661  CB  GLU A 427       6.948 -24.884   7.661  1.00 69.72           C  
ANISOU 1661  CB  GLU A 427     9808   6998   9683    763   1220   -343       C  
ATOM   1662  CG  GLU A 427       7.406 -23.496   7.220  1.00 75.47           C  
ANISOU 1662  CG  GLU A 427    10424   7978  10272    780   1148   -380       C  
ATOM   1663  CD  GLU A 427       6.482 -22.383   7.689  1.00 75.28           C  
ANISOU 1663  CD  GLU A 427    10319   8160  10126    722   1026   -246       C  
ATOM   1664  OE1 GLU A 427       5.317 -22.671   8.033  1.00 75.76           O  
ANISOU 1664  OE1 GLU A 427    10401   8200  10185    614   1003   -166       O  
ATOM   1665  OE2 GLU A 427       6.921 -21.213   7.706  1.00 74.97           O  
ANISOU 1665  OE2 GLU A 427    10190   8299   9997    782    960   -226       O  
ATOM   1666  N   SER A 428       8.379 -23.572  10.458  1.00 64.06           N  
ANISOU 1666  N   SER A 428     8898   6461   8982   1248   1073     32       N  
ATOM   1667  CA  SER A 428       9.626 -23.024  10.981  1.00 62.18           C  
ANISOU 1667  CA  SER A 428     8570   6305   8752   1452   1038     68       C  
ATOM   1668  C   SER A 428       9.902 -23.538  12.390  1.00 61.64           C  
ANISOU 1668  C   SER A 428     8510   6146   8764   1634   1016    253       C  
ATOM   1669  O   SER A 428       9.510 -22.914  13.377  1.00 60.23           O  
ANISOU 1669  O   SER A 428     8289   6086   8507   1668    933    401       O  
ATOM   1670  CB  SER A 428       9.583 -21.493  10.973  1.00 58.82           C  
ANISOU 1670  CB  SER A 428     8037   6138   8175   1423    938     82       C  
ATOM   1671  OG  SER A 428      10.857 -20.942  11.261  1.00 59.78           O  
ANISOU 1671  OG  SER A 428     8066   6345   8301   1585    910     79       O  
ATOM   1672  N   SER A 429      10.587 -24.674  12.473  1.00 60.29           N  
ANISOU 1672  N   SER A 429     8399   5764   8744   1756   1093    244       N  
ATOM   1673  CA  SER A 429      10.853 -25.331  13.751  1.00 61.65           C  
ANISOU 1673  CA  SER A 429     8600   5821   9002   1931   1076    431       C  
ATOM   1674  C   SER A 429      11.722 -24.490  14.683  1.00 53.11           C  
ANISOU 1674  C   SER A 429     7396   4918   7863   2112    974    538       C  
ATOM   1675  O   SER A 429      12.719 -23.904  14.261  1.00 52.87           O  
ANISOU 1675  O   SER A 429     7264   5001   7824   2185    959    439       O  
ATOM   1676  CB  SER A 429      11.503 -26.700  13.527  1.00 67.12           C  
ANISOU 1676  CB  SER A 429     9380   6237   9883   2041   1181    388       C  
ATOM   1677  OG  SER A 429      12.666 -26.587  12.726  1.00 69.00           O  
ANISOU 1677  OG  SER A 429     9547   6497  10171   2132   1225    225       O  
ATOM   1678  N   GLN A 430      11.334 -24.451  15.954  1.00 50.06           N  
ANISOU 1678  N   GLN A 430     7023   4563   7435   2173    908    737       N  
ATOM   1679  CA  GLN A 430      12.065 -23.711  16.980  1.00 52.90           C  
ANISOU 1679  CA  GLN A 430     7283   5092   7726   2334    801    850       C  
ATOM   1680  C   GLN A 430      12.264 -22.233  16.633  1.00 49.34           C  
ANISOU 1680  C   GLN A 430     6713   4896   7138   2275    731    756       C  
ATOM   1681  O   GLN A 430      13.260 -21.627  17.028  1.00 49.51           O  
ANISOU 1681  O   GLN A 430     6631   5047   7133   2401    662    767       O  
ATOM   1682  CB  GLN A 430      13.416 -24.373  17.269  1.00 53.03           C  
ANISOU 1682  CB  GLN A 430     7262   5014   7872   2562    805    878       C  
ATOM   1683  CG  GLN A 430      13.314 -25.798  17.804  1.00 55.98           C  
ANISOU 1683  CG  GLN A 430     7759   5124   8385   2657    860   1008       C  
ATOM   1684  CD  GLN A 430      12.616 -25.874  19.150  1.00 60.00           C  
ANISOU 1684  CD  GLN A 430     8328   5655   8816   2671    798   1240       C  
ATOM   1685  OE1 GLN A 430      12.939 -25.130  20.076  1.00 59.42           O  
ANISOU 1685  OE1 GLN A 430     8176   5771   8630   2759    691   1345       O  
ATOM   1686  NE2 GLN A 430      11.656 -26.782  19.267  1.00 63.91           N  
ANISOU 1686  NE2 GLN A 430     8964   5957   9362   2574    869   1315       N  
ATOM   1687  N   LEU A 431      11.319 -21.660  15.895  1.00 46.62           N  
ANISOU 1687  N   LEU A 431     6384   4619   6711   2082    744    670       N  
ATOM   1688  CA  LEU A 431      11.366 -20.234  15.581  1.00 47.19           C  
ANISOU 1688  CA  LEU A 431     6365   4911   6653   2017    677    600       C  
ATOM   1689  C   LEU A 431      11.248 -19.418  16.863  1.00 46.61           C  
ANISOU 1689  C   LEU A 431     6249   4990   6472   2088    576    741       C  
ATOM   1690  O   LEU A 431      11.821 -18.334  16.982  1.00 47.23           O  
ANISOU 1690  O   LEU A 431     6240   5233   6471   2119    506    709       O  
ATOM   1691  CB  LEU A 431      10.246 -19.853  14.610  1.00 43.19           C  
ANISOU 1691  CB  LEU A 431     5891   4438   6080   1805    702    510       C  
ATOM   1692  CG  LEU A 431      10.174 -18.370  14.241  1.00 39.60           C  
ANISOU 1692  CG  LEU A 431     5361   4191   5495   1733    633    453       C  
ATOM   1693  CD1 LEU A 431      11.524 -17.894  13.715  1.00 39.76           C  
ANISOU 1693  CD1 LEU A 431     5302   4278   5527   1800    629    345       C  
ATOM   1694  CD2 LEU A 431       9.070 -18.100  13.224  1.00 34.56           C  
ANISOU 1694  CD2 LEU A 431     4754   3578   4799   1535    651    376       C  
ATOM   1695  N   PHE A 432      10.497 -19.953  17.819  1.00 46.13           N  
ANISOU 1695  N   PHE A 432     6255   4869   6402   2104    576    892       N  
ATOM   1696  CA  PHE A 432      10.318 -19.317  19.118  1.00 44.79           C  
ANISOU 1696  CA  PHE A 432     6063   4835   6120   2171    495   1029       C  
ATOM   1697  C   PHE A 432      11.665 -19.186  19.826  1.00 42.62           C  
ANISOU 1697  C   PHE A 432     5721   4622   5851   2355    423   1073       C  
ATOM   1698  O   PHE A 432      12.051 -18.100  20.256  1.00 45.34           O  
ANISOU 1698  O   PHE A 432     5992   5144   6090   2384    340   1063       O  
ATOM   1699  CB  PHE A 432       9.335 -20.134  19.961  1.00 46.16           C  
ANISOU 1699  CB  PHE A 432     6330   4913   6295   2152    530   1188       C  
ATOM   1700  CG  PHE A 432       9.100 -19.584  21.340  1.00 44.70           C  
ANISOU 1700  CG  PHE A 432     6136   4866   5981   2217    463   1331       C  
ATOM   1701  CD1 PHE A 432       8.679 -18.277  21.518  1.00 42.18           C  
ANISOU 1701  CD1 PHE A 432     5762   4738   5527   2165    411   1294       C  
ATOM   1702  CD2 PHE A 432       9.274 -20.384  22.456  1.00 46.13           C  
ANISOU 1702  CD2 PHE A 432     6376   4981   6171   2329    456   1504       C  
ATOM   1703  CE1 PHE A 432       8.453 -17.772  22.787  1.00 37.91           C  
ANISOU 1703  CE1 PHE A 432     5222   4323   4858   2222    361   1408       C  
ATOM   1704  CE2 PHE A 432       9.047 -19.887  23.727  1.00 47.34           C  
ANISOU 1704  CE2 PHE A 432     6529   5273   6183   2380    399   1632       C  
ATOM   1705  CZ  PHE A 432       8.634 -18.578  23.892  1.00 42.32           C  
ANISOU 1705  CZ  PHE A 432     5838   4833   5410   2324    356   1574       C  
ATOM   1706  N   ALA A 433      12.377 -20.301  19.938  1.00 43.98           N  
ANISOU 1706  N   ALA A 433     5917   4645   6150   2478    453   1118       N  
ATOM   1707  CA  ALA A 433      13.709 -20.309  20.534  1.00 45.62           C  
ANISOU 1707  CA  ALA A 433     6042   4908   6384   2665    382   1162       C  
ATOM   1708  C   ALA A 433      14.659 -19.379  19.780  1.00 48.36           C  
ANISOU 1708  C   ALA A 433     6263   5392   6721   2659    352   1001       C  
ATOM   1709  O   ALA A 433      15.410 -18.617  20.386  1.00 50.21           O  
ANISOU 1709  O   ALA A 433     6403   5791   6884   2734    255   1019       O  
ATOM   1710  CB  ALA A 433      14.262 -21.724  20.568  1.00 49.22           C  
ANISOU 1710  CB  ALA A 433     6543   5151   7006   2801    435   1225       C  
ATOM   1711  N   LYS A 434      14.615 -19.440  18.454  1.00 48.75           N  
ANISOU 1711  N   LYS A 434     6312   5378   6833   2557    436    841       N  
ATOM   1712  CA  LYS A 434      15.495 -18.628  17.622  1.00 45.30           C  
ANISOU 1712  CA  LYS A 434     5764   5061   6388   2533    429    687       C  
ATOM   1713  C   LYS A 434      15.222 -17.136  17.795  1.00 46.85           C  
ANISOU 1713  C   LYS A 434     5915   5458   6427   2435    349    663       C  
ATOM   1714  O   LYS A 434      16.148 -16.326  17.821  1.00 50.24           O  
ANISOU 1714  O   LYS A 434     6238   6028   6822   2466    291    611       O  
ATOM   1715  CB  LYS A 434      15.372 -19.042  16.154  1.00 50.75           C  
ANISOU 1715  CB  LYS A 434     6486   5641   7154   2425    546    525       C  
ATOM   1716  CG  LYS A 434      15.964 -20.414  15.864  1.00 57.71           C  
ANISOU 1716  CG  LYS A 434     7393   6326   8208   2542    636    505       C  
ATOM   1717  CD  LYS A 434      15.583 -20.924  14.481  1.00 65.41           C  
ANISOU 1717  CD  LYS A 434     8439   7175   9240   2409    761    344       C  
ATOM   1718  CE  LYS A 434      16.149 -22.319  14.251  1.00 75.07           C  
ANISOU 1718  CE  LYS A 434     9703   8176  10643   2536    860    316       C  
ATOM   1719  NZ  LYS A 434      15.635 -22.963  13.008  1.00 79.87           N  
ANISOU 1719  NZ  LYS A 434    10412   8634  11301   2396    986    160       N  
ATOM   1720  N   LEU A 435      13.950 -16.777  17.931  1.00 39.32           N  
ANISOU 1720  N   LEU A 435     5041   4514   5385   2319    346    703       N  
ATOM   1721  CA  LEU A 435      13.574 -15.384  18.144  1.00 40.49           C  
ANISOU 1721  CA  LEU A 435     5164   4828   5394   2239    277    687       C  
ATOM   1722  C   LEU A 435      14.065 -14.865  19.496  1.00 43.13           C  
ANISOU 1722  C   LEU A 435     5454   5286   5647   2350    173    784       C  
ATOM   1723  O   LEU A 435      14.599 -13.760  19.589  1.00 43.53           O  
ANISOU 1723  O   LEU A 435     5438   5478   5624   2334    107    728       O  
ATOM   1724  CB  LEU A 435      12.059 -15.213  18.018  1.00 37.80           C  
ANISOU 1724  CB  LEU A 435     4905   4465   4991   2111    304    714       C  
ATOM   1725  CG  LEU A 435      11.498 -13.816  18.285  1.00 37.77           C  
ANISOU 1725  CG  LEU A 435     4888   4609   4856   2044    242    708       C  
ATOM   1726  CD1 LEU A 435      12.321 -12.757  17.562  1.00 40.61           C  
ANISOU 1726  CD1 LEU A 435     5177   5064   5187   2002    209    586       C  
ATOM   1727  CD2 LEU A 435      10.029 -13.738  17.872  1.00 38.94           C  
ANISOU 1727  CD2 LEU A 435     5093   4730   4972   1917    281    716       C  
ATOM   1728  N   LEU A 436      13.882 -15.663  20.543  1.00 45.18           N  
ANISOU 1728  N   LEU A 436     5760   5493   5912   2451    159    929       N  
ATOM   1729  CA  LEU A 436      14.319 -15.272  21.879  1.00 45.23           C  
ANISOU 1729  CA  LEU A 436     5737   5625   5823   2554     56   1030       C  
ATOM   1730  C   LEU A 436      15.834 -15.079  21.939  1.00 48.02           C  
ANISOU 1730  C   LEU A 436     5968   6065   6213   2657    -13    986       C  
ATOM   1731  O   LEU A 436      16.334 -14.222  22.668  1.00 47.44           O  
ANISOU 1731  O   LEU A 436     5837   6150   6037   2683   -112    992       O  
ATOM   1732  CB  LEU A 436      13.877 -16.309  22.914  1.00 47.13           C  
ANISOU 1732  CB  LEU A 436     6059   5782   6065   2643     62   1208       C  
ATOM   1733  CG  LEU A 436      12.370 -16.439  23.145  1.00 49.51           C  
ANISOU 1733  CG  LEU A 436     6467   6036   6310   2542    122   1275       C  
ATOM   1734  CD1 LEU A 436      12.090 -17.408  24.282  1.00 51.28           C  
ANISOU 1734  CD1 LEU A 436     6768   6195   6520   2630    123   1466       C  
ATOM   1735  CD2 LEU A 436      11.757 -15.082  23.435  1.00 49.11           C  
ANISOU 1735  CD2 LEU A 436     6405   6144   6109   2459     82   1231       C  
ATOM   1736  N   GLN A 437      16.562 -15.881  21.170  1.00 51.88           N  
ANISOU 1736  N   GLN A 437     6411   6452   6848   2713     43    935       N  
ATOM   1737  CA  GLN A 437      18.016 -15.783  21.135  1.00 52.08           C  
ANISOU 1737  CA  GLN A 437     6296   6563   6931   2816     -9    889       C  
ATOM   1738  C   GLN A 437      18.478 -14.477  20.496  1.00 51.63           C  
ANISOU 1738  C   GLN A 437     6150   6652   6815   2702    -33    740       C  
ATOM   1739  O   GLN A 437      19.624 -14.066  20.667  1.00 53.41           O  
ANISOU 1739  O   GLN A 437     6245   7003   7046   2756    -99    703       O  
ATOM   1740  CB  GLN A 437      18.619 -16.971  20.385  1.00 59.27           C  
ANISOU 1740  CB  GLN A 437     7179   7317   8022   2907     80    855       C  
ATOM   1741  CG  GLN A 437      18.508 -18.292  21.122  1.00 70.12           C  
ANISOU 1741  CG  GLN A 437     8623   8540   9478   3056     87   1016       C  
ATOM   1742  CD  GLN A 437      19.366 -19.374  20.498  1.00 79.56           C  
ANISOU 1742  CD  GLN A 437     9771   9594  10866   3186    161    977       C  
ATOM   1743  OE1 GLN A 437      19.846 -19.229  19.374  1.00 86.55           O  
ANISOU 1743  OE1 GLN A 437    10589  10476  11821   3138    236    813       O  
ATOM   1744  NE2 GLN A 437      19.565 -20.466  21.226  1.00 80.77           N  
ANISOU 1744  NE2 GLN A 437     9961   9624  11104   3354    147   1129       N  
ATOM   1745  N   LYS A 438      17.582 -13.829  19.757  1.00 48.95           N  
ANISOU 1745  N   LYS A 438     5879   6299   6421   2541     18    661       N  
ATOM   1746  CA  LYS A 438      17.906 -12.565  19.101  1.00 52.34           C  
ANISOU 1746  CA  LYS A 438     6251   6844   6792   2420      2    533       C  
ATOM   1747  C   LYS A 438      18.037 -11.427  20.110  1.00 53.64           C  
ANISOU 1747  C   LYS A 438     6393   7165   6824   2410   -115    561       C  
ATOM   1748  O   LYS A 438      18.477 -10.330  19.769  1.00 50.96           O  
ANISOU 1748  O   LYS A 438     6000   6926   6436   2320   -145    467       O  
ATOM   1749  CB  LYS A 438      16.866 -12.226  18.030  1.00 51.86           C  
ANISOU 1749  CB  LYS A 438     6277   6718   6709   2261     80    460       C  
ATOM   1750  CG  LYS A 438      16.918 -13.146  16.820  1.00 52.41           C  
ANISOU 1750  CG  LYS A 438     6359   6661   6892   2234    196    384       C  
ATOM   1751  CD  LYS A 438      18.288 -13.095  16.161  1.00 51.59           C  
ANISOU 1751  CD  LYS A 438     6130   6612   6860   2260    222    277       C  
ATOM   1752  CE  LYS A 438      18.428 -14.156  15.082  1.00 57.80           C  
ANISOU 1752  CE  LYS A 438     6933   7266   7765   2263    348    196       C  
ATOM   1753  NZ  LYS A 438      18.606 -15.514  15.672  1.00 67.19           N  
ANISOU 1753  NZ  LYS A 438     8135   8324   9070   2428    369    281       N  
ATOM   1754  N   MET A 439      17.658 -11.699  21.354  1.00 58.36           N  
ANISOU 1754  N   MET A 439     7039   7780   7357   2495   -175    688       N  
ATOM   1755  CA  MET A 439      17.802 -10.724  22.427  1.00 55.74           C  
ANISOU 1755  CA  MET A 439     6695   7596   6886   2495   -285    711       C  
ATOM   1756  C   MET A 439      19.272 -10.451  22.717  1.00 63.12           C  
ANISOU 1756  C   MET A 439     7485   8664   7834   2553   -375    675       C  
ATOM   1757  O   MET A 439      19.648  -9.337  23.083  1.00 68.53           O  
ANISOU 1757  O   MET A 439     8133   9482   8425   2491   -453    617       O  
ATOM   1758  CB  MET A 439      17.105 -11.219  23.694  1.00 52.20           C  
ANISOU 1758  CB  MET A 439     6334   7143   6357   2577   -318    861       C  
ATOM   1759  CG  MET A 439      15.599 -11.335  23.560  1.00 51.02           C  
ANISOU 1759  CG  MET A 439     6311   6896   6177   2506   -236    897       C  
ATOM   1760  SD  MET A 439      14.875  -9.834  22.874  1.00 88.70           S  
ANISOU 1760  SD  MET A 439    11116  11711  10877   2343   -217    768       S  
ATOM   1761  CE  MET A 439      15.467  -8.603  24.034  1.00 62.19           C  
ANISOU 1761  CE  MET A 439     7730   8530   7368   2355   -340    744       C  
ATOM   1762  N   THR A 440      20.098 -11.477  22.550  1.00 62.03           N  
ANISOU 1762  N   THR A 440     7261   8488   7820   2672   -362    707       N  
ATOM   1763  CA  THR A 440      21.533 -11.352  22.767  1.00 64.32           C  
ANISOU 1763  CA  THR A 440     7382   8912   8146   2743   -444    679       C  
ATOM   1764  C   THR A 440      22.130 -10.288  21.853  1.00 63.62           C  
ANISOU 1764  C   THR A 440     7205   8906   8062   2602   -427    518       C  
ATOM   1765  O   THR A 440      22.831  -9.384  22.306  1.00 65.25           O  
ANISOU 1765  O   THR A 440     7325   9269   8196   2559   -524    474       O  
ATOM   1766  CB  THR A 440      22.254 -12.690  22.520  1.00 63.80           C  
ANISOU 1766  CB  THR A 440     7235   8763   8244   2905   -405    728       C  
ATOM   1767  OG1 THR A 440      21.761 -13.676  23.436  1.00 64.18           O  
ANISOU 1767  OG1 THR A 440     7372   8725   8287   3036   -428    898       O  
ATOM   1768  CG2 THR A 440      23.755 -12.530  22.707  1.00 65.10           C  
ANISOU 1768  CG2 THR A 440     7194   9085   8455   2982   -491    697       C  
ATOM   1769  N   ASP A 441      21.848 -10.405  20.562  1.00 62.62           N  
ANISOU 1769  N   ASP A 441     7106   8676   8013   2519   -303    429       N  
ATOM   1770  CA  ASP A 441      22.345  -9.449  19.582  1.00 66.92           C  
ANISOU 1770  CA  ASP A 441     7584   9285   8558   2374   -269    288       C  
ATOM   1771  C   ASP A 441      21.747  -8.068  19.828  1.00 61.50           C  
ANISOU 1771  C   ASP A 441     6981   8655   7732   2229   -321    254       C  
ATOM   1772  O   ASP A 441      22.408  -7.046  19.640  1.00 62.02           O  
ANISOU 1772  O   ASP A 441     6978   8826   7763   2126   -358    169       O  
ATOM   1773  CB  ASP A 441      22.005  -9.924  18.170  1.00 73.04           C  
ANISOU 1773  CB  ASP A 441     8400   9932   9421   2312   -123    212       C  
ATOM   1774  CG  ASP A 441      22.424 -11.360  17.924  1.00 83.09           C  
ANISOU 1774  CG  ASP A 441     9625  11108  10839   2460    -53    237       C  
ATOM   1775  OD1 ASP A 441      23.491 -11.770  18.431  1.00 90.22           O  
ANISOU 1775  OD1 ASP A 441    10388  12085  11809   2594   -104    265       O  
ATOM   1776  OD2 ASP A 441      21.686 -12.080  17.220  1.00 84.54           O  
ANISOU 1776  OD2 ASP A 441     9909  11140  11073   2444     51    227       O  
ATOM   1777  N   LEU A 442      20.491  -8.050  20.257  1.00 53.49           N  
ANISOU 1777  N   LEU A 442     6115   7564   6643   2223   -318    322       N  
ATOM   1778  CA  LEU A 442      19.781  -6.802  20.498  1.00 51.90           C  
ANISOU 1778  CA  LEU A 442     6007   7392   6321   2109   -354    294       C  
ATOM   1779  C   LEU A 442      20.477  -5.985  21.588  1.00 51.31           C  
ANISOU 1779  C   LEU A 442     5878   7465   6152   2112   -479    284       C  
ATOM   1780  O   LEU A 442      20.817  -4.820  21.382  1.00 51.57           O  
ANISOU 1780  O   LEU A 442     5897   7559   6139   1991   -509    193       O  
ATOM   1781  CB  LEU A 442      18.328  -7.095  20.874  1.00 50.73           C  
ANISOU 1781  CB  LEU A 442     6003   7148   6122   2130   -323    378       C  
ATOM   1782  CG  LEU A 442      17.272  -6.051  20.515  1.00 51.20           C  
ANISOU 1782  CG  LEU A 442     6170   7174   6110   2011   -299    338       C  
ATOM   1783  CD1 LEU A 442      17.494  -5.513  19.105  1.00 47.82           C  
ANISOU 1783  CD1 LEU A 442     5725   6717   5730   1883   -241    237       C  
ATOM   1784  CD2 LEU A 442      15.879  -6.648  20.654  1.00 49.39           C  
ANISOU 1784  CD2 LEU A 442     6047   6849   5871   2039   -244    421       C  
ATOM   1785  N   ARG A 443      20.702  -6.604  22.742  1.00 53.46           N  
ANISOU 1785  N   ARG A 443     6127   7794   6391   2243   -555    380       N  
ATOM   1786  CA  ARG A 443      21.364  -5.921  23.849  1.00 59.19           C  
ANISOU 1786  CA  ARG A 443     6802   8677   7010   2246   -687    373       C  
ATOM   1787  C   ARG A 443      22.815  -5.566  23.532  1.00 57.29           C  
ANISOU 1787  C   ARG A 443     6384   8559   6824   2207   -739    288       C  
ATOM   1788  O   ARG A 443      23.370  -4.627  24.099  1.00 59.12           O  
ANISOU 1788  O   ARG A 443     6575   8919   6970   2135   -836    230       O  
ATOM   1789  CB  ARG A 443      21.276  -6.752  25.130  1.00 67.44           C  
ANISOU 1789  CB  ARG A 443     7864   9765   7996   2398   -759    512       C  
ATOM   1790  CG  ARG A 443      19.853  -6.922  25.635  1.00 71.91           C  
ANISOU 1790  CG  ARG A 443     8599  10244   8480   2415   -713    593       C  
ATOM   1791  CD  ARG A 443      19.811  -7.255  27.112  1.00 73.38           C  
ANISOU 1791  CD  ARG A 443     8818  10522   8540   2517   -807    709       C  
ATOM   1792  NE  ARG A 443      18.441  -7.459  27.572  1.00 77.27           N  
ANISOU 1792  NE  ARG A 443     9464  10939   8957   2528   -744    787       N  
ATOM   1793  CZ  ARG A 443      18.117  -7.906  28.780  1.00 81.69           C  
ANISOU 1793  CZ  ARG A 443    10084  11551   9402   2612   -788    910       C  
ATOM   1794  NH1 ARG A 443      19.069  -8.198  29.657  1.00 83.46           N  
ANISOU 1794  NH1 ARG A 443    10237  11906   9570   2699   -910    975       N  
ATOM   1795  NH2 ARG A 443      16.842  -8.063  29.111  1.00 80.68           N  
ANISOU 1795  NH2 ARG A 443    10085  11359   9212   2606   -711    973       N  
ATOM   1796  N   GLN A 444      23.425  -6.319  22.625  1.00 56.94           N  
ANISOU 1796  N   GLN A 444     6233   8478   6922   2248   -669    272       N  
ATOM   1797  CA  GLN A 444      24.780  -6.018  22.187  1.00 61.33           C  
ANISOU 1797  CA  GLN A 444     6603   9155   7545   2205   -693    185       C  
ATOM   1798  C   GLN A 444      24.776  -4.703  21.418  1.00 56.71           C  
ANISOU 1798  C   GLN A 444     6046   8577   6924   1998   -658     58       C  
ATOM   1799  O   GLN A 444      25.644  -3.853  21.612  1.00 53.65           O  
ANISOU 1799  O   GLN A 444     5559   8321   6504   1904   -730    -15       O  
ATOM   1800  CB  GLN A 444      25.319  -7.140  21.301  1.00 71.14           C  
ANISOU 1800  CB  GLN A 444     7737  10339   8952   2300   -596    186       C  
ATOM   1801  CG  GLN A 444      26.832  -7.207  21.250  1.00 84.17           C  
ANISOU 1801  CG  GLN A 444     9153  12146  10684   2337   -642    139       C  
ATOM   1802  CD  GLN A 444      27.429  -7.676  22.561  1.00 97.51           C  
ANISOU 1802  CD  GLN A 444    10745  13958  12347   2494   -790    244       C  
ATOM   1803  OE1 GLN A 444      28.558  -7.325  22.904  1.00103.20           O  
ANISOU 1803  OE1 GLN A 444    11282  14857  13071   2488   -887    210       O  
ATOM   1804  NE2 GLN A 444      26.669  -8.472  23.307  1.00100.59           N  
ANISOU 1804  NE2 GLN A 444    11255  14259  12704   2628   -814    378       N  
ATOM   1805  N   ILE A 445      23.783  -4.543  20.549  1.00 56.46           N  
ANISOU 1805  N   ILE A 445     6152   8404   6897   1923   -551     38       N  
ATOM   1806  CA  ILE A 445      23.630  -3.326  19.760  1.00 58.17           C  
ANISOU 1806  CA  ILE A 445     6424   8600   7078   1734   -512    -58       C  
ATOM   1807  C   ILE A 445      23.562  -2.071  20.626  1.00 55.56           C  
ANISOU 1807  C   ILE A 445     6152   8332   6625   1645   -615    -91       C  
ATOM   1808  O   ILE A 445      24.240  -1.082  20.348  1.00 55.42           O  
ANISOU 1808  O   ILE A 445     6087   8377   6595   1502   -636   -180       O  
ATOM   1809  CB  ILE A 445      22.366  -3.384  18.885  1.00 61.30           C  
ANISOU 1809  CB  ILE A 445     6978   8837   7477   1691   -407    -45       C  
ATOM   1810  CG1 ILE A 445      22.557  -4.378  17.741  1.00 65.64           C  
ANISOU 1810  CG1 ILE A 445     7474   9326   8140   1718   -291    -59       C  
ATOM   1811  CG2 ILE A 445      22.031  -2.005  18.340  1.00 61.49           C  
ANISOU 1811  CG2 ILE A 445     7091   8832   7440   1515   -396   -113       C  
ATOM   1812  CD1 ILE A 445      21.320  -4.560  16.897  1.00 69.18           C  
ANISOU 1812  CD1 ILE A 445     8067   9633   8584   1674   -200    -43       C  
ATOM   1813  N   VAL A 446      22.744  -2.114  21.674  1.00 54.45           N  
ANISOU 1813  N   VAL A 446     6122   8172   6395   1722   -669    -25       N  
ATOM   1814  CA  VAL A 446      22.543  -0.946  22.528  1.00 55.99           C  
ANISOU 1814  CA  VAL A 446     6400   8410   6465   1646   -752    -68       C  
ATOM   1815  C   VAL A 446      23.810  -0.546  23.289  1.00 59.16           C  
ANISOU 1815  C   VAL A 446     6666   8986   6827   1613   -875   -119       C  
ATOM   1816  O   VAL A 446      24.117   0.640  23.410  1.00 60.23           O  
ANISOU 1816  O   VAL A 446     6823   9157   6905   1470   -920   -214       O  
ATOM   1817  CB  VAL A 446      21.367  -1.143  23.518  1.00 60.15           C  
ANISOU 1817  CB  VAL A 446     7070   8892   6894   1743   -769     10       C  
ATOM   1818  CG1 VAL A 446      20.123  -1.602  22.776  1.00 57.17           C  
ANISOU 1818  CG1 VAL A 446     6799   8359   6563   1771   -654     64       C  
ATOM   1819  CG2 VAL A 446      21.735  -2.137  24.602  1.00 66.55           C  
ANISOU 1819  CG2 VAL A 446     7813   9800   7674   1895   -846    105       C  
ATOM   1820  N   THR A 447      24.546  -1.533  23.793  1.00 58.57           N  
ANISOU 1820  N   THR A 447     6452   9015   6785   1743   -933    -56       N  
ATOM   1821  CA  THR A 447      25.778  -1.254  24.525  1.00 62.29           C  
ANISOU 1821  CA  THR A 447     6768   9678   7221   1722  -1065    -93       C  
ATOM   1822  C   THR A 447      26.778  -0.551  23.614  1.00 63.18           C  
ANISOU 1822  C   THR A 447     6751   9845   7409   1561  -1041   -208       C  
ATOM   1823  O   THR A 447      27.455   0.393  24.022  1.00 63.92           O  
ANISOU 1823  O   THR A 447     6794  10051   7443   1432  -1129   -293       O  
ATOM   1824  CB  THR A 447      26.415  -2.540  25.093  1.00 67.67           C  
ANISOU 1824  CB  THR A 447     7305  10457   7950   1913  -1128     15       C  
ATOM   1825  OG1 THR A 447      26.698  -3.448  24.022  1.00 73.45           O  
ANISOU 1825  OG1 THR A 447     7942  11119   8845   1980  -1019     35       O  
ATOM   1826  CG2 THR A 447      25.478  -3.212  26.086  1.00 65.14           C  
ANISOU 1826  CG2 THR A 447     7119  10093   7540   2057  -1156    142       C  
ATOM   1827  N   GLU A 448      26.857  -1.015  22.372  1.00 62.18           N  
ANISOU 1827  N   GLU A 448     6576   9640   7408   1557   -915   -215       N  
ATOM   1828  CA  GLU A 448      27.737  -0.410  21.384  1.00 61.64           C  
ANISOU 1828  CA  GLU A 448     6393   9618   7409   1398   -864   -317       C  
ATOM   1829  C   GLU A 448      27.277   1.012  21.064  1.00 57.75           C  
ANISOU 1829  C   GLU A 448     6051   9048   6845   1194   -845   -398       C  
ATOM   1830  O   GLU A 448      28.081   1.943  21.013  1.00 56.80           O  
ANISOU 1830  O   GLU A 448     5859   9011   6711   1030   -885   -487       O  
ATOM   1831  CB  GLU A 448      27.759  -1.262  20.114  1.00 64.13           C  
ANISOU 1831  CB  GLU A 448     6657   9855   7853   1444   -717   -307       C  
ATOM   1832  CG  GLU A 448      28.846  -0.891  19.125  1.00 72.54           C  
ANISOU 1832  CG  GLU A 448     7560  11004   8997   1308   -652   -402       C  
ATOM   1833  CD  GLU A 448      28.847  -1.789  17.899  1.00 78.08           C  
ANISOU 1833  CD  GLU A 448     8222  11633   9811   1361   -497   -403       C  
ATOM   1834  OE1 GLU A 448      27.807  -2.426  17.624  1.00 76.06           O  
ANISOU 1834  OE1 GLU A 448     8112  11228   9559   1447   -432   -346       O  
ATOM   1835  OE2 GLU A 448      29.887  -1.855  17.211  1.00 80.72           O  
ANISOU 1835  OE2 GLU A 448     8377  12066  10226   1309   -437   -469       O  
ATOM   1836  N   HIS A 449      25.975   1.172  20.858  1.00 55.52           N  
ANISOU 1836  N   HIS A 449     5974   8599   6522   1205   -785   -363       N  
ATOM   1837  CA  HIS A 449      25.402   2.471  20.531  1.00 59.91           C  
ANISOU 1837  CA  HIS A 449     6691   9050   7022   1043   -761   -423       C  
ATOM   1838  C   HIS A 449      25.702   3.511  21.609  1.00 63.04           C  
ANISOU 1838  C   HIS A 449     7120   9516   7316    955   -881   -490       C  
ATOM   1839  O   HIS A 449      26.082   4.642  21.307  1.00 65.32           O  
ANISOU 1839  O   HIS A 449     7435   9791   7593    772   -885   -577       O  
ATOM   1840  CB  HIS A 449      23.893   2.346  20.324  1.00 62.63           C  
ANISOU 1840  CB  HIS A 449     7230   9225   7340   1110   -695   -358       C  
ATOM   1841  CG  HIS A 449      23.239   3.613  19.870  1.00 66.87           C  
ANISOU 1841  CG  HIS A 449     7931   9637   7838    971   -663   -403       C  
ATOM   1842  ND1 HIS A 449      23.183   3.988  18.545  1.00 66.87           N  
ANISOU 1842  ND1 HIS A 449     7962   9555   7890    854   -572   -418       N  
ATOM   1843  CD2 HIS A 449      22.614   4.592  20.565  1.00 68.01           C  
ANISOU 1843  CD2 HIS A 449     8223   9719   7898    937   -710   -432       C  
ATOM   1844  CE1 HIS A 449      22.551   5.144  18.443  1.00 68.38           C  
ANISOU 1844  CE1 HIS A 449     8312   9632   8036    759   -571   -441       C  
ATOM   1845  NE2 HIS A 449      22.196   5.532  19.655  1.00 67.88           N  
ANISOU 1845  NE2 HIS A 449     8321   9573   7898    811   -650   -457       N  
ATOM   1846  N   VAL A 450      25.528   3.121  22.867  1.00 63.50           N  
ANISOU 1846  N   VAL A 450     7187   9645   7294   1079   -976   -450       N  
ATOM   1847  CA  VAL A 450      25.775   4.018  23.989  1.00 61.08           C  
ANISOU 1847  CA  VAL A 450     6921   9417   6869   1005  -1095   -522       C  
ATOM   1848  C   VAL A 450      27.213   4.527  23.991  1.00 65.22           C  
ANISOU 1848  C   VAL A 450     7269  10098   7414    857  -1171   -613       C  
ATOM   1849  O   VAL A 450      27.465   5.705  24.248  1.00 67.20           O  
ANISOU 1849  O   VAL A 450     7577  10350   7606    687  -1218   -717       O  
ATOM   1850  CB  VAL A 450      25.473   3.328  25.331  1.00 61.85           C  
ANISOU 1850  CB  VAL A 450     7033   9600   6865   1172  -1185   -450       C  
ATOM   1851  CG1 VAL A 450      26.078   4.114  26.486  1.00 61.60           C  
ANISOU 1851  CG1 VAL A 450     6991   9708   6705   1085  -1327   -536       C  
ATOM   1852  CG2 VAL A 450      23.969   3.155  25.510  1.00 58.99           C  
ANISOU 1852  CG2 VAL A 450     6869   9088   6455   1274  -1114   -385       C  
ATOM   1853  N   GLN A 451      28.155   3.634  23.704  1.00 65.39           N  
ANISOU 1853  N   GLN A 451     7071  10250   7525    921  -1179   -577       N  
ATOM   1854  CA  GLN A 451      29.562   4.009  23.654  1.00 69.55           C  
ANISOU 1854  CA  GLN A 451     7389  10950   8087    788  -1245   -657       C  
ATOM   1855  C   GLN A 451      29.807   5.084  22.599  1.00 67.70           C  
ANISOU 1855  C   GLN A 451     7187  10636   7900    555  -1159   -752       C  
ATOM   1856  O   GLN A 451      30.590   6.009  22.814  1.00 68.95           O  
ANISOU 1856  O   GLN A 451     7286  10881   8032    369  -1225   -850       O  
ATOM   1857  CB  GLN A 451      30.442   2.786  23.383  1.00 75.16           C  
ANISOU 1857  CB  GLN A 451     7852  11796   8910    925  -1241   -596       C  
ATOM   1858  CG  GLN A 451      30.527   1.813  24.548  1.00 80.79           C  
ANISOU 1858  CG  GLN A 451     8495  12625   9575   1135  -1361   -499       C  
ATOM   1859  CD  GLN A 451      31.444   0.639  24.263  1.00 89.44           C  
ANISOU 1859  CD  GLN A 451     9343  13840  10802   1284  -1357   -437       C  
ATOM   1860  OE1 GLN A 451      31.686   0.290  23.107  1.00 92.64           O  
ANISOU 1860  OE1 GLN A 451     9669  14192  11336   1278  -1226   -452       O  
ATOM   1861  NE2 GLN A 451      31.960   0.021  25.321  1.00 91.78           N  
ANISOU 1861  NE2 GLN A 451     9516  14297  11060   1424  -1501   -368       N  
ATOM   1862  N   LEU A 452      29.131   4.960  21.462  1.00 64.15           N  
ANISOU 1862  N   LEU A 452     6836  10024   7515    557  -1014   -717       N  
ATOM   1863  CA  LEU A 452      29.280   5.927  20.379  1.00 65.93           C  
ANISOU 1863  CA  LEU A 452     7112  10161   7778    343   -923   -781       C  
ATOM   1864  C   LEU A 452      28.729   7.301  20.759  1.00 63.17           C  
ANISOU 1864  C   LEU A 452     6974   9686   7340    196   -960   -845       C  
ATOM   1865  O   LEU A 452      29.309   8.328  20.407  1.00 66.75           O  
ANISOU 1865  O   LEU A 452     7428  10133   7800    -22   -955   -926       O  
ATOM   1866  CB  LEU A 452      28.613   5.417  19.100  1.00 67.59           C  
ANISOU 1866  CB  LEU A 452     7390  10235   8057    389   -771   -720       C  
ATOM   1867  CG  LEU A 452      29.330   4.269  18.387  1.00 72.05           C  
ANISOU 1867  CG  LEU A 452     7747  10902   8728    475   -697   -694       C  
ATOM   1868  CD1 LEU A 452      28.570   3.851  17.138  1.00 71.51           C  
ANISOU 1868  CD1 LEU A 452     7779  10690   8701    499   -549   -649       C  
ATOM   1869  CD2 LEU A 452      30.760   4.663  18.044  1.00 74.59           C  
ANISOU 1869  CD2 LEU A 452     7852  11388   9102    312   -697   -776       C  
ATOM   1870  N   LEU A 453      27.610   7.316  21.477  1.00 55.27           N  
ANISOU 1870  N   LEU A 453     6156   8582   6261    315   -988   -810       N  
ATOM   1871  CA  LEU A 453      27.014   8.567  21.934  1.00 55.66           C  
ANISOU 1871  CA  LEU A 453     6414   8502   6230    211  -1016   -877       C  
ATOM   1872  C   LEU A 453      27.940   9.296  22.906  1.00 61.08           C  
ANISOU 1872  C   LEU A 453     7039   9319   6848     75  -1144   -990       C  
ATOM   1873  O   LEU A 453      27.998  10.526  22.923  1.00 65.86           O  
ANISOU 1873  O   LEU A 453     7763   9834   7427   -108  -1153  -1083       O  
ATOM   1874  CB  LEU A 453      25.663   8.309  22.602  1.00 54.73           C  
ANISOU 1874  CB  LEU A 453     6473   8280   6043    389  -1015   -820       C  
ATOM   1875  CG  LEU A 453      24.537   7.737  21.740  1.00 56.45           C  
ANISOU 1875  CG  LEU A 453     6782   8352   6313    509   -899   -716       C  
ATOM   1876  CD1 LEU A 453      23.315   7.462  22.600  1.00 57.55           C  
ANISOU 1876  CD1 LEU A 453     7060   8430   6377    677   -909   -667       C  
ATOM   1877  CD2 LEU A 453      24.186   8.676  20.594  1.00 56.73           C  
ANISOU 1877  CD2 LEU A 453     6942   8217   6396    366   -811   -730       C  
ATOM   1878  N   GLN A 454      28.662   8.531  23.718  1.00 59.16           N  
ANISOU 1878  N   GLN A 454     6615   9288   6577    162  -1247   -980       N  
ATOM   1879  CA  GLN A 454      29.579   9.113  24.690  1.00 59.21           C  
ANISOU 1879  CA  GLN A 454     6539   9455   6506     37  -1389  -1084       C  
ATOM   1880  C   GLN A 454      30.719   9.849  23.994  1.00 59.25           C  
ANISOU 1880  C   GLN A 454     6414   9517   6583   -212  -1379  -1173       C  
ATOM   1881  O   GLN A 454      31.187  10.882  24.472  1.00 64.59           O  
ANISOU 1881  O   GLN A 454     7123  10216   7203   -408  -1454  -1291       O  
ATOM   1882  CB  GLN A 454      30.128   8.036  25.627  1.00 66.42           C  
ANISOU 1882  CB  GLN A 454     7265  10597   7376    200  -1508  -1029       C  
ATOM   1883  CG  GLN A 454      29.075   7.412  26.532  1.00 71.77           C  
ANISOU 1883  CG  GLN A 454     8079  11237   7952    415  -1534   -947       C  
ATOM   1884  CD  GLN A 454      29.642   6.328  27.433  1.00 78.75           C  
ANISOU 1884  CD  GLN A 454     8787  12342   8792    577  -1656   -869       C  
ATOM   1885  OE1 GLN A 454      28.949   5.809  28.310  1.00 80.91           O  
ANISOU 1885  OE1 GLN A 454     9155  12623   8965    737  -1694   -799       O  
ATOM   1886  NE2 GLN A 454      30.908   5.982  27.221  1.00 79.98           N  
ANISOU 1886  NE2 GLN A 454     8683  12682   9024    540  -1715   -875       N  
ATOM   1887  N   VAL A 455      31.159   9.315  22.860  1.00 58.40           N  
ANISOU 1887  N   VAL A 455     6161   9432   6597   -214  -1280  -1121       N  
ATOM   1888  CA  VAL A 455      32.212   9.952  22.081  1.00 61.89           C  
ANISOU 1888  CA  VAL A 455     6471   9933   7112   -454  -1244  -1193       C  
ATOM   1889  C   VAL A 455      31.775  11.325  21.577  1.00 59.57           C  
ANISOU 1889  C   VAL A 455     6407   9421   6806   -669  -1179  -1256       C  
ATOM   1890  O   VAL A 455      32.436  12.332  21.835  1.00 61.72           O  
ANISOU 1890  O   VAL A 455     6674   9720   7055   -898  -1235  -1364       O  
ATOM   1891  CB  VAL A 455      32.630   9.086  20.879  1.00 63.78           C  
ANISOU 1891  CB  VAL A 455     6536  10223   7476   -401  -1119  -1125       C  
ATOM   1892  CG1 VAL A 455      33.479   9.897  19.913  1.00 65.24           C  
ANISOU 1892  CG1 VAL A 455     6642  10423   7725   -670  -1043  -1193       C  
ATOM   1893  CG2 VAL A 455      33.376   7.846  21.350  1.00 65.09           C  
ANISOU 1893  CG2 VAL A 455     6433  10617   7680   -219  -1189  -1081       C  
ATOM   1894  N   ILE A 456      30.657  11.361  20.859  1.00 59.44           N  
ANISOU 1894  N   ILE A 456     6592   9187   6807   -596  -1066  -1184       N  
ATOM   1895  CA  ILE A 456      30.164  12.609  20.283  1.00 62.95           C  
ANISOU 1895  CA  ILE A 456     7263   9404   7252   -771   -999  -1216       C  
ATOM   1896  C   ILE A 456      29.887  13.666  21.353  1.00 61.34           C  
ANISOU 1896  C   ILE A 456     7236   9112   6957   -854  -1094  -1319       C  
ATOM   1897  O   ILE A 456      30.099  14.856  21.126  1.00 62.78           O  
ANISOU 1897  O   ILE A 456     7532   9173   7146  -1076  -1081  -1394       O  
ATOM   1898  CB  ILE A 456      28.905  12.389  19.414  1.00 64.84           C  
ANISOU 1898  CB  ILE A 456     7683   9438   7516   -645   -881  -1108       C  
ATOM   1899  CG1 ILE A 456      27.793  11.730  20.230  1.00 66.42           C  
ANISOU 1899  CG1 ILE A 456     7981   9599   7658   -389   -918  -1054       C  
ATOM   1900  CG2 ILE A 456      29.240  11.542  18.192  1.00 64.55           C  
ANISOU 1900  CG2 ILE A 456     7499   9468   7562   -621   -772  -1032       C  
ATOM   1901  CD1 ILE A 456      26.629  11.250  19.392  1.00 68.14           C  
ANISOU 1901  CD1 ILE A 456     8316   9668   7907   -247   -812   -940       C  
ATOM   1902  N   LYS A 457      29.424  13.226  22.519  1.00 58.20           N  
ANISOU 1902  N   LYS A 457     6869   8773   6473   -679  -1183  -1324       N  
ATOM   1903  CA  LYS A 457      29.175  14.138  23.632  1.00 61.59           C  
ANISOU 1903  CA  LYS A 457     7461   9143   6798   -743  -1272  -1438       C  
ATOM   1904  C   LYS A 457      30.439  14.907  24.019  1.00 66.36           C  
ANISOU 1904  C   LYS A 457     7957   9872   7383  -1003  -1366  -1575       C  
ATOM   1905  O   LYS A 457      30.369  16.053  24.464  1.00 71.12           O  
ANISOU 1905  O   LYS A 457     8729  10355   7938  -1163  -1398  -1693       O  
ATOM   1906  CB  LYS A 457      28.631  13.375  24.842  1.00 59.36           C  
ANISOU 1906  CB  LYS A 457     7187   8959   6408   -515  -1353  -1414       C  
ATOM   1907  N   LYS A 458      31.594  14.272  23.842  1.00 64.87           N  
ANISOU 1907  N   LYS A 458     7482   9925   7241  -1048  -1407  -1563       N  
ATOM   1908  CA  LYS A 458      32.870  14.888  24.191  1.00 62.60           C  
ANISOU 1908  CA  LYS A 458     7043   9800   6943  -1298  -1504  -1687       C  
ATOM   1909  C   LYS A 458      33.487  15.660  23.026  1.00 60.10           C  
ANISOU 1909  C   LYS A 458     6700   9403   6730  -1561  -1405  -1713       C  
ATOM   1910  O   LYS A 458      34.187  16.653  23.233  1.00 65.89           O  
ANISOU 1910  O   LYS A 458     7437  10145   7453  -1829  -1454  -1835       O  
ATOM   1911  CB  LYS A 458      33.853  13.828  24.694  1.00 65.25           C  
ANISOU 1911  CB  LYS A 458     7056  10462   7275  -1206  -1613  -1661       C  
ATOM   1912  CG  LYS A 458      33.541  13.301  26.085  1.00 65.76           C  
ANISOU 1912  CG  LYS A 458     7135  10648   7204  -1022  -1754  -1661       C  
ATOM   1913  CD  LYS A 458      34.585  12.291  26.536  1.00 68.79           C  
ANISOU 1913  CD  LYS A 458     7191  11353   7592   -934  -1873  -1621       C  
ATOM   1914  CE  LYS A 458      34.429  11.954  28.011  1.00 72.16           C  
ANISOU 1914  CE  LYS A 458     7636  11923   7857   -805  -2038  -1631       C  
ATOM   1915  NZ  LYS A 458      34.563  13.165  28.870  1.00 76.99           N  
ANISOU 1915  NZ  LYS A 458     8386  12526   8340  -1026  -2141  -1801       N  
ATOM   1916  N   THR A 459      33.225  15.205  21.805  1.00 55.64           N  
ANISOU 1916  N   THR A 459     6118   8763   6260  -1498  -1263  -1600       N  
ATOM   1917  CA  THR A 459      33.822  15.818  20.622  1.00 63.84           C  
ANISOU 1917  CA  THR A 459     7122   9748   7387  -1739  -1155  -1604       C  
ATOM   1918  C   THR A 459      32.950  16.918  20.014  1.00 62.80           C  
ANISOU 1918  C   THR A 459     7309   9290   7262  -1847  -1061  -1593       C  
ATOM   1919  O   THR A 459      33.464  17.858  19.409  1.00 63.39           O  
ANISOU 1919  O   THR A 459     7424   9284   7377  -2115  -1011  -1634       O  
ATOM   1920  CB  THR A 459      34.159  14.764  19.548  1.00 66.59           C  
ANISOU 1920  CB  THR A 459     7264  10215   7825  -1643  -1045  -1499       C  
ATOM   1921  OG1 THR A 459      32.983  14.011  19.227  1.00 70.52           O  
ANISOU 1921  OG1 THR A 459     7890  10584   8318  -1381   -976  -1383       O  
ATOM   1922  CG2 THR A 459      35.234  13.814  20.054  1.00 72.05           C  
ANISOU 1922  CG2 THR A 459     7612  11227   8535  -1570  -1132  -1517       C  
ATOM   1923  N   GLU A 460      31.635  16.794  20.170  1.00 60.35           N  
ANISOU 1923  N   GLU A 460     7220   8795   6916  -1637  -1038  -1531       N  
ATOM   1924  CA  GLU A 460      30.707  17.831  19.718  1.00 65.03           C  
ANISOU 1924  CA  GLU A 460     8120   9072   7516  -1697   -965  -1514       C  
ATOM   1925  C   GLU A 460      29.952  18.459  20.882  1.00 63.42           C  
ANISOU 1925  C   GLU A 460     8134   8730   7232  -1632  -1044  -1601       C  
ATOM   1926  O   GLU A 460      28.811  18.094  21.166  1.00 62.32           O  
ANISOU 1926  O   GLU A 460     8124   8496   7060  -1396  -1030  -1543       O  
ATOM   1927  CB  GLU A 460      29.714  17.281  18.693  1.00 67.93           C  
ANISOU 1927  CB  GLU A 460     8574   9315   7923  -1520   -849  -1361       C  
ATOM   1928  CG  GLU A 460      30.117  17.523  17.250  1.00 74.47           C  
ANISOU 1928  CG  GLU A 460     9378  10097   8820  -1690   -729  -1291       C  
ATOM   1929  CD  GLU A 460      31.267  16.646  16.813  1.00 75.48           C  
ANISOU 1929  CD  GLU A 460     9192  10498   8987  -1736   -704  -1287       C  
ATOM   1930  OE1 GLU A 460      31.232  15.435  17.112  1.00 75.26           O  
ANISOU 1930  OE1 GLU A 460     9005  10636   8956  -1518   -728  -1253       O  
ATOM   1931  OE2 GLU A 460      32.200  17.166  16.166  1.00 76.20           O  
ANISOU 1931  OE2 GLU A 460     9200  10636   9118  -1988   -653  -1315       O  
ATOM   1932  N   THR A 461      30.593  19.412  21.547  1.00 65.64           N  
ANISOU 1932  N   THR A 461     8455   9005   7481  -1852  -1120  -1748       N  
ATOM   1933  CA  THR A 461      29.994  20.072  22.697  1.00 65.61           C  
ANISOU 1933  CA  THR A 461     8659   8880   7391  -1816  -1191  -1861       C  
ATOM   1934  C   THR A 461      28.910  21.061  22.276  1.00 60.35           C  
ANISOU 1934  C   THR A 461     8314   7855   6760  -1809  -1100  -1841       C  
ATOM   1935  O   THR A 461      28.199  21.605  23.116  1.00 57.03           O  
ANISOU 1935  O   THR A 461     8095   7292   6281  -1739  -1128  -1926       O  
ATOM   1936  CB  THR A 461      31.056  20.806  23.530  1.00 68.93           C  
ANISOU 1936  CB  THR A 461     9025   9405   7761  -2076  -1304  -2041       C  
ATOM   1937  OG1 THR A 461      31.758  21.732  22.693  1.00 72.59           O  
ANISOU 1937  OG1 THR A 461     9510   9762   8309  -2379  -1248  -2070       O  
ATOM   1938  CG2 THR A 461      32.045  19.813  24.121  1.00 69.42           C  
ANISOU 1938  CG2 THR A 461     8765   9836   7776  -2046  -1418  -2058       C  
ATOM   1939  N   ASP A 462      28.783  21.292  20.974  1.00 56.65           N  
ANISOU 1939  N   ASP A 462     7894   7245   6385  -1875   -991  -1728       N  
ATOM   1940  CA  ASP A 462      27.777  22.219  20.468  1.00 58.18           C  
ANISOU 1940  CA  ASP A 462     8384   7099   6624  -1860   -911  -1682       C  
ATOM   1941  C   ASP A 462      26.482  21.493  20.110  1.00 58.29           C  
ANISOU 1941  C   ASP A 462     8458   7047   6643  -1555   -852  -1536       C  
ATOM   1942  O   ASP A 462      25.515  22.112  19.670  1.00 58.54           O  
ANISOU 1942  O   ASP A 462     8712   6817   6714  -1490   -791  -1473       O  
ATOM   1943  CB  ASP A 462      28.308  22.976  19.252  1.00 62.55           C  
ANISOU 1943  CB  ASP A 462     8984   7520   7262  -2116   -830  -1627       C  
ATOM   1944  CG  ASP A 462      28.463  22.087  18.037  1.00 68.48           C  
ANISOU 1944  CG  ASP A 462     9568   8397   8054  -2072   -751  -1468       C  
ATOM   1945  OD1 ASP A 462      29.077  21.006  18.161  1.00 71.08           O  
ANISOU 1945  OD1 ASP A 462     9631   9011   8364  -2011   -779  -1464       O  
ATOM   1946  OD2 ASP A 462      27.970  22.472  16.955  1.00 71.04           O  
ANISOU 1946  OD2 ASP A 462    10031   8533   8426  -2096   -659  -1346       O  
ATOM   1947  N   MET A 463      26.470  20.179  20.307  1.00 57.16           N  
ANISOU 1947  N   MET A 463     8112   7140   6465  -1370   -875  -1479       N  
ATOM   1948  CA  MET A 463      25.317  19.359  19.955  1.00 60.46           C  
ANISOU 1948  CA  MET A 463     8556   7526   6889  -1099   -822  -1342       C  
ATOM   1949  C   MET A 463      24.499  18.977  21.177  1.00 65.91           C  
ANISOU 1949  C   MET A 463     9298   8245   7501   -872   -874  -1386       C  
ATOM   1950  O   MET A 463      25.051  18.678  22.235  1.00 64.27           O  
ANISOU 1950  O   MET A 463     8987   8215   7216   -874   -962  -1484       O  
ATOM   1951  CB  MET A 463      25.767  18.088  19.242  1.00 63.00           C  
ANISOU 1951  CB  MET A 463     8636   8066   7236  -1040   -793  -1239       C  
ATOM   1952  CG  MET A 463      25.956  18.236  17.751  1.00 66.56           C  
ANISOU 1952  CG  MET A 463     9086   8449   7757  -1162   -696  -1136       C  
ATOM   1953  SD  MET A 463      26.264  16.628  17.007  1.00 78.11           S  
ANISOU 1953  SD  MET A 463    10288  10152   9240  -1040   -648  -1032       S  
ATOM   1954  CE  MET A 463      25.015  15.637  17.825  1.00 52.93           C  
ANISOU 1954  CE  MET A 463     7128   6979   6006   -704   -681   -983       C  
ATOM   1955  N   SER A 464      23.179  18.972  21.015  1.00 73.92           N  
ANISOU 1955  N   SER A 464    10462   9096   8527   -677   -818  -1305       N  
ATOM   1956  CA  SER A 464      22.273  18.661  22.114  1.00 81.67           C  
ANISOU 1956  CA  SER A 464    11506  10091   9435   -460   -843  -1338       C  
ATOM   1957  C   SER A 464      21.414  17.431  21.831  1.00 79.17           C  
ANISOU 1957  C   SER A 464    11104   9855   9122   -219   -803  -1195       C  
ATOM   1958  O   SER A 464      20.712  17.369  20.822  1.00 78.89           O  
ANISOU 1958  O   SER A 464    11118   9703   9154   -158   -733  -1074       O  
ATOM   1959  CB  SER A 464      21.384  19.868  22.432  1.00 82.95           C  
ANISOU 1959  CB  SER A 464    11934   9978   9605   -435   -811  -1403       C  
ATOM   1960  OG  SER A 464      20.860  20.451  21.250  1.00 80.57           O  
ANISOU 1960  OG  SER A 464    11755   9454   9402   -458   -737  -1297       O  
ATOM   1961  N   LEU A 465      21.480  16.453  22.729  1.00 77.95           N  
ANISOU 1961  N   LEU A 465    10823   9903   8891    -91   -853  -1205       N  
ATOM   1962  CA  LEU A 465      20.623  15.279  22.645  1.00 74.19           C  
ANISOU 1962  CA  LEU A 465    10280   9495   8412    134   -817  -1081       C  
ATOM   1963  C   LEU A 465      19.255  15.619  23.229  1.00 68.41           C  
ANISOU 1963  C   LEU A 465     9721   8625   7648    303   -781  -1084       C  
ATOM   1964  O   LEU A 465      19.163  16.187  24.315  1.00 70.02           O  
ANISOU 1964  O   LEU A 465    10021   8811   7772    308   -814  -1203       O  
ATOM   1965  CB  LEU A 465      21.247  14.105  23.403  1.00 76.03           C  
ANISOU 1965  CB  LEU A 465    10321   9986   8579    204   -885  -1078       C  
ATOM   1966  CG  LEU A 465      20.656  12.714  23.162  1.00 79.22           C  
ANISOU 1966  CG  LEU A 465    10621  10479   8999    399   -847   -940       C  
ATOM   1967  CD1 LEU A 465      20.915  12.258  21.732  1.00 80.88           C  
ANISOU 1967  CD1 LEU A 465    10739  10678   9312    351   -786   -844       C  
ATOM   1968  CD2 LEU A 465      21.230  11.710  24.153  1.00 79.92           C  
ANISOU 1968  CD2 LEU A 465    10558  10795   9012    478   -925   -943       C  
ATOM   1969  N   HIS A 466      18.201  15.280  22.494  1.00 62.92           N  
ANISOU 1969  N   HIS A 466     9058   7839   7010    437   -709   -959       N  
ATOM   1970  CA  HIS A 466      16.832  15.581  22.903  1.00 61.78           C  
ANISOU 1970  CA  HIS A 466     9052   7566   6854    607   -662   -947       C  
ATOM   1971  C   HIS A 466      16.570  15.145  24.345  1.00 63.72           C  
ANISOU 1971  C   HIS A 466     9287   7940   6984    729   -689  -1014       C  
ATOM   1972  O   HIS A 466      16.969  14.054  24.749  1.00 63.06           O  
ANISOU 1972  O   HIS A 466     9057   8055   6847    774   -726   -978       O  
ATOM   1973  CB  HIS A 466      15.843  14.900  21.954  1.00 59.86           C  
ANISOU 1973  CB  HIS A 466     8775   7290   6678    738   -599   -787       C  
ATOM   1974  CG  HIS A 466      14.423  15.337  22.138  1.00 58.85           C  
ANISOU 1974  CG  HIS A 466     8776   7018   6566    900   -546   -761       C  
ATOM   1975  ND1 HIS A 466      13.639  14.901  23.185  1.00 57.46           N  
ANISOU 1975  ND1 HIS A 466     8600   6910   6322   1067   -528   -780       N  
ATOM   1976  CD2 HIS A 466      13.642  16.162  21.402  1.00 55.76           C  
ANISOU 1976  CD2 HIS A 466     8507   6425   6253    927   -504   -711       C  
ATOM   1977  CE1 HIS A 466      12.439  15.445  23.089  1.00 53.94           C  
ANISOU 1977  CE1 HIS A 466     8259   6316   5918   1190   -471   -753       C  
ATOM   1978  NE2 HIS A 466      12.414  16.213  22.015  1.00 54.69           N  
ANISOU 1978  NE2 HIS A 466     8429   6244   6106   1116   -462   -707       N  
ATOM   1979  N   PRO A 467      15.894  16.003  25.125  1.00 66.93           N  
ANISOU 1979  N   PRO A 467     9855   8228   7348    787   -667  -1110       N  
ATOM   1980  CA  PRO A 467      15.626  15.757  26.547  1.00 69.50           C  
ANISOU 1980  CA  PRO A 467    10198   8667   7541    887   -683  -1193       C  
ATOM   1981  C   PRO A 467      15.039  14.373  26.810  1.00 63.81           C  
ANISOU 1981  C   PRO A 467     9354   8110   6779   1058   -663  -1070       C  
ATOM   1982  O   PRO A 467      15.508  13.673  27.709  1.00 57.71           O  
ANISOU 1982  O   PRO A 467     8500   7528   5898   1076   -717  -1088       O  
ATOM   1983  CB  PRO A 467      14.602  16.838  26.895  1.00 72.44           C  
ANISOU 1983  CB  PRO A 467    10768   8835   7921    968   -614  -1273       C  
ATOM   1984  CG  PRO A 467      14.911  17.949  25.958  1.00 73.61           C  
ANISOU 1984  CG  PRO A 467    11021   8766   8182    828   -608  -1295       C  
ATOM   1985  CD  PRO A 467      15.344  17.294  24.676  1.00 71.30           C  
ANISOU 1985  CD  PRO A 467    10592   8521   7978    763   -618  -1147       C  
ATOM   1986  N   LEU A 468      14.026  13.989  26.040  1.00 61.80           N  
ANISOU 1986  N   LEU A 468     9089   7783   6611   1177   -590   -941       N  
ATOM   1987  CA  LEU A 468      13.415  12.675  26.192  1.00 56.38           C  
ANISOU 1987  CA  LEU A 468     8291   7229   5901   1322   -562   -820       C  
ATOM   1988  C   LEU A 468      14.470  11.583  26.063  1.00 57.12           C  
ANISOU 1988  C   LEU A 468     8220   7501   5982   1264   -627   -764       C  
ATOM   1989  O   LEU A 468      14.474  10.618  26.827  1.00 60.81           O  
ANISOU 1989  O   LEU A 468     8612   8123   6370   1348   -645   -724       O  
ATOM   1990  CB  LEU A 468      12.303  12.467  25.161  1.00 58.97           C  
ANISOU 1990  CB  LEU A 468     8616   7451   6339   1416   -488   -692       C  
ATOM   1991  CG  LEU A 468      11.556  11.132  25.237  1.00 61.99           C  
ANISOU 1991  CG  LEU A 468     8892   7950   6712   1552   -450   -566       C  
ATOM   1992  CD1 LEU A 468      11.009  10.890  26.638  1.00 65.36           C  
ANISOU 1992  CD1 LEU A 468     9346   8469   7017   1667   -425   -607       C  
ATOM   1993  CD2 LEU A 468      10.435  11.077  24.211  1.00 60.09           C  
ANISOU 1993  CD2 LEU A 468     8651   7604   6575   1625   -387   -457       C  
ATOM   1994  N   LEU A 469      15.372  11.751  25.101  1.00 53.97           N  
ANISOU 1994  N   LEU A 469     7766   7078   5662   1124   -656   -758       N  
ATOM   1995  CA  LEU A 469      16.431  10.777  24.862  1.00 52.49           C  
ANISOU 1995  CA  LEU A 469     7410   7050   5484   1072   -707   -713       C  
ATOM   1996  C   LEU A 469      17.510  10.818  25.942  1.00 56.63           C  
ANISOU 1996  C   LEU A 469     7884   7727   5905   1005   -804   -811       C  
ATOM   1997  O   LEU A 469      18.154   9.806  26.225  1.00 56.35           O  
ANISOU 1997  O   LEU A 469     7707   7859   5845   1036   -853   -763       O  
ATOM   1998  CB  LEU A 469      17.053  10.986  23.478  1.00 51.75           C  
ANISOU 1998  CB  LEU A 469     7269   6893   5501    938   -694   -684       C  
ATOM   1999  CG  LEU A 469      16.140  10.664  22.292  1.00 47.75           C  
ANISOU 1999  CG  LEU A 469     6775   6284   5084    997   -616   -566       C  
ATOM   2000  CD1 LEU A 469      16.869  10.894  20.978  1.00 45.49           C  
ANISOU 2000  CD1 LEU A 469     6448   5958   4878    846   -603   -546       C  
ATOM   2001  CD2 LEU A 469      15.615   9.235  22.379  1.00 40.36           C  
ANISOU 2001  CD2 LEU A 469     5740   5449   4146   1142   -590   -460       C  
ATOM   2002  N   GLN A 470      17.705  11.988  26.543  1.00 59.35           N  
ANISOU 2002  N   GLN A 470     8348   8012   6192    915   -834   -950       N  
ATOM   2003  CA  GLN A 470      18.678  12.129  27.621  1.00 68.64           C  
ANISOU 2003  CA  GLN A 470     9487   9340   7252    836   -937  -1058       C  
ATOM   2004  C   GLN A 470      18.244  11.362  28.864  1.00 68.86           C  
ANISOU 2004  C   GLN A 470     9507   9515   7143    985   -960  -1033       C  
ATOM   2005  O   GLN A 470      19.031  10.621  29.452  1.00 66.21           O  
ANISOU 2005  O   GLN A 470     9047   9373   6737    988  -1047  -1012       O  
ATOM   2006  CB  GLN A 470      18.898  13.601  27.970  1.00 74.35           C  
ANISOU 2006  CB  GLN A 470    10364   9945   7942    693   -957  -1227       C  
ATOM   2007  CG  GLN A 470      19.702  14.366  26.941  1.00 79.68           C  
ANISOU 2007  CG  GLN A 470    11030  10518   8727    495   -962  -1263       C  
ATOM   2008  CD  GLN A 470      20.459  15.527  27.549  1.00 85.60           C  
ANISOU 2008  CD  GLN A 470    11865  11241   9418    308  -1028  -1443       C  
ATOM   2009  OE1 GLN A 470      20.466  15.708  28.767  1.00 86.45           O  
ANISOU 2009  OE1 GLN A 470    12028  11428   9390    324  -1081  -1550       O  
ATOM   2010  NE2 GLN A 470      21.109  16.318  26.704  1.00 88.04           N  
ANISOU 2010  NE2 GLN A 470    12191  11441   9820    117  -1024  -1480       N  
ATOM   2011  N   GLU A 471      16.987  11.549  29.258  1.00 68.33           N  
ANISOU 2011  N   GLU A 471     9569   9357   7038   1110   -880  -1029       N  
ATOM   2012  CA  GLU A 471      16.445  10.897  30.446  1.00 68.24           C  
ANISOU 2012  CA  GLU A 471     9570   9474   6884   1246   -879  -1004       C  
ATOM   2013  C   GLU A 471      16.473   9.380  30.302  1.00 69.01           C  
ANISOU 2013  C   GLU A 471     9517   9702   7002   1352   -886   -833       C  
ATOM   2014  O   GLU A 471      16.523   8.652  31.293  1.00 73.02           O  
ANISOU 2014  O   GLU A 471     9991  10366   7385   1428   -926   -793       O  
ATOM   2015  CB  GLU A 471      15.017  11.375  30.720  1.00 64.55           C  
ANISOU 2015  CB  GLU A 471     9252   8876   6398   1364   -767  -1024       C  
ATOM   2016  N   ILE A 472      16.443   8.908  29.061  1.00 60.77           N  
ANISOU 2016  N   ILE A 472     8392   8587   6111   1354   -844   -733       N  
ATOM   2017  CA  ILE A 472      16.495   7.477  28.790  1.00 59.55           C  
ANISOU 2017  CA  ILE A 472     8103   8523   5998   1446   -840   -582       C  
ATOM   2018  C   ILE A 472      17.895   6.917  29.024  1.00 68.56           C  
ANISOU 2018  C   ILE A 472     9097   9832   7120   1392   -952   -577       C  
ATOM   2019  O   ILE A 472      18.055   5.852  29.622  1.00 72.46           O  
ANISOU 2019  O   ILE A 472     9513  10456   7560   1489   -989   -485       O  
ATOM   2020  CB  ILE A 472      16.056   7.162  27.348  1.00 52.67           C  
ANISOU 2020  CB  ILE A 472     7196   7526   5289   1452   -760   -495       C  
ATOM   2021  CG1 ILE A 472      14.589   7.544  27.145  1.00 52.32           C  
ANISOU 2021  CG1 ILE A 472     7269   7343   5267   1530   -659   -472       C  
ATOM   2022  CG2 ILE A 472      16.269   5.691  27.037  1.00 50.21           C  
ANISOU 2022  CG2 ILE A 472     6749   7298   5029   1528   -758   -362       C  
ATOM   2023  CD1 ILE A 472      14.109   7.386  25.722  1.00 48.84           C  
ANISOU 2023  CD1 ILE A 472     6806   6783   4967   1521   -594   -395       C  
ATOM   2024  N   TYR A 473      18.907   7.644  28.560  1.00 69.50           N  
ANISOU 2024  N   TYR A 473     9174   9947   7285   1239  -1005   -671       N  
ATOM   2025  CA  TYR A 473      20.289   7.178  28.651  1.00 71.17           C  
ANISOU 2025  CA  TYR A 473     9216  10324   7500   1180  -1108   -671       C  
ATOM   2026  C   TYR A 473      20.950   7.479  29.996  1.00 75.13           C  
ANISOU 2026  C   TYR A 473     9714  10991   7839   1142  -1233   -756       C  
ATOM   2027  O   TYR A 473      21.922   6.824  30.373  1.00 76.84           O  
ANISOU 2027  O   TYR A 473     9780  11385   8030   1151  -1333   -721       O  
ATOM   2028  CB  TYR A 473      21.128   7.753  27.507  1.00 70.14           C  
ANISOU 2028  CB  TYR A 473     9017  10138   7494   1020  -1103   -727       C  
ATOM   2029  CG  TYR A 473      20.912   7.048  26.187  1.00 69.09           C  
ANISOU 2029  CG  TYR A 473     8816   9926   7508   1058  -1011   -623       C  
ATOM   2030  CD1 TYR A 473      21.363   5.750  25.994  1.00 66.93           C  
ANISOU 2030  CD1 TYR A 473     8386   9758   7287   1152  -1019   -522       C  
ATOM   2031  CD2 TYR A 473      20.261   7.678  25.134  1.00 65.91           C  
ANISOU 2031  CD2 TYR A 473     8512   9342   7187   1003   -918   -627       C  
ATOM   2032  CE1 TYR A 473      21.172   5.097  24.796  1.00 63.89           C  
ANISOU 2032  CE1 TYR A 473     7950   9299   7027   1180   -930   -446       C  
ATOM   2033  CE2 TYR A 473      20.067   7.031  23.926  1.00 64.13           C  
ANISOU 2033  CE2 TYR A 473     8230   9061   7075   1027   -839   -539       C  
ATOM   2034  CZ  TYR A 473      20.526   5.739  23.766  1.00 62.87           C  
ANISOU 2034  CZ  TYR A 473     7920   9008   6960   1110   -842   -459       C  
ATOM   2035  OH  TYR A 473      20.341   5.080  22.573  1.00 60.97           O  
ANISOU 2035  OH  TYR A 473     7633   8709   6824   1127   -759   -390       O  
ATOM   2036  N   LYS A 474      20.426   8.467  30.713  1.00 75.91           N  
ANISOU 2036  N   LYS A 474     9978  11035   7828   1103  -1228   -870       N  
ATOM   2037  CA  LYS A 474      20.968   8.824  32.019  1.00 79.52           C  
ANISOU 2037  CA  LYS A 474    10459  11650   8107   1053  -1343   -970       C  
ATOM   2038  C   LYS A 474      20.983   7.611  32.940  1.00 83.80           C  
ANISOU 2038  C   LYS A 474    10925  12379   8536   1200  -1404   -847       C  
ATOM   2039  O   LYS A 474      19.947   6.987  33.174  1.00 79.27           O  
ANISOU 2039  O   LYS A 474    10418  11769   7934   1347  -1323   -745       O  
ATOM   2040  CB  LYS A 474      20.155   9.956  32.651  1.00 78.50           C  
ANISOU 2040  CB  LYS A 474    10545  11409   7874   1024  -1296  -1108       C  
ATOM   2041  N   ASP A 475      22.163   7.278  33.454  1.00 92.78           N  
ANISOU 2041  N   ASP A 475    11922  13720   9612   1158  -1548   -847       N  
ATOM   2042  CA  ASP A 475      22.325   6.137  34.350  1.00 99.48           C  
ANISOU 2042  CA  ASP A 475    12693  14755  10350   1295  -1627   -716       C  
ATOM   2043  C   ASP A 475      21.830   4.841  33.711  1.00101.64           C  
ANISOU 2043  C   ASP A 475    12899  14968  10752   1461  -1542   -523       C  
ATOM   2044  O   ASP A 475      21.173   4.026  34.361  1.00100.82           O  
ANISOU 2044  O   ASP A 475    12841  14903  10564   1601  -1520   -404       O  
ATOM   2045  CB  ASP A 475      21.603   6.388  35.675  1.00101.04           C  
ANISOU 2045  CB  ASP A 475    13056  15015  10321   1339  -1636   -756       C  
ATOM   2046  CG  ASP A 475      22.178   7.566  36.436  1.00104.45           C  
ANISOU 2046  CG  ASP A 475    13555  15529  10604   1173  -1736   -956       C  
ATOM   2047  OD1 ASP A 475      23.321   7.971  36.135  1.00105.13           O  
ANISOU 2047  OD1 ASP A 475    13521  15682  10741   1031  -1837  -1034       O  
ATOM   2048  OD2 ASP A 475      21.489   8.086  37.339  1.00106.80           O  
ANISOU 2048  OD2 ASP A 475    14024  15827  10730   1178  -1708  -1042       O  
ATOM   2049  N   LEU A 476      22.151   4.657  32.435  1.00103.48           N  
ANISOU 2049  N   LEU A 476    13030  15104  11182   1433  -1488   -498       N  
ATOM   2050  CA  LEU A 476      21.771   3.449  31.715  1.00104.64           C  
ANISOU 2050  CA  LEU A 476    13112  15183  11462   1569  -1405   -338       C  
ATOM   2051  C   LEU A 476      22.916   2.441  31.745  1.00108.50           C  
ANISOU 2051  C   LEU A 476    13397  15825  12003   1631  -1504   -245       C  
ATOM   2052  O   LEU A 476      23.946   2.644  31.100  1.00111.47           O  
ANISOU 2052  O   LEU A 476    13629  16244  12481   1543  -1544   -300       O  
ATOM   2053  CB  LEU A 476      21.406   3.788  30.268  1.00102.24           C  
ANISOU 2053  CB  LEU A 476    12823  14687  11334   1509  -1281   -365       C  
ATOM   2054  CG  LEU A 476      20.594   2.753  29.488  1.00 98.98           C  
ANISOU 2054  CG  LEU A 476    12410  14158  11040   1630  -1164   -230       C  
ATOM   2055  CD1 LEU A 476      19.204   2.614  30.081  1.00 97.32           C  
ANISOU 2055  CD1 LEU A 476    12354  13882  10743   1725  -1090   -176       C  
ATOM   2056  CD2 LEU A 476      20.510   3.137  28.021  1.00 97.64           C  
ANISOU 2056  CD2 LEU A 476    12231  13839  11027   1543  -1071   -268       C  
ATOM   2057  N   TYR A 477      22.734   1.361  32.499  1.00108.99           N  
ANISOU 2057  N   TYR A 477    13445  15968  11998   1786  -1539   -100       N  
ATOM   2058  CA  TYR A 477      23.765   0.334  32.643  1.00113.63           C  
ANISOU 2058  CA  TYR A 477    13846  16695  12634   1880  -1639      8       C  
ATOM   2059  C   TYR A 477      25.059   0.900  33.225  1.00118.52           C  
ANISOU 2059  C   TYR A 477    14336  17524  13173   1782  -1810    -82       C  
ATOM   2060  O   TYR A 477      25.164   2.091  33.520  1.00120.56           O  
ANISOU 2060  O   TYR A 477    14661  17810  13335   1627  -1849   -237       O  
ATOM   2061  CB  TYR A 477      24.053  -0.347  31.301  1.00111.55           C  
ANISOU 2061  CB  TYR A 477    13460  16324  12599   1917  -1551     55       C  
ATOM   2062  CG  TYR A 477      22.931  -1.223  30.795  1.00107.78           C  
ANISOU 2062  CG  TYR A 477    13076  15673  12204   2031  -1409    171       C  
ATOM   2063  CD1 TYR A 477      22.661  -2.449  31.389  1.00107.15           C  
ANISOU 2063  CD1 TYR A 477    13000  15610  12101   2198  -1420    340       C  
ATOM   2064  CD2 TYR A 477      22.148  -0.831  29.716  1.00103.48           C  
ANISOU 2064  CD2 TYR A 477    12614  14945  11757   1965  -1268    117       C  
ATOM   2065  CE1 TYR A 477      21.641  -3.256  30.930  1.00104.52           C  
ANISOU 2065  CE1 TYR A 477    12751  15117  11847   2282  -1289    439       C  
ATOM   2066  CE2 TYR A 477      21.124  -1.633  29.249  1.00101.18           C  
ANISOU 2066  CE2 TYR A 477    12397  14510  11538   2054  -1148    216       C  
ATOM   2067  CZ  TYR A 477      20.875  -2.846  29.861  1.00102.04           C  
ANISOU 2067  CZ  TYR A 477    12507  14636  11627   2205  -1156    371       C  
ATOM   2068  OH  TYR A 477      19.859  -3.654  29.406  1.00100.02           O  
ANISOU 2068  OH  TYR A 477    12324  14233  11444   2274  -1036    465       O  
ATOM   2069  OXT TYR A 477      26.034   0.173  33.415  1.00119.85           O  
ANISOU 2069  OXT TYR A 477    14325  17837  13375   1856  -1916     -2       O  
TER    2070      TYR A 477                                                      
ATOM   2071  N   GLU B 207       8.631 -39.405  17.891  1.00 79.38           N  
ANISOU 2071  N   GLU B 207     9091  10582  10489  -1128   -439   -954       N  
ATOM   2072  CA  GLU B 207       9.490 -38.242  18.078  1.00 78.48           C  
ANISOU 2072  CA  GLU B 207     9029  10469  10321   -850   -430   -822       C  
ATOM   2073  C   GLU B 207       9.750 -37.986  19.558  1.00 73.85           C  
ANISOU 2073  C   GLU B 207     8501   9715   9844   -736   -320   -658       C  
ATOM   2074  O   GLU B 207      10.878 -37.698  19.955  1.00 74.78           O  
ANISOU 2074  O   GLU B 207     8771   9666   9976   -573   -269   -604       O  
ATOM   2075  CB  GLU B 207       8.871 -37.002  17.426  1.00 82.65           C  
ANISOU 2075  CB  GLU B 207     9365  11325  10714   -739   -531   -746       C  
ATOM   2076  CG  GLU B 207       9.700 -35.730  17.567  1.00 83.12           C  
ANISOU 2076  CG  GLU B 207     9481  11380  10720   -467   -521   -608       C  
ATOM   2077  CD  GLU B 207      10.945 -35.736  16.699  1.00 87.55           C  
ANISOU 2077  CD  GLU B 207    10204  11863  11200   -398   -540   -691       C  
ATOM   2078  OE1 GLU B 207      11.394 -34.642  16.292  1.00 88.27           O  
ANISOU 2078  OE1 GLU B 207    10292  12050  11195   -224   -575   -605       O  
ATOM   2079  OE2 GLU B 207      11.473 -36.832  16.418  1.00 90.29           O  
ANISOU 2079  OE2 GLU B 207    10680  12048  11580   -517   -515   -842       O  
ATOM   2080  N   SER B 208       8.704 -38.094  20.370  1.00 71.35           N  
ANISOU 2080  N   SER B 208     8053   9462   9593   -828   -284   -582       N  
ATOM   2081  CA  SER B 208       8.835 -37.906  21.811  1.00 68.71           C  
ANISOU 2081  CA  SER B 208     7762   8998   9347   -741   -175   -432       C  
ATOM   2082  C   SER B 208       9.844 -38.883  22.398  1.00 65.58           C  
ANISOU 2082  C   SER B 208     7596   8271   9048   -768    -89   -452       C  
ATOM   2083  O   SER B 208      10.739 -38.491  23.145  1.00 65.50           O  
ANISOU 2083  O   SER B 208     7702   8130   9054   -598    -31   -356       O  
ATOM   2084  CB  SER B 208       7.483 -38.074  22.505  1.00 74.10           C  
ANISOU 2084  CB  SER B 208     8258   9814  10081   -879   -142   -371       C  
ATOM   2085  OG  SER B 208       6.615 -37.000  22.193  1.00 77.70           O  
ANISOU 2085  OG  SER B 208     8492  10575  10454   -789   -207   -314       O  
ATOM   2086  N   ALA B 209       9.692 -40.159  22.058  1.00 65.15           N  
ANISOU 2086  N   ALA B 209     7609   8085   9061   -981    -82   -579       N  
ATOM   2087  CA  ALA B 209      10.600 -41.194  22.535  1.00 64.59           C  
ANISOU 2087  CA  ALA B 209     7762   7683   9095  -1005     -2   -600       C  
ATOM   2088  C   ALA B 209      12.038 -40.881  22.139  1.00 62.91           C  
ANISOU 2088  C   ALA B 209     7706   7361   8837   -801    -11   -629       C  
ATOM   2089  O   ALA B 209      12.966 -41.101  22.916  1.00 64.80           O  
ANISOU 2089  O   ALA B 209     8094   7391   9136   -690     60   -554       O  
ATOM   2090  CB  ALA B 209      10.184 -42.554  21.997  1.00 63.51           C  
ANISOU 2090  CB  ALA B 209     7677   7422   9033  -1268     -3   -762       C  
ATOM   2091  N   ASP B 210      12.215 -40.368  20.925  1.00 61.01           N  
ANISOU 2091  N   ASP B 210     7420   7280   8481   -755   -100   -732       N  
ATOM   2092  CA  ASP B 210      13.538 -40.008  20.431  1.00 60.64           C  
ANISOU 2092  CA  ASP B 210     7496   7170   8373   -575   -109   -764       C  
ATOM   2093  C   ASP B 210      14.144 -38.882  21.264  1.00 55.39           C  
ANISOU 2093  C   ASP B 210     6836   6527   7683   -353    -78   -590       C  
ATOM   2094  O   ASP B 210      15.330 -38.909  21.591  1.00 57.08           O  
ANISOU 2094  O   ASP B 210     7186   6586   7915   -222    -34   -564       O  
ATOM   2095  CB  ASP B 210      13.471 -39.597  18.958  1.00 67.95           C  
ANISOU 2095  CB  ASP B 210     8351   8308   9158   -585   -211   -891       C  
ATOM   2096  CG  ASP B 210      13.102 -40.752  18.045  1.00 76.57           C  
ANISOU 2096  CG  ASP B 210     9468   9365  10258   -801   -241  -1101       C  
ATOM   2097  OD1 ASP B 210      12.663 -41.803  18.557  1.00 79.69           O  
ANISOU 2097  OD1 ASP B 210     9910   9589  10778   -967   -189  -1139       O  
ATOM   2098  OD2 ASP B 210      13.252 -40.607  16.813  1.00 79.75           O  
ANISOU 2098  OD2 ASP B 210     9851   9913  10538   -812   -315  -1231       O  
ATOM   2099  N   LEU B 211      13.322 -37.894  21.603  1.00 50.15           N  
ANISOU 2099  N   LEU B 211     6016   6060   6977   -312   -100   -480       N  
ATOM   2100  CA  LEU B 211      13.770 -36.772  22.417  1.00 46.75           C  
ANISOU 2100  CA  LEU B 211     5588   5653   6524   -118    -67   -330       C  
ATOM   2101  C   LEU B 211      14.151 -37.233  23.819  1.00 47.84           C  
ANISOU 2101  C   LEU B 211     5824   5595   6759    -97     32   -234       C  
ATOM   2102  O   LEU B 211      15.133 -36.760  24.389  1.00 51.27           O  
ANISOU 2102  O   LEU B 211     6347   5952   7182     55     67   -162       O  
ATOM   2103  CB  LEU B 211      12.689 -35.692  22.490  1.00 45.03           C  
ANISOU 2103  CB  LEU B 211     5181   5673   6254    -79   -103   -244       C  
ATOM   2104  CG  LEU B 211      12.330 -35.018  21.163  1.00 49.84           C  
ANISOU 2104  CG  LEU B 211     5683   6504   6749    -59   -209   -296       C  
ATOM   2105  CD1 LEU B 211      11.200 -34.018  21.355  1.00 49.79           C  
ANISOU 2105  CD1 LEU B 211     5486   6720   6713     -1   -237   -194       C  
ATOM   2106  CD2 LEU B 211      13.551 -34.343  20.549  1.00 50.34           C  
ANISOU 2106  CD2 LEU B 211     5854   6542   6732     93   -233   -300       C  
ATOM   2107  N   ARG B 212      13.368 -38.156  24.370  1.00 47.30           N  
ANISOU 2107  N   ARG B 212     5735   5460   6777   -259     76   -227       N  
ATOM   2108  CA  ARG B 212      13.645 -38.706  25.692  1.00 47.73           C  
ANISOU 2108  CA  ARG B 212     5884   5336   6916   -259    171   -121       C  
ATOM   2109  C   ARG B 212      14.956 -39.487  25.691  1.00 49.26           C  
ANISOU 2109  C   ARG B 212     6275   5285   7157   -202    199   -156       C  
ATOM   2110  O   ARG B 212      15.732 -39.418  26.644  1.00 46.14           O  
ANISOU 2110  O   ARG B 212     5970   4785   6778    -86    252    -51       O  
ATOM   2111  CB  ARG B 212      12.495 -39.602  26.157  1.00 51.76           C  
ANISOU 2111  CB  ARG B 212     6332   5825   7509   -472    214   -107       C  
ATOM   2112  CG  ARG B 212      11.172 -38.873  26.308  1.00 58.45           C  
ANISOU 2112  CG  ARG B 212     6961   6930   8316   -518    200    -59       C  
ATOM   2113  CD  ARG B 212      11.357 -37.591  27.101  1.00 62.71           C  
ANISOU 2113  CD  ARG B 212     7456   7577   8794   -316    227     65       C  
ATOM   2114  NE  ARG B 212      11.763 -37.857  28.477  1.00 65.78           N  
ANISOU 2114  NE  ARG B 212     7941   7829   9224   -280    324    186       N  
ATOM   2115  CZ  ARG B 212      12.501 -37.033  29.213  1.00 64.84           C  
ANISOU 2115  CZ  ARG B 212     7876   7703   9056    -98    354    269       C  
ATOM   2116  NH1 ARG B 212      12.932 -35.884  28.705  1.00 57.64           N  
ANISOU 2116  NH1 ARG B 212     6943   6889   8070     60    301    246       N  
ATOM   2117  NH2 ARG B 212      12.817 -37.365  30.456  1.00 67.17           N  
ANISOU 2117  NH2 ARG B 212     8251   7896   9373    -83    437    377       N  
ATOM   2118  N   ALA B 213      15.195 -40.232  24.616  1.00 50.22           N  
ANISOU 2118  N   ALA B 213     6457   5329   7294   -279    162   -310       N  
ATOM   2119  CA  ALA B 213      16.440 -40.973  24.464  1.00 53.61           C  
ANISOU 2119  CA  ALA B 213     7064   5537   7768   -207    189   -364       C  
ATOM   2120  C   ALA B 213      17.619 -40.008  24.400  1.00 53.42           C  
ANISOU 2120  C   ALA B 213     7067   5571   7659     11    172   -327       C  
ATOM   2121  O   ALA B 213      18.636 -40.208  25.062  1.00 52.26           O  
ANISOU 2121  O   ALA B 213     7027   5286   7543    131    217   -260       O  
ATOM   2122  CB  ALA B 213      16.393 -41.844  23.217  1.00 55.29           C  
ANISOU 2122  CB  ALA B 213     7323   5686   7997   -330    154   -565       C  
ATOM   2123  N   LEU B 214      17.471 -38.958  23.600  1.00 52.26           N  
ANISOU 2123  N   LEU B 214     6819   5637   7402     58    105   -362       N  
ATOM   2124  CA  LEU B 214      18.504 -37.938  23.480  1.00 47.47           C  
ANISOU 2124  CA  LEU B 214     6228   5100   6709    238     89   -324       C  
ATOM   2125  C   LEU B 214      18.773 -37.301  24.838  1.00 46.24           C  
ANISOU 2125  C   LEU B 214     6077   4931   6562    345    137   -162       C  
ATOM   2126  O   LEU B 214      19.922 -37.044  25.199  1.00 39.62           O  
ANISOU 2126  O   LEU B 214     5311   4038   5705    475    157   -121       O  
ATOM   2127  CB  LEU B 214      18.084 -36.870  22.469  1.00 46.16           C  
ANISOU 2127  CB  LEU B 214     5948   5164   6428    253     13   -358       C  
ATOM   2128  CG  LEU B 214      19.032 -35.682  22.295  1.00 42.70           C  
ANISOU 2128  CG  LEU B 214     5520   4807   5899    416     -3   -306       C  
ATOM   2129  CD1 LEU B 214      20.440 -36.169  21.969  1.00 38.25           C  
ANISOU 2129  CD1 LEU B 214     5075   4127   5331    489     20   -374       C  
ATOM   2130  CD2 LEU B 214      18.520 -34.738  21.221  1.00 38.79           C  
ANISOU 2130  CD2 LEU B 214     4921   4523   5294    419    -78   -327       C  
ATOM   2131  N   ALA B 215      17.705 -37.054  25.589  1.00 46.60           N  
ANISOU 2131  N   ALA B 215     6035   5044   6628    285    157    -77       N  
ATOM   2132  CA  ALA B 215      17.826 -36.472  26.921  1.00 42.01           C  
ANISOU 2132  CA  ALA B 215     5452   4467   6041    370    210     63       C  
ATOM   2133  C   ALA B 215      18.615 -37.390  27.849  1.00 41.79           C  
ANISOU 2133  C   ALA B 215     5553   4248   6079    394    270    123       C  
ATOM   2134  O   ALA B 215      19.524 -36.945  28.550  1.00 42.40           O  
ANISOU 2134  O   ALA B 215     5678   4309   6122    519    290    196       O  
ATOM   2135  CB  ALA B 215      16.447 -36.181  27.504  1.00 41.16           C  
ANISOU 2135  CB  ALA B 215     5218   4475   5944    291    231    126       C  
ATOM   2136  N   LYS B 216      18.265 -38.673  27.846  1.00 41.96           N  
ANISOU 2136  N   LYS B 216     5628   4123   6194    270    297     96       N  
ATOM   2137  CA  LYS B 216      18.933 -39.646  28.703  1.00 45.32           C  
ANISOU 2137  CA  LYS B 216     6181   4345   6692    294    355    172       C  
ATOM   2138  C   LYS B 216      20.395 -39.839  28.301  1.00 46.45           C  
ANISOU 2138  C   LYS B 216     6429   4391   6829    436    341    126       C  
ATOM   2139  O   LYS B 216      21.280 -39.922  29.154  1.00 44.55           O  
ANISOU 2139  O   LYS B 216     6255   4084   6588    550    370    225       O  
ATOM   2140  CB  LYS B 216      18.196 -40.986  28.674  1.00 51.28           C  
ANISOU 2140  CB  LYS B 216     6983   4939   7561    118    390    147       C  
ATOM   2141  CG  LYS B 216      18.853 -42.054  29.529  1.00 58.06           C  
ANISOU 2141  CG  LYS B 216     7990   5562   8507    148    453    244       C  
ATOM   2142  CD  LYS B 216      18.067 -43.351  29.512  1.00 69.30           C  
ANISOU 2142  CD  LYS B 216     9473   6803  10055    -46    496    226       C  
ATOM   2143  CE  LYS B 216      18.827 -44.449  30.239  1.00 73.77           C  
ANISOU 2143  CE  LYS B 216    10209   7101  10718      8    556    328       C  
ATOM   2144  NZ  LYS B 216      19.378 -43.973  31.538  1.00 75.05           N  
ANISOU 2144  NZ  LYS B 216    10377   7320  10819    151    584    521       N  
ATOM   2145  N   HIS B 217      20.637 -39.920  26.997  1.00 48.14           N  
ANISOU 2145  N   HIS B 217     6646   4616   7028    427    296    -26       N  
ATOM   2146  CA  HIS B 217      21.991 -40.059  26.473  1.00 43.87           C  
ANISOU 2146  CA  HIS B 217     6182   4015   6471    560    287    -89       C  
ATOM   2147  C   HIS B 217      22.890 -38.931  26.964  1.00 39.73           C  
ANISOU 2147  C   HIS B 217     5627   3615   5856    714    276     -4       C  
ATOM   2148  O   HIS B 217      23.992 -39.171  27.454  1.00 40.30           O  
ANISOU 2148  O   HIS B 217     5762   3614   5935    834    297     46       O  
ATOM   2149  CB  HIS B 217      21.975 -40.085  24.943  1.00 43.24           C  
ANISOU 2149  CB  HIS B 217     6084   3992   6353    517    240   -269       C  
ATOM   2150  CG  HIS B 217      23.329 -39.929  24.326  1.00 41.01           C  
ANISOU 2150  CG  HIS B 217     5844   3717   6020    659    232   -336       C  
ATOM   2151  ND1 HIS B 217      24.217 -40.977  24.200  1.00 44.44           N  
ANISOU 2151  ND1 HIS B 217     6389   3970   6528    727    270   -394       N  
ATOM   2152  CD2 HIS B 217      23.953 -38.845  23.805  1.00 35.99           C  
ANISOU 2152  CD2 HIS B 217     5151   3252   5272    747    197   -348       C  
ATOM   2153  CE1 HIS B 217      25.325 -40.547  23.625  1.00 42.35           C  
ANISOU 2153  CE1 HIS B 217     6117   3785   6190    853    259   -446       C  
ATOM   2154  NE2 HIS B 217      25.192 -39.257  23.377  1.00 42.74           N  
ANISOU 2154  NE2 HIS B 217     6069   4047   6125    856    215   -417       N  
ATOM   2155  N   LEU B 218      22.411 -37.698  26.829  1.00 38.78           N  
ANISOU 2155  N   LEU B 218     5406   3680   5649    709    243     11       N  
ATOM   2156  CA  LEU B 218      23.163 -36.528  27.268  1.00 33.86           C  
ANISOU 2156  CA  LEU B 218     4756   3169   4940    828    234     78       C  
ATOM   2157  C   LEU B 218      23.415 -36.542  28.776  1.00 36.43           C  
ANISOU 2157  C   LEU B 218     5109   3457   5276    878    278    217       C  
ATOM   2158  O   LEU B 218      24.525 -36.258  29.233  1.00 37.21           O  
ANISOU 2158  O   LEU B 218     5236   3567   5334    987    280    260       O  
ATOM   2159  CB  LEU B 218      22.437 -35.242  26.863  1.00 33.74           C  
ANISOU 2159  CB  LEU B 218     4642   3328   4850    807    198     73       C  
ATOM   2160  CG  LEU B 218      22.389 -34.967  25.359  1.00 37.93           C  
ANISOU 2160  CG  LEU B 218     5139   3943   5331    783    144    -41       C  
ATOM   2161  CD1 LEU B 218      21.616 -33.691  25.070  1.00 39.43           C  
ANISOU 2161  CD1 LEU B 218     5234   4295   5454    781    109    -11       C  
ATOM   2162  CD2 LEU B 218      23.798 -34.880  24.804  1.00 32.06           C  
ANISOU 2162  CD2 LEU B 218     4446   3194   4540    876    138    -90       C  
ATOM   2163  N   TYR B 219      22.382 -36.864  29.547  1.00 41.91           N  
ANISOU 2163  N   TYR B 219     5787   4127   6012    793    312    287       N  
ATOM   2164  CA  TYR B 219      22.523 -36.923  30.997  1.00 43.67           C  
ANISOU 2164  CA  TYR B 219     6035   4332   6227    829    357    424       C  
ATOM   2165  C   TYR B 219      23.587 -37.939  31.406  1.00 42.66           C  
ANISOU 2165  C   TYR B 219     6009   4056   6144    904    375    474       C  
ATOM   2166  O   TYR B 219      24.432 -37.653  32.251  1.00 43.69           O  
ANISOU 2166  O   TYR B 219     6157   4223   6221   1004    380    559       O  
ATOM   2167  CB  TYR B 219      21.190 -37.256  31.668  1.00 45.23           C  
ANISOU 2167  CB  TYR B 219     6194   4529   6463    708    401    490       C  
ATOM   2168  CG  TYR B 219      21.319 -37.517  33.152  1.00 51.01           C  
ANISOU 2168  CG  TYR B 219     6963   5238   7179    732    456    639       C  
ATOM   2169  CD1 TYR B 219      21.627 -36.489  34.030  1.00 51.86           C  
ANISOU 2169  CD1 TYR B 219     7039   5479   7186    811    464    698       C  
ATOM   2170  CD2 TYR B 219      21.138 -38.790  33.674  1.00 57.65           C  
ANISOU 2170  CD2 TYR B 219     7879   5924   8102    670    500    720       C  
ATOM   2171  CE1 TYR B 219      21.748 -36.719  35.385  1.00 53.10           C  
ANISOU 2171  CE1 TYR B 219     7227   5643   7306    829    511    830       C  
ATOM   2172  CE2 TYR B 219      21.258 -39.028  35.032  1.00 60.62           C  
ANISOU 2172  CE2 TYR B 219     8290   6295   8447    692    549    875       C  
ATOM   2173  CZ  TYR B 219      21.563 -37.987  35.881  1.00 57.18           C  
ANISOU 2173  CZ  TYR B 219     7811   6021   7892    773    552    927       C  
ATOM   2174  OH  TYR B 219      21.686 -38.207  37.233  1.00 62.03           O  
ANISOU 2174  OH  TYR B 219     8457   6660   8453    793    597   1077       O  
ATOM   2175  N   ASP B 220      23.541 -39.124  30.802  1.00 45.15           N  
ANISOU 2175  N   ASP B 220     6392   4206   6558    859    384    419       N  
ATOM   2176  CA  ASP B 220      24.521 -40.168  31.086  1.00 47.36           C  
ANISOU 2176  CA  ASP B 220     6777   4318   6901    949    405    463       C  
ATOM   2177  C   ASP B 220      25.943 -39.690  30.799  1.00 46.29           C  
ANISOU 2177  C   ASP B 220     6636   4251   6702   1109    372    431       C  
ATOM   2178  O   ASP B 220      26.860 -39.934  31.579  1.00 46.64           O  
ANISOU 2178  O   ASP B 220     6714   4272   6736   1225    380    530       O  
ATOM   2179  CB  ASP B 220      24.218 -41.435  30.276  1.00 48.96           C  
ANISOU 2179  CB  ASP B 220     7060   4316   7226    872    422    369       C  
ATOM   2180  CG  ASP B 220      23.031 -42.212  30.824  1.00 53.30           C  
ANISOU 2180  CG  ASP B 220     7639   4752   7859    714    468    437       C  
ATOM   2181  OD1 ASP B 220      22.730 -42.072  32.028  1.00 53.97           O  
ANISOU 2181  OD1 ASP B 220     7713   4874   7919    705    500    594       O  
ATOM   2182  OD2 ASP B 220      22.401 -42.968  30.052  1.00 53.80           O  
ANISOU 2182  OD2 ASP B 220     7736   4697   8007    587    475    330       O  
ATOM   2183  N   SER B 221      26.120 -39.005  29.674  1.00 44.40           N  
ANISOU 2183  N   SER B 221     6344   4113   6412   1110    335    300       N  
ATOM   2184  CA  SER B 221      27.432 -38.497  29.290  1.00 42.61           C  
ANISOU 2184  CA  SER B 221     6097   3973   6121   1237    310    261       C  
ATOM   2185  C   SER B 221      27.886 -37.380  30.224  1.00 43.80           C  
ANISOU 2185  C   SER B 221     6192   4281   6171   1291    296    357       C  
ATOM   2186  O   SER B 221      29.057 -37.295  30.596  1.00 42.09           O  
ANISOU 2186  O   SER B 221     5971   4106   5915   1403    288    396       O  
ATOM   2187  CB  SER B 221      27.395 -37.987  27.852  1.00 45.76           C  
ANISOU 2187  CB  SER B 221     6453   4455   6477   1202    278    110       C  
ATOM   2188  OG  SER B 221      28.543 -37.213  27.571  1.00 50.47           O  
ANISOU 2188  OG  SER B 221     7009   5178   6989   1299    258     90       O  
ATOM   2189  N   TYR B 222      26.941 -36.521  30.585  1.00 43.97           N  
ANISOU 2189  N   TYR B 222     6165   4394   6148   1209    294    385       N  
ATOM   2190  CA  TYR B 222      27.171 -35.434  31.526  1.00 38.99           C  
ANISOU 2190  CA  TYR B 222     5493   3898   5424   1239    291    458       C  
ATOM   2191  C   TYR B 222      27.718 -35.978  32.849  1.00 41.44           C  
ANISOU 2191  C   TYR B 222     5839   4180   5726   1303    311    587       C  
ATOM   2192  O   TYR B 222      28.663 -35.428  33.417  1.00 39.18           O  
ANISOU 2192  O   TYR B 222     5531   3995   5359   1376    293    624       O  
ATOM   2193  CB  TYR B 222      25.850 -34.692  31.726  1.00 38.22           C  
ANISOU 2193  CB  TYR B 222     5348   3864   5308   1146    302    464       C  
ATOM   2194  CG  TYR B 222      25.817 -33.616  32.787  1.00 36.42           C  
ANISOU 2194  CG  TYR B 222     5090   3753   4994   1162    314    525       C  
ATOM   2195  CD1 TYR B 222      25.585 -33.935  34.119  1.00 37.11           C  
ANISOU 2195  CD1 TYR B 222     5195   3842   5065   1159    352    632       C  
ATOM   2196  CD2 TYR B 222      25.953 -32.274  32.448  1.00 34.84           C  
ANISOU 2196  CD2 TYR B 222     4850   3659   4728   1173    294    473       C  
ATOM   2197  CE1 TYR B 222      25.522 -32.951  35.091  1.00 38.92           C  
ANISOU 2197  CE1 TYR B 222     5398   4188   5203   1169    368    666       C  
ATOM   2198  CE2 TYR B 222      25.893 -31.281  33.414  1.00 35.78           C  
ANISOU 2198  CE2 TYR B 222     4954   3867   4774   1182    312    507       C  
ATOM   2199  CZ  TYR B 222      25.674 -31.627  34.733  1.00 39.38           C  
ANISOU 2199  CZ  TYR B 222     5424   4335   5205   1180    349    593       C  
ATOM   2200  OH  TYR B 222      25.613 -30.652  35.699  1.00 40.17           O  
ANISOU 2200  OH  TYR B 222     5512   4531   5220   1186    372    607       O  
ATOM   2201  N   ILE B 223      27.129 -37.070  33.326  1.00 37.85           N  
ANISOU 2201  N   ILE B 223     5439   3595   5349   1269    345    660       N  
ATOM   2202  CA  ILE B 223      27.583 -37.713  34.554  1.00 40.84           C  
ANISOU 2202  CA  ILE B 223     5862   3937   5720   1332    365    807       C  
ATOM   2203  C   ILE B 223      28.983 -38.303  34.375  1.00 43.34           C  
ANISOU 2203  C   ILE B 223     6206   4208   6052   1474    342    817       C  
ATOM   2204  O   ILE B 223      29.794 -38.311  35.300  1.00 42.43           O  
ANISOU 2204  O   ILE B 223     6085   4160   5875   1566    330    923       O  
ATOM   2205  CB  ILE B 223      26.608 -38.823  34.992  1.00 45.85           C  
ANISOU 2205  CB  ILE B 223     6559   4415   6446   1250    414    892       C  
ATOM   2206  CG1 ILE B 223      25.331 -38.209  35.572  1.00 49.16           C  
ANISOU 2206  CG1 ILE B 223     6927   4928   6822   1130    446    923       C  
ATOM   2207  CG2 ILE B 223      27.262 -39.748  36.011  1.00 47.00           C  
ANISOU 2207  CG2 ILE B 223     6775   4479   6604   1339    431   1054       C  
ATOM   2208  CD1 ILE B 223      25.555 -37.432  36.844  1.00 47.54           C  
ANISOU 2208  CD1 ILE B 223     6690   4883   6490   1168    454   1018       C  
ATOM   2209  N   LYS B 224      29.262 -38.789  33.173  1.00 44.83           N  
ANISOU 2209  N   LYS B 224     6417   4302   6316   1496    336    702       N  
ATOM   2210  CA  LYS B 224      30.563 -39.367  32.863  1.00 52.08           C  
ANISOU 2210  CA  LYS B 224     7351   5180   7259   1644    324    690       C  
ATOM   2211  C   LYS B 224      31.639 -38.285  32.783  1.00 49.46           C  
ANISOU 2211  C   LYS B 224     6926   5057   6810   1713    283    656       C  
ATOM   2212  O   LYS B 224      32.789 -38.513  33.158  1.00 48.86           O  
ANISOU 2212  O   LYS B 224     6826   5030   6708   1843    266    710       O  
ATOM   2213  CB  LYS B 224      30.484 -40.138  31.541  1.00 59.44           C  
ANISOU 2213  CB  LYS B 224     8330   5961   8292   1637    339    549       C  
ATOM   2214  CG  LYS B 224      31.604 -41.139  31.302  1.00 68.66           C  
ANISOU 2214  CG  LYS B 224     9543   7015   9529   1799    351    544       C  
ATOM   2215  CD  LYS B 224      32.843 -40.477  30.722  1.00 73.52           C  
ANISOU 2215  CD  LYS B 224    10068   7802  10063   1906    323    466       C  
ATOM   2216  CE  LYS B 224      33.791 -41.510  30.124  1.00 78.80           C  
ANISOU 2216  CE  LYS B 224    10774   8352  10814   2062    347    408       C  
ATOM   2217  NZ  LYS B 224      34.121 -42.600  31.085  1.00 79.71           N  
ANISOU 2217  NZ  LYS B 224    10963   8309  11013   2189    367    562       N  
ATOM   2218  N   SER B 225      31.253 -37.102  32.311  1.00 44.51           N  
ANISOU 2218  N   SER B 225     6242   4555   6114   1622    266    572       N  
ATOM   2219  CA  SER B 225      32.213 -36.038  32.025  1.00 42.46           C  
ANISOU 2219  CA  SER B 225     5904   4472   5756   1655    234    521       C  
ATOM   2220  C   SER B 225      32.478 -35.081  33.187  1.00 42.48           C  
ANISOU 2220  C   SER B 225     5862   4630   5649   1645    215    599       C  
ATOM   2221  O   SER B 225      33.582 -34.556  33.317  1.00 46.18           O  
ANISOU 2221  O   SER B 225     6271   5235   6043   1696    188    594       O  
ATOM   2222  CB  SER B 225      31.774 -35.239  30.793  1.00 42.40           C  
ANISOU 2222  CB  SER B 225     5871   4508   5732   1570    227    392       C  
ATOM   2223  OG  SER B 225      31.994 -35.969  29.600  1.00 46.57           O  
ANISOU 2223  OG  SER B 225     6418   4956   6319   1598    236    292       O  
ATOM   2224  N   PHE B 226      31.470 -34.843  34.018  1.00 43.80           N  
ANISOU 2224  N   PHE B 226     6052   4788   5801   1570    233    661       N  
ATOM   2225  CA  PHE B 226      31.592 -33.862  35.093  1.00 43.33           C  
ANISOU 2225  CA  PHE B 226     5959   4877   5629   1545    223    708       C  
ATOM   2226  C   PHE B 226      31.539 -34.511  36.475  1.00 48.10           C  
ANISOU 2226  C   PHE B 226     6590   5483   6204   1580    234    851       C  
ATOM   2227  O   PHE B 226      30.468 -34.892  36.948  1.00 52.45           O  
ANISOU 2227  O   PHE B 226     7182   5960   6787   1525    272    909       O  
ATOM   2228  CB  PHE B 226      30.502 -32.795  34.968  1.00 39.83           C  
ANISOU 2228  CB  PHE B 226     5509   4461   5163   1439    241    650       C  
ATOM   2229  CG  PHE B 226      30.447 -32.137  33.617  1.00 40.02           C  
ANISOU 2229  CG  PHE B 226     5513   4485   5208   1404    229    534       C  
ATOM   2230  CD1 PHE B 226      31.445 -31.264  33.216  1.00 33.78           C  
ANISOU 2230  CD1 PHE B 226     4683   3798   4353   1414    202    478       C  
ATOM   2231  CD2 PHE B 226      29.390 -32.382  32.752  1.00 43.17           C  
ANISOU 2231  CD2 PHE B 226     5927   4795   5682   1351    242    486       C  
ATOM   2232  CE1 PHE B 226      31.395 -30.652  31.974  1.00 35.82           C  
ANISOU 2232  CE1 PHE B 226     4928   4061   4620   1379    194    391       C  
ATOM   2233  CE2 PHE B 226      29.333 -31.772  31.508  1.00 39.93           C  
ANISOU 2233  CE2 PHE B 226     5496   4405   5272   1323    225    394       C  
ATOM   2234  CZ  PHE B 226      30.338 -30.908  31.117  1.00 34.88           C  
ANISOU 2234  CZ  PHE B 226     4828   3860   4567   1340    203    353       C  
ATOM   2235  N   PRO B 227      32.703 -34.629  37.132  1.00 51.82           N  
ANISOU 2235  N   PRO B 227     7027   6058   6603   1670    200    917       N  
ATOM   2236  CA  PRO B 227      32.843 -35.293  38.434  1.00 53.32           C  
ANISOU 2236  CA  PRO B 227     7238   6275   6747   1724    199   1075       C  
ATOM   2237  C   PRO B 227      31.936 -34.699  39.515  1.00 52.16           C  
ANISOU 2237  C   PRO B 227     7103   6206   6510   1631    228   1119       C  
ATOM   2238  O   PRO B 227      31.204 -35.441  40.169  1.00 52.96           O  
ANISOU 2238  O   PRO B 227     7256   6233   6635   1616    265   1232       O  
ATOM   2239  CB  PRO B 227      34.324 -35.065  38.781  1.00 55.17           C  
ANISOU 2239  CB  PRO B 227     7396   6680   6886   1819    141   1097       C  
ATOM   2240  CG  PRO B 227      34.745 -33.913  37.901  1.00 60.64           C  
ANISOU 2240  CG  PRO B 227     8029   7464   7549   1762    123    941       C  
ATOM   2241  CD  PRO B 227      34.005 -34.164  36.631  1.00 55.72           C  
ANISOU 2241  CD  PRO B 227     7451   6670   7052   1726    157    852       C  
ATOM   2242  N   LEU B 228      31.983 -33.385  39.703  1.00 52.08           N  
ANISOU 2242  N   LEU B 228     7049   6339   6400   1566    217   1031       N  
ATOM   2243  CA  LEU B 228      31.154 -32.743  40.720  1.00 48.39           C  
ANISOU 2243  CA  LEU B 228     6591   5955   5841   1489    253   1048       C  
ATOM   2244  C   LEU B 228      29.853 -32.231  40.117  1.00 43.36           C  
ANISOU 2244  C   LEU B 228     5970   5231   5274   1402    303    960       C  
ATOM   2245  O   LEU B 228      29.813 -31.149  39.538  1.00 44.45           O  
ANISOU 2245  O   LEU B 228     6087   5398   5404   1362    298    840       O  
ATOM   2246  CB  LEU B 228      31.911 -31.597  41.396  1.00 50.36           C  
ANISOU 2246  CB  LEU B 228     6793   6403   5938   1468    220    992       C  
ATOM   2247  CG  LEU B 228      31.195 -30.886  42.549  1.00 53.67           C  
ANISOU 2247  CG  LEU B 228     7224   6930   6239   1398    260    990       C  
ATOM   2248  CD1 LEU B 228      30.683 -31.885  43.579  1.00 48.64           C  
ANISOU 2248  CD1 LEU B 228     6618   6297   5567   1418    292   1153       C  
ATOM   2249  CD2 LEU B 228      32.110 -29.861  43.204  1.00 56.90           C  
ANISOU 2249  CD2 LEU B 228     7594   7532   6494   1371    220    922       C  
ATOM   2250  N   THR B 229      28.791 -33.018  40.252  1.00 44.78           N  
ANISOU 2250  N   THR B 229     6184   5307   5525   1370    352   1030       N  
ATOM   2251  CA  THR B 229      27.492 -32.664  39.694  1.00 46.64           C  
ANISOU 2251  CA  THR B 229     6413   5478   5828   1292    396    961       C  
ATOM   2252  C   THR B 229      26.784 -31.662  40.598  1.00 45.64           C  
ANISOU 2252  C   THR B 229     6265   5473   5602   1244    441    938       C  
ATOM   2253  O   THR B 229      27.176 -31.480  41.750  1.00 44.70           O  
ANISOU 2253  O   THR B 229     6148   5474   5360   1257    446    991       O  
ATOM   2254  CB  THR B 229      26.598 -33.909  39.536  1.00 46.70           C  
ANISOU 2254  CB  THR B 229     6453   5342   5947   1255    435   1039       C  
ATOM   2255  OG1 THR B 229      26.357 -34.498  40.821  1.00 47.73           O  
ANISOU 2255  OG1 THR B 229     6609   5508   6019   1247    473   1183       O  
ATOM   2256  CG2 THR B 229      27.261 -34.935  38.627  1.00 44.87           C  
ANISOU 2256  CG2 THR B 229     6259   4967   5823   1307    400   1041       C  
ATOM   2257  N   LYS B 230      25.744 -31.013  40.079  1.00 37.48           N  
ANISOU 2257  N   LYS B 230     5207   4419   4616   1197    474    857       N  
ATOM   2258  CA  LYS B 230      24.956 -30.099  40.902  1.00 37.18           C  
ANISOU 2258  CA  LYS B 230     5147   4482   4498   1167    531    827       C  
ATOM   2259  C   LYS B 230      24.343 -30.837  42.096  1.00 40.86           C  
ANISOU 2259  C   LYS B 230     5617   4998   4912   1138    591    948       C  
ATOM   2260  O   LYS B 230      24.350 -30.333  43.220  1.00 42.45           O  
ANISOU 2260  O   LYS B 230     5816   5329   4983   1137    625    957       O  
ATOM   2261  CB  LYS B 230      23.856 -29.410  40.089  1.00 36.32           C  
ANISOU 2261  CB  LYS B 230     4998   4337   4465   1143    558    739       C  
ATOM   2262  CG  LYS B 230      23.068 -28.394  40.904  1.00 37.02           C  
ANISOU 2262  CG  LYS B 230     5062   4524   4480   1139    625    694       C  
ATOM   2263  CD  LYS B 230      22.038 -27.645  40.071  1.00 36.54           C  
ANISOU 2263  CD  LYS B 230     4953   4433   4497   1144    645    616       C  
ATOM   2264  CE  LYS B 230      21.293 -26.638  40.938  1.00 34.45           C  
ANISOU 2264  CE  LYS B 230     4665   4260   4163   1163    722    564       C  
ATOM   2265  NZ  LYS B 230      20.306 -25.842  40.166  1.00 33.59           N  
ANISOU 2265  NZ  LYS B 230     4504   4128   4132   1197    742    498       N  
ATOM   2266  N   ALA B 231      23.813 -32.030  41.844  1.00 39.58           N  
ANISOU 2266  N   ALA B 231     5462   4732   4844   1105    608   1038       N  
ATOM   2267  CA  ALA B 231      23.245 -32.856  42.906  1.00 46.31           C  
ANISOU 2267  CA  ALA B 231     6325   5613   5657   1064    669   1177       C  
ATOM   2268  C   ALA B 231      24.243 -33.052  44.046  1.00 47.57           C  
ANISOU 2268  C   ALA B 231     6523   5873   5680   1113    650   1277       C  
ATOM   2269  O   ALA B 231      23.901 -32.892  45.215  1.00 49.11           O  
ANISOU 2269  O   ALA B 231     6711   6199   5749   1090    702   1336       O  
ATOM   2270  CB  ALA B 231      22.803 -34.202  42.353  1.00 47.40           C  
ANISOU 2270  CB  ALA B 231     6489   5587   5934   1015    677   1260       C  
ATOM   2271  N   LYS B 232      25.480 -33.393  43.698  1.00 50.73           N  
ANISOU 2271  N   LYS B 232     6954   6229   6093   1184    574   1293       N  
ATOM   2272  CA  LYS B 232      26.533 -33.565  44.694  1.00 56.22           C  
ANISOU 2272  CA  LYS B 232     7666   7040   6654   1244    537   1389       C  
ATOM   2273  C   LYS B 232      26.853 -32.245  45.385  1.00 56.02           C  
ANISOU 2273  C   LYS B 232     7608   7210   6466   1237    532   1289       C  
ATOM   2274  O   LYS B 232      27.028 -32.200  46.602  1.00 59.41           O  
ANISOU 2274  O   LYS B 232     8040   7796   6740   1236    545   1361       O  
ATOM   2275  CB  LYS B 232      27.804 -34.129  44.054  1.00 61.12           C  
ANISOU 2275  CB  LYS B 232     8303   7587   7333   1335    457   1410       C  
ATOM   2276  CG  LYS B 232      27.673 -35.555  43.543  1.00 67.18           C  
ANISOU 2276  CG  LYS B 232     9124   8150   8250   1358    464   1517       C  
ATOM   2277  CD  LYS B 232      28.984 -36.045  42.946  1.00 72.79           C  
ANISOU 2277  CD  LYS B 232     9844   8804   9011   1473    392   1523       C  
ATOM   2278  CE  LYS B 232      28.805 -37.377  42.235  1.00 78.08           C  
ANISOU 2278  CE  LYS B 232    10579   9234   9853   1497    407   1582       C  
ATOM   2279  NZ  LYS B 232      28.324 -38.445  43.155  1.00 82.38           N  
ANISOU 2279  NZ  LYS B 232    11190   9704  10405   1484    455   1779       N  
ATOM   2280  N   ALA B 233      26.932 -31.175  44.601  1.00 50.62           N  
ANISOU 2280  N   ALA B 233     6902   6517   5816   1228    514   1122       N  
ATOM   2281  CA  ALA B 233      27.263 -29.854  45.127  1.00 48.49           C  
ANISOU 2281  CA  ALA B 233     6617   6393   5415   1212    512   1001       C  
ATOM   2282  C   ALA B 233      26.218 -29.346  46.118  1.00 49.17           C  
ANISOU 2282  C   ALA B 233     6698   6580   5404   1165    600    983       C  
ATOM   2283  O   ALA B 233      26.566 -28.806  47.167  1.00 47.01           O  
ANISOU 2283  O   ALA B 233     6426   6471   4964   1154    607    958       O  
ATOM   2284  CB  ALA B 233      27.452 -28.854  43.987  1.00 45.56           C  
ANISOU 2284  CB  ALA B 233     6237   5951   5124   1206    486    843       C  
ATOM   2285  N   ARG B 234      24.940 -29.514  45.784  1.00 51.68           N  
ANISOU 2285  N   ARG B 234     7001   6818   5819   1136    669    986       N  
ATOM   2286  CA  ARG B 234      23.865 -29.042  46.653  1.00 50.82           C  
ANISOU 2286  CA  ARG B 234     6869   6813   5628   1102    766    963       C  
ATOM   2287  C   ARG B 234      23.835 -29.838  47.954  1.00 55.92           C  
ANISOU 2287  C   ARG B 234     7525   7584   6137   1082    802   1117       C  
ATOM   2288  O   ARG B 234      23.416 -29.330  48.993  1.00 54.49           O  
ANISOU 2288  O   ARG B 234     7334   7559   5812   1060    869   1090       O  
ATOM   2289  CB  ARG B 234      22.501 -29.123  45.956  1.00 52.21           C  
ANISOU 2289  CB  ARG B 234     7001   6895   5941   1076    827    944       C  
ATOM   2290  CG  ARG B 234      22.444 -28.511  44.561  1.00 51.62           C  
ANISOU 2290  CG  ARG B 234     6913   6694   6006   1100    786    827       C  
ATOM   2291  CD  ARG B 234      23.273 -27.238  44.441  1.00 53.13           C  
ANISOU 2291  CD  ARG B 234     7134   6912   6143   1133    748    689       C  
ATOM   2292  NE  ARG B 234      22.670 -26.097  45.124  1.00 56.61           N  
ANISOU 2292  NE  ARG B 234     7568   7440   6503   1140    822    582       N  
ATOM   2293  CZ  ARG B 234      23.087 -24.842  44.982  1.00 54.82           C  
ANISOU 2293  CZ  ARG B 234     7373   7203   6251   1159    813    442       C  
ATOM   2294  NH1 ARG B 234      24.104 -24.566  44.173  1.00 46.66           N  
ANISOU 2294  NH1 ARG B 234     6371   6095   5261   1160    731    403       N  
ATOM   2295  NH2 ARG B 234      22.486 -23.860  45.640  1.00 51.44           N  
ANISOU 2295  NH2 ARG B 234     6950   6837   5759   1174    892    338       N  
ATOM   2296  N   ALA B 235      24.282 -31.089  47.891  1.00 57.67           N  
ANISOU 2296  N   ALA B 235     7773   7736   6403   1094    760   1279       N  
ATOM   2297  CA  ALA B 235      24.353 -31.930  49.080  1.00 60.66           C  
ANISOU 2297  CA  ALA B 235     8173   8220   6656   1084    785   1461       C  
ATOM   2298  C   ALA B 235      25.411 -31.401  50.040  1.00 64.23           C  
ANISOU 2298  C   ALA B 235     8631   8871   6902   1116    736   1447       C  
ATOM   2299  O   ALA B 235      25.191 -31.336  51.249  1.00 66.12           O  
ANISOU 2299  O   ALA B 235     8868   9292   6962   1090    784   1503       O  
ATOM   2300  CB  ALA B 235      24.650 -33.370  48.698  1.00 54.65           C  
ANISOU 2300  CB  ALA B 235     7453   7300   6012   1106    750   1638       C  
ATOM   2301  N   ILE B 236      26.560 -31.019  49.492  1.00 61.46           N  
ANISOU 2301  N   ILE B 236     8280   8505   6568   1164    640   1368       N  
ATOM   2302  CA  ILE B 236      27.646 -30.463  50.289  1.00 61.21           C  
ANISOU 2302  CA  ILE B 236     8238   8674   6346   1179    579   1334       C  
ATOM   2303  C   ILE B 236      27.255 -29.112  50.879  1.00 67.65           C  
ANISOU 2303  C   ILE B 236     9045   9627   7030   1122    633   1151       C  
ATOM   2304  O   ILE B 236      27.515 -28.834  52.050  1.00 74.14           O  
ANISOU 2304  O   ILE B 236     9864  10661   7642   1100    639   1154       O  
ATOM   2305  CB  ILE B 236      28.924 -30.290  49.450  1.00 56.93           C  
ANISOU 2305  CB  ILE B 236     7679   8085   5866   1228    471   1274       C  
ATOM   2306  CG1 ILE B 236      29.393 -31.640  48.909  1.00 56.79           C  
ANISOU 2306  CG1 ILE B 236     7672   7932   5972   1306    422   1443       C  
ATOM   2307  CG2 ILE B 236      30.022 -29.638  50.274  1.00 58.60           C  
ANISOU 2307  CG2 ILE B 236     7862   8527   5875   1221    405   1221       C  
ATOM   2308  CD1 ILE B 236      30.581 -31.540  47.978  1.00 59.49           C  
ANISOU 2308  CD1 ILE B 236     7986   8229   6389   1363    331   1381       C  
ATOM   2309  N   LEU B 237      26.638 -28.275  50.068  1.00 63.07           N  
ANISOU 2309  N   LEU B 237     8465   8928   6571   1104    673    990       N  
ATOM   2310  CA  LEU B 237      26.253 -26.954  50.493  1.00 61.36           C  
ANISOU 2310  CA  LEU B 237     8254   8795   6266   1067    732    802       C  
ATOM   2311  C   LEU B 237      25.192 -26.927  51.578  1.00 68.18           C  
ANISOU 2311  C   LEU B 237     9110   9788   7006   1041    845    821       C  
ATOM   2312  O   LEU B 237      25.125 -25.986  52.334  1.00 68.68           O  
ANISOU 2312  O   LEU B 237     9184   9985   6926   1015    889    684       O  
ATOM   2313  CB  LEU B 237      25.809 -26.123  49.299  1.00 55.86           C  
ANISOU 2313  CB  LEU B 237     7561   7920   5744   1075    748    653       C  
ATOM   2314  CG  LEU B 237      26.901 -25.732  48.319  1.00 55.72           C  
ANISOU 2314  CG  LEU B 237     7554   7812   5807   1083    652    582       C  
ATOM   2315  CD1 LEU B 237      26.331 -25.267  47.053  1.00 51.27           C  
ANISOU 2315  CD1 LEU B 237     6992   7062   5426   1099    668    503       C  
ATOM   2316  CD2 LEU B 237      27.771 -24.689  48.890  1.00 56.02           C  
ANISOU 2316  CD2 LEU B 237     7611   7973   5701   1040    622    443       C  
ATOM   2317  N   THR B 238      24.363 -27.951  51.653  1.00 70.94           N  
ANISOU 2317  N   THR B 238     9442  10101   7410   1038    898    983       N  
ATOM   2318  CA  THR B 238      23.317 -27.981  52.653  1.00 76.47           C  
ANISOU 2318  CA  THR B 238    10122  10940   7994   1005   1016   1014       C  
ATOM   2319  C   THR B 238      23.587 -29.024  53.713  1.00 83.47           C  
ANISOU 2319  C   THR B 238    11018  11973   8723    987   1013   1227       C  
ATOM   2320  O   THR B 238      24.234 -28.747  54.693  1.00 85.16           O  
ANISOU 2320  O   THR B 238    11245  12386   8726    980    990   1218       O  
ATOM   2321  CB  THR B 238      21.980 -28.336  52.052  1.00 73.06           C  
ANISOU 2321  CB  THR B 238     9648  10385   7727    993   1100   1047       C  
ATOM   2322  OG1 THR B 238      22.032 -29.668  51.553  1.00 72.25           O  
ANISOU 2322  OG1 THR B 238     9551  10152   7747    982   1060   1238       O  
ATOM   2323  CG2 THR B 238      21.618 -27.407  50.965  1.00 68.65           C  
ANISOU 2323  CG2 THR B 238     9073   9685   7327   1024   1100    871       C  
ATOM   2324  N   GLY B 239      23.095 -30.237  53.511  1.00 87.66           N  
ANISOU 2324  N   GLY B 239    11546  12404   9356    974   1034   1424       N  
ATOM   2325  CA  GLY B 239      23.298 -31.290  54.489  1.00 91.96           C  
ANISOU 2325  CA  GLY B 239    12113  13062   9767    960   1037   1658       C  
ATOM   2326  C   GLY B 239      23.801 -32.601  53.928  1.00 92.92           C  
ANISOU 2326  C   GLY B 239    12273  13004  10031    993    965   1861       C  
ATOM   2327  O   GLY B 239      23.135 -33.244  53.125  1.00 93.50           O  
ANISOU 2327  O   GLY B 239    12348  12877  10302    968    995   1911       O  
ATOM   2328  N   SER B 245      32.076 -32.214  56.045  1.00 95.37           N  
ANISOU 2328  N   SER B 245    12457  14225   9553   1348    244   2020       N  
ATOM   2329  CA  SER B 245      31.809 -30.863  55.565  1.00 92.47           C  
ANISOU 2329  CA  SER B 245    12084  13830   9221   1253    280   1722       C  
ATOM   2330  C   SER B 245      33.067 -30.211  54.997  1.00 88.08           C  
ANISOU 2330  C   SER B 245    11466  13324   8677   1260    169   1577       C  
ATOM   2331  O   SER B 245      34.178 -30.508  55.434  1.00 92.36           O  
ANISOU 2331  O   SER B 245    11946  14055   9092   1312     62   1670       O  
ATOM   2332  CB  SER B 245      31.227 -30.000  56.686  1.00 94.77           C  
ANISOU 2332  CB  SER B 245    12385  14344   9280   1152    351   1603       C  
ATOM   2333  OG  SER B 245      29.896 -30.384  56.983  1.00 97.21           O  
ANISOU 2333  OG  SER B 245    12741  14581   9615   1126    479   1682       O  
ATOM   2334  N   PRO B 246      32.888 -29.313  54.017  1.00 76.94           N  
ANISOU 2334  N   PRO B 246    10065  11752   7415   1207    195   1358       N  
ATOM   2335  CA  PRO B 246      33.980 -28.609  53.336  1.00 71.48           C  
ANISOU 2335  CA  PRO B 246     9320  11080   6759   1190    109   1208       C  
ATOM   2336  C   PRO B 246      34.698 -27.640  54.265  1.00 68.48           C  
ANISOU 2336  C   PRO B 246     8897  10990   6133   1096     57   1069       C  
ATOM   2337  O   PRO B 246      34.083 -27.108  55.188  1.00 70.44           O  
ANISOU 2337  O   PRO B 246     9181  11361   6220   1023    120    993       O  
ATOM   2338  CB  PRO B 246      33.243 -27.815  52.252  1.00 71.57           C  
ANISOU 2338  CB  PRO B 246     9380  10848   6966   1137    183   1022       C  
ATOM   2339  CG  PRO B 246      31.873 -27.622  52.822  1.00 73.57           C  
ANISOU 2339  CG  PRO B 246     9694  11076   7185   1096    302   1000       C  
ATOM   2340  CD  PRO B 246      31.582 -28.949  53.443  1.00 75.50           C  
ANISOU 2340  CD  PRO B 246     9943  11358   7387   1164    312   1256       C  
ATOM   2341  N   PHE B 247      35.984 -27.409  54.021  1.00 64.85           N  
ANISOU 2341  N   PHE B 247     8355  10647   5638   1093    -52   1026       N  
ATOM   2342  CA  PHE B 247      36.721 -26.410  54.782  1.00 62.87           C  
ANISOU 2342  CA  PHE B 247     8057  10666   5166    975   -108    863       C  
ATOM   2343  C   PHE B 247      36.382 -25.021  54.263  1.00 59.31           C  
ANISOU 2343  C   PHE B 247     7664  10082   4787    845    -45    582       C  
ATOM   2344  O   PHE B 247      36.471 -24.762  53.066  1.00 55.20           O  
ANISOU 2344  O   PHE B 247     7153   9348   4474    847    -38    516       O  
ATOM   2345  CB  PHE B 247      38.227 -26.650  54.687  1.00 60.90           C  
ANISOU 2345  CB  PHE B 247     7679  10606   4855   1008   -249    917       C  
ATOM   2346  CG  PHE B 247      39.046 -25.624  55.417  1.00 64.03           C  
ANISOU 2346  CG  PHE B 247     8013  11292   5025    862   -316    737       C  
ATOM   2347  CD1 PHE B 247      39.515 -24.497  54.762  1.00 59.94           C  
ANISOU 2347  CD1 PHE B 247     7484  10720   4569    732   -324    503       C  
ATOM   2348  CD2 PHE B 247      39.337 -25.782  56.763  1.00 69.10           C  
ANISOU 2348  CD2 PHE B 247     8609  12264   5382    844   -371    803       C  
ATOM   2349  CE1 PHE B 247      40.262 -23.549  55.435  1.00 63.94           C  
ANISOU 2349  CE1 PHE B 247     7940  11483   4872    574   -383    324       C  
ATOM   2350  CE2 PHE B 247      40.086 -24.839  57.441  1.00 69.41           C  
ANISOU 2350  CE2 PHE B 247     8588  12583   5200    692   -438    620       C  
ATOM   2351  CZ  PHE B 247      40.550 -23.721  56.776  1.00 67.99           C  
ANISOU 2351  CZ  PHE B 247     8401  12333   5098    551   -443    373       C  
ATOM   2352  N   VAL B 248      36.000 -24.127  55.167  1.00 61.24           N  
ANISOU 2352  N   VAL B 248     7954  10455   4859    734      4    419       N  
ATOM   2353  CA  VAL B 248      35.551 -22.796  54.776  1.00 58.43           C  
ANISOU 2353  CA  VAL B 248     7676   9947   4576    624     81    156       C  
ATOM   2354  C   VAL B 248      36.667 -21.760  54.819  1.00 59.22           C  
ANISOU 2354  C   VAL B 248     7739  10178   4583    481      7    -43       C  
ATOM   2355  O   VAL B 248      37.327 -21.582  55.843  1.00 60.98           O  
ANISOU 2355  O   VAL B 248     7910  10696   4562    406    -58    -85       O  
ATOM   2356  CB  VAL B 248      34.398 -22.309  55.671  1.00 58.00           C  
ANISOU 2356  CB  VAL B 248     7708   9919   4410    587    200     56       C  
ATOM   2357  CG1 VAL B 248      33.995 -20.891  55.290  1.00 54.48           C  
ANISOU 2357  CG1 VAL B 248     7349   9305   4044    491    280   -220       C  
ATOM   2358  CG2 VAL B 248      33.214 -23.259  55.569  1.00 55.33           C  
ANISOU 2358  CG2 VAL B 248     7400   9445   4177    703    286    241       C  
ATOM   2359  N   ILE B 249      36.873 -21.080  53.696  1.00 58.98           N  
ANISOU 2359  N   ILE B 249     7733   9936   4742    435     16   -162       N  
ATOM   2360  CA  ILE B 249      37.791 -19.952  53.640  1.00 57.97           C  
ANISOU 2360  CA  ILE B 249     7591   9880   4556    270    -30   -373       C  
ATOM   2361  C   ILE B 249      36.977 -18.668  53.707  1.00 55.69           C  
ANISOU 2361  C   ILE B 249     7441   9420   4300    171     84   -614       C  
ATOM   2362  O   ILE B 249      36.286 -18.307  52.754  1.00 51.92           O  
ANISOU 2362  O   ILE B 249     7042   8648   4038    207    161   -649       O  
ATOM   2363  CB  ILE B 249      38.640 -19.966  52.356  1.00 52.31           C  
ANISOU 2363  CB  ILE B 249     6811   9049   4016    267    -90   -347       C  
ATOM   2364  CG1 ILE B 249      39.453 -21.260  52.271  1.00 52.53           C  
ANISOU 2364  CG1 ILE B 249     6698   9238   4022    390   -195   -114       C  
ATOM   2365  CG2 ILE B 249      39.555 -18.752  52.312  1.00 50.12           C  
ANISOU 2365  CG2 ILE B 249     6521   8842   3680     68   -127   -566       C  
ATOM   2366  CD1 ILE B 249      40.266 -21.394  50.999  1.00 54.08           C  
ANISOU 2366  CD1 ILE B 249     6821   9340   4388    410   -243    -81       C  
ATOM   2367  N   TYR B 250      37.057 -17.987  54.844  1.00 55.95           N  
ANISOU 2367  N   TYR B 250     7503   9642   4114     55     94   -781       N  
ATOM   2368  CA  TYR B 250      36.236 -16.811  55.095  1.00 58.68           C  
ANISOU 2368  CA  TYR B 250     7989   9837   4470    -20    215  -1019       C  
ATOM   2369  C   TYR B 250      37.084 -15.575  55.373  1.00 63.78           C  
ANISOU 2369  C   TYR B 250     8665  10550   5016   -231    185  -1280       C  
ATOM   2370  O   TYR B 250      36.557 -14.469  55.485  1.00 65.40           O  
ANISOU 2370  O   TYR B 250     9002  10596   5252   -307    283  -1504       O  
ATOM   2371  CB  TYR B 250      35.301 -17.071  56.276  1.00 56.36           C  
ANISOU 2371  CB  TYR B 250     7732   9680   4002     33    292  -1014       C  
ATOM   2372  CG  TYR B 250      36.030 -17.510  57.525  1.00 58.52           C  
ANISOU 2372  CG  TYR B 250     7917  10350   3969    -22    202   -974       C  
ATOM   2373  CD1 TYR B 250      36.513 -16.579  58.434  1.00 59.78           C  
ANISOU 2373  CD1 TYR B 250     8101  10705   3907   -193    188  -1215       C  
ATOM   2374  CD2 TYR B 250      36.247 -18.858  57.787  1.00 60.29           C  
ANISOU 2374  CD2 TYR B 250     8036  10750   4122     95    127   -693       C  
ATOM   2375  CE1 TYR B 250      37.184 -16.977  59.575  1.00 65.29           C  
ANISOU 2375  CE1 TYR B 250     8708  11796   4303   -246     95  -1176       C  
ATOM   2376  CE2 TYR B 250      36.917 -19.265  58.925  1.00 65.16           C  
ANISOU 2376  CE2 TYR B 250     8567  11740   4449     58     37   -633       C  
ATOM   2377  CZ  TYR B 250      37.384 -18.320  59.815  1.00 67.46           C  
ANISOU 2377  CZ  TYR B 250     8871  12252   4507   -114     17   -874       C  
ATOM   2378  OH  TYR B 250      38.053 -18.719  60.948  1.00 72.03           O  
ANISOU 2378  OH  TYR B 250     9356  13234   4778   -154    -82   -813       O  
ATOM   2379  N   ASP B 251      38.393 -15.768  55.501  1.00 62.03           N  
ANISOU 2379  N   ASP B 251     8322  10569   4679   -325     52  -1254       N  
ATOM   2380  CA  ASP B 251      39.313 -14.651  55.702  1.00 62.60           C  
ANISOU 2380  CA  ASP B 251     8403  10722   4661   -554     11  -1496       C  
ATOM   2381  C   ASP B 251      40.759 -15.032  55.389  1.00 64.63           C  
ANISOU 2381  C   ASP B 251     8488  11197   4873   -624   -139  -1408       C  
ATOM   2382  O   ASP B 251      41.044 -16.155  54.970  1.00 58.73           O  
ANISOU 2382  O   ASP B 251     7622  10514   4178   -475   -206  -1162       O  
ATOM   2383  CB  ASP B 251      39.191 -14.070  57.120  1.00 61.69           C  
ANISOU 2383  CB  ASP B 251     8338  10830   4272   -674     34  -1701       C  
ATOM   2384  CG  ASP B 251      39.758 -14.989  58.187  1.00 63.20           C  
ANISOU 2384  CG  ASP B 251     8383  11448   4181   -652    -79  -1565       C  
ATOM   2385  OD1 ASP B 251      39.990 -16.180  57.895  1.00 64.31           O  
ANISOU 2385  OD1 ASP B 251     8407  11671   4358   -499   -151  -1286       O  
ATOM   2386  OD2 ASP B 251      39.971 -14.517  59.324  1.00 65.07           O  
ANISOU 2386  OD2 ASP B 251     8628  11939   4156   -784    -95  -1737       O  
ATOM   2387  N   MET B 252      41.667 -14.085  55.600  1.00 69.11           N  
ANISOU 2387  N   MET B 252     9038  11875   5344   -854   -187  -1619       N  
ATOM   2388  CA  MET B 252      43.066 -14.264  55.234  1.00 71.66           C  
ANISOU 2388  CA  MET B 252     9188  12405   5636   -949   -320  -1568       C  
ATOM   2389  C   MET B 252      43.741 -15.369  56.046  1.00 75.09           C  
ANISOU 2389  C   MET B 252     9432  13255   5845   -865   -453  -1384       C  
ATOM   2390  O   MET B 252      44.632 -16.058  55.551  1.00 76.24           O  
ANISOU 2390  O   MET B 252     9410  13535   6021   -807   -553  -1219       O  
ATOM   2391  CB  MET B 252      43.826 -12.946  55.397  1.00 72.64           C  
ANISOU 2391  CB  MET B 252     9341  12570   5691  -1246   -335  -1854       C  
ATOM   2392  CG  MET B 252      44.923 -12.741  54.373  1.00 74.58           C  
ANISOU 2392  CG  MET B 252     9475  12802   6058  -1357   -400  -1834       C  
ATOM   2393  SD  MET B 252      44.271 -12.729  52.692  1.00 81.16           S  
ANISOU 2393  SD  MET B 252    10415  13165   7259  -1222   -295  -1717       S  
ATOM   2394  CE  MET B 252      43.124 -11.357  52.790  1.00 99.15           C  
ANISOU 2394  CE  MET B 252    12975  15062   9634  -1315   -133  -1971       C  
ATOM   2395  N   ASN B 253      43.313 -15.532  57.294  1.00 74.37           N  
ANISOU 2395  N   ASN B 253     9365  13369   5522   -851   -450  -1409       N  
ATOM   2396  CA  ASN B 253      43.882 -16.555  58.167  1.00 74.85           C  
ANISOU 2396  CA  ASN B 253     9260  13833   5347   -765   -574  -1220       C  
ATOM   2397  C   ASN B 253      43.441 -17.966  57.793  1.00 70.09           C  
ANISOU 2397  C   ASN B 253     8615  13156   4860   -484   -575   -888       C  
ATOM   2398  O   ASN B 253      44.239 -18.904  57.825  1.00 69.01           O  
ANISOU 2398  O   ASN B 253     8311  13245   4664   -379   -692   -677       O  
ATOM   2399  CB  ASN B 253      43.552 -16.261  59.633  1.00 81.40           C  
ANISOU 2399  CB  ASN B 253    10136  14922   5871   -849   -566  -1349       C  
ATOM   2400  CG  ASN B 253      44.440 -15.181  60.224  1.00 87.54           C  
ANISOU 2400  CG  ASN B 253    10878  15936   6449  -1135   -632  -1637       C  
ATOM   2401  OD1 ASN B 253      45.491 -14.856  59.671  1.00 91.01           O  
ANISOU 2401  OD1 ASN B 253    11207  16435   6937  -1264   -716  -1688       O  
ATOM   2402  ND2 ASN B 253      44.022 -14.620  61.352  1.00 88.30           N  
ANISOU 2402  ND2 ASN B 253    11063  16175   6311  -1245   -591  -1834       N  
ATOM   2403  N   SER B 254      42.168 -18.114  57.438  1.00 64.91           N  
ANISOU 2403  N   SER B 254     8109  12181   4373   -362   -442   -845       N  
ATOM   2404  CA  SER B 254      41.636 -19.417  57.061  1.00 61.31           C  
ANISOU 2404  CA  SER B 254     7636  11617   4044   -119   -427   -551       C  
ATOM   2405  C   SER B 254      42.148 -19.844  55.688  1.00 64.03           C  
ANISOU 2405  C   SER B 254     7912  11778   4640    -35   -460   -433       C  
ATOM   2406  O   SER B 254      42.216 -21.035  55.387  1.00 64.99           O  
ANISOU 2406  O   SER B 254     7964  11896   4833    152   -497   -183       O  
ATOM   2407  CB  SER B 254      40.105 -19.412  57.092  1.00 56.66           C  
ANISOU 2407  CB  SER B 254     7212  10764   3553    -36   -275   -554       C  
ATOM   2408  OG  SER B 254      39.578 -18.329  56.349  1.00 55.31           O  
ANISOU 2408  OG  SER B 254     7169  10281   3567   -123   -173   -765       O  
ATOM   2409  N   LEU B 255      42.511 -18.868  54.862  1.00 63.33           N  
ANISOU 2409  N   LEU B 255     7849  11533   4681   -176   -441   -615       N  
ATOM   2410  CA  LEU B 255      43.076 -19.155  53.546  1.00 61.85           C  
ANISOU 2410  CA  LEU B 255     7590  11201   4709   -121   -468   -528       C  
ATOM   2411  C   LEU B 255      44.408 -19.885  53.672  1.00 67.83           C  
ANISOU 2411  C   LEU B 255     8134  12281   5359    -80   -613   -389       C  
ATOM   2412  O   LEU B 255      44.620 -20.923  53.044  1.00 65.03           O  
ANISOU 2412  O   LEU B 255     7701  11886   5123    103   -642   -182       O  
ATOM   2413  CB  LEU B 255      43.270 -17.867  52.744  1.00 57.06           C  
ANISOU 2413  CB  LEU B 255     7053  10399   4229   -309   -420   -751       C  
ATOM   2414  CG  LEU B 255      44.032 -18.030  51.426  1.00 62.90           C  
ANISOU 2414  CG  LEU B 255     7701  11048   5150   -293   -452   -684       C  
ATOM   2415  CD1 LEU B 255      43.245 -18.885  50.441  1.00 57.68           C  
ANISOU 2415  CD1 LEU B 255     7091  10111   4714    -79   -390   -506       C  
ATOM   2416  CD2 LEU B 255      44.358 -16.677  50.817  1.00 64.45           C  
ANISOU 2416  CD2 LEU B 255     7960  11103   5426   -517   -413   -902       C  
ATOM   2417  N   MET B 256      45.303 -19.332  54.485  1.00 72.17           N  
ANISOU 2417  N   MET B 256     8584  13156   5683   -249   -702   -513       N  
ATOM   2418  CA  MET B 256      46.612 -19.932  54.711  1.00 80.18           C  
ANISOU 2418  CA  MET B 256     9369  14528   6566   -218   -849   -394       C  
ATOM   2419  C   MET B 256      46.471 -21.356  55.232  1.00 80.73           C  
ANISOU 2419  C   MET B 256     9375  14730   6568     36   -900   -105       C  
ATOM   2420  O   MET B 256      47.174 -22.264  54.789  1.00 83.89           O  
ANISOU 2420  O   MET B 256     9631  15215   7027    195   -972     86       O  
ATOM   2421  CB  MET B 256      47.426 -19.091  55.695  1.00 87.26           C  
ANISOU 2421  CB  MET B 256    10179  15783   7194   -456   -937   -586       C  
ATOM   2422  CG  MET B 256      47.730 -17.684  55.208  1.00 90.68           C  
ANISOU 2422  CG  MET B 256    10667  16096   7690   -731   -896   -871       C  
ATOM   2423  SD  MET B 256      48.786 -16.771  56.350  1.00125.11           S  
ANISOU 2423  SD  MET B 256    14909  20898  11730  -1034  -1011  -1105       S  
ATOM   2424  CE  MET B 256      50.258 -17.791  56.344  1.00 85.97           C  
ANISOU 2424  CE  MET B 256     9620  16378   6664   -925  -1193   -881       C  
ATOM   2425  N   MET B 257      45.559 -21.544  56.178  1.00 78.73           N  
ANISOU 2425  N   MET B 257     9233  14491   6190     75   -854    -72       N  
ATOM   2426  CA  MET B 257      45.282 -22.868  56.715  1.00 77.34           C  
ANISOU 2426  CA  MET B 257     9029  14404   5953    303   -884    214       C  
ATOM   2427  C   MET B 257      44.665 -23.755  55.637  1.00 74.78           C  
ANISOU 2427  C   MET B 257     8772  13721   5919    506   -809    390       C  
ATOM   2428  O   MET B 257      44.978 -24.941  55.539  1.00 73.89           O  
ANISOU 2428  O   MET B 257     8579  13651   5844    708   -862    639       O  
ATOM   2429  CB  MET B 257      44.352 -22.764  57.926  1.00 76.12           C  
ANISOU 2429  CB  MET B 257     8991  14331   5601    271   -830    193       C  
ATOM   2430  CG  MET B 257      43.889 -24.097  58.487  1.00 75.16           C  
ANISOU 2430  CG  MET B 257     8874  14259   5426    489   -835    498       C  
ATOM   2431  SD  MET B 257      43.120 -23.922  60.111  1.00 95.31           S  
ANISOU 2431  SD  MET B 257    11509  17049   7655    420   -799    473       S  
ATOM   2432  CE  MET B 257      42.360 -25.532  60.307  1.00 72.04           C  
ANISOU 2432  CE  MET B 257     8608  13997   4768    682   -762    857       C  
ATOM   2433  N   GLY B 258      43.795 -23.165  54.824  1.00 74.33           N  
ANISOU 2433  N   GLY B 258     8864  13311   6066    451   -686    256       N  
ATOM   2434  CA  GLY B 258      43.140 -23.888  53.749  1.00 74.46           C  
ANISOU 2434  CA  GLY B 258     8951  12987   6353    611   -612    387       C  
ATOM   2435  C   GLY B 258      44.131 -24.561  52.823  1.00 75.97           C  
ANISOU 2435  C   GLY B 258     9004  13187   6672    727   -683    506       C  
ATOM   2436  O   GLY B 258      43.871 -25.642  52.296  1.00 72.46           O  
ANISOU 2436  O   GLY B 258     8571  12581   6377    919   -665    695       O  
ATOM   2437  N   GLU B 259      45.278 -23.920  52.631  1.00 83.70           N  
ANISOU 2437  N   GLU B 259     9851  14359   7590    606   -760    387       N  
ATOM   2438  CA  GLU B 259      46.313 -24.448  51.753  1.00 90.71           C  
ANISOU 2438  CA  GLU B 259    10584  15296   8585    704   -823    475       C  
ATOM   2439  C   GLU B 259      47.168 -25.482  52.475  1.00 98.32           C  
ANISOU 2439  C   GLU B 259    11379  16576   9400    868   -944    688       C  
ATOM   2440  O   GLU B 259      48.304 -25.745  52.082  1.00102.95           O  
ANISOU 2440  O   GLU B 259    11785  17339   9993    922  -1025    734       O  
ATOM   2441  CB  GLU B 259      47.190 -23.311  51.230  1.00 92.06           C  
ANISOU 2441  CB  GLU B 259    10671  15555   8753    491   -848    264       C  
ATOM   2442  CG  GLU B 259      46.402 -22.166  50.617  1.00 90.89           C  
ANISOU 2442  CG  GLU B 259    10697  15106   8731    319   -734     56       C  
ATOM   2443  CD  GLU B 259      47.285 -21.016  50.178  1.00 91.94           C  
ANISOU 2443  CD  GLU B 259    10760  15322   8852     87   -755   -143       C  
ATOM   2444  OE1 GLU B 259      46.883 -20.284  49.249  1.00 91.49           O  
ANISOU 2444  OE1 GLU B 259    10814  14987   8960     -6   -667   -258       O  
ATOM   2445  OE2 GLU B 259      48.379 -20.845  50.755  1.00 94.28           O  
ANISOU 2445  OE2 GLU B 259    10886  15965   8972     -8   -860   -176       O  
ATOM   2446  N   ASP B 260      46.614 -26.067  53.532  1.00101.22           N  
ANISOU 2446  N   ASP B 260    11803  17025   9633    953   -953    827       N  
ATOM   2447  CA  ASP B 260      47.339 -27.043  54.334  1.00104.12           C  
ANISOU 2447  CA  ASP B 260    12026  17695   9840   1118  -1069   1055       C  
ATOM   2448  C   ASP B 260      46.394 -28.113  54.869  1.00105.07           C  
ANISOU 2448  C   ASP B 260    12270  17683   9970   1296  -1023   1287       C  
ATOM   2449  O   ASP B 260      45.478 -27.818  55.637  1.00107.52           O  
ANISOU 2449  O   ASP B 260    12707  17974  10171   1211   -965   1250       O  
ATOM   2450  CB  ASP B 260      48.058 -26.345  55.491  0.50109.13           C  
ANISOU 2450  CB  ASP B 260    12540  18762  10164    954  -1177    958       C  
ATOM   2451  CG  ASP B 260      48.996 -27.271  56.239  0.50114.53           C  
ANISOU 2451  CG  ASP B 260    13035  19810  10671   1125  -1319   1194       C  
ATOM   2452  OD1 ASP B 260      49.595 -26.827  57.241  0.50117.04           O  
ANISOU 2452  OD1 ASP B 260    13239  20520  10711   1008  -1422   1141       O  
ATOM   2453  OD2 ASP B 260      49.137 -28.441  55.825  0.50116.04           O  
ANISOU 2453  OD2 ASP B 260    13194  19897  10999   1380  -1328   1432       O  
ATOM   2454  N   PHE B 264      46.014 -27.994  47.243  1.00 74.83           N  
ANISOU 2454  N   PHE B 264     8599  12369   7462   1419   -668    923       N  
ATOM   2455  CA  PHE B 264      45.834 -27.381  45.931  1.00 75.47           C  
ANISOU 2455  CA  PHE B 264     8728  12238   7707   1331   -596    779       C  
ATOM   2456  C   PHE B 264      46.963 -27.761  44.978  1.00 76.42           C  
ANISOU 2456  C   PHE B 264     8692  12440   7905   1423   -627    796       C  
ATOM   2457  O   PHE B 264      48.100 -27.978  45.397  1.00 77.59           O  
ANISOU 2457  O   PHE B 264     8659  12882   7942   1473   -716    849       O  
ATOM   2458  CB  PHE B 264      45.731 -25.860  46.059  1.00 73.53           C  
ANISOU 2458  CB  PHE B 264     8523  12029   7386   1071   -577    569       C  
ATOM   2459  CG  PHE B 264      44.600 -25.404  46.934  1.00 74.07           C  
ANISOU 2459  CG  PHE B 264     8747  12014   7385    986   -531    524       C  
ATOM   2460  CD1 PHE B 264      44.760 -25.315  48.306  1.00 76.37           C  
ANISOU 2460  CD1 PHE B 264     9004  12551   7462    945   -589    544       C  
ATOM   2461  CD2 PHE B 264      43.373 -25.071  46.385  1.00 72.77           C  
ANISOU 2461  CD2 PHE B 264     8750  11542   7356    953   -428    462       C  
ATOM   2462  CE1 PHE B 264      43.719 -24.897  49.114  1.00 76.01           C  
ANISOU 2462  CE1 PHE B 264     9096  12443   7342    871   -535    493       C  
ATOM   2463  CE2 PHE B 264      42.329 -24.652  47.188  1.00 71.40           C  
ANISOU 2463  CE2 PHE B 264     8704  11305   7120    888   -377    417       C  
ATOM   2464  CZ  PHE B 264      42.503 -24.566  48.554  1.00 72.52           C  
ANISOU 2464  CZ  PHE B 264     8816  11690   7049    847   -425    427       C  
ATOM   2465  N   LYS B 265      46.638 -27.834  43.692  1.00 75.72           N  
ANISOU 2465  N   LYS B 265     8664  12108   7998   1447   -552    749       N  
ATOM   2466  CA  LYS B 265      47.586 -28.286  42.681  1.00 74.72           C  
ANISOU 2466  CA  LYS B 265     8404  12031   7957   1552   -559    762       C  
ATOM   2467  C   LYS B 265      48.278 -27.126  41.966  1.00 71.50           C  
ANISOU 2467  C   LYS B 265     7911  11725   7531   1355   -551    598       C  
ATOM   2468  O   LYS B 265      49.231 -27.331  41.216  1.00 70.04           O  
ANISOU 2468  O   LYS B 265     7579  11654   7379   1409   -560    592       O  
ATOM   2469  CB  LYS B 265      46.873 -29.187  41.671  1.00 73.20           C  
ANISOU 2469  CB  LYS B 265     8323  11527   7962   1705   -482    811       C  
ATOM   2470  CG  LYS B 265      46.546 -30.571  42.210  1.00 76.52           C  
ANISOU 2470  CG  LYS B 265     8787  11864   8422   1931   -494    996       C  
ATOM   2471  CD  LYS B 265      45.118 -30.981  41.876  1.00 77.00           C  
ANISOU 2471  CD  LYS B 265     9053  11583   8621   1948   -411   1014       C  
ATOM   2472  CE  LYS B 265      44.763 -30.673  40.430  1.00 76.75           C  
ANISOU 2472  CE  LYS B 265     9079  11350   8733   1892   -337    887       C  
ATOM   2473  NZ  LYS B 265      43.382 -31.123  40.085  1.00 73.58           N  
ANISOU 2473  NZ  LYS B 265     8855  10640   8460   1908   -265    903       N  
ATOM   2474  N   HIS B 266      47.800 -25.910  42.206  1.00 72.01           N  
ANISOU 2474  N   HIS B 266     8069  11747   7544   1127   -527    466       N  
ATOM   2475  CA  HIS B 266      48.349 -24.733  41.538  1.00 74.88           C  
ANISOU 2475  CA  HIS B 266     8386  12164   7901    915   -508    316       C  
ATOM   2476  C   HIS B 266      49.435 -24.043  42.366  1.00 81.80           C  
ANISOU 2476  C   HIS B 266     9102  13383   8597    758   -592    252       C  
ATOM   2477  O   HIS B 266      49.751 -22.874  42.138  1.00 82.85           O  
ANISOU 2477  O   HIS B 266     9229  13553   8697    524   -578    111       O  
ATOM   2478  CB  HIS B 266      47.232 -23.745  41.189  1.00 70.73           C  
ANISOU 2478  CB  HIS B 266     8064  11364   7445    758   -426    204       C  
ATOM   2479  CG  HIS B 266      46.562 -23.144  42.383  1.00 69.89           C  
ANISOU 2479  CG  HIS B 266     8066  11256   7235    651   -434    153       C  
ATOM   2480  ND1 HIS B 266      45.590 -23.806  43.106  1.00 69.33           N  
ANISOU 2480  ND1 HIS B 266     8098  11084   7160    773   -424    241       N  
ATOM   2481  CD2 HIS B 266      46.719 -21.941  42.983  1.00 69.81           C  
ANISOU 2481  CD2 HIS B 266     8077  11331   7117    429   -444     14       C  
ATOM   2482  CE1 HIS B 266      45.183 -23.038  44.098  1.00 68.41           C  
ANISOU 2482  CE1 HIS B 266     8055  11008   6929    641   -425    158       C  
ATOM   2483  NE2 HIS B 266      45.852 -21.899  44.047  1.00 69.51           N  
ANISOU 2483  NE2 HIS B 266     8152  11253   7006    433   -438     12       N  
ATOM   2484  N   ILE B 267      50.002 -24.779  43.318  1.00 84.58           N  
ANISOU 2484  N   ILE B 267     9325  13984   8829    882   -682    360       N  
ATOM   2485  CA  ILE B 267      51.071 -24.272  44.177  1.00 85.81           C  
ANISOU 2485  CA  ILE B 267     9299  14513   8791    751   -780    314       C  
ATOM   2486  C   ILE B 267      50.733 -22.897  44.740  1.00 84.41           C  
ANISOU 2486  C   ILE B 267     9226  14328   8518    461   -768    137       C  
ATOM   2487  O   ILE B 267      50.418 -22.764  45.921  1.00 85.45           O  
ANISOU 2487  O   ILE B 267     9402  14557   8509    419   -810    129       O  
ATOM   2488  CB  ILE B 267      52.428 -24.204  43.436  1.00 87.07           C  
ANISOU 2488  CB  ILE B 267     9224  14908   8952    727   -810    290       C  
ATOM   2489  CG1 ILE B 267      53.579 -24.494  44.401  1.00 92.69           C  
ANISOU 2489  CG1 ILE B 267     9690  16052   9477    760   -939    351       C  
ATOM   2490  CG2 ILE B 267      52.615 -22.851  42.762  1.00 88.08           C  
ANISOU 2490  CG2 ILE B 267     9378  14987   9101    434   -757    108       C  
ATOM   2491  CD1 ILE B 267      53.493 -25.856  45.055  1.00 94.77           C  
ANISOU 2491  CD1 ILE B 267     9920  16371   9718   1065   -995    559       C  
ATOM   2492  N   GLU B 276      51.461 -12.733  46.338  1.00 92.71           N  
ANISOU 2492  N   GLU B 276    10856  15160   9211  -1784   -590  -1364       N  
ATOM   2493  CA  GLU B 276      50.309 -11.985  46.828  1.00 92.47           C  
ANISOU 2493  CA  GLU B 276    11096  14828   9208  -1829   -506  -1496       C  
ATOM   2494  C   GLU B 276      49.054 -12.853  46.865  1.00 89.00           C  
ANISOU 2494  C   GLU B 276    10774  14198   8845  -1516   -462  -1354       C  
ATOM   2495  O   GLU B 276      48.894 -13.768  46.058  1.00 87.63           O  
ANISOU 2495  O   GLU B 276    10546  13963   8786  -1295   -454  -1168       O  
ATOM   2496  CB  GLU B 276      50.071 -10.739  45.969  1.00 94.54           C  
ANISOU 2496  CB  GLU B 276    11545  14739   9635  -2029   -396  -1614       C  
ATOM   2497  CG  GLU B 276      48.868  -9.913  46.395  1.00 97.55           C  
ANISOU 2497  CG  GLU B 276    12211  14783  10070  -2055   -298  -1753       C  
ATOM   2498  CD  GLU B 276      48.654  -8.692  45.522  1.00101.16           C  
ANISOU 2498  CD  GLU B 276    12859  14877  10701  -2233   -190  -1846       C  
ATOM   2499  OE1 GLU B 276      47.576  -8.069  45.626  1.00100.80           O  
ANISOU 2499  OE1 GLU B 276    13052  14501  10745  -2199    -95  -1926       O  
ATOM   2500  OE2 GLU B 276      49.563  -8.353  44.734  1.00104.05           O  
ANISOU 2500  OE2 GLU B 276    13133  15289  11113  -2401   -197  -1832       O  
ATOM   2501  N   VAL B 277      48.166 -12.556  47.809  1.00 86.32           N  
ANISOU 2501  N   VAL B 277    10592  13768   8436  -1507   -428  -1452       N  
ATOM   2502  CA  VAL B 277      46.952 -13.339  48.002  1.00 80.34           C  
ANISOU 2502  CA  VAL B 277     9936  12860   7728  -1238   -384  -1330       C  
ATOM   2503  C   VAL B 277      46.023 -13.299  46.792  1.00 78.45           C  
ANISOU 2503  C   VAL B 277     9845  12230   7734  -1111   -277  -1251       C  
ATOM   2504  O   VAL B 277      45.801 -14.318  46.138  1.00 77.64           O  
ANISOU 2504  O   VAL B 277     9683  12091   7725   -895   -282  -1063       O  
ATOM   2505  CB  VAL B 277      46.174 -12.862  49.239  1.00 77.70           C  
ANISOU 2505  CB  VAL B 277     9746  12509   7266  -1282   -350  -1478       C  
ATOM   2506  CG1 VAL B 277      44.837 -13.579  49.332  1.00 73.77           C  
ANISOU 2506  CG1 VAL B 277     9359  11832   6840  -1022   -284  -1354       C  
ATOM   2507  CG2 VAL B 277      46.998 -13.083  50.497  1.00 81.92           C  
ANISOU 2507  CG2 VAL B 277    10126  13469   7529  -1373   -466  -1530       C  
ATOM   2508  N   ALA B 278      45.478 -12.119  46.508  1.00 77.37           N  
ANISOU 2508  N   ALA B 278     9901  11799   7697  -1244   -182  -1397       N  
ATOM   2509  CA  ALA B 278      44.519 -11.949  45.421  1.00 74.03           C  
ANISOU 2509  CA  ALA B 278     9628  11008   7492  -1129    -83  -1329       C  
ATOM   2510  C   ALA B 278      44.988 -12.610  44.129  1.00 71.18           C  
ANISOU 2510  C   ALA B 278     9151  10645   7248  -1038   -103  -1157       C  
ATOM   2511  O   ALA B 278      44.197 -13.228  43.416  1.00 69.84           O  
ANISOU 2511  O   ALA B 278     9025  10306   7207   -837    -64  -1022       O  
ATOM   2512  CB  ALA B 278      44.240 -10.471  45.191  1.00 75.34           C  
ANISOU 2512  CB  ALA B 278     9989  10892   7746  -1322      6  -1505       C  
ATOM   2513  N   ILE B 279      46.278 -12.479  43.838  1.00 73.39           N  
ANISOU 2513  N   ILE B 279     9277  11132   7477  -1193   -162  -1170       N  
ATOM   2514  CA  ILE B 279      46.854 -13.038  42.620  1.00 72.82           C  
ANISOU 2514  CA  ILE B 279     9079  11091   7497  -1126   -173  -1029       C  
ATOM   2515  C   ILE B 279      46.837 -14.563  42.639  1.00 68.70           C  
ANISOU 2515  C   ILE B 279     8418  10729   6956   -858   -230   -851       C  
ATOM   2516  O   ILE B 279      46.496 -15.200  41.642  1.00 66.44           O  
ANISOU 2516  O   ILE B 279     8133  10316   6797   -694   -200   -724       O  
ATOM   2517  CB  ILE B 279      48.298 -12.550  42.412  1.00 80.07           C  
ANISOU 2517  CB  ILE B 279     9838  12239   8345  -1364   -221  -1092       C  
ATOM   2518  CG1 ILE B 279      48.359 -11.023  42.498  1.00 86.42           C  
ANISOU 2518  CG1 ILE B 279    10793  12876   9166  -1658   -164  -1279       C  
ATOM   2519  CG2 ILE B 279      48.842 -13.046  41.081  1.00 78.38           C  
ANISOU 2519  CG2 ILE B 279     9504  12047   8229  -1296   -213   -957       C  
ATOM   2520  CD1 ILE B 279      49.763 -10.462  42.424  1.00 91.47           C  
ANISOU 2520  CD1 ILE B 279    11277  13751   9724  -1938   -209  -1361       C  
ATOM   2521  N   ARG B 280      47.210 -15.141  43.778  1.00 67.72           N  
ANISOU 2521  N   ARG B 280     8179  10882   6668   -818   -313   -844       N  
ATOM   2522  CA  ARG B 280      47.209 -16.593  43.944  1.00 68.46           C  
ANISOU 2522  CA  ARG B 280     8154  11121   6738   -562   -369   -667       C  
ATOM   2523  C   ARG B 280      45.816 -17.184  43.748  1.00 62.47           C  
ANISOU 2523  C   ARG B 280     7548  10092   6096   -351   -302   -574       C  
ATOM   2524  O   ARG B 280      45.657 -18.214  43.092  1.00 59.17           O  
ANISOU 2524  O   ARG B 280     7085   9628   5770   -154   -302   -426       O  
ATOM   2525  CB  ARG B 280      47.773 -16.981  45.316  1.00 72.99           C  
ANISOU 2525  CB  ARG B 280     8600  12034   7099   -567   -469   -671       C  
ATOM   2526  CG  ARG B 280      49.284 -17.168  45.323  1.00 77.39           C  
ANISOU 2526  CG  ARG B 280     8907  12947   7551   -642   -567   -656       C  
ATOM   2527  CD  ARG B 280      49.911 -16.809  46.665  1.00 81.84           C  
ANISOU 2527  CD  ARG B 280     9378  13836   7883   -795   -658   -757       C  
ATOM   2528  NE  ARG B 280      49.478 -17.680  47.753  0.50 82.80           N  
ANISOU 2528  NE  ARG B 280     9493  14089   7880   -617   -709   -656       N  
ATOM   2529  CZ  ARG B 280      48.689 -17.294  48.751  0.50 83.14           C  
ANISOU 2529  CZ  ARG B 280     9679  14086   7823   -666   -686   -745       C  
ATOM   2530  NH1 ARG B 280      48.244 -16.047  48.802  0.50 82.99           N  
ANISOU 2530  NH1 ARG B 280     9827  13879   7827   -876   -613   -949       N  
ATOM   2531  NH2 ARG B 280      48.349 -18.151  49.702  0.50 83.88           N  
ANISOU 2531  NH2 ARG B 280     9753  14323   7795   -503   -731   -628       N  
ATOM   2532  N   ILE B 281      44.812 -16.526  44.318  1.00 59.87           N  
ANISOU 2532  N   ILE B 281     7394   9589   5763   -397   -243   -669       N  
ATOM   2533  CA  ILE B 281      43.429 -16.967  44.179  1.00 58.05           C  
ANISOU 2533  CA  ILE B 281     7300   9116   5639   -220   -175   -595       C  
ATOM   2534  C   ILE B 281      42.990 -16.931  42.718  1.00 57.16           C  
ANISOU 2534  C   ILE B 281     7251   8744   5724   -161   -112   -540       C  
ATOM   2535  O   ILE B 281      42.329 -17.850  42.238  1.00 55.10           O  
ANISOU 2535  O   ILE B 281     7000   8378   5555     25    -94   -414       O  
ATOM   2536  CB  ILE B 281      42.473 -16.105  45.024  1.00 54.36           C  
ANISOU 2536  CB  ILE B 281     7001   8521   5132   -292   -111   -731       C  
ATOM   2537  CG1 ILE B 281      42.772 -16.291  46.512  1.00 57.20           C  
ANISOU 2537  CG1 ILE B 281     7302   9155   5274   -328   -171   -774       C  
ATOM   2538  CG2 ILE B 281      41.025 -16.454  44.715  1.00 50.27           C  
ANISOU 2538  CG2 ILE B 281     6610   7749   4743   -122    -31   -659       C  
ATOM   2539  CD1 ILE B 281      41.892 -15.466  47.426  1.00 59.61           C  
ANISOU 2539  CD1 ILE B 281     7764   9370   5516   -398   -103   -928       C  
ATOM   2540  N   PHE B 282      43.364 -15.868  42.016  1.00 60.47           N  
ANISOU 2540  N   PHE B 282     7714   9063   6200   -329    -79   -632       N  
ATOM   2541  CA  PHE B 282      43.044 -15.744  40.598  1.00 61.99           C  
ANISOU 2541  CA  PHE B 282     7960   9037   6556   -291    -25   -575       C  
ATOM   2542  C   PHE B 282      43.677 -16.866  39.782  1.00 61.27           C  
ANISOU 2542  C   PHE B 282     7715   9068   6496   -164    -66   -441       C  
ATOM   2543  O   PHE B 282      43.030 -17.456  38.916  1.00 60.33           O  
ANISOU 2543  O   PHE B 282     7632   8800   6492    -18    -34   -349       O  
ATOM   2544  CB  PHE B 282      43.495 -14.388  40.057  1.00 63.01           C  
ANISOU 2544  CB  PHE B 282     8155   9064   6721   -515     15   -684       C  
ATOM   2545  CG  PHE B 282      43.295 -14.232  38.577  1.00 64.58           C  
ANISOU 2545  CG  PHE B 282     8398   9077   7063   -489     65   -611       C  
ATOM   2546  CD1 PHE B 282      44.379 -14.215  37.714  1.00 63.80           C  
ANISOU 2546  CD1 PHE B 282     8180   9096   6964   -579     48   -579       C  
ATOM   2547  CD2 PHE B 282      42.021 -14.108  38.046  1.00 64.24           C  
ANISOU 2547  CD2 PHE B 282     8502   8763   7141   -373    129   -569       C  
ATOM   2548  CE1 PHE B 282      44.197 -14.072  36.350  1.00 58.54           C  
ANISOU 2548  CE1 PHE B 282     7554   8279   6409   -559     96   -507       C  
ATOM   2549  CE2 PHE B 282      41.834 -13.965  36.682  1.00 61.23           C  
ANISOU 2549  CE2 PHE B 282     8156   8235   6872   -350    167   -495       C  
ATOM   2550  CZ  PHE B 282      42.923 -13.947  35.834  1.00 57.26           C  
ANISOU 2550  CZ  PHE B 282     7547   7850   6360   -444    152   -463       C  
ATOM   2551  N   GLN B 283      44.945 -17.154  40.059  1.00 60.48           N  
ANISOU 2551  N   GLN B 283     7440   9248   6293   -218   -137   -438       N  
ATOM   2552  CA  GLN B 283      45.650 -18.234  39.380  1.00 58.84           C  
ANISOU 2552  CA  GLN B 283     7072   9179   6107    -83   -173   -323       C  
ATOM   2553  C   GLN B 283      44.943 -19.564  39.614  1.00 59.17           C  
ANISOU 2553  C   GLN B 283     7120   9181   6182    166   -185   -198       C  
ATOM   2554  O   GLN B 283      44.872 -20.405  38.719  1.00 61.73           O  
ANISOU 2554  O   GLN B 283     7412   9445   6598    313   -171   -108       O  
ATOM   2555  CB  GLN B 283      47.103 -18.313  39.853  1.00 59.67           C  
ANISOU 2555  CB  GLN B 283     6969   9624   6078   -169   -253   -342       C  
ATOM   2556  N   GLY B 284      44.418 -19.749  40.821  1.00 52.86           N  
ANISOU 2556  N   GLY B 284     6367   8414   5302    203   -206   -197       N  
ATOM   2557  CA  GLY B 284      43.657 -20.944  41.134  1.00 49.98           C  
ANISOU 2557  CA  GLY B 284     6028   7994   4969    414   -207    -73       C  
ATOM   2558  C   GLY B 284      42.415 -21.016  40.267  1.00 49.84           C  
ANISOU 2558  C   GLY B 284     6153   7677   5108    488   -129    -50       C  
ATOM   2559  O   GLY B 284      42.066 -22.075  39.746  1.00 49.47           O  
ANISOU 2559  O   GLY B 284     6097   7553   5146    650   -122     54       O  
ATOM   2560  N   CYS B 285      41.751 -19.896  40.068  1.00 50.07           N  
ANISOU 2560  N   CYS B 285     6311   7535   5179    371    -71   -148       N  
ATOM   2561  CA  CYS B 285      40.575 -19.902  39.228  1.00 51.54           C  
ANISOU 2561  CA  CYS B 285     6615   7464   5504    443     -5   -121       C  
ATOM   2562  C   CYS B 285      40.970 -20.290  37.820  1.00 52.98           C  
ANISOU 2562  C   CYS B 285     6745   7606   5781    488     -1    -70       C  
ATOM   2563  O   CYS B 285      40.259 -21.021  37.187  1.00 52.51           O  
ANISOU 2563  O   CYS B 285     6716   7423   5813    613     21     -2       O  
ATOM   2564  CB  CYS B 285      39.817 -18.581  39.248  1.00 51.55           C  
ANISOU 2564  CB  CYS B 285     6761   7287   5539    329     58   -227       C  
ATOM   2565  SG  CYS B 285      38.162 -18.659  38.494  1.00103.16           S  
ANISOU 2565  SG  CYS B 285    13426  13543  12226    448    130   -180       S  
ATOM   2566  N   GLN B 286      42.111 -19.807  37.339  1.00 55.55           N  
ANISOU 2566  N   GLN B 286     6984   8049   6072    377    -19   -110       N  
ATOM   2567  CA AGLN B 286      42.556 -20.166  35.998  0.60 53.94           C  
ANISOU 2567  CA AGLN B 286     6719   7837   5938    417     -8    -68       C  
ATOM   2568  CA BGLN B 286      42.580 -20.163  36.002  0.40 54.63           C  
ANISOU 2568  CA BGLN B 286     6805   7929   6024    415     -9    -68       C  
ATOM   2569  C   GLN B 286      42.828 -21.662  35.878  1.00 52.63           C  
ANISOU 2569  C   GLN B 286     6451   7758   5787    607    -40     27       C  
ATOM   2570  O   GLN B 286      42.379 -22.303  34.930  1.00 54.12           O  
ANISOU 2570  O   GLN B 286     6664   7832   6067    713    -13     71       O  
ATOM   2571  CB AGLN B 286      43.796 -19.359  35.608  0.60 57.89           C  
ANISOU 2571  CB AGLN B 286     7130   8481   6385    246    -16   -126       C  
ATOM   2572  CB BGLN B 286      43.865 -19.402  35.667  0.40 57.97           C  
ANISOU 2572  CB BGLN B 286     7129   8508   6388    248    -21   -125       C  
ATOM   2573  CG AGLN B 286      43.548 -17.861  35.522  0.60 59.83           C  
ANISOU 2573  CG AGLN B 286     7498   8594   6642     50     28   -214       C  
ATOM   2574  CG BGLN B 286      43.678 -17.908  35.463  0.40 58.62           C  
ANISOU 2574  CG BGLN B 286     7328   8461   6485     49     25   -211       C  
ATOM   2575  CD AGLN B 286      42.379 -17.517  34.618  0.60 61.71           C  
ANISOU 2575  CD AGLN B 286     7887   8563   6996     92     90   -188       C  
ATOM   2576  CD BGLN B 286      44.975 -17.202  35.118  0.40 59.68           C  
ANISOU 2576  CD BGLN B 286     7359   8753   6563   -139     17   -260       C  
ATOM   2577  OE1AGLN B 286      41.566 -16.649  34.938  0.60 65.24           O  
ANISOU 2577  OE1AGLN B 286     8476   8838   7474     37    127   -235       O  
ATOM   2578  OE1BGLN B 286      46.021 -17.473  35.709  0.40 60.83           O  
ANISOU 2578  OE1BGLN B 286     7350   9151   6611   -178    -38   -277       O  
ATOM   2579  NE2AGLN B 286      42.285 -18.201  33.484  0.60 59.08           N  
ANISOU 2579  NE2AGLN B 286     7521   8202   6724    198    102   -116       N  
ATOM   2580  NE2BGLN B 286      44.913 -16.289  34.155  0.40 59.77           N  
ANISOU 2580  NE2BGLN B 286     7450   8628   6632   -261     73   -274       N  
ATOM   2581  N   PHE B 287      43.555 -22.214  36.844  1.00 50.60           N  
ANISOU 2581  N   PHE B 287     6086   7702   5438    652    -99     56       N  
ATOM   2582  CA  PHE B 287      43.865 -23.639  36.851  1.00 49.93           C  
ANISOU 2582  CA  PHE B 287     5911   7689   5371    848   -130    156       C  
ATOM   2583  C   PHE B 287      42.601 -24.474  36.678  1.00 50.29           C  
ANISOU 2583  C   PHE B 287     6074   7514   5519    986    -95    220       C  
ATOM   2584  O   PHE B 287      42.543 -25.362  35.827  1.00 46.51           O  
ANISOU 2584  O   PHE B 287     5583   6962   5126   1109    -78    262       O  
ATOM   2585  CB  PHE B 287      44.573 -24.029  38.152  1.00 52.79           C  
ANISOU 2585  CB  PHE B 287     6167   8281   5609    883   -203    198       C  
ATOM   2586  CG  PHE B 287      45.002 -25.471  38.202  1.00 54.09           C  
ANISOU 2586  CG  PHE B 287     6237   8519   5794   1099   -236    317       C  
ATOM   2587  CD1 PHE B 287      44.094 -26.468  38.526  1.00 52.89           C  
ANISOU 2587  CD1 PHE B 287     6177   8215   5704   1249   -223    412       C  
ATOM   2588  CD2 PHE B 287      46.313 -25.830  37.926  1.00 57.11           C  
ANISOU 2588  CD2 PHE B 287     6440   9118   6141   1154   -276    335       C  
ATOM   2589  CE1 PHE B 287      44.485 -27.795  38.571  1.00 53.91           C  
ANISOU 2589  CE1 PHE B 287     6239   8377   5866   1451   -248    525       C  
ATOM   2590  CE2 PHE B 287      46.711 -27.156  37.971  1.00 57.73           C  
ANISOU 2590  CE2 PHE B 287     6438   9245   6250   1376   -301    446       C  
ATOM   2591  CZ  PHE B 287      45.796 -28.139  38.294  1.00 54.28           C  
ANISOU 2591  CZ  PHE B 287     6115   8626   5884   1526   -287    542       C  
ATOM   2592  N   ARG B 288      41.591 -24.183  37.491  1.00 48.71           N  
ANISOU 2592  N   ARG B 288     5985   7216   5306    957    -80    217       N  
ATOM   2593  CA  ARG B 288      40.337 -24.924  37.458  1.00 43.61           C  
ANISOU 2593  CA  ARG B 288     5440   6381   4748   1063    -46    277       C  
ATOM   2594  C   ARG B 288      39.604 -24.747  36.129  1.00 39.78           C  
ANISOU 2594  C   ARG B 288     5028   5705   4381   1057      5    246       C  
ATOM   2595  O   ARG B 288      39.052 -25.704  35.585  1.00 40.27           O  
ANISOU 2595  O   ARG B 288     5115   5653   4531   1165     22    296       O  
ATOM   2596  CB  ARG B 288      39.442 -24.507  38.628  1.00 47.68           C  
ANISOU 2596  CB  ARG B 288     6041   6864   5209   1017    -32    269       C  
ATOM   2597  CG  ARG B 288      38.009 -25.003  38.532  1.00 49.05           C  
ANISOU 2597  CG  ARG B 288     6319   6844   5476   1086     18    314       C  
ATOM   2598  CD  ARG B 288      37.941 -26.515  38.376  1.00 48.92           C  
ANISOU 2598  CD  ARG B 288     6279   6786   5522   1236      7    427       C  
ATOM   2599  NE  ARG B 288      36.639 -26.945  37.871  1.00 51.53           N  
ANISOU 2599  NE  ARG B 288     6696   6918   5965   1272     56    448       N  
ATOM   2600  CZ  ARG B 288      36.414 -28.111  37.272  1.00 51.56           C  
ANISOU 2600  CZ  ARG B 288     6706   6820   6066   1372     63    509       C  
ATOM   2601  NH1 ARG B 288      37.407 -28.973  37.098  1.00 50.96           N  
ANISOU 2601  NH1 ARG B 288     6561   6805   5995   1468     30    557       N  
ATOM   2602  NH2 ARG B 288      35.197 -28.414  36.842  1.00 47.08           N  
ANISOU 2602  NH2 ARG B 288     6209   6090   5591   1375    104    514       N  
ATOM   2603  N   SER B 289      39.599 -23.524  35.609  1.00 38.32           N  
ANISOU 2603  N   SER B 289     4880   5485   4196    926     29    167       N  
ATOM   2604  CA  SER B 289      38.934 -23.247  34.339  1.00 43.45           C  
ANISOU 2604  CA  SER B 289     5595   5978   4938    917     71    150       C  
ATOM   2605  C   SER B 289      39.528 -24.087  33.208  1.00 45.56           C  
ANISOU 2605  C   SER B 289     5788   6275   5246    996     67    172       C  
ATOM   2606  O   SER B 289      38.803 -24.593  32.351  1.00 41.76           O  
ANISOU 2606  O   SER B 289     5352   5672   4844   1058     89    186       O  
ATOM   2607  CB  SER B 289      39.019 -21.758  33.993  1.00 48.02           C  
ANISOU 2607  CB  SER B 289     6222   6521   5500    764     95     79       C  
ATOM   2608  OG  SER B 289      38.214 -20.983  34.869  1.00 58.23           O  
ANISOU 2608  OG  SER B 289     7610   7733   6780    712    116     43       O  
ATOM   2609  N   VAL B 290      40.850 -24.232  33.216  1.00 44.03           N  
ANISOU 2609  N   VAL B 290     5475   6260   4993    992     39    167       N  
ATOM   2610  CA  VAL B 290      41.537 -25.054  32.225  1.00 38.94           C  
ANISOU 2610  CA  VAL B 290     4746   5671   4379   1082     43    177       C  
ATOM   2611  C   VAL B 290      41.123 -26.517  32.358  1.00 35.24           C  
ANISOU 2611  C   VAL B 290     4289   5126   3976   1258     38    236       C  
ATOM   2612  O   VAL B 290      40.927 -27.208  31.361  1.00 37.81           O  
ANISOU 2612  O   VAL B 290     4625   5373   4368   1334     63    227       O  
ATOM   2613  CB  VAL B 290      43.068 -24.913  32.334  1.00 41.71           C  
ANISOU 2613  CB  VAL B 290     4942   6258   4647   1052     16    162       C  
ATOM   2614  CG1 VAL B 290      43.769 -26.085  31.661  1.00 33.24           C  
ANISOU 2614  CG1 VAL B 290     3768   5257   3605   1207     19    183       C  
ATOM   2615  CG2 VAL B 290      43.514 -23.593  31.729  1.00 41.73           C  
ANISOU 2615  CG2 VAL B 290     4935   6309   4609    868     39    101       C  
ATOM   2616  N   GLU B 291      40.984 -26.987  33.593  1.00 38.46           N  
ANISOU 2616  N   GLU B 291     4701   5554   4359   1314      8    295       N  
ATOM   2617  CA  GLU B 291      40.456 -28.324  33.830  1.00 37.76           C  
ANISOU 2617  CA  GLU B 291     4649   5357   4340   1462     10    367       C  
ATOM   2618  C   GLU B 291      39.053 -28.444  33.253  1.00 42.05           C  
ANISOU 2618  C   GLU B 291     5314   5688   4975   1447     51    353       C  
ATOM   2619  O   GLU B 291      38.739 -29.395  32.533  1.00 46.52           O  
ANISOU 2619  O   GLU B 291     5906   6145   5626   1533     70    357       O  
ATOM   2620  CB  GLU B 291      40.401 -28.622  35.325  1.00 37.78           C  
ANISOU 2620  CB  GLU B 291     4653   5419   4284   1498    -24    449       C  
ATOM   2621  CG  GLU B 291      41.719 -29.045  35.935  1.00 44.49           C  
ANISOU 2621  CG  GLU B 291     5371   6477   5058   1578    -76    500       C  
ATOM   2622  CD  GLU B 291      41.554 -29.506  37.364  1.00 48.47           C  
ANISOU 2622  CD  GLU B 291     5886   7033   5499   1632   -111    604       C  
ATOM   2623  OE1 GLU B 291      40.959 -28.753  38.163  1.00 48.11           O  
ANISOU 2623  OE1 GLU B 291     5896   6997   5385   1522   -111    587       O  
ATOM   2624  OE2 GLU B 291      42.015 -30.619  37.686  1.00 49.46           O  
ANISOU 2624  OE2 GLU B 291     5966   7187   5639   1789   -136    706       O  
ATOM   2625  N   ALA B 292      38.213 -27.470  33.585  1.00 40.47           N  
ANISOU 2625  N   ALA B 292     5184   5436   4756   1339     64    330       N  
ATOM   2626  CA  ALA B 292      36.822 -27.467  33.155  1.00 38.53           C  
ANISOU 2626  CA  ALA B 292     5034   5020   4587   1322     97    322       C  
ATOM   2627  C   ALA B 292      36.710 -27.543  31.637  1.00 33.20           C  
ANISOU 2627  C   ALA B 292     4363   4283   3968   1322    115    272       C  
ATOM   2628  O   ALA B 292      35.809 -28.189  31.108  1.00 38.45           O  
ANISOU 2628  O   ALA B 292     5076   4826   4707   1356    131    274       O  
ATOM   2629  CB  ALA B 292      36.102 -26.229  33.692  1.00 38.77           C  
ANISOU 2629  CB  ALA B 292     5122   5027   4582   1217    113    294       C  
ATOM   2630  N   VAL B 293      37.636 -26.895  30.939  1.00 30.81           N  
ANISOU 2630  N   VAL B 293     4007   4080   3621   1273    113    227       N  
ATOM   2631  CA  VAL B 293      37.624 -26.905  29.479  1.00 33.31           C  
ANISOU 2631  CA  VAL B 293     4321   4371   3963   1266    132    182       C  
ATOM   2632  C   VAL B 293      37.719 -28.328  28.929  1.00 36.20           C  
ANISOU 2632  C   VAL B 293     4672   4697   4388   1386    139    175       C  
ATOM   2633  O   VAL B 293      37.013 -28.685  27.988  1.00 36.34           O  
ANISOU 2633  O   VAL B 293     4732   4625   4452   1393    154    142       O  
ATOM   2634  CB  VAL B 293      38.756 -26.034  28.895  1.00 40.67           C  
ANISOU 2634  CB  VAL B 293     5185   5442   4825   1188    136    147       C  
ATOM   2635  CG1 VAL B 293      38.916 -26.282  27.393  1.00 39.44           C  
ANISOU 2635  CG1 VAL B 293     5012   5297   4677   1201    160    107       C  
ATOM   2636  CG2 VAL B 293      38.486 -24.564  29.181  1.00 34.99           C  
ANISOU 2636  CG2 VAL B 293     4516   4709   4070   1053    141    142       C  
ATOM   2637  N   GLN B 294      38.579 -29.146  29.527  1.00 37.93           N  
ANISOU 2637  N   GLN B 294     4830   4979   4604   1484    126    205       N  
ATOM   2638  CA  GLN B 294      38.748 -30.523  29.073  1.00 37.06           C  
ANISOU 2638  CA  GLN B 294     4715   4806   4561   1615    139    195       C  
ATOM   2639  C   GLN B 294      37.519 -31.383  29.355  1.00 38.17           C  
ANISOU 2639  C   GLN B 294     4954   4758   4790   1647    147    226       C  
ATOM   2640  O   GLN B 294      37.174 -32.261  28.565  1.00 36.27           O  
ANISOU 2640  O   GLN B 294     4752   4411   4619   1694    168    181       O  
ATOM   2641  CB  GLN B 294      39.993 -31.157  29.691  1.00 39.80           C  
ANISOU 2641  CB  GLN B 294     4967   5267   4886   1734    122    236       C  
ATOM   2642  CG  GLN B 294      41.293 -30.560  29.184  1.00 44.51           C  
ANISOU 2642  CG  GLN B 294     5441   6066   5406   1713    123    192       C  
ATOM   2643  CD  GLN B 294      41.332 -30.422  27.667  1.00 46.79           C  
ANISOU 2643  CD  GLN B 294     5726   6357   5696   1682    164    100       C  
ATOM   2644  OE1 GLN B 294      41.746 -29.388  27.141  1.00 43.35           O  
ANISOU 2644  OE1 GLN B 294     5244   6036   5189   1570    172     69       O  
ATOM   2645  NE2 GLN B 294      40.902 -31.464  26.959  1.00 45.00           N  
ANISOU 2645  NE2 GLN B 294     5552   6003   5545   1773    191     57       N  
ATOM   2646  N   GLU B 295      36.858 -31.130  30.479  1.00 33.82           N  
ANISOU 2646  N   GLU B 295     4444   4173   4233   1609    134    295       N  
ATOM   2647  CA  GLU B 295      35.635 -31.851  30.809  1.00 30.22           C  
ANISOU 2647  CA  GLU B 295     4072   3555   3854   1614    148    332       C  
ATOM   2648  C   GLU B 295      34.541 -31.528  29.793  1.00 31.01           C  
ANISOU 2648  C   GLU B 295     4218   3573   3990   1531    164    266       C  
ATOM   2649  O   GLU B 295      33.847 -32.421  29.304  1.00 33.75           O  
ANISOU 2649  O   GLU B 295     4611   3797   4415   1544    178    243       O  
ATOM   2650  CB  GLU B 295      35.158 -31.484  32.214  1.00 36.16           C  
ANISOU 2650  CB  GLU B 295     4846   4324   4569   1579    140    415       C  
ATOM   2651  CG  GLU B 295      36.170 -31.754  33.315  1.00 40.41           C  
ANISOU 2651  CG  GLU B 295     5333   4972   5047   1653    114    493       C  
ATOM   2652  CD  GLU B 295      35.717 -31.214  34.663  1.00 44.40           C  
ANISOU 2652  CD  GLU B 295     5857   5529   5483   1599    107    556       C  
ATOM   2653  OE1 GLU B 295      34.573 -30.720  34.761  1.00 41.91           O  
ANISOU 2653  OE1 GLU B 295     5596   5147   5181   1518    132    540       O  
ATOM   2654  OE2 GLU B 295      36.505 -31.280  35.626  1.00 53.09           O  
ANISOU 2654  OE2 GLU B 295     6911   6753   6507   1641     77    618       O  
ATOM   2655  N   ILE B 296      34.393 -30.241  29.488  1.00 31.21           N  
ANISOU 2655  N   ILE B 296     4231   3668   3958   1443    159    237       N  
ATOM   2656  CA  ILE B 296      33.385 -29.765  28.545  1.00 31.52           C  
ANISOU 2656  CA  ILE B 296     4301   3658   4015   1374    164    193       C  
ATOM   2657  C   ILE B 296      33.675 -30.277  27.138  1.00 35.54           C  
ANISOU 2657  C   ILE B 296     4798   4169   4535   1393    168    116       C  
ATOM   2658  O   ILE B 296      32.768 -30.697  26.416  1.00 33.97           O  
ANISOU 2658  O   ILE B 296     4630   3899   4377   1371    169     78       O  
ATOM   2659  CB  ILE B 296      33.337 -28.228  28.525  1.00 31.93           C  
ANISOU 2659  CB  ILE B 296     4350   3777   4004   1295    160    192       C  
ATOM   2660  CG1 ILE B 296      32.930 -27.689  29.900  1.00 29.50           C  
ANISOU 2660  CG1 ILE B 296     4063   3463   3681   1272    164    243       C  
ATOM   2661  CG2 ILE B 296      32.389 -27.729  27.435  1.00 35.98           C  
ANISOU 2661  CG2 ILE B 296     4886   4255   4529   1246    159    164       C  
ATOM   2662  CD1 ILE B 296      33.211 -26.206  30.076  1.00 31.18           C  
ANISOU 2662  CD1 ILE B 296     4281   3732   3832   1201    166    230       C  
ATOM   2663  N   THR B 297      34.948 -30.243  26.757  1.00 36.00           N  
ANISOU 2663  N   THR B 297     4802   4328   4547   1431    172     88       N  
ATOM   2664  CA  THR B 297      35.382 -30.774  25.471  1.00 36.17           C  
ANISOU 2664  CA  THR B 297     4805   4375   4565   1461    187      5       C  
ATOM   2665  C   THR B 297      35.007 -32.245  25.310  1.00 38.02           C  
ANISOU 2665  C   THR B 297     5081   4477   4886   1534    200    -34       C  
ATOM   2666  O   THR B 297      34.498 -32.654  24.265  1.00 36.54           O  
ANISOU 2666  O   THR B 297     4921   4250   4714   1512    208   -115       O  
ATOM   2667  CB  THR B 297      36.897 -30.608  25.283  1.00 37.40           C  
ANISOU 2667  CB  THR B 297     4876   4676   4658   1505    198    -14       C  
ATOM   2668  OG1 THR B 297      37.212 -29.214  25.185  1.00 35.97           O  
ANISOU 2668  OG1 THR B 297     4665   4605   4397   1406    192      7       O  
ATOM   2669  CG2 THR B 297      37.365 -31.324  24.019  1.00 39.45           C  
ANISOU 2669  CG2 THR B 297     5113   4964   4912   1558    227   -110       C  
ATOM   2670  N   GLU B 298      35.252 -33.040  26.348  1.00 33.89           N  
ANISOU 2670  N   GLU B 298     4571   3886   4419   1614    203     24       N  
ATOM   2671  CA  GLU B 298      34.880 -34.450  26.314  1.00 38.80           C  
ANISOU 2671  CA  GLU B 298     5253   4346   5142   1678    222      3       C  
ATOM   2672  C   GLU B 298      33.364 -34.612  26.218  1.00 40.57           C  
ANISOU 2672  C   GLU B 298     5544   4451   5418   1581    218     -4       C  
ATOM   2673  O   GLU B 298      32.866 -35.481  25.502  1.00 44.85           O  
ANISOU 2673  O   GLU B 298     6134   4887   6021   1570    233    -83       O  
ATOM   2674  CB  GLU B 298      35.406 -35.187  27.547  1.00 45.52           C  
ANISOU 2674  CB  GLU B 298     6110   5146   6038   1785    223    102       C  
ATOM   2675  CG  GLU B 298      35.015 -36.656  27.577  1.00 58.15           C  
ANISOU 2675  CG  GLU B 298     7793   6543   7757   1849    250     97       C  
ATOM   2676  CD  GLU B 298      35.335 -37.328  28.896  1.00 69.31           C  
ANISOU 2676  CD  GLU B 298     9228   7894   9212   1947    248    233       C  
ATOM   2677  OE1 GLU B 298      36.135 -36.773  29.678  1.00 72.87           O  
ANISOU 2677  OE1 GLU B 298     9607   8490   9588   1992    223    312       O  
ATOM   2678  OE2 GLU B 298      34.783 -38.419  29.150  1.00 75.32           O  
ANISOU 2678  OE2 GLU B 298    10078   8464  10078   1970    271    265       O  
ATOM   2679  N   TYR B 299      32.633 -33.774  26.944  1.00 39.18           N  
ANISOU 2679  N   TYR B 299     5367   4301   5218   1507    202     70       N  
ATOM   2680  CA  TYR B 299      31.178 -33.820  26.898  1.00 40.37           C  
ANISOU 2680  CA  TYR B 299     5553   4374   5410   1416    199     71       C  
ATOM   2681  C   TYR B 299      30.654 -33.491  25.502  1.00 40.35           C  
ANISOU 2681  C   TYR B 299     5539   4412   5380   1348    185    -27       C  
ATOM   2682  O   TYR B 299      29.745 -34.149  24.999  1.00 45.61           O  
ANISOU 2682  O   TYR B 299     6232   5001   6095   1295    184    -79       O  
ATOM   2683  CB  TYR B 299      30.568 -32.861  27.917  1.00 37.49           C  
ANISOU 2683  CB  TYR B 299     5177   4054   5015   1368    192    159       C  
ATOM   2684  CG  TYR B 299      29.058 -32.836  27.878  1.00 39.89           C  
ANISOU 2684  CG  TYR B 299     5493   4307   5357   1283    193    163       C  
ATOM   2685  CD1 TYR B 299      28.322 -33.957  28.230  1.00 36.28           C  
ANISOU 2685  CD1 TYR B 299     5073   3727   4984   1259    212    182       C  
ATOM   2686  CD2 TYR B 299      28.369 -31.693  27.490  1.00 36.88           C  
ANISOU 2686  CD2 TYR B 299     5080   4002   4932   1228    177    154       C  
ATOM   2687  CE1 TYR B 299      26.945 -33.947  28.198  1.00 36.52           C  
ANISOU 2687  CE1 TYR B 299     5092   3735   5048   1170    215    184       C  
ATOM   2688  CE2 TYR B 299      26.984 -31.673  27.454  1.00 38.09           C  
ANISOU 2688  CE2 TYR B 299     5221   4134   5119   1163    176    161       C  
ATOM   2689  CZ  TYR B 299      26.279 -32.805  27.811  1.00 37.83           C  
ANISOU 2689  CZ  TYR B 299     5208   4002   5164   1128    194    172       C  
ATOM   2690  OH  TYR B 299      24.904 -32.811  27.785  1.00 34.98           O  
ANISOU 2690  OH  TYR B 299     4814   3643   4835   1052    195    178       O  
ATOM   2691  N   ALA B 300      31.230 -32.469  24.883  1.00 32.64           N  
ANISOU 2691  N   ALA B 300     4520   3565   4315   1341    173    -46       N  
ATOM   2692  CA  ALA B 300      30.805 -32.043  23.553  1.00 35.41           C  
ANISOU 2692  CA  ALA B 300     4857   3983   4614   1282    155   -117       C  
ATOM   2693  C   ALA B 300      30.886 -33.180  22.536  1.00 34.26           C  
ANISOU 2693  C   ALA B 300     4732   3796   4491   1294    166   -235       C  
ATOM   2694  O   ALA B 300      30.061 -33.275  21.627  1.00 39.36           O  
ANISOU 2694  O   ALA B 300     5381   4457   5119   1226    146   -300       O  
ATOM   2695  CB  ALA B 300      31.636 -30.856  23.089  1.00 37.34           C  
ANISOU 2695  CB  ALA B 300     5063   4366   4760   1277    152   -103       C  
ATOM   2696  N   LYS B 301      31.881 -34.045  22.695  1.00 36.76           N  
ANISOU 2696  N   LYS B 301     5061   4065   4841   1384    197   -269       N  
ATOM   2697  CA  LYS B 301      32.076 -35.156  21.768  1.00 43.86           C  
ANISOU 2697  CA  LYS B 301     5991   4908   5768   1412    220   -400       C  
ATOM   2698  C   LYS B 301      30.932 -36.168  21.808  1.00 47.60           C  
ANISOU 2698  C   LYS B 301     6529   5218   6338   1352    219   -443       C  
ATOM   2699  O   LYS B 301      30.685 -36.875  20.829  1.00 43.69           O  
ANISOU 2699  O   LYS B 301     6064   4688   5849   1321    226   -576       O  
ATOM   2700  CB  LYS B 301      33.405 -35.856  22.045  1.00 51.03           C  
ANISOU 2700  CB  LYS B 301     6895   5790   6706   1549    259   -416       C  
ATOM   2701  CG  LYS B 301      34.623 -35.005  21.742  1.00 55.90           C  
ANISOU 2701  CG  LYS B 301     7429   6591   7220   1593    267   -408       C  
ATOM   2702  CD  LYS B 301      35.890 -35.838  21.808  1.00 64.22           C  
ANISOU 2702  CD  LYS B 301     8458   7639   8303   1741    308   -447       C  
ATOM   2703  CE  LYS B 301      37.117 -34.996  21.509  1.00 64.46           C  
ANISOU 2703  CE  LYS B 301     8384   7879   8227   1770    319   -440       C  
ATOM   2704  NZ  LYS B 301      38.334 -35.839  21.405  1.00 63.85           N  
ANISOU 2704  NZ  LYS B 301     8262   7824   8173   1927    364   -494       N  
ATOM   2705  N   SER B 302      30.232 -36.231  22.937  1.00 42.78           N  
ANISOU 2705  N   SER B 302     5940   4519   5796   1325    213   -337       N  
ATOM   2706  CA  SER B 302      29.132 -37.176  23.100  1.00 38.93           C  
ANISOU 2706  CA  SER B 302     5508   3879   5405   1248    218   -359       C  
ATOM   2707  C   SER B 302      27.821 -36.655  22.505  1.00 41.85           C  
ANISOU 2707  C   SER B 302     5839   4325   5736   1113    178   -389       C  
ATOM   2708  O   SER B 302      26.847 -37.396  22.381  1.00 44.48           O  
ANISOU 2708  O   SER B 302     6198   4568   6134   1020    176   -435       O  
ATOM   2709  CB  SER B 302      28.925 -37.499  24.577  1.00 40.02           C  
ANISOU 2709  CB  SER B 302     5676   3907   5622   1270    236   -221       C  
ATOM   2710  OG  SER B 302      28.139 -36.498  25.197  1.00 42.58           O  
ANISOU 2710  OG  SER B 302     5952   4320   5907   1206    214   -126       O  
ATOM   2711  N   ILE B 303      27.789 -35.376  22.153  1.00 41.17           N  
ANISOU 2711  N   ILE B 303     5688   4406   5548   1102    146   -355       N  
ATOM   2712  CA  ILE B 303      26.593 -34.797  21.557  1.00 42.91           C  
ANISOU 2712  CA  ILE B 303     5859   4720   5725   1002    102   -366       C  
ATOM   2713  C   ILE B 303      26.424 -35.289  20.121  1.00 43.44           C  
ANISOU 2713  C   ILE B 303     5926   4836   5743    945     80   -516       C  
ATOM   2714  O   ILE B 303      27.273 -35.029  19.270  1.00 46.69           O  
ANISOU 2714  O   ILE B 303     6332   5339   6068    988     82   -576       O  
ATOM   2715  CB  ILE B 303      26.642 -33.260  21.577  1.00 36.84           C  
ANISOU 2715  CB  ILE B 303     5036   4095   4867   1022     77   -275       C  
ATOM   2716  CG1 ILE B 303      26.701 -32.749  23.019  1.00 36.09           C  
ANISOU 2716  CG1 ILE B 303     4943   3958   4811   1063     99   -150       C  
ATOM   2717  CG2 ILE B 303      25.437 -32.684  20.853  1.00 32.90           C  
ANISOU 2717  CG2 ILE B 303     4479   3700   4320    945     27   -279       C  
ATOM   2718  CD1 ILE B 303      26.986 -31.264  23.138  1.00 30.08           C  
ANISOU 2718  CD1 ILE B 303     4153   3302   3976   1090     88    -75       C  
ATOM   2719  N   PRO B 304      25.324 -36.011  19.850  1.00 41.39           N  
ANISOU 2719  N   PRO B 304     5668   4529   5529    838     62   -583       N  
ATOM   2720  CA  PRO B 304      25.086 -36.602  18.529  1.00 43.74           C  
ANISOU 2720  CA  PRO B 304     5970   4872   5776    763     39   -748       C  
ATOM   2721  C   PRO B 304      25.260 -35.579  17.414  1.00 44.29           C  
ANISOU 2721  C   PRO B 304     5979   5161   5689    770     -5   -762       C  
ATOM   2722  O   PRO B 304      24.604 -34.536  17.424  1.00 40.64           O  
ANISOU 2722  O   PRO B 304     5448   4821   5173    751    -49   -661       O  
ATOM   2723  CB  PRO B 304      23.628 -37.061  18.611  1.00 46.15           C  
ANISOU 2723  CB  PRO B 304     6246   5152   6136    622      8   -768       C  
ATOM   2724  CG  PRO B 304      23.411 -37.334  20.061  1.00 45.57           C  
ANISOU 2724  CG  PRO B 304     6199   4928   6186    637     49   -647       C  
ATOM   2725  CD  PRO B 304      24.231 -36.306  20.792  1.00 43.77           C  
ANISOU 2725  CD  PRO B 304     5960   4747   5925    766     64   -511       C  
ATOM   2726  N   GLY B 305      26.155 -35.875  16.476  1.00 43.28           N  
ANISOU 2726  N   GLY B 305     5878   5078   5488    804     14   -880       N  
ATOM   2727  CA  GLY B 305      26.416 -34.994  15.355  1.00 41.63           C  
ANISOU 2727  CA  GLY B 305     5619   5081   5116    804    -18   -891       C  
ATOM   2728  C   GLY B 305      27.685 -34.170  15.497  1.00 43.17           C  
ANISOU 2728  C   GLY B 305     5810   5335   5258    910     18   -809       C  
ATOM   2729  O   GLY B 305      28.330 -33.846  14.502  1.00 41.25           O  
ANISOU 2729  O   GLY B 305     5551   5235   4889    922     23   -859       O  
ATOM   2730  N   PHE B 306      28.047 -33.828  16.730  1.00 41.16           N  
ANISOU 2730  N   PHE B 306     5565   4987   5088    974     43   -685       N  
ATOM   2731  CA  PHE B 306      29.177 -32.931  16.968  1.00 34.92           C  
ANISOU 2731  CA  PHE B 306     4758   4263   4248   1050     70   -599       C  
ATOM   2732  C   PHE B 306      30.473 -33.392  16.296  1.00 37.54           C  
ANISOU 2732  C   PHE B 306     5096   4644   4525   1111    120   -703       C  
ATOM   2733  O   PHE B 306      31.142 -32.610  15.619  1.00 39.76           O  
ANISOU 2733  O   PHE B 306     5341   5078   4688   1116    127   -685       O  
ATOM   2734  CB  PHE B 306      29.409 -32.725  18.467  1.00 34.58           C  
ANISOU 2734  CB  PHE B 306     4727   4108   4305   1103     91   -481       C  
ATOM   2735  CG  PHE B 306      30.433 -31.669  18.775  1.00 35.00           C  
ANISOU 2735  CG  PHE B 306     4755   4241   4303   1150    108   -392       C  
ATOM   2736  CD1 PHE B 306      30.073 -30.333  18.835  1.00 31.00           C  
ANISOU 2736  CD1 PHE B 306     4227   3806   3745   1116     81   -285       C  
ATOM   2737  CD2 PHE B 306      31.758 -32.010  18.992  1.00 34.58           C  
ANISOU 2737  CD2 PHE B 306     4697   4189   4252   1227    152   -417       C  
ATOM   2738  CE1 PHE B 306      31.014 -29.359  19.112  1.00 32.52           C  
ANISOU 2738  CE1 PHE B 306     4406   4058   3893   1135    101   -213       C  
ATOM   2739  CE2 PHE B 306      32.703 -31.041  19.271  1.00 33.14           C  
ANISOU 2739  CE2 PHE B 306     4479   4097   4016   1246    166   -342       C  
ATOM   2740  CZ  PHE B 306      32.332 -29.715  19.328  1.00 31.93           C  
ANISOU 2740  CZ  PHE B 306     4317   4001   3814   1188    141   -244       C  
ATOM   2741  N   VAL B 307      30.827 -34.658  16.487  1.00 39.24           N  
ANISOU 2741  N   VAL B 307     5355   4728   4826   1160    160   -808       N  
ATOM   2742  CA  VAL B 307      32.065 -35.191  15.924  1.00 44.69           C  
ANISOU 2742  CA  VAL B 307     6045   5456   5480   1245    218   -916       C  
ATOM   2743  C   VAL B 307      32.046 -35.186  14.395  1.00 49.08           C  
ANISOU 2743  C   VAL B 307     6585   6171   5893   1193    216  -1050       C  
ATOM   2744  O   VAL B 307      33.094 -35.098  13.753  1.00 50.10           O  
ANISOU 2744  O   VAL B 307     6683   6421   5933   1247    262  -1107       O  
ATOM   2745  CB  VAL B 307      32.362 -36.614  16.444  1.00 45.76           C  
ANISOU 2745  CB  VAL B 307     6245   5386   5754   1327    264  -1000       C  
ATOM   2746  CG1 VAL B 307      33.572 -37.196  15.741  1.00 56.39           C  
ANISOU 2746  CG1 VAL B 307     7584   6779   7063   1431    330  -1132       C  
ATOM   2747  CG2 VAL B 307      32.591 -36.583  17.949  1.00 46.42           C  
ANISOU 2747  CG2 VAL B 307     6335   5350   5951   1394    269   -851       C  
ATOM   2748  N   ASN B 308      30.853 -35.265  13.814  1.00 46.66           N  
ANISOU 2748  N   ASN B 308     6289   5887   5552   1084    163  -1098       N  
ATOM   2749  CA  ASN B 308      30.716 -35.296  12.361  1.00 48.71           C  
ANISOU 2749  CA  ASN B 308     6533   6318   5657   1022    151  -1227       C  
ATOM   2750  C   ASN B 308      30.880 -33.916  11.730  1.00 47.57           C  
ANISOU 2750  C   ASN B 308     6326   6400   5350    993    122  -1112       C  
ATOM   2751  O   ASN B 308      30.929 -33.781  10.506  1.00 46.16           O  
ANISOU 2751  O   ASN B 308     6126   6401   5011    950    116  -1190       O  
ATOM   2752  CB  ASN B 308      29.367 -35.900  11.962  1.00 53.71           C  
ANISOU 2752  CB  ASN B 308     7189   6916   6303    904     94  -1323       C  
ATOM   2753  CG  ASN B 308      29.177 -37.309  12.495  1.00 62.20           C  
ANISOU 2753  CG  ASN B 308     8343   7749   7542    909    129  -1443       C  
ATOM   2754  OD1 ASN B 308      28.089 -37.673  12.948  1.00 68.64           O  
ANISOU 2754  OD1 ASN B 308     9175   8457   8448    823     91  -1431       O  
ATOM   2755  ND2 ASN B 308      30.237 -38.108  12.450  1.00 57.46           N  
ANISOU 2755  ND2 ASN B 308     7790   7057   6984   1012    207  -1554       N  
ATOM   2756  N   LEU B 309      30.959 -32.890  12.570  1.00 40.00           N  
ANISOU 2756  N   LEU B 309     5343   5427   4426   1013    108   -925       N  
ATOM   2757  CA  LEU B 309      31.092 -31.521  12.090  1.00 36.95           C  
ANISOU 2757  CA  LEU B 309     4916   5213   3912    984     86   -793       C  
ATOM   2758  C   LEU B 309      32.507 -31.244  11.603  1.00 42.57           C  
ANISOU 2758  C   LEU B 309     5601   6049   4526   1026    153   -810       C  
ATOM   2759  O   LEU B 309      33.461 -31.876  12.050  1.00 44.55           O  
ANISOU 2759  O   LEU B 309     5851   6235   4844   1104    215   -874       O  
ATOM   2760  CB  LEU B 309      30.742 -30.527  13.196  1.00 34.89           C  
ANISOU 2760  CB  LEU B 309     4653   4870   3733    990     60   -607       C  
ATOM   2761  CG  LEU B 309      29.337 -30.553  13.792  1.00 35.02           C  
ANISOU 2761  CG  LEU B 309     4676   4790   3841    955      1   -557       C  
ATOM   2762  CD1 LEU B 309      29.236 -29.514  14.916  1.00 31.45           C  
ANISOU 2762  CD1 LEU B 309     4224   4264   3460    981     -3   -388       C  
ATOM   2763  CD2 LEU B 309      28.283 -30.306  12.709  1.00 35.22           C  
ANISOU 2763  CD2 LEU B 309     4671   4956   3755    883    -68   -566       C  
ATOM   2764  N   ASP B 310      32.630 -30.293  10.684  1.00 42.18           N  
ANISOU 2764  N   ASP B 310     5522   6188   4317    976    143   -742       N  
ATOM   2765  CA  ASP B 310      33.927 -29.786  10.258  1.00 44.95           C  
ANISOU 2765  CA  ASP B 310     5835   6679   4566    991    209   -720       C  
ATOM   2766  C   ASP B 310      34.826 -29.578  11.474  1.00 45.29           C  
ANISOU 2766  C   ASP B 310     5862   6616   4728   1050    250   -649       C  
ATOM   2767  O   ASP B 310      34.393 -29.029  12.487  1.00 38.70           O  
ANISOU 2767  O   ASP B 310     5049   5660   3996   1045    216   -529       O  
ATOM   2768  CB  ASP B 310      33.737 -28.465   9.517  1.00 44.40           C  
ANISOU 2768  CB  ASP B 310     5752   6769   4349    915    180   -570       C  
ATOM   2769  CG  ASP B 310      35.040 -27.862   9.055  1.00 45.75           C  
ANISOU 2769  CG  ASP B 310     5881   7094   4407    902    253   -530       C  
ATOM   2770  OD1 ASP B 310      35.226 -27.750   7.829  1.00 44.94           O  
ANISOU 2770  OD1 ASP B 310     5757   7190   4126    860    270   -562       O  
ATOM   2771  OD2 ASP B 310      35.874 -27.493   9.908  1.00 52.64           O  
ANISOU 2771  OD2 ASP B 310     6734   7907   5359    925    293   -466       O  
ATOM   2772  N   LEU B 311      36.078 -30.008  11.371  1.00 43.13           N  
ANISOU 2772  N   LEU B 311     5545   6409   4434   1108    325   -727       N  
ATOM   2773  CA  LEU B 311      36.976 -29.997  12.521  1.00 43.68           C  
ANISOU 2773  CA  LEU B 311     5583   6402   4612   1174    358   -680       C  
ATOM   2774  C   LEU B 311      37.223 -28.578  13.037  1.00 36.21           C  
ANISOU 2774  C   LEU B 311     4621   5487   3650   1105    345   -501       C  
ATOM   2775  O   LEU B 311      37.320 -28.353  14.241  1.00 31.79           O  
ANISOU 2775  O   LEU B 311     4065   4813   3198   1125    331   -429       O  
ATOM   2776  CB  LEU B 311      38.298 -30.680  12.170  1.00 49.13           C  
ANISOU 2776  CB  LEU B 311     6205   7197   5265   1258    441   -797       C  
ATOM   2777  CG  LEU B 311      38.758 -31.757  13.152  1.00 60.22           C  
ANISOU 2777  CG  LEU B 311     7605   8454   6821   1390    464   -860       C  
ATOM   2778  CD1 LEU B 311      37.805 -32.941  13.120  1.00 60.01           C  
ANISOU 2778  CD1 LEU B 311     7665   8251   6885   1426    442   -977       C  
ATOM   2779  CD2 LEU B 311      40.174 -32.208  12.835  1.00 66.27           C  
ANISOU 2779  CD2 LEU B 311     8279   9356   7545   1488    549   -948       C  
ATOM   2780  N   ASN B 312      37.328 -27.623  12.118  1.00 40.37           N  
ANISOU 2780  N   ASN B 312     5135   6166   4036   1019    351   -432       N  
ATOM   2781  CA  ASN B 312      37.514 -26.223  12.489  1.00 38.94           C  
ANISOU 2781  CA  ASN B 312     4959   5993   3842    938    344   -265       C  
ATOM   2782  C   ASN B 312      36.300 -25.666  13.226  1.00 37.21           C  
ANISOU 2782  C   ASN B 312     4814   5605   3718    920    275   -162       C  
ATOM   2783  O   ASN B 312      36.434 -24.844  14.130  1.00 34.06           O  
ANISOU 2783  O   ASN B 312     4432   5125   3384    892    271    -62       O  
ATOM   2784  CB  ASN B 312      37.804 -25.371  11.251  1.00 37.59           C  
ANISOU 2784  CB  ASN B 312     4775   6010   3497    847    370   -199       C  
ATOM   2785  CG  ASN B 312      39.145 -25.695  10.618  1.00 41.24           C  
ANISOU 2785  CG  ASN B 312     5147   6665   3856    851    455   -281       C  
ATOM   2786  OD1 ASN B 312      40.196 -25.524  11.233  1.00 45.34           O  
ANISOU 2786  OD1 ASN B 312     5603   7212   4411    853    499   -268       O  
ATOM   2787  ND2 ASN B 312      39.113 -26.151   9.374  1.00 40.26           N  
ANISOU 2787  ND2 ASN B 312     5008   6697   3593    851    478   -370       N  
ATOM   2788  N   ASP B 313      35.115 -26.118  12.831  1.00 37.78           N  
ANISOU 2788  N   ASP B 313     4923   5638   3795    933    223   -197       N  
ATOM   2789  CA  ASP B 313      33.882 -25.669  13.463  1.00 37.44           C  
ANISOU 2789  CA  ASP B 313     4930   5457   3838    929    161   -109       C  
ATOM   2790  C   ASP B 313      33.759 -26.215  14.885  1.00 38.22           C  
ANISOU 2790  C   ASP B 313     5041   5386   4096    984    158   -133       C  
ATOM   2791  O   ASP B 313      33.310 -25.510  15.788  1.00 39.05           O  
ANISOU 2791  O   ASP B 313     5175   5385   4275    978    139    -38       O  
ATOM   2792  CB  ASP B 313      32.668 -26.058  12.618  1.00 32.43           C  
ANISOU 2792  CB  ASP B 313     4307   4862   3154    919    103   -146       C  
ATOM   2793  CG  ASP B 313      32.494 -25.162  11.403  1.00 36.30           C  
ANISOU 2793  CG  ASP B 313     4796   5510   3485    863     84    -56       C  
ATOM   2794  OD1 ASP B 313      33.296 -24.220  11.232  1.00 39.54           O  
ANISOU 2794  OD1 ASP B 313     5210   5978   3835    825    123     42       O  
ATOM   2795  OD2 ASP B 313      31.551 -25.395  10.618  1.00 40.25           O  
ANISOU 2795  OD2 ASP B 313     5292   6085   3917    850     29    -77       O  
ATOM   2796  N   GLN B 314      34.165 -27.468  15.079  1.00 37.90           N  
ANISOU 2796  N   GLN B 314     4981   5317   4103   1044    183   -258       N  
ATOM   2797  CA  GLN B 314      34.195 -28.059  16.414  1.00 34.72           C  
ANISOU 2797  CA  GLN B 314     4589   4766   3838   1103    186   -266       C  
ATOM   2798  C   GLN B 314      35.059 -27.214  17.345  1.00 31.93           C  
ANISOU 2798  C   GLN B 314     4216   4412   3503   1095    207   -177       C  
ATOM   2799  O   GLN B 314      34.664 -26.905  18.467  1.00 31.37           O  
ANISOU 2799  O   GLN B 314     4172   4233   3514   1099    188   -113       O  
ATOM   2800  CB  GLN B 314      34.738 -29.491  16.368  1.00 33.66           C  
ANISOU 2800  CB  GLN B 314     4440   4605   3744   1181    220   -401       C  
ATOM   2801  CG  GLN B 314      33.876 -30.471  15.587  1.00 36.08           C  
ANISOU 2801  CG  GLN B 314     4777   4880   4050   1176    202   -518       C  
ATOM   2802  CD  GLN B 314      34.488 -31.863  15.532  1.00 39.56           C  
ANISOU 2802  CD  GLN B 314     5222   5265   4542   1262    248   -660       C  
ATOM   2803  OE1 GLN B 314      34.431 -32.543  14.503  1.00 44.68           O  
ANISOU 2803  OE1 GLN B 314     5879   5961   5135   1259    263   -795       O  
ATOM   2804  NE2 GLN B 314      35.089 -32.287  16.638  1.00 33.59           N  
ANISOU 2804  NE2 GLN B 314     4464   4410   3891   1344    270   -631       N  
ATOM   2805  N   VAL B 315      36.247 -26.852  16.871  1.00 32.86           N  
ANISOU 2805  N   VAL B 315     4282   4665   3537   1076    249   -181       N  
ATOM   2806  CA  VAL B 315      37.165 -26.028  17.648  1.00 34.80           C  
ANISOU 2806  CA  VAL B 315     4497   4938   3786   1042    269   -111       C  
ATOM   2807  C   VAL B 315      36.561 -24.653  17.914  1.00 35.21           C  
ANISOU 2807  C   VAL B 315     4607   4933   3837    956    245      8       C  
ATOM   2808  O   VAL B 315      36.668 -24.118  19.017  1.00 36.40           O  
ANISOU 2808  O   VAL B 315     4774   5011   4045    938    239     56       O  
ATOM   2809  CB  VAL B 315      38.520 -25.864  16.930  1.00 37.63           C  
ANISOU 2809  CB  VAL B 315     4775   5482   4043   1016    323   -138       C  
ATOM   2810  CG1 VAL B 315      39.360 -24.789  17.610  1.00 36.91           C  
ANISOU 2810  CG1 VAL B 315     4651   5432   3941    936    338    -57       C  
ATOM   2811  CG2 VAL B 315      39.268 -27.194  16.890  1.00 35.78           C  
ANISOU 2811  CG2 VAL B 315     4473   5293   3827   1130    357   -256       C  
ATOM   2812  N   THR B 316      35.920 -24.086  16.899  1.00 33.55           N  
ANISOU 2812  N   THR B 316     4432   4756   3560    910    231     52       N  
ATOM   2813  CA  THR B 316      35.287 -22.781  17.040  1.00 34.39           C  
ANISOU 2813  CA  THR B 316     4603   4791   3673    851    211    172       C  
ATOM   2814  C   THR B 316      34.145 -22.803  18.058  1.00 34.16           C  
ANISOU 2814  C   THR B 316     4621   4602   3756    897    173    193       C  
ATOM   2815  O   THR B 316      34.051 -21.922  18.915  1.00 35.69           O  
ANISOU 2815  O   THR B 316     4857   4705   4000    872    177    255       O  
ATOM   2816  CB  THR B 316      34.767 -22.260  15.689  1.00 36.65           C  
ANISOU 2816  CB  THR B 316     4913   5157   3857    814    197    232       C  
ATOM   2817  OG1 THR B 316      35.879 -21.959  14.835  1.00 39.65           O  
ANISOU 2817  OG1 THR B 316     5254   5690   4121    750    245    240       O  
ATOM   2818  CG2 THR B 316      33.926 -21.005  15.889  1.00 34.21           C  
ANISOU 2818  CG2 THR B 316     4678   4740   3579    790    172    365       C  
ATOM   2819  N   LEU B 317      33.279 -23.808  17.960  1.00 30.25           N  
ANISOU 2819  N   LEU B 317     4120   4077   3298    956    143    133       N  
ATOM   2820  CA  LEU B 317      32.163 -23.939  18.892  1.00 32.09           C  
ANISOU 2820  CA  LEU B 317     4381   4181   3632    994    114    151       C  
ATOM   2821  C   LEU B 317      32.672 -24.031  20.326  1.00 35.49           C  
ANISOU 2821  C   LEU B 317     4814   4535   4136   1012    136    144       C  
ATOM   2822  O   LEU B 317      32.116 -23.415  21.233  1.00 34.56           O  
ANISOU 2822  O   LEU B 317     4731   4326   4072   1013    132    194       O  
ATOM   2823  CB  LEU B 317      31.312 -25.169  18.560  1.00 31.00           C  
ANISOU 2823  CB  LEU B 317     4224   4033   3520   1031     86     73       C  
ATOM   2824  CG  LEU B 317      30.516 -25.144  17.251  1.00 31.88           C  
ANISOU 2824  CG  LEU B 317     4327   4231   3556   1010     47     71       C  
ATOM   2825  CD1 LEU B 317      29.752 -26.443  17.074  1.00 28.35           C  
ANISOU 2825  CD1 LEU B 317     3861   3766   3146   1023     22    -30       C  
ATOM   2826  CD2 LEU B 317      29.563 -23.957  17.237  1.00 31.75           C  
ANISOU 2826  CD2 LEU B 317     4333   4191   3541   1005     16    192       C  
ATOM   2827  N   LEU B 318      33.735 -24.803  20.529  1.00 29.69           N  
ANISOU 2827  N   LEU B 318     4037   3848   3396   1034    159     82       N  
ATOM   2828  CA  LEU B 318      34.304 -24.950  21.864  1.00 30.27           C  
ANISOU 2828  CA  LEU B 318     4100   3882   3519   1056    171     84       C  
ATOM   2829  C   LEU B 318      34.947 -23.653  22.339  1.00 28.76           C  
ANISOU 2829  C   LEU B 318     3919   3711   3297    983    186    137       C  
ATOM   2830  O   LEU B 318      34.709 -23.209  23.459  1.00 32.14           O  
ANISOU 2830  O   LEU B 318     4378   4069   3767    975    183    163       O  
ATOM   2831  CB  LEU B 318      35.311 -26.104  21.908  1.00 30.20           C  
ANISOU 2831  CB  LEU B 318     4033   3931   3511   1117    188     15       C  
ATOM   2832  CG  LEU B 318      34.650 -27.485  21.887  1.00 34.16           C  
ANISOU 2832  CG  LEU B 318     4548   4352   4078   1191    179    -41       C  
ATOM   2833  CD1 LEU B 318      35.670 -28.596  21.725  1.00 34.87           C  
ANISOU 2833  CD1 LEU B 318     4592   4486   4173   1271    204   -112       C  
ATOM   2834  CD2 LEU B 318      33.805 -27.694  23.145  1.00 34.29           C  
ANISOU 2834  CD2 LEU B 318     4602   4247   4179   1210    163      3       C  
ATOM   2835  N   LYS B 319      35.756 -23.048  21.476  1.00 30.80           N  
ANISOU 2835  N   LYS B 319     4156   4068   3479    920    206    148       N  
ATOM   2836  CA  LYS B 319      36.463 -21.817  21.813  1.00 37.72           C  
ANISOU 2836  CA  LYS B 319     5044   4962   4325    823    227    193       C  
ATOM   2837  C   LYS B 319      35.532 -20.741  22.360  1.00 37.67           C  
ANISOU 2837  C   LYS B 319     5130   4817   4366    793    219    252       C  
ATOM   2838  O   LYS B 319      35.849 -20.081  23.353  1.00 34.86           O  
ANISOU 2838  O   LYS B 319     4798   4418   4029    744    229    254       O  
ATOM   2839  CB  LYS B 319      37.201 -21.276  20.588  1.00 41.39           C  
ANISOU 2839  CB  LYS B 319     5485   5543   4700    746    255    216       C  
ATOM   2840  CG  LYS B 319      37.809 -19.900  20.794  1.00 47.76           C  
ANISOU 2840  CG  LYS B 319     6322   6342   5481    618    281    273       C  
ATOM   2841  CD  LYS B 319      38.516 -19.408  19.536  1.00 53.18           C  
ANISOU 2841  CD  LYS B 319     6984   7150   6070    531    316    312       C  
ATOM   2842  CE  LYS B 319      38.997 -17.972  19.700  1.00 61.48           C  
ANISOU 2842  CE  LYS B 319     8090   8161   7111    383    346    382       C  
ATOM   2843  NZ  LYS B 319      39.727 -17.480  18.496  1.00 69.06           N  
ANISOU 2843  NZ  LYS B 319     9024   9246   7970    280    389    437       N  
ATOM   2844  N   TYR B 320      34.392 -20.559  21.702  1.00 33.00           N  
ANISOU 2844  N   TYR B 320     4585   4164   3788    825    202    294       N  
ATOM   2845  CA  TYR B 320      33.458 -19.510  22.091  1.00 38.61           C  
ANISOU 2845  CA  TYR B 320     5378   4744   4547    821    200    356       C  
ATOM   2846  C   TYR B 320      32.407 -20.001  23.077  1.00 41.54           C  
ANISOU 2846  C   TYR B 320     5758   5030   4996    901    184    333       C  
ATOM   2847  O   TYR B 320      31.687 -19.199  23.665  1.00 50.57           O  
ANISOU 2847  O   TYR B 320     6959   6068   6187    913    192    364       O  
ATOM   2848  CB  TYR B 320      32.781 -18.898  20.860  1.00 40.05           C  
ANISOU 2848  CB  TYR B 320     5598   4923   4697    822    187    437       C  
ATOM   2849  CG  TYR B 320      33.713 -18.067  20.009  1.00 42.16           C  
ANISOU 2849  CG  TYR B 320     5883   5248   4887    725    215    492       C  
ATOM   2850  CD1 TYR B 320      34.010 -16.753  20.350  1.00 43.42           C  
ANISOU 2850  CD1 TYR B 320     6121   5310   5066    647    247    551       C  
ATOM   2851  CD2 TYR B 320      34.297 -18.597  18.868  1.00 41.82           C  
ANISOU 2851  CD2 TYR B 320     5781   5357   4751    704    218    482       C  
ATOM   2852  CE1 TYR B 320      34.865 -15.991  19.577  1.00 45.90           C  
ANISOU 2852  CE1 TYR B 320     6455   5672   5313    538    279    612       C  
ATOM   2853  CE2 TYR B 320      35.155 -17.846  18.091  1.00 46.37           C  
ANISOU 2853  CE2 TYR B 320     6367   6005   5248    604    252    541       C  
ATOM   2854  CZ  TYR B 320      35.434 -16.544  18.448  1.00 51.46           C  
ANISOU 2854  CZ  TYR B 320     7090   6546   5917    516    282    614       C  
ATOM   2855  OH  TYR B 320      36.288 -15.795  17.671  1.00 54.68           O  
ANISOU 2855  OH  TYR B 320     7510   7020   6247    398    322    683       O  
ATOM   2856  N   GLY B 321      32.324 -21.314  23.267  1.00 36.72           N  
ANISOU 2856  N   GLY B 321     5092   4459   4402    955    168    278       N  
ATOM   2857  CA  GLY B 321      31.285 -21.878  24.110  1.00 36.35           C  
ANISOU 2857  CA  GLY B 321     5048   4342   4423   1016    158    267       C  
ATOM   2858  C   GLY B 321      31.685 -22.159  25.550  1.00 35.20           C  
ANISOU 2858  C   GLY B 321     4897   4174   4301   1023    173    240       C  
ATOM   2859  O   GLY B 321      30.849 -22.095  26.453  1.00 31.15           O  
ANISOU 2859  O   GLY B 321     4407   3597   3833   1052    180    248       O  
ATOM   2860  N   VAL B 322      32.958 -22.478  25.767  1.00 38.73           N  
ANISOU 2860  N   VAL B 322     5309   4697   4711   1000    178    211       N  
ATOM   2861  CA  VAL B 322      33.417 -22.919  27.084  1.00 37.33           C  
ANISOU 2861  CA  VAL B 322     5112   4533   4538   1017    181    193       C  
ATOM   2862  C   VAL B 322      33.163 -21.898  28.190  1.00 34.37           C  
ANISOU 2862  C   VAL B 322     4788   4108   4165    978    197    199       C  
ATOM   2863  O   VAL B 322      32.789 -22.267  29.300  1.00 33.42           O  
ANISOU 2863  O   VAL B 322     4671   3969   4058   1010    200    197       O  
ATOM   2864  CB  VAL B 322      34.912 -23.326  27.080  1.00 39.14           C  
ANISOU 2864  CB  VAL B 322     5273   4881   4718   1005    178    168       C  
ATOM   2865  CG1 VAL B 322      35.095 -24.649  26.360  1.00 38.20           C  
ANISOU 2865  CG1 VAL B 322     5108   4794   4614   1080    171    144       C  
ATOM   2866  CG2 VAL B 322      35.766 -22.243  26.441  1.00 39.94           C  
ANISOU 2866  CG2 VAL B 322     5369   5044   4762    910    192    167       C  
ATOM   2867  N   HIS B 323      33.360 -20.619  27.892  1.00 32.07           N  
ANISOU 2867  N   HIS B 323     4543   3789   3855    906    212    205       N  
ATOM   2868  CA  HIS B 323      33.157 -19.582  28.898  1.00 36.70           C  
ANISOU 2868  CA  HIS B 323     5192   4309   4444    864    236    188       C  
ATOM   2869  C   HIS B 323      31.722 -19.558  29.423  1.00 35.31           C  
ANISOU 2869  C   HIS B 323     5053   4038   4323    937    251    199       C  
ATOM   2870  O   HIS B 323      31.499 -19.512  30.630  1.00 35.28           O  
ANISOU 2870  O   HIS B 323     5064   4026   4313    944    267    171       O  
ATOM   2871  CB  HIS B 323      33.549 -18.207  28.357  1.00 49.78           C  
ANISOU 2871  CB  HIS B 323     6909   5915   6088    772    257    196       C  
ATOM   2872  CG  HIS B 323      34.997 -17.875  28.541  1.00 62.61           C  
ANISOU 2872  CG  HIS B 323     8503   7634   7652    660    259    162       C  
ATOM   2873  ND1 HIS B 323      35.949 -18.135  27.578  1.00 67.38           N  
ANISOU 2873  ND1 HIS B 323     9043   8344   8214    618    251    177       N  
ATOM   2874  CD2 HIS B 323      35.656 -17.301  29.575  1.00 67.90           C  
ANISOU 2874  CD2 HIS B 323     9186   8326   8287    574    267    106       C  
ATOM   2875  CE1 HIS B 323      37.132 -17.736  28.012  1.00 70.57           C  
ANISOU 2875  CE1 HIS B 323     9412   8837   8566    511    255    140       C  
ATOM   2876  NE2 HIS B 323      36.981 -17.225  29.221  1.00 71.73           N  
ANISOU 2876  NE2 HIS B 323     9604   8934   8714    476    260     95       N  
ATOM   2877  N   GLU B 324      30.752 -19.587  28.514  1.00 34.09           N  
ANISOU 2877  N   GLU B 324     4905   3836   4211    988    244    241       N  
ATOM   2878  CA  GLU B 324      29.346 -19.588  28.904  1.00 33.98           C  
ANISOU 2878  CA  GLU B 324     4902   3758   4251   1061    258    256       C  
ATOM   2879  C   GLU B 324      29.012 -20.815  29.743  1.00 30.74           C  
ANISOU 2879  C   GLU B 324     4441   3389   3849   1099    255    243       C  
ATOM   2880  O   GLU B 324      28.271 -20.726  30.721  1.00 33.40           O  
ANISOU 2880  O   GLU B 324     4788   3701   4202   1128    284    236       O  
ATOM   2881  CB  GLU B 324      28.443 -19.528  27.668  1.00 34.78           C  
ANISOU 2881  CB  GLU B 324     4992   3841   4384   1106    237    307       C  
ATOM   2882  CG  GLU B 324      28.425 -18.166  26.992  1.00 35.82           C  
ANISOU 2882  CG  GLU B 324     5190   3902   4519   1092    248    350       C  
ATOM   2883  CD  GLU B 324      27.979 -18.228  25.544  1.00 39.98           C  
ANISOU 2883  CD  GLU B 324     5692   4461   5036   1118    211    413       C  
ATOM   2884  OE1 GLU B 324      27.105 -19.056  25.210  1.00 41.16           O  
ANISOU 2884  OE1 GLU B 324     5778   4659   5201   1169    182    420       O  
ATOM   2885  OE2 GLU B 324      28.508 -17.441  24.735  1.00 46.25           O  
ANISOU 2885  OE2 GLU B 324     6531   5243   5801   1077    211    458       O  
ATOM   2886  N   ILE B 325      29.565 -21.960  29.359  1.00 32.87           N  
ANISOU 2886  N   ILE B 325     4662   3720   4107   1100    227    244       N  
ATOM   2887  CA  ILE B 325      29.309 -23.204  30.074  1.00 35.32           C  
ANISOU 2887  CA  ILE B 325     4938   4048   4434   1134    226    249       C  
ATOM   2888  C   ILE B 325      29.975 -23.207  31.447  1.00 36.93           C  
ANISOU 2888  C   ILE B 325     5149   4291   4593   1121    239    239       C  
ATOM   2889  O   ILE B 325      29.418 -23.724  32.411  1.00 33.10           O  
ANISOU 2889  O   ILE B 325     4659   3805   4113   1146    257    257       O  
ATOM   2890  CB  ILE B 325      29.772 -24.427  29.273  1.00 36.17           C  
ANISOU 2890  CB  ILE B 325     5005   4184   4552   1150    198    245       C  
ATOM   2891  CG1 ILE B 325      28.975 -24.533  27.975  1.00 43.34           C  
ANISOU 2891  CG1 ILE B 325     5903   5075   5490   1154    180    244       C  
ATOM   2892  CG2 ILE B 325      29.610 -25.701  30.101  1.00 27.07           C  
ANISOU 2892  CG2 ILE B 325     3837   3022   3427   1184    202    263       C  
ATOM   2893  CD1 ILE B 325      29.369 -25.716  27.130  1.00 49.70           C  
ANISOU 2893  CD1 ILE B 325     6680   5902   6302   1164    159    214       C  
ATOM   2894  N   ILE B 326      31.164 -22.620  31.533  1.00 34.96           N  
ANISOU 2894  N   ILE B 326     4903   4093   4288   1073    231    213       N  
ATOM   2895  CA  ILE B 326      31.869 -22.525  32.808  1.00 32.01           C  
ANISOU 2895  CA  ILE B 326     4525   3787   3850   1048    234    196       C  
ATOM   2896  C   ILE B 326      31.066 -21.758  33.863  1.00 32.67           C  
ANISOU 2896  C   ILE B 326     4659   3833   3921   1039    273    173       C  
ATOM   2897  O   ILE B 326      30.982 -22.176  35.015  1.00 34.55           O  
ANISOU 2897  O   ILE B 326     4888   4121   4117   1052    281    180       O  
ATOM   2898  CB  ILE B 326      33.257 -21.886  32.633  1.00 31.40           C  
ANISOU 2898  CB  ILE B 326     4431   3786   3712    974    217    161       C  
ATOM   2899  CG1 ILE B 326      34.214 -22.889  31.977  1.00 33.74           C  
ANISOU 2899  CG1 ILE B 326     4654   4164   4002   1006    185    180       C  
ATOM   2900  CG2 ILE B 326      33.798 -21.411  33.978  1.00 35.70           C  
ANISOU 2900  CG2 ILE B 326     4981   4404   4180    923    218    124       C  
ATOM   2901  CD1 ILE B 326      35.564 -22.310  31.612  1.00 35.48           C  
ANISOU 2901  CD1 ILE B 326     4831   4483   4165    930    173    150       C  
ATOM   2902  N   TYR B 327      30.460 -20.644  33.465  1.00 33.90           N  
ANISOU 2902  N   TYR B 327     4869   3903   4110   1024    300    148       N  
ATOM   2903  CA  TYR B 327      29.676 -19.848  34.405  1.00 36.00           C  
ANISOU 2903  CA  TYR B 327     5185   4122   4370   1031    349    110       C  
ATOM   2904  C   TYR B 327      28.328 -20.493  34.692  1.00 38.88           C  
ANISOU 2904  C   TYR B 327     5523   4469   4779   1108    374    148       C  
ATOM   2905  O   TYR B 327      27.780 -20.353  35.784  1.00 37.04           O  
ANISOU 2905  O   TYR B 327     5302   4254   4518   1123    417    125       O  
ATOM   2906  CB  TYR B 327      29.514 -18.418  33.893  1.00 39.60           C  
ANISOU 2906  CB  TYR B 327     5716   4472   4860   1006    375     76       C  
ATOM   2907  CG  TYR B 327      30.846 -17.763  33.631  1.00 49.25           C  
ANISOU 2907  CG  TYR B 327     6964   5711   6039    902    357     41       C  
ATOM   2908  CD1 TYR B 327      31.876 -17.859  34.559  1.00 57.33           C  
ANISOU 2908  CD1 TYR B 327     7967   6840   6977    830    343     -9       C  
ATOM   2909  CD2 TYR B 327      31.083 -17.060  32.459  1.00 53.93           C  
ANISOU 2909  CD2 TYR B 327     7590   6234   6667    869    353     65       C  
ATOM   2910  CE1 TYR B 327      33.105 -17.274  34.327  1.00 63.44           C  
ANISOU 2910  CE1 TYR B 327     8743   7652   7708    719    326    -44       C  
ATOM   2911  CE2 TYR B 327      32.309 -16.465  32.219  1.00 60.31           C  
ANISOU 2911  CE2 TYR B 327     8414   7067   7435    755    344     38       C  
ATOM   2912  CZ  TYR B 327      33.316 -16.576  33.157  1.00 64.86           C  
ANISOU 2912  CZ  TYR B 327     8959   7753   7932    675    331    -22       C  
ATOM   2913  OH  TYR B 327      34.536 -15.986  32.924  1.00 71.81           O  
ANISOU 2913  OH  TYR B 327     9836   8678   8770    546    322    -53       O  
ATOM   2914  N   THR B 328      27.803 -21.214  33.710  1.00 35.82           N  
ANISOU 2914  N   THR B 328     5095   4062   4453   1145    351    199       N  
ATOM   2915  CA  THR B 328      26.584 -21.976  33.914  1.00 37.96           C  
ANISOU 2915  CA  THR B 328     5325   4333   4767   1193    369    237       C  
ATOM   2916  C   THR B 328      26.799 -23.013  35.011  1.00 40.17           C  
ANISOU 2916  C   THR B 328     5581   4677   5003   1187    376    263       C  
ATOM   2917  O   THR B 328      26.013 -23.114  35.957  1.00 38.20           O  
ANISOU 2917  O   THR B 328     5324   4450   4740   1202    422    272       O  
ATOM   2918  CB  THR B 328      26.150 -22.688  32.624  1.00 35.59           C  
ANISOU 2918  CB  THR B 328     4981   4014   4528   1209    332    273       C  
ATOM   2919  OG1 THR B 328      25.749 -21.711  31.657  1.00 35.10           O  
ANISOU 2919  OG1 THR B 328     4933   3907   4495   1227    325    271       O  
ATOM   2920  CG2 THR B 328      24.990 -23.634  32.899  1.00 31.68           C  
ANISOU 2920  CG2 THR B 328     4433   3528   4075   1229    349    308       C  
ATOM   2921  N   MET B 329      27.879 -23.774  34.886  1.00 35.61           N  
ANISOU 2921  N   MET B 329     4992   4137   4401   1172    335    282       N  
ATOM   2922  CA  MET B 329      28.150 -24.858  35.818  1.00 41.00           C  
ANISOU 2922  CA  MET B 329     5658   4873   5049   1182    334    332       C  
ATOM   2923  C   MET B 329      28.701 -24.348  37.149  1.00 39.74           C  
ANISOU 2923  C   MET B 329     5516   4800   4785   1160    348    313       C  
ATOM   2924  O   MET B 329      28.523 -24.986  38.186  1.00 38.66           O  
ANISOU 2924  O   MET B 329     5371   4717   4601   1171    365    362       O  
ATOM   2925  CB  MET B 329      29.077 -25.894  35.179  1.00 42.08           C  
ANISOU 2925  CB  MET B 329     5771   5012   5205   1199    287    363       C  
ATOM   2926  CG  MET B 329      28.519 -26.462  33.880  1.00 43.63           C  
ANISOU 2926  CG  MET B 329     5954   5132   5491   1210    274    363       C  
ATOM   2927  SD  MET B 329      29.356 -27.955  33.328  1.00 50.40           S  
ANISOU 2927  SD  MET B 329     6796   5968   6385   1248    241    389       S  
ATOM   2928  CE  MET B 329      28.977 -29.073  34.677  1.00 41.00           C  
ANISOU 2928  CE  MET B 329     5617   4764   5197   1271    266    481       C  
ATOM   2929  N   LEU B 330      29.351 -23.189  37.118  1.00 38.12           N  
ANISOU 2929  N   LEU B 330     5337   4609   4536   1119    343    240       N  
ATOM   2930  CA  LEU B 330      29.832 -22.556  38.343  1.00 38.88           C  
ANISOU 2930  CA  LEU B 330     5455   4792   4524   1078    357    191       C  
ATOM   2931  C   LEU B 330      28.658 -22.190  39.252  1.00 38.32           C  
ANISOU 2931  C   LEU B 330     5411   4715   4434   1094    425    170       C  
ATOM   2932  O   LEU B 330      28.776 -22.200  40.476  1.00 35.90           O  
ANISOU 2932  O   LEU B 330     5109   4507   4026   1077    443    159       O  
ATOM   2933  CB  LEU B 330      30.656 -21.308  38.017  1.00 36.79           C  
ANISOU 2933  CB  LEU B 330     5225   4518   4234   1008    346    103       C  
ATOM   2934  CG  LEU B 330      31.237 -20.530  39.200  1.00 39.52           C  
ANISOU 2934  CG  LEU B 330     5598   4954   4464    938    355     22       C  
ATOM   2935  CD1 LEU B 330      32.225 -21.393  39.982  1.00 41.31           C  
ANISOU 2935  CD1 LEU B 330     5762   5346   4587    930    304     68       C  
ATOM   2936  CD2 LEU B 330      31.897 -19.242  38.726  1.00 38.92           C  
ANISOU 2936  CD2 LEU B 330     5570   4826   4390    849    354    -69       C  
ATOM   2937  N   ALA B 331      27.524 -21.865  38.642  1.00 38.01           N  
ANISOU 2937  N   ALA B 331     5378   4579   4484   1131    462    164       N  
ATOM   2938  CA  ALA B 331      26.320 -21.542  39.398  1.00 37.27           C  
ANISOU 2938  CA  ALA B 331     5289   4487   4384   1162    535    144       C  
ATOM   2939  C   ALA B 331      25.898 -22.725  40.262  1.00 39.62           C  
ANISOU 2939  C   ALA B 331     5544   4869   4639   1173    554    227       C  
ATOM   2940  O   ALA B 331      25.360 -22.544  41.354  1.00 40.07           O  
ANISOU 2940  O   ALA B 331     5604   4995   4625   1175    614    208       O  
ATOM   2941  CB  ALA B 331      25.195 -21.139  38.459  1.00 34.08           C  
ANISOU 2941  CB  ALA B 331     4874   3985   4091   1215    560    145       C  
ATOM   2942  N   SER B 332      26.150 -23.933  39.765  1.00 36.64           N  
ANISOU 2942  N   SER B 332     5133   4482   4306   1177    508    317       N  
ATOM   2943  CA  SER B 332      25.826 -25.153  40.498  1.00 39.35           C  
ANISOU 2943  CA  SER B 332     5450   4876   4625   1180    524    417       C  
ATOM   2944  C   SER B 332      26.620 -25.255  41.794  1.00 41.42           C  
ANISOU 2944  C   SER B 332     5727   5265   4745   1164    520    437       C  
ATOM   2945  O   SER B 332      26.182 -25.901  42.744  1.00 40.88           O  
ANISOU 2945  O   SER B 332     5649   5266   4619   1163    556    512       O  
ATOM   2946  CB  SER B 332      26.105 -26.391  39.642  1.00 38.30           C  
ANISOU 2946  CB  SER B 332     5298   4677   4577   1190    475    497       C  
ATOM   2947  OG  SER B 332      25.292 -26.419  38.486  1.00 36.61           O  
ANISOU 2947  OG  SER B 332     5062   4371   4475   1194    475    480       O  
ATOM   2948  N   LEU B 333      27.792 -24.628  41.823  1.00 39.15           N  
ANISOU 2948  N   LEU B 333     5458   5024   4395   1142    473    375       N  
ATOM   2949  CA  LEU B 333      28.669 -24.701  42.988  1.00 41.50           C  
ANISOU 2949  CA  LEU B 333     5755   5471   4543   1120    451    388       C  
ATOM   2950  C   LEU B 333      28.495 -23.500  43.914  1.00 41.42           C  
ANISOU 2950  C   LEU B 333     5779   5537   4423   1077    498    269       C  
ATOM   2951  O   LEU B 333      29.225 -23.352  44.896  1.00 42.68           O  
ANISOU 2951  O   LEU B 333     5938   5841   4436   1041    478    250       O  
ATOM   2952  CB  LEU B 333      30.131 -24.807  42.550  1.00 45.42           C  
ANISOU 2952  CB  LEU B 333     6229   6006   5021   1113    367    388       C  
ATOM   2953  CG  LEU B 333      30.464 -25.833  41.464  1.00 48.30           C  
ANISOU 2953  CG  LEU B 333     6566   6285   5501   1163    323    468       C  
ATOM   2954  CD1 LEU B 333      31.970 -25.911  41.251  1.00 48.09           C  
ANISOU 2954  CD1 LEU B 333     6499   6343   5431   1166    250    466       C  
ATOM   2955  CD2 LEU B 333      29.900 -27.200  41.808  1.00 45.94           C  
ANISOU 2955  CD2 LEU B 333     6263   5958   5234   1213    339    603       C  
ATOM   2956  N   MET B 334      27.520 -22.651  43.603  1.00 39.65           N  
ANISOU 2956  N   MET B 334     5581   5219   4263   1085    562    187       N  
ATOM   2957  CA  MET B 334      27.343 -21.396  44.323  1.00 40.56           C  
ANISOU 2957  CA  MET B 334     5746   5365   4300   1054    618     47       C  
ATOM   2958  C   MET B 334      26.015 -21.295  45.065  1.00 43.43           C  
ANISOU 2958  C   MET B 334     6106   5755   4639   1092    717     33       C  
ATOM   2959  O   MET B 334      24.992 -21.817  44.620  1.00 43.12           O  
ANISOU 2959  O   MET B 334     6026   5658   4698   1140    751    105       O  
ATOM   2960  CB  MET B 334      27.425 -20.211  43.354  1.00 41.25           C  
ANISOU 2960  CB  MET B 334     5882   5306   4484   1044    619    -59       C  
ATOM   2961  CG  MET B 334      28.818 -19.848  42.864  1.00 43.54           C  
ANISOU 2961  CG  MET B 334     6186   5596   4759    975    543    -96       C  
ATOM   2962  SD  MET B 334      28.738 -18.505  41.657  1.00 44.23           S  
ANISOU 2962  SD  MET B 334     6343   5490   4973    961    559   -186       S  
ATOM   2963  CE  MET B 334      30.406 -17.863  41.747  1.00 44.74           C  
ANISOU 2963  CE  MET B 334     6430   5618   4953    830    498   -268       C  
ATOM   2964  N   ASN B 335      26.049 -20.606  46.199  1.00 42.67           N  
ANISOU 2964  N   ASN B 335     6045   5762   4407   1062    766    -69       N  
ATOM   2965  CA  ASN B 335      24.849 -20.020  46.776  1.00 44.85           C  
ANISOU 2965  CA  ASN B 335     6331   6043   4667   1103    878   -146       C  
ATOM   2966  C   ASN B 335      25.115 -18.538  47.024  1.00 48.67           C  
ANISOU 2966  C   ASN B 335     6900   6478   5116   1077    914   -341       C  
ATOM   2967  O   ASN B 335      26.139 -18.014  46.586  1.00 48.34           O  
ANISOU 2967  O   ASN B 335     6902   6379   5084   1018    850   -399       O  
ATOM   2968  CB  ASN B 335      24.396 -20.752  48.044  1.00 41.77           C  
ANISOU 2968  CB  ASN B 335     5903   5837   4132   1098    931    -80       C  
ATOM   2969  CG  ASN B 335      25.446 -20.754  49.140  1.00 45.25           C  
ANISOU 2969  CG  ASN B 335     6367   6455   4370   1027    892   -110       C  
ATOM   2970  OD1 ASN B 335      26.331 -19.901  49.182  1.00 48.26           O  
ANISOU 2970  OD1 ASN B 335     6799   6835   4703    973    854   -237       O  
ATOM   2971  ND2 ASN B 335      25.341 -21.718  50.044  1.00 45.71           N  
ANISOU 2971  ND2 ASN B 335     6386   6676   4304   1019    901     14       N  
ATOM   2972  N   LYS B 336      24.209 -17.858  47.714  1.00 49.00           N  
ANISOU 2972  N   LYS B 336     6964   6535   5119   1119   1022   -447       N  
ATOM   2973  CA  LYS B 336      24.362 -16.420  47.910  1.00 50.39           C  
ANISOU 2973  CA  LYS B 336     7238   6623   5283   1104   1070   -646       C  
ATOM   2974  C   LYS B 336      25.533 -16.077  48.829  1.00 50.96           C  
ANISOU 2974  C   LYS B 336     7364   6823   5177    984   1033   -755       C  
ATOM   2975  O   LYS B 336      25.946 -14.921  48.909  1.00 49.36           O  
ANISOU 2975  O   LYS B 336     7254   6534   4966    932   1051   -926       O  
ATOM   2976  CB  LYS B 336      23.068 -15.801  48.444  1.00 50.90           C  
ANISOU 2976  CB  LYS B 336     7311   6676   5353   1198   1206   -744       C  
ATOM   2977  CG  LYS B 336      22.630 -16.328  49.800  1.00 52.62           C  
ANISOU 2977  CG  LYS B 336     7483   7120   5389   1190   1276   -743       C  
ATOM   2978  CD  LYS B 336      21.293 -15.732  50.205  1.00 57.49           C  
ANISOU 2978  CD  LYS B 336     8089   7730   6026   1299   1420   -838       C  
ATOM   2979  CE  LYS B 336      20.839 -16.252  51.561  1.00 62.85           C  
ANISOU 2979  CE  LYS B 336     8717   8655   6508   1283   1501   -835       C  
ATOM   2980  NZ  LYS B 336      21.834 -15.961  52.629  1.00 64.27           N  
ANISOU 2980  NZ  LYS B 336     8968   8979   6472   1174   1481   -953       N  
ATOM   2981  N   ASP B 337      26.078 -17.084  49.503  1.00 48.28           N  
ANISOU 2981  N   ASP B 337     6964   6685   4695    935    977   -652       N  
ATOM   2982  CA  ASP B 337      27.104 -16.851  50.515  1.00 51.55           C  
ANISOU 2982  CA  ASP B 337     7403   7277   4906    825    937   -745       C  
ATOM   2983  C   ASP B 337      28.509 -17.303  50.112  1.00 50.49           C  
ANISOU 2983  C   ASP B 337     7233   7197   4752    747    801   -668       C  
ATOM   2984  O   ASP B 337      29.484 -16.964  50.783  1.00 48.33           O  
ANISOU 2984  O   ASP B 337     6971   7066   4324    642    752   -759       O  
ATOM   2985  CB  ASP B 337      26.705 -17.508  51.839  1.00 54.23           C  
ANISOU 2985  CB  ASP B 337     7700   7857   5049    830    982   -699       C  
ATOM   2986  CG  ASP B 337      25.512 -16.836  52.487  1.00 58.38           C  
ANISOU 2986  CG  ASP B 337     8261   8381   5540    886   1128   -831       C  
ATOM   2987  OD1 ASP B 337      25.539 -15.597  52.643  1.00 57.02           O  
ANISOU 2987  OD1 ASP B 337     8178   8124   5363    861   1181  -1046       O  
ATOM   2988  OD2 ASP B 337      24.550 -17.548  52.843  1.00 61.08           O  
ANISOU 2988  OD2 ASP B 337     8541   8804   5863    952   1195   -723       O  
ATOM   2989  N   GLY B 338      28.620 -18.070  49.032  1.00 47.65           N  
ANISOU 2989  N   GLY B 338     6823   6742   4539    796    741   -510       N  
ATOM   2990  CA  GLY B 338      29.927 -18.518  48.584  1.00 44.59           C  
ANISOU 2990  CA  GLY B 338     6391   6409   4144    742    623   -440       C  
ATOM   2991  C   GLY B 338      29.928 -19.554  47.478  1.00 45.60           C  
ANISOU 2991  C   GLY B 338     6460   6446   4422    814    572   -262       C  
ATOM   2992  O   GLY B 338      28.891 -19.852  46.886  1.00 45.26           O  
ANISOU 2992  O   GLY B 338     6414   6273   4510    894    621   -200       O  
ATOM   2993  N   VAL B 339      31.106 -20.109  47.206  1.00 46.28           N  
ANISOU 2993  N   VAL B 339     6491   6611   4484    787    472   -188       N  
ATOM   2994  CA  VAL B 339      31.282 -21.047  46.104  1.00 44.79           C  
ANISOU 2994  CA  VAL B 339     6251   6333   4432    852    422    -47       C  
ATOM   2995  C   VAL B 339      32.162 -22.234  46.496  1.00 47.27           C  
ANISOU 2995  C   VAL B 339     6488   6807   4663    880    341     96       C  
ATOM   2996  O   VAL B 339      33.192 -22.069  47.148  1.00 47.67           O  
ANISOU 2996  O   VAL B 339     6505   7035   4572    823    282     66       O  
ATOM   2997  CB  VAL B 339      31.895 -20.345  44.872  1.00 42.36           C  
ANISOU 2997  CB  VAL B 339     5959   5896   4239    810    390   -114       C  
ATOM   2998  CG1 VAL B 339      33.238 -19.724  45.228  1.00 40.56           C  
ANISOU 2998  CG1 VAL B 339     5714   5801   3897    698    329   -206       C  
ATOM   2999  CG2 VAL B 339      32.041 -21.321  43.712  1.00 41.94           C  
ANISOU 2999  CG2 VAL B 339     5855   5763   4317    880    346     15       C  
ATOM   3000  N   LEU B 340      31.740 -23.431  46.100  1.00 49.79           N  
ANISOU 3000  N   LEU B 340     6781   7064   5073    969    339    251       N  
ATOM   3001  CA  LEU B 340      32.537 -24.638  46.297  1.00 48.09           C  
ANISOU 3001  CA  LEU B 340     6505   6951   4818   1024    267    404       C  
ATOM   3002  C   LEU B 340      33.823 -24.566  45.483  1.00 50.55           C  
ANISOU 3002  C   LEU B 340     6763   7279   5166   1016    186    384       C  
ATOM   3003  O   LEU B 340      33.807 -24.169  44.318  1.00 49.58           O  
ANISOU 3003  O   LEU B 340     6653   7013   5173   1005    193    325       O  
ATOM   3004  CB  LEU B 340      31.740 -25.872  45.872  1.00 47.20           C  
ANISOU 3004  CB  LEU B 340     6395   6709   4828   1111    294    555       C  
ATOM   3005  CG  LEU B 340      30.992 -26.664  46.943  1.00 52.40           C  
ANISOU 3005  CG  LEU B 340     7065   7435   5409   1138    339    680       C  
ATOM   3006  CD1 LEU B 340      30.565 -25.770  48.089  1.00 61.89           C  
ANISOU 3006  CD1 LEU B 340     8290   8774   6451   1075    393    584       C  
ATOM   3007  CD2 LEU B 340      29.803 -27.392  46.336  1.00 47.24           C  
ANISOU 3007  CD2 LEU B 340     6433   6605   4912   1173    399    756       C  
ATOM   3008  N   ILE B 341      34.936 -24.952  46.097  1.00 50.77           N  
ANISOU 3008  N   ILE B 341     6722   7499   5070   1024    110    440       N  
ATOM   3009  CA  ILE B 341      36.213 -24.995  45.392  1.00 53.61           C  
ANISOU 3009  CA  ILE B 341     7004   7912   5454   1026     35    433       C  
ATOM   3010  C   ILE B 341      36.912 -26.332  45.610  1.00 54.85           C  
ANISOU 3010  C   ILE B 341     7085   8166   5589   1147    -29    607       C  
ATOM   3011  O   ILE B 341      36.521 -27.115  46.478  1.00 49.81           O  
ANISOU 3011  O   ILE B 341     6460   7578   4887   1209    -23    735       O  
ATOM   3012  CB  ILE B 341      37.161 -23.865  45.845  1.00 54.25           C  
ANISOU 3012  CB  ILE B 341     7048   8167   5399    896     -7    293       C  
ATOM   3013  CG1 ILE B 341      37.636 -24.111  47.280  1.00 51.82           C  
ANISOU 3013  CG1 ILE B 341     6690   8121   4880    888    -57    339       C  
ATOM   3014  CG2 ILE B 341      36.490 -22.505  45.698  1.00 51.44           C  
ANISOU 3014  CG2 ILE B 341     6786   7689   5070    783     63    118       C  
ATOM   3015  CD1 ILE B 341      38.782 -23.218  47.711  1.00 53.24           C  
ANISOU 3015  CD1 ILE B 341     6801   8515   4914    757   -122    214       C  
ATOM   3016  N   SER B 342      37.947 -26.581  44.812  1.00 52.91           N  
ANISOU 3016  N   SER B 342     6760   7945   5397   1185    -84    617       N  
ATOM   3017  CA  SER B 342      38.776 -27.772  44.958  1.00 53.24           C  
ANISOU 3017  CA  SER B 342     6719   8085   5425   1320   -147    772       C  
ATOM   3018  C   SER B 342      37.944 -29.044  45.078  1.00 52.70           C  
ANISOU 3018  C   SER B 342     6714   7869   5441   1442   -111    934       C  
ATOM   3019  O   SER B 342      38.033 -29.760  46.075  1.00 51.63           O  
ANISOU 3019  O   SER B 342     6567   7840   5210   1510   -137   1076       O  
ATOM   3020  CB  SER B 342      39.692 -27.635  46.174  1.00 58.91           C  
ANISOU 3020  CB  SER B 342     7347   9100   5934   1300   -224    802       C  
ATOM   3021  OG  SER B 342      40.635 -28.691  46.215  1.00 64.67           O  
ANISOU 3021  OG  SER B 342     7977   9938   6656   1446   -294    951       O  
ATOM   3022  N   GLU B 343      37.130 -29.310  44.062  1.00 51.39           N  
ANISOU 3022  N   GLU B 343     6616   7462   5448   1460    -52    915       N  
ATOM   3023  CA  GLU B 343      36.303 -30.511  44.031  1.00 54.09           C  
ANISOU 3023  CA  GLU B 343     7023   7636   5893   1549    -11   1050       C  
ATOM   3024  C   GLU B 343      35.367 -30.600  45.232  1.00 57.91           C  
ANISOU 3024  C   GLU B 343     7564   8156   6282   1514     31   1125       C  
ATOM   3025  O   GLU B 343      35.037 -31.693  45.691  1.00 61.20           O  
ANISOU 3025  O   GLU B 343     8014   8522   6717   1589     44   1288       O  
ATOM   3026  CB  GLU B 343      37.179 -31.764  43.953  1.00 59.06           C  
ANISOU 3026  CB  GLU B 343     7606   8275   6559   1703    -61   1196       C  
ATOM   3027  N   GLY B 344      34.945 -29.445  45.740  1.00 54.13           N  
ANISOU 3027  N   GLY B 344     7102   7761   5705   1399     59   1005       N  
ATOM   3028  CA  GLY B 344      33.985 -29.394  46.827  1.00 52.96           C  
ANISOU 3028  CA  GLY B 344     7003   7660   5459   1358    115   1046       C  
ATOM   3029  C   GLY B 344      34.577 -29.621  48.207  1.00 55.40           C  
ANISOU 3029  C   GLY B 344     7276   8214   5561   1374     69   1146       C  
ATOM   3030  O   GLY B 344      33.848 -29.692  49.196  1.00 59.28           O  
ANISOU 3030  O   GLY B 344     7804   8774   5947   1346    116   1201       O  
ATOM   3031  N   GLN B 345      35.899 -29.737  48.280  1.00 53.54           N  
ANISOU 3031  N   GLN B 345     6957   8131   5256   1420    -24   1174       N  
ATOM   3032  CA  GLN B 345      36.570 -29.920  49.563  1.00 60.75           C  
ANISOU 3032  CA  GLN B 345     7816   9314   5953   1439    -87   1272       C  
ATOM   3033  C   GLN B 345      36.578 -28.618  50.348  1.00 58.25           C  
ANISOU 3033  C   GLN B 345     7493   9188   5452   1296    -84   1102       C  
ATOM   3034  O   GLN B 345      36.627 -28.623  51.575  1.00 57.89           O  
ANISOU 3034  O   GLN B 345     7435   9356   5203   1276   -101   1156       O  
ATOM   3035  CB  GLN B 345      38.004 -30.414  49.364  1.00 64.86           C  
ANISOU 3035  CB  GLN B 345     8227   9961   6455   1539   -193   1349       C  
ATOM   3036  CG  GLN B 345      38.102 -31.819  48.803  1.00 72.57           C  
ANISOU 3036  CG  GLN B 345     9215  10767   7590   1706   -197   1533       C  
ATOM   3037  CD  GLN B 345      39.529 -32.219  48.486  1.00 82.65           C  
ANISOU 3037  CD  GLN B 345    10370  12166   8866   1823   -292   1585       C  
ATOM   3038  OE1 GLN B 345      39.780 -32.961  47.536  1.00 88.33           O  
ANISOU 3038  OE1 GLN B 345    11087  12717   9758   1937   -288   1627       O  
ATOM   3039  NE2 GLN B 345      40.475 -31.722  49.277  1.00 83.81           N  
ANISOU 3039  NE2 GLN B 345    10408  12623   8814   1795   -377   1571       N  
ATOM   3040  N   GLY B 346      36.528 -27.500  49.632  1.00 52.44           N  
ANISOU 3040  N   GLY B 346     6772   8368   4783   1196    -59    895       N  
ATOM   3041  CA  GLY B 346      36.539 -26.199  50.270  1.00 49.59           C  
ANISOU 3041  CA  GLY B 346     6423   8143   4274   1055    -47    707       C  
ATOM   3042  C   GLY B 346      35.325 -25.365  49.915  1.00 50.57           C  
ANISOU 3042  C   GLY B 346     6648   8071   4494    987     62    563       C  
ATOM   3043  O   GLY B 346      34.513 -25.747  49.074  1.00 50.11           O  
ANISOU 3043  O   GLY B 346     6635   7786   4619   1041    118    604       O  
ATOM   3044  N   PHE B 347      35.208 -24.216  50.569  1.00 52.13           N  
ANISOU 3044  N   PHE B 347     6879   8364   4565    872     91    388       N  
ATOM   3045  CA  PHE B 347      34.124 -23.279  50.311  1.00 51.68           C  
ANISOU 3045  CA  PHE B 347     6915   8134   4588    819    196    235       C  
ATOM   3046  C   PHE B 347      34.636 -21.872  50.579  1.00 50.22           C  
ANISOU 3046  C   PHE B 347     6753   8018   4309    681    191      8       C  
ATOM   3047  O   PHE B 347      34.981 -21.533  51.709  1.00 48.15           O  
ANISOU 3047  O   PHE B 347     6480   7977   3838    610    172    -59       O  
ATOM   3048  CB  PHE B 347      32.924 -23.595  51.207  1.00 56.74           C  
ANISOU 3048  CB  PHE B 347     7601   8801   5157    850    285    289       C  
ATOM   3049  CG  PHE B 347      31.785 -22.621  51.072  1.00 55.98           C  
ANISOU 3049  CG  PHE B 347     7584   8559   5127    816    398    130       C  
ATOM   3050  CD1 PHE B 347      30.897 -22.714  50.013  1.00 54.66           C  
ANISOU 3050  CD1 PHE B 347     7443   8149   5174    872    453    150       C  
ATOM   3051  CD2 PHE B 347      31.593 -21.624  52.014  1.00 56.87           C  
ANISOU 3051  CD2 PHE B 347     7740   8784   5083    737    449    -42       C  
ATOM   3052  CE1 PHE B 347      29.845 -21.823  49.890  1.00 52.03           C  
ANISOU 3052  CE1 PHE B 347     7169   7694   4904    864    554     17       C  
ATOM   3053  CE2 PHE B 347      30.544 -20.730  51.897  1.00 56.42           C  
ANISOU 3053  CE2 PHE B 347     7755   8584   5097    731    560   -189       C  
ATOM   3054  CZ  PHE B 347      29.669 -20.831  50.834  1.00 54.98           C  
ANISOU 3054  CZ  PHE B 347     7590   8167   5135    802    610   -150       C  
ATOM   3055  N   MET B 348      34.710 -21.057  49.534  1.00 51.05           N  
ANISOU 3055  N   MET B 348     6894   7938   4564    635    207   -110       N  
ATOM   3056  CA  MET B 348      35.218 -19.701  49.684  1.00 54.52           C  
ANISOU 3056  CA  MET B 348     7372   8401   4942    490    208   -325       C  
ATOM   3057  C   MET B 348      34.056 -18.725  49.744  1.00 52.20           C  
ANISOU 3057  C   MET B 348     7198   7931   4704    471    326   -473       C  
ATOM   3058  O   MET B 348      33.265 -18.634  48.807  1.00 51.69           O  
ANISOU 3058  O   MET B 348     7180   7635   4827    537    382   -453       O  
ATOM   3059  CB  MET B 348      36.161 -19.341  48.534  1.00 56.52           C  
ANISOU 3059  CB  MET B 348     7592   8573   5312    435    152   -357       C  
ATOM   3060  CG  MET B 348      36.953 -18.062  48.762  1.00 58.27           C  
ANISOU 3060  CG  MET B 348     7836   8853   5451    255    135   -560       C  
ATOM   3061  SD  MET B 348      38.264 -17.831  47.547  1.00 69.69           S  
ANISOU 3061  SD  MET B 348     9203  10281   6993    175     60   -561       S  
ATOM   3062  CE  MET B 348      39.366 -19.177  47.974  1.00 67.97           C  
ANISOU 3062  CE  MET B 348     8804  10370   6650    252    -63   -384       C  
ATOM   3063  N   THR B 349      33.956 -18.001  50.854  1.00 53.18           N  
ANISOU 3063  N   THR B 349     7370   8176   4662    389    362   -625       N  
ATOM   3064  CA  THR B 349      32.833 -17.099  51.071  1.00 54.29           C  
ANISOU 3064  CA  THR B 349     7621   8168   4839    393    485   -774       C  
ATOM   3065  C   THR B 349      32.792 -15.984  50.035  1.00 53.46           C  
ANISOU 3065  C   THR B 349     7601   7799   4913    349    521   -903       C  
ATOM   3066  O   THR B 349      33.827 -15.542  49.536  1.00 47.65           O  
ANISOU 3066  O   THR B 349     6855   7052   4199    244    456   -954       O  
ATOM   3067  CB  THR B 349      32.857 -16.481  52.485  1.00 53.72           C  
ANISOU 3067  CB  THR B 349     7588   8289   4535    302    520   -943       C  
ATOM   3068  OG1 THR B 349      33.973 -15.591  52.606  1.00 54.60           O  
ANISOU 3068  OG1 THR B 349     7715   8463   4568    137    461  -1112       O  
ATOM   3069  CG2 THR B 349      32.968 -17.570  53.535  1.00 54.79           C  
ANISOU 3069  CG2 THR B 349     7638   8709   4469    340    477   -796       C  
ATOM   3070  N   ARG B 350      31.580 -15.545  49.716  1.00 56.88           N  
ANISOU 3070  N   ARG B 350     8110   8028   5473    432    627   -942       N  
ATOM   3071  CA  ARG B 350      31.367 -14.433  48.804  1.00 54.91           C  
ANISOU 3071  CA  ARG B 350     7957   7513   5393    414    674  -1051       C  
ATOM   3072  C   ARG B 350      32.021 -13.174  49.354  1.00 56.89           C  
ANISOU 3072  C   ARG B 350     8299   7762   5554    257    688  -1282       C  
ATOM   3073  O   ARG B 350      32.570 -12.368  48.603  1.00 53.18           O  
ANISOU 3073  O   ARG B 350     7887   7135   5185    169    674  -1352       O  
ATOM   3074  CB  ARG B 350      29.868 -14.201  48.627  1.00 53.86           C  
ANISOU 3074  CB  ARG B 350     7877   7210   5378    552    789  -1056       C  
ATOM   3075  CG  ARG B 350      29.497 -13.085  47.674  1.00 54.79           C  
ANISOU 3075  CG  ARG B 350     8096   7042   5679    570    843  -1139       C  
ATOM   3076  CD  ARG B 350      27.993 -13.065  47.470  1.00 55.48           C  
ANISOU 3076  CD  ARG B 350     8195   7006   5879    735    942  -1105       C  
ATOM   3077  NE  ARG B 350      27.579 -12.125  46.435  1.00 57.67           N  
ANISOU 3077  NE  ARG B 350     8555   7012   6344    786    982  -1137       N  
ATOM   3078  CZ  ARG B 350      26.333 -12.017  45.987  1.00 58.67           C  
ANISOU 3078  CZ  ARG B 350     8680   7014   6598    939   1053  -1093       C  
ATOM   3079  NH1 ARG B 350      25.379 -12.798  46.480  1.00 57.18           N  
ANISOU 3079  NH1 ARG B 350     8404   6949   6372   1038   1096  -1024       N  
ATOM   3080  NH2 ARG B 350      26.040 -11.132  45.044  1.00 57.61           N  
ANISOU 3080  NH2 ARG B 350     8623   6641   6626    990   1079  -1108       N  
ATOM   3081  N   GLU B 351      31.959 -13.019  50.674  1.00 59.34           N  
ANISOU 3081  N   GLU B 351     8625   8254   5669    210    718  -1402       N  
ATOM   3082  CA  GLU B 351      32.499 -11.840  51.343  1.00 62.57           C  
ANISOU 3082  CA  GLU B 351     9127   8675   5970     48    740  -1652       C  
ATOM   3083  C   GLU B 351      34.022 -11.766  51.294  1.00 63.69           C  
ANISOU 3083  C   GLU B 351     9212   8963   6026   -133    619  -1679       C  
ATOM   3084  O   GLU B 351      34.587 -10.684  51.140  1.00 65.54           O  
ANISOU 3084  O   GLU B 351     9530   9087   6284   -286    626  -1853       O  
ATOM   3085  CB  GLU B 351      32.009 -11.774  52.791  1.00 67.62           C  
ANISOU 3085  CB  GLU B 351     9788   9505   6398     47    804  -1777       C  
ATOM   3086  CG  GLU B 351      30.594 -11.245  52.928  1.00 75.09           C  
ANISOU 3086  CG  GLU B 351    10829  10273   7429    177    956  -1864       C  
ATOM   3087  CD  GLU B 351      30.451  -9.837  52.380  1.00 84.62           C  
ANISOU 3087  CD  GLU B 351    12191  11168   8795    141   1030  -2055       C  
ATOM   3088  OE1 GLU B 351      31.316  -8.990  52.688  1.00 89.24           O  
ANISOU 3088  OE1 GLU B 351    12850  11749   9308    -37   1009  -2244       O  
ATOM   3089  OE2 GLU B 351      29.475  -9.577  51.643  1.00 85.89           O  
ANISOU 3089  OE2 GLU B 351    12397  11086   9152    287   1109  -2011       O  
ATOM   3090  N   PHE B 352      34.687 -12.908  51.433  1.00 63.25           N  
ANISOU 3090  N   PHE B 352     9010   9152   5872   -117    512  -1506       N  
ATOM   3091  CA  PHE B 352      36.144 -12.929  51.370  1.00 64.75           C  
ANISOU 3091  CA  PHE B 352     9110   9514   5976   -269    392  -1513       C  
ATOM   3092  C   PHE B 352      36.635 -12.559  49.978  1.00 63.92           C  
ANISOU 3092  C   PHE B 352     9014   9197   6074   -311    371  -1478       C  
ATOM   3093  O   PHE B 352      37.557 -11.760  49.830  1.00 67.38           O  
ANISOU 3093  O   PHE B 352     9467   9637   6496   -493    338  -1605       O  
ATOM   3094  CB  PHE B 352      36.705 -14.293  51.774  1.00 63.97           C  
ANISOU 3094  CB  PHE B 352     8848   9715   5745   -203    285  -1312       C  
ATOM   3095  CG  PHE B 352      38.184 -14.423  51.544  1.00 64.13           C  
ANISOU 3095  CG  PHE B 352     8745   9917   5703   -323    159  -1288       C  
ATOM   3096  CD1 PHE B 352      39.076 -13.602  52.215  1.00 67.74           C  
ANISOU 3096  CD1 PHE B 352     9197  10543   5999   -532    115  -1482       C  
ATOM   3097  CD2 PHE B 352      38.683 -15.355  50.650  1.00 63.16           C  
ANISOU 3097  CD2 PHE B 352     8508   9806   5683   -230     89  -1084       C  
ATOM   3098  CE1 PHE B 352      40.437 -13.712  52.004  1.00 68.23           C  
ANISOU 3098  CE1 PHE B 352     9122  10799   6001   -648     -1  -1460       C  
ATOM   3099  CE2 PHE B 352      40.044 -15.470  50.435  1.00 63.71           C  
ANISOU 3099  CE2 PHE B 352     8448  10063   5698   -328    -20  -1064       C  
ATOM   3100  CZ  PHE B 352      40.921 -14.648  51.113  1.00 66.00           C  
ANISOU 3100  CZ  PHE B 352     8715  10537   5825   -538    -67  -1246       C  
ATOM   3101  N   LEU B 353      36.019 -13.150  48.960  1.00 63.19           N  
ANISOU 3101  N   LEU B 353     8910   8936   6164   -153    391  -1305       N  
ATOM   3102  CA  LEU B 353      36.351 -12.832  47.577  1.00 62.90           C  
ANISOU 3102  CA  LEU B 353     8886   8698   6314   -175    381  -1257       C  
ATOM   3103  C   LEU B 353      36.105 -11.355  47.295  1.00 67.49           C  
ANISOU 3103  C   LEU B 353     9631   9021   6992   -278    464  -1440       C  
ATOM   3104  O   LEU B 353      36.907 -10.692  46.637  1.00 68.60           O  
ANISOU 3104  O   LEU B 353     9792   9081   7192   -418    442  -1487       O  
ATOM   3105  CB  LEU B 353      35.527 -13.692  46.618  1.00 57.32           C  
ANISOU 3105  CB  LEU B 353     8153   7857   5770     19    399  -1062       C  
ATOM   3106  CG  LEU B 353      35.973 -15.148  46.480  1.00 53.81           C  
ANISOU 3106  CG  LEU B 353     7558   7599   5290    111    312   -864       C  
ATOM   3107  CD1 LEU B 353      34.848 -16.018  45.926  1.00 53.46           C  
ANISOU 3107  CD1 LEU B 353     7510   7430   5372    297    351   -709       C  
ATOM   3108  CD2 LEU B 353      37.220 -15.236  45.608  1.00 52.71           C  
ANISOU 3108  CD2 LEU B 353     7331   7509   5186     32    232   -818       C  
ATOM   3109  N   LYS B 354      34.985 -10.851  47.801  1.00 67.12           N  
ANISOU 3109  N   LYS B 354     9700   8840   6962   -203    567  -1538       N  
ATOM   3110  CA  LYS B 354      34.596  -9.462  47.596  1.00 74.48           C  
ANISOU 3110  CA  LYS B 354    10806   9493   8001   -261    662  -1708       C  
ATOM   3111  C   LYS B 354      35.560  -8.506  48.300  1.00 77.36           C  
ANISOU 3111  C   LYS B 354    11231   9921   8243   -502    648  -1933       C  
ATOM   3112  O   LYS B 354      35.681  -7.342  47.920  1.00 80.43           O  
ANISOU 3112  O   LYS B 354    11758  10071   8733   -611    701  -2063       O  
ATOM   3113  CB  LYS B 354      33.171  -9.246  48.110  1.00 79.60           C  
ANISOU 3113  CB  LYS B 354    11541  10025   8677   -102    778  -1766       C  
ATOM   3114  CG  LYS B 354      32.443  -8.062  47.500  1.00 82.29           C  
ANISOU 3114  CG  LYS B 354    12048  10015   9204    -58    883  -1854       C  
ATOM   3115  CD  LYS B 354      31.020  -7.977  48.034  1.00 84.53           C  
ANISOU 3115  CD  LYS B 354    12381  10229   9508    127    996  -1898       C  
ATOM   3116  CE  LYS B 354      30.237  -6.861  47.363  1.00 88.29           C  
ANISOU 3116  CE  LYS B 354    13010  10353  10184    214   1098  -1958       C  
ATOM   3117  NZ  LYS B 354      28.887  -6.700  47.970  1.00 91.99           N  
ANISOU 3117  NZ  LYS B 354    13514  10775  10663    396   1217  -2025       N  
ATOM   3118  N   SER B 355      36.250  -9.006  49.321  1.00 75.47           N  
ANISOU 3118  N   SER B 355    10887  10004   7783   -590    575  -1974       N  
ATOM   3119  CA  SER B 355      37.139  -8.174  50.127  1.00 74.35           C  
ANISOU 3119  CA  SER B 355    10784   9976   7490   -831    553  -2202       C  
ATOM   3120  C   SER B 355      38.525  -8.024  49.508  1.00 74.80           C  
ANISOU 3120  C   SER B 355    10758  10108   7554  -1025    457  -2183       C  
ATOM   3121  O   SER B 355      39.375  -7.314  50.044  1.00 76.56           O  
ANISOU 3121  O   SER B 355    10998  10428   7663  -1258    428  -2369       O  
ATOM   3122  CB  SER B 355      37.267  -8.740  51.542  1.00 76.24           C  
ANISOU 3122  CB  SER B 355    10939  10564   7463   -845    511  -2257       C  
ATOM   3123  OG  SER B 355      38.162  -9.838  51.574  1.00 75.34           O  
ANISOU 3123  OG  SER B 355    10629  10759   7239   -847    378  -2083       O  
ATOM   3124  N   LEU B 356      38.753  -8.692  48.383  1.00 75.06           N  
ANISOU 3124  N   LEU B 356    10696  10109   7714   -939    410  -1967       N  
ATOM   3125  CA  LEU B 356      40.050  -8.638  47.720  1.00 78.38           C  
ANISOU 3125  CA  LEU B 356    11016  10623   8143  -1104    326  -1929       C  
ATOM   3126  C   LEU B 356      40.314  -7.260  47.120  1.00 82.13           C  
ANISOU 3126  C   LEU B 356    11642  10819   8743  -1295    388  -2070       C  
ATOM   3127  O   LEU B 356      39.390  -6.578  46.675  1.00 81.40           O  
ANISOU 3127  O   LEU B 356    11722  10395   8810  -1219    492  -2098       O  
ATOM   3128  CB  LEU B 356      40.150  -9.719  46.642  1.00 76.49           C  
ANISOU 3128  CB  LEU B 356    10644  10411   8007   -945    276  -1672       C  
ATOM   3129  CG  LEU B 356      40.049 -11.164  47.136  1.00 74.54           C  
ANISOU 3129  CG  LEU B 356    10244  10425   7652   -768    207  -1510       C  
ATOM   3130  CD1 LEU B 356      40.237 -12.142  45.986  1.00 71.19           C  
ANISOU 3130  CD1 LEU B 356     9707   9995   7345   -631    165  -1287       C  
ATOM   3131  CD2 LEU B 356      41.067 -11.425  48.233  1.00 75.92           C  
ANISOU 3131  CD2 LEU B 356    10288  10967   7592   -892    110  -1574       C  
ATOM   3132  N   ARG B 357      41.581  -6.856  47.116  1.00 86.09           N  
ANISOU 3132  N   ARG B 357    12075  11462   9173  -1544    325  -2151       N  
ATOM   3133  CA  ARG B 357      41.972  -5.550  46.596  1.00 89.57           C  
ANISOU 3133  CA  ARG B 357    12656  11653   9722  -1768    380  -2284       C  
ATOM   3134  C   ARG B 357      41.667  -5.425  45.109  1.00 90.17           C  
ANISOU 3134  C   ARG B 357    12789  11447  10024  -1679    428  -2112       C  
ATOM   3135  O   ARG B 357      41.825  -6.383  44.351  1.00 86.55           O  
ANISOU 3135  O   ARG B 357    12187  11099   9600  -1547    375  -1903       O  
ATOM   3136  CB  ARG B 357      43.461  -5.298  46.845  1.00 89.95           C  
ANISOU 3136  CB  ARG B 357    12577  11962   9637  -2063    292  -2380       C  
ATOM   3137  N   LYS B 358      41.231  -4.238  44.699  1.00 93.77           N  
ANISOU 3137  N   LYS B 358    13460  11539  10629  -1748    529  -2202       N  
ATOM   3138  CA  LYS B 358      40.900  -3.976  43.304  1.00 92.10           C  
ANISOU 3138  CA  LYS B 358    13324  11047  10623  -1672    579  -2040       C  
ATOM   3139  C   LYS B 358      42.069  -4.322  42.391  1.00 91.44           C  
ANISOU 3139  C   LYS B 358    13081  11126  10537  -1801    507  -1908       C  
ATOM   3140  O   LYS B 358      43.229  -4.166  42.773  1.00 91.90           O  
ANISOU 3140  O   LYS B 358    13038  11401  10477  -2041    448  -2003       O  
ATOM   3141  CB  LYS B 358      40.505  -2.509  43.114  1.00 92.27           C  
ANISOU 3141  CB  LYS B 358    13606  10665  10787  -1777    692  -2172       C  
ATOM   3142  N   PRO B 359      41.764  -4.798  41.175  1.00 90.08           N  
ANISOU 3142  N   PRO B 359    12874  10868  10486  -1644    511  -1693       N  
ATOM   3143  CA  PRO B 359      40.403  -5.047  40.696  1.00 90.30           C  
ANISOU 3143  CA  PRO B 359    12991  10677  10640  -1365    567  -1575       C  
ATOM   3144  C   PRO B 359      39.960  -6.486  40.954  1.00 87.92           C  
ANISOU 3144  C   PRO B 359    12530  10607  10268  -1129    507  -1456       C  
ATOM   3145  O   PRO B 359      38.980  -6.941  40.363  1.00 85.45           O  
ANISOU 3145  O   PRO B 359    12237  10177  10054   -907    533  -1323       O  
ATOM   3146  CB  PRO B 359      40.560  -4.831  39.196  1.00 89.69           C  
ANISOU 3146  CB  PRO B 359    12934  10444  10699  -1372    586  -1407       C  
ATOM   3147  CG  PRO B 359      41.880  -5.480  38.942  1.00 87.09           C  
ANISOU 3147  CG  PRO B 359    12393  10431  10266  -1506    500  -1353       C  
ATOM   3148  CD  PRO B 359      42.735  -4.927  40.073  1.00 89.05           C  
ANISOU 3148  CD  PRO B 359    12631  10820  10386  -1758    476  -1565       C  
ATOM   3149  N   PHE B 360      40.675  -7.188  41.827  1.00 87.09           N  
ANISOU 3149  N   PHE B 360    12268  10828   9994  -1181    427  -1500       N  
ATOM   3150  CA  PHE B 360      40.425  -8.609  42.059  1.00 80.49           C  
ANISOU 3150  CA  PHE B 360    11276  10217   9090   -976    365  -1370       C  
ATOM   3151  C   PHE B 360      39.209  -8.881  42.938  1.00 79.48           C  
ANISOU 3151  C   PHE B 360    11216  10045   8937   -800    407  -1405       C  
ATOM   3152  O   PHE B 360      38.658  -9.979  42.922  1.00 81.11           O  
ANISOU 3152  O   PHE B 360    11339  10339   9140   -603    384  -1271       O  
ATOM   3153  CB  PHE B 360      41.665  -9.281  42.655  1.00 78.18           C  
ANISOU 3153  CB  PHE B 360    10784  10296   8625  -1080    261  -1379       C  
ATOM   3154  CG  PHE B 360      42.801  -9.421  41.683  1.00 77.29           C  
ANISOU 3154  CG  PHE B 360    10542  10291   8533  -1186    214  -1293       C  
ATOM   3155  CD1 PHE B 360      43.778  -8.445  41.593  1.00 78.96           C  
ANISOU 3155  CD1 PHE B 360    10763  10515   8722  -1460    214  -1407       C  
ATOM   3156  CD2 PHE B 360      42.887 -10.527  40.854  1.00 75.80           C  
ANISOU 3156  CD2 PHE B 360    10222  10192   8387  -1019    176  -1107       C  
ATOM   3157  CE1 PHE B 360      44.823  -8.572  40.698  1.00 78.02           C  
ANISOU 3157  CE1 PHE B 360    10510  10517   8617  -1564    180  -1326       C  
ATOM   3158  CE2 PHE B 360      43.928 -10.658  39.957  1.00 75.87           C  
ANISOU 3158  CE2 PHE B 360    10105  10315   8408  -1107    144  -1037       C  
ATOM   3159  CZ  PHE B 360      44.898  -9.680  39.879  1.00 77.02           C  
ANISOU 3159  CZ  PHE B 360    10246  10493   8524  -1379    147  -1142       C  
ATOM   3160  N   GLY B 361      38.788  -7.884  43.706  1.00 78.70           N  
ANISOU 3160  N   GLY B 361    11271   9810   8823   -875    476  -1589       N  
ATOM   3161  CA  GLY B 361      37.658  -8.063  44.596  1.00 78.67           C  
ANISOU 3161  CA  GLY B 361    11326   9785   8781   -719    528  -1640       C  
ATOM   3162  C   GLY B 361      36.328  -8.006  43.871  1.00 77.76           C  
ANISOU 3162  C   GLY B 361    11304   9401   8841   -508    608  -1543       C  
ATOM   3163  O   GLY B 361      35.272  -8.099  44.496  1.00 77.55           O  
ANISOU 3163  O   GLY B 361    11325   9337   8805   -365    667  -1578       O  
ATOM   3164  N   ASP B 362      36.375  -7.868  42.550  1.00 80.26           N  
ANISOU 3164  N   ASP B 362    11636   9554   9305   -486    609  -1417       N  
ATOM   3165  CA  ASP B 362      35.159  -7.638  41.780  1.00 84.65           C  
ANISOU 3165  CA  ASP B 362    12285   9850  10027   -303    680  -1329       C  
ATOM   3166  C   ASP B 362      35.056  -8.503  40.522  1.00 81.35           C  
ANISOU 3166  C   ASP B 362    11766   9450   9695   -184    633  -1110       C  
ATOM   3167  O   ASP B 362      34.444  -8.093  39.536  1.00 84.39           O  
ANISOU 3167  O   ASP B 362    12225   9619  10219   -101    672  -1027       O  
ATOM   3168  CB  ASP B 362      35.060  -6.156  41.403  1.00 92.32           C  
ANISOU 3168  CB  ASP B 362    13451  10506  11118   -394    760  -1427       C  
ATOM   3169  CG  ASP B 362      33.627  -5.690  41.222  1.00 99.19           C  
ANISOU 3169  CG  ASP B 362    14443  11121  12122   -189    853  -1413       C  
ATOM   3170  OD1 ASP B 362      32.818  -6.437  40.631  1.00 99.32           O  
ANISOU 3170  OD1 ASP B 362    14385  11151  12199      7    842  -1253       O  
ATOM   3171  OD2 ASP B 362      33.313  -4.567  41.671  1.00103.28           O  
ANISOU 3171  OD2 ASP B 362    15129  11426  12686   -224    939  -1569       O  
ATOM   3172  N   PHE B 363      35.645  -9.695  40.545  1.00 75.60           N  
ANISOU 3172  N   PHE B 363    10869   8977   8877   -170    549  -1018       N  
ATOM   3173  CA  PHE B 363      35.544 -10.581  39.388  1.00 70.64           C  
ANISOU 3173  CA  PHE B 363    10148   8369   8322    -57    509   -834       C  
ATOM   3174  C   PHE B 363      34.514 -11.694  39.585  1.00 61.64           C  
ANISOU 3174  C   PHE B 363     8943   7291   7188    148    506   -739       C  
ATOM   3175  O   PHE B 363      33.899 -12.152  38.624  1.00 58.90           O  
ANISOU 3175  O   PHE B 363     8573   6869   6936    270    505   -615       O  
ATOM   3176  CB  PHE B 363      36.916 -11.139  38.970  1.00 76.43           C  
ANISOU 3176  CB  PHE B 363    10746   9306   8990   -168    429   -780       C  
ATOM   3177  CG  PHE B 363      37.426 -12.255  39.843  1.00 83.87           C  
ANISOU 3177  CG  PHE B 363    11542  10529   9796   -142    360   -766       C  
ATOM   3178  CD1 PHE B 363      37.314 -13.578  39.439  1.00 85.60           C  
ANISOU 3178  CD1 PHE B 363    11644  10856  10025      4    315   -623       C  
ATOM   3179  CD2 PHE B 363      38.041 -11.983  41.054  1.00 87.11           C  
ANISOU 3179  CD2 PHE B 363    11935  11095  10066   -267    338   -895       C  
ATOM   3180  CE1 PHE B 363      37.793 -14.607  40.236  1.00 86.44           C  
ANISOU 3180  CE1 PHE B 363    11627  11202  10015     41    253   -591       C  
ATOM   3181  CE2 PHE B 363      38.521 -13.007  41.855  1.00 87.19           C  
ANISOU 3181  CE2 PHE B 363    11809  11376   9943   -231    268   -860       C  
ATOM   3182  CZ  PHE B 363      38.396 -14.321  41.446  1.00 86.63           C  
ANISOU 3182  CZ  PHE B 363    11630  11392   9895    -70    227   -699       C  
ATOM   3183  N   MET B 364      34.313 -12.108  40.832  1.00 58.43           N  
ANISOU 3183  N   MET B 364     8505   7023   6671    172    506   -800       N  
ATOM   3184  CA  MET B 364      33.359 -13.174  41.132  1.00 59.04           C  
ANISOU 3184  CA  MET B 364     8520   7166   6745    341    510   -709       C  
ATOM   3185  C   MET B 364      31.957 -12.642  41.420  1.00 59.43           C  
ANISOU 3185  C   MET B 364     8664   7057   6861    453    602   -755       C  
ATOM   3186  O   MET B 364      30.968 -13.353  41.239  1.00 57.82           O  
ANISOU 3186  O   MET B 364     8417   6846   6707    597    618   -660       O  
ATOM   3187  CB  MET B 364      33.842 -14.024  42.312  1.00 63.04           C  
ANISOU 3187  CB  MET B 364     8934   7928   7090    323    464   -716       C  
ATOM   3188  CG  MET B 364      34.927 -15.033  41.973  1.00 65.59           C  
ANISOU 3188  CG  MET B 364     9123   8432   7367    304    370   -610       C  
ATOM   3189  SD  MET B 364      34.350 -16.368  40.905  1.00 68.16           S  
ANISOU 3189  SD  MET B 364     9373   8718   7808    474    349   -418       S  
ATOM   3190  CE  MET B 364      34.585 -15.646  39.283  1.00 87.55           C  
ANISOU 3190  CE  MET B 364    11871  10997  10399    432    355   -402       C  
ATOM   3191  N   GLU B 365      31.876 -11.395  41.871  1.00 58.88           N  
ANISOU 3191  N   GLU B 365     8719   6860   6793    384    665   -907       N  
ATOM   3192  CA  GLU B 365      30.595 -10.807  42.250  1.00 61.84           C  
ANISOU 3192  CA  GLU B 365     9182   7091   7224    501    763   -973       C  
ATOM   3193  C   GLU B 365      29.543 -10.908  41.142  1.00 61.36           C  
ANISOU 3193  C   GLU B 365     9118   6875   7322    662    786   -843       C  
ATOM   3194  O   GLU B 365      28.421 -11.353  41.391  1.00 62.47           O  
ANISOU 3194  O   GLU B 365     9218   7036   7483    805    826   -803       O  
ATOM   3195  CB  GLU B 365      30.772  -9.356  42.712  1.00 65.21           C  
ANISOU 3195  CB  GLU B 365     9765   7358   7655    401    831  -1164       C  
ATOM   3196  CG  GLU B 365      29.546  -8.765  43.390  1.00 67.49           C  
ANISOU 3196  CG  GLU B 365    10139   7534   7971    526    942  -1269       C  
ATOM   3197  CD  GLU B 365      29.110  -9.551  44.615  1.00 69.74           C  
ANISOU 3197  CD  GLU B 365    10342   8047   8109    577    959  -1302       C  
ATOM   3198  OE1 GLU B 365      29.814 -10.506  45.006  1.00 71.51           O  
ANISOU 3198  OE1 GLU B 365    10458   8506   8207    509    880  -1244       O  
ATOM   3199  OE2 GLU B 365      28.055  -9.210  45.189  1.00 72.31           O  
ANISOU 3199  OE2 GLU B 365    10710   8321   8444    691   1055  -1379       O  
ATOM   3200  N   PRO B 366      29.900 -10.500  39.913  1.00 59.88           N  
ANISOU 3200  N   PRO B 366     8964   6551   7236    633    760   -771       N  
ATOM   3201  CA  PRO B 366      28.956 -10.618  38.796  1.00 57.50           C  
ANISOU 3201  CA  PRO B 366     8648   6132   7066    780    766   -638       C  
ATOM   3202  C   PRO B 366      28.503 -12.060  38.581  1.00 56.00           C  
ANISOU 3202  C   PRO B 366     8313   6104   6861    874    718   -510       C  
ATOM   3203  O   PRO B 366      27.372 -12.294  38.158  1.00 58.45           O  
ANISOU 3203  O   PRO B 366     8590   6370   7248   1014    739   -436       O  
ATOM   3204  CB  PRO B 366      29.777 -10.144  37.595  1.00 57.30           C  
ANISOU 3204  CB  PRO B 366     8663   6007   7101    689    727   -574       C  
ATOM   3205  CG  PRO B 366      30.815  -9.253  38.177  1.00 60.99           C  
ANISOU 3205  CG  PRO B 366     9221   6439   7512    506    742   -713       C  
ATOM   3206  CD  PRO B 366      31.159  -9.852  39.503  1.00 61.62           C  
ANISOU 3206  CD  PRO B 366     9235   6729   7448    455    727   -810       C  
ATOM   3207  N   LYS B 367      29.384 -13.014  38.865  1.00 49.50           N  
ANISOU 3207  N   LYS B 367     7401   5465   5941    798    652   -484       N  
ATOM   3208  CA  LYS B 367      29.046 -14.426  38.731  1.00 48.89           C  
ANISOU 3208  CA  LYS B 367     7203   5521   5852    875    610   -369       C  
ATOM   3209  C   LYS B 367      28.038 -14.847  39.799  1.00 45.34           C  
ANISOU 3209  C   LYS B 367     6726   5142   5361    958    663   -389       C  
ATOM   3210  O   LYS B 367      27.109 -15.606  39.523  1.00 47.56           O  
ANISOU 3210  O   LYS B 367     6940   5440   5691   1057    668   -300       O  
ATOM   3211  CB  LYS B 367      30.304 -15.290  38.826  1.00 49.90           C  
ANISOU 3211  CB  LYS B 367     7253   5814   5892    787    533   -335       C  
ATOM   3212  CG  LYS B 367      31.487 -14.754  38.035  1.00 51.88           C  
ANISOU 3212  CG  LYS B 367     7522   6038   6151    673    493   -345       C  
ATOM   3213  CD  LYS B 367      31.200 -14.714  36.550  1.00 57.97           C  
ANISOU 3213  CD  LYS B 367     8295   6697   7032    721    482   -251       C  
ATOM   3214  CE  LYS B 367      32.461 -14.405  35.749  1.00 63.59           C  
ANISOU 3214  CE  LYS B 367     9002   7427   7734    601    443   -241       C  
ATOM   3215  NZ  LYS B 367      33.042 -13.076  36.079  1.00 65.71           N  
ANISOU 3215  NZ  LYS B 367     9370   7609   7986    467    476   -346       N  
ATOM   3216  N   PHE B 368      28.230 -14.351  41.018  1.00 40.48           N  
ANISOU 3216  N   PHE B 368     6157   4577   4645    906    704   -511       N  
ATOM   3217  CA  PHE B 368      27.312 -14.636  42.117  1.00 43.94           C  
ANISOU 3217  CA  PHE B 368     6574   5099   5022    975    768   -543       C  
ATOM   3218  C   PHE B 368      25.915 -14.114  41.811  1.00 48.28           C  
ANISOU 3218  C   PHE B 368     7146   5516   5683   1108    848   -547       C  
ATOM   3219  O   PHE B 368      24.918 -14.803  42.033  1.00 48.47           O  
ANISOU 3219  O   PHE B 368     7093   5607   5715   1198    879   -484       O  
ATOM   3220  CB  PHE B 368      27.819 -14.011  43.420  1.00 48.63           C  
ANISOU 3220  CB  PHE B 368     7228   5772   5476    885    802   -699       C  
ATOM   3221  CG  PHE B 368      28.862 -14.832  44.124  1.00 47.93           C  
ANISOU 3221  CG  PHE B 368     7075   5900   5238    792    730   -674       C  
ATOM   3222  CD1 PHE B 368      28.521 -16.026  44.738  1.00 46.77           C  
ANISOU 3222  CD1 PHE B 368     6840   5916   5016    843    720   -573       C  
ATOM   3223  CD2 PHE B 368      30.178 -14.404  44.185  1.00 46.00           C  
ANISOU 3223  CD2 PHE B 368     6851   5700   4926    652    672   -743       C  
ATOM   3224  CE1 PHE B 368      29.473 -16.783  45.391  1.00 46.81           C  
ANISOU 3224  CE1 PHE B 368     6786   6117   4884    779    651   -530       C  
ATOM   3225  CE2 PHE B 368      31.136 -15.156  44.840  1.00 48.48           C  
ANISOU 3225  CE2 PHE B 368     7087   6236   5098    583    599   -711       C  
ATOM   3226  CZ  PHE B 368      30.782 -16.347  45.443  1.00 47.96           C  
ANISOU 3226  CZ  PHE B 368     6940   6324   4960    657    587   -599       C  
ATOM   3227  N   GLU B 369      25.851 -12.889  41.301  1.00 50.16           N  
ANISOU 3227  N   GLU B 369     7485   5567   6008   1119    882   -614       N  
ATOM   3228  CA  GLU B 369      24.578 -12.259  40.981  1.00 56.02           C  
ANISOU 3228  CA  GLU B 369     8250   6174   6862   1266    956   -616       C  
ATOM   3229  C   GLU B 369      23.821 -13.087  39.955  1.00 48.45           C  
ANISOU 3229  C   GLU B 369     7182   5235   5993   1362    915   -454       C  
ATOM   3230  O   GLU B 369      22.612 -13.287  40.067  1.00 48.68           O  
ANISOU 3230  O   GLU B 369     7145   5289   6061   1482    964   -425       O  
ATOM   3231  CB  GLU B 369      24.801 -10.840  40.458  1.00 61.81           C  
ANISOU 3231  CB  GLU B 369     9124   6677   7685   1260    987   -687       C  
ATOM   3232  CG  GLU B 369      25.519  -9.929  41.440  1.00 68.47           C  
ANISOU 3232  CG  GLU B 369    10089   7478   8450   1146   1033   -872       C  
ATOM   3233  CD  GLU B 369      25.541  -8.482  40.987  1.00 74.92           C  
ANISOU 3233  CD  GLU B 369    11064   8026   9377   1153   1085   -946       C  
ATOM   3234  OE1 GLU B 369      25.772  -7.595  41.837  1.00 77.74           O  
ANISOU 3234  OE1 GLU B 369    11538   8305   9694   1093   1152  -1124       O  
ATOM   3235  OE2 GLU B 369      25.323  -8.230  39.782  1.00 76.21           O  
ANISOU 3235  OE2 GLU B 369    11240   8052   9663   1215   1061   -826       O  
ATOM   3236  N   PHE B 370      24.540 -13.572  38.951  1.00 46.05           N  
ANISOU 3236  N   PHE B 370     6851   4931   5714   1302    826   -358       N  
ATOM   3237  CA  PHE B 370      23.936 -14.427  37.945  1.00 43.08           C  
ANISOU 3237  CA  PHE B 370     6375   4587   5407   1368    778   -222       C  
ATOM   3238  C   PHE B 370      23.467 -15.743  38.552  1.00 42.05           C  
ANISOU 3238  C   PHE B 370     6133   4621   5223   1379    775   -172       C  
ATOM   3239  O   PHE B 370      22.356 -16.195  38.291  1.00 44.24           O  
ANISOU 3239  O   PHE B 370     6328   4928   5554   1463    791   -110       O  
ATOM   3240  CB  PHE B 370      24.915 -14.709  36.806  1.00 43.33           C  
ANISOU 3240  CB  PHE B 370     6406   4602   5455   1292    691   -149       C  
ATOM   3241  CG  PHE B 370      24.510 -15.867  35.952  1.00 46.25           C  
ANISOU 3241  CG  PHE B 370     6668   5045   5859   1327    634    -33       C  
ATOM   3242  CD1 PHE B 370      23.463 -15.746  35.055  1.00 46.48           C  
ANISOU 3242  CD1 PHE B 370     6657   5027   5975   1426    632     34       C  
ATOM   3243  CD2 PHE B 370      25.154 -17.087  36.064  1.00 41.15           C  
ANISOU 3243  CD2 PHE B 370     5960   4517   5158   1264    582      4       C  
ATOM   3244  CE1 PHE B 370      23.077 -16.814  34.276  1.00 47.46           C  
ANISOU 3244  CE1 PHE B 370     6683   5226   6122   1439    578    121       C  
ATOM   3245  CE2 PHE B 370      24.772 -18.160  35.286  1.00 42.95           C  
ANISOU 3245  CE2 PHE B 370     6105   4792   5424   1288    537     91       C  
ATOM   3246  CZ  PHE B 370      23.731 -18.024  34.393  1.00 42.49           C  
ANISOU 3246  CZ  PHE B 370     6009   4692   5444   1365    534    141       C  
ATOM   3247  N   ALA B 371      24.325 -16.354  39.361  1.00 42.42           N  
ANISOU 3247  N   ALA B 371     6175   4780   5163   1288    753   -193       N  
ATOM   3248  CA  ALA B 371      24.051 -17.670  39.927  1.00 37.14           C  
ANISOU 3248  CA  ALA B 371     5417   4254   4441   1285    745   -123       C  
ATOM   3249  C   ALA B 371      22.821 -17.679  40.829  1.00 44.14           C  
ANISOU 3249  C   ALA B 371     6264   5199   5307   1354    835   -145       C  
ATOM   3250  O   ALA B 371      21.998 -18.592  40.756  1.00 44.96           O  
ANISOU 3250  O   ALA B 371     6278   5364   5439   1387    842    -60       O  
ATOM   3251  CB  ALA B 371      25.265 -18.178  40.686  1.00 38.43           C  
ANISOU 3251  CB  ALA B 371     5590   4528   4485   1190    704   -133       C  
ATOM   3252  N   VAL B 372      22.705 -16.675  41.692  1.00 43.49           N  
ANISOU 3252  N   VAL B 372     6249   5102   5174   1368    909   -267       N  
ATOM   3253  CA  VAL B 372      21.549 -16.574  42.572  1.00 48.75           C  
ANISOU 3253  CA  VAL B 372     6876   5835   5812   1443   1010   -306       C  
ATOM   3254  C   VAL B 372      20.262 -16.593  41.753  1.00 48.38           C  
ANISOU 3254  C   VAL B 372     6748   5740   5893   1557   1034   -240       C  
ATOM   3255  O   VAL B 372      19.316 -17.305  42.084  1.00 53.33           O  
ANISOU 3255  O   VAL B 372     7273   6476   6515   1589   1074   -185       O  
ATOM   3256  CB  VAL B 372      21.601 -15.301  43.439  1.00 53.58           C  
ANISOU 3256  CB  VAL B 372     7587   6403   6366   1457   1093   -476       C  
ATOM   3257  CG1 VAL B 372      20.239 -15.024  44.060  1.00 54.85           C  
ANISOU 3257  CG1 VAL B 372     7700   6607   6533   1572   1210   -522       C  
ATOM   3258  CG2 VAL B 372      22.667 -15.438  44.513  1.00 52.25           C  
ANISOU 3258  CG2 VAL B 372     7467   6352   6034   1337   1077   -545       C  
ATOM   3259  N   LYS B 373      20.239 -15.817  40.677  1.00 48.58           N  
ANISOU 3259  N   LYS B 373     6814   5618   6028   1609   1006   -239       N  
ATOM   3260  CA  LYS B 373      19.075 -15.762  39.802  1.00 53.93           C  
ANISOU 3260  CA  LYS B 373     7407   6264   6820   1724   1012   -169       C  
ATOM   3261  C   LYS B 373      18.907 -17.064  39.026  1.00 53.40           C  
ANISOU 3261  C   LYS B 373     7232   6275   6783   1680    933    -39       C  
ATOM   3262  O   LYS B 373      17.807 -17.611  38.944  1.00 58.71           O  
ANISOU 3262  O   LYS B 373     7786   7031   7491   1727    956     16       O  
ATOM   3263  CB  LYS B 373      19.190 -14.582  38.837  1.00 57.89           C  
ANISOU 3263  CB  LYS B 373     7992   6586   7419   1791    995   -182       C  
ATOM   3264  N   PHE B 374      20.004 -17.563  38.465  1.00 44.29           N  
ANISOU 3264  N   PHE B 374     6116   5097   5614   1585    846      0       N  
ATOM   3265  CA  PHE B 374      19.966 -18.790  37.677  1.00 38.91           C  
ANISOU 3265  CA  PHE B 374     5355   4467   4964   1540    773    102       C  
ATOM   3266  C   PHE B 374      19.491 -19.965  38.524  1.00 38.90           C  
ANISOU 3266  C   PHE B 374     5275   4591   4916   1500    804    144       C  
ATOM   3267  O   PHE B 374      18.671 -20.770  38.080  1.00 38.28           O  
ANISOU 3267  O   PHE B 374     5098   4559   4888   1499    792    213       O  
ATOM   3268  CB  PHE B 374      21.340 -19.083  37.067  1.00 39.50           C  
ANISOU 3268  CB  PHE B 374     5489   4500   5019   1455    689    119       C  
ATOM   3269  CG  PHE B 374      21.325 -20.172  36.034  1.00 37.93           C  
ANISOU 3269  CG  PHE B 374     5226   4322   4865   1425    616    202       C  
ATOM   3270  CD1 PHE B 374      20.780 -19.947  34.780  1.00 38.05           C  
ANISOU 3270  CD1 PHE B 374     5204   4299   4954   1469    578    238       C  
ATOM   3271  CD2 PHE B 374      21.856 -21.420  36.313  1.00 37.91           C  
ANISOU 3271  CD2 PHE B 374     5203   4374   4826   1356    587    241       C  
ATOM   3272  CE1 PHE B 374      20.766 -20.947  33.820  1.00 36.18           C  
ANISOU 3272  CE1 PHE B 374     4912   4090   4746   1430    513    292       C  
ATOM   3273  CE2 PHE B 374      21.844 -22.425  35.358  1.00 36.41           C  
ANISOU 3273  CE2 PHE B 374     4968   4184   4684   1328    528    296       C  
ATOM   3274  CZ  PHE B 374      21.297 -22.187  34.110  1.00 34.05           C  
ANISOU 3274  CZ  PHE B 374     4632   3856   4449   1357    492    311       C  
ATOM   3275  N   ASN B 375      20.000 -20.047  39.749  1.00 39.23           N  
ANISOU 3275  N   ASN B 375     5359   4691   4855   1457    844    106       N  
ATOM   3276  CA  ASN B 375      19.656 -21.132  40.661  1.00 42.07           C  
ANISOU 3276  CA  ASN B 375     5661   5170   5152   1413    878    163       C  
ATOM   3277  C   ASN B 375      18.192 -21.117  41.091  1.00 45.58           C  
ANISOU 3277  C   ASN B 375     6010   5693   5615   1467    968    168       C  
ATOM   3278  O   ASN B 375      17.653 -22.144  41.501  1.00 46.61           O  
ANISOU 3278  O   ASN B 375     6067   5913   5729   1421    993    244       O  
ATOM   3279  CB  ASN B 375      20.570 -21.113  41.890  1.00 37.36           C  
ANISOU 3279  CB  ASN B 375     5134   4642   4420   1361    896    124       C  
ATOM   3280  CG  ASN B 375      21.993 -21.517  41.559  1.00 39.89           C  
ANISOU 3280  CG  ASN B 375     5508   4934   4714   1297    803    150       C  
ATOM   3281  OD1 ASN B 375      22.265 -22.022  40.470  1.00 38.87           O  
ANISOU 3281  OD1 ASN B 375     5364   4739   4666   1288    734    205       O  
ATOM   3282  ND2 ASN B 375      22.908 -21.300  42.497  1.00 39.59           N  
ANISOU 3282  ND2 ASN B 375     5524   4962   4554   1254    801    105       N  
ATOM   3283  N   ALA B 376      17.553 -19.953  40.999  1.00 45.81           N  
ANISOU 3283  N   ALA B 376     6036   5687   5682   1567   1021     92       N  
ATOM   3284  CA  ALA B 376      16.145 -19.831  41.364  1.00 50.36           C  
ANISOU 3284  CA  ALA B 376     6502   6353   6280   1641   1112     89       C  
ATOM   3285  C   ALA B 376      15.268 -20.620  40.398  1.00 52.36           C  
ANISOU 3285  C   ALA B 376     6626   6639   6630   1634   1070    186       C  
ATOM   3286  O   ALA B 376      14.118 -20.932  40.702  1.00 53.47           O  
ANISOU 3286  O   ALA B 376     6641   6893   6782   1653   1134    213       O  
ATOM   3287  CB  ALA B 376      15.722 -18.364  41.405  1.00 53.30           C  
ANISOU 3287  CB  ALA B 376     6908   6658   6685   1775   1176    -17       C  
ATOM   3288  N   LEU B 377      15.820 -20.937  39.231  1.00 49.02           N  
ANISOU 3288  N   LEU B 377     6227   6130   6269   1597    964    230       N  
ATOM   3289  CA  LEU B 377      15.125 -21.758  38.247  1.00 46.07           C  
ANISOU 3289  CA  LEU B 377     5742   5789   5973   1565    910    307       C  
ATOM   3290  C   LEU B 377      15.047 -23.204  38.723  1.00 42.68           C  
ANISOU 3290  C   LEU B 377     5270   5429   5516   1441    915    377       C  
ATOM   3291  O   LEU B 377      14.226 -23.982  38.242  1.00 47.03           O  
ANISOU 3291  O   LEU B 377     5712   6035   6122   1391    901    430       O  
ATOM   3292  CB  LEU B 377      15.834 -21.689  36.893  1.00 46.67           C  
ANISOU 3292  CB  LEU B 377     5870   5762   6102   1556    800    322       C  
ATOM   3293  CG  LEU B 377      15.458 -20.546  35.946  1.00 53.70           C  
ANISOU 3293  CG  LEU B 377     6751   6600   7054   1672    775    307       C  
ATOM   3294  CD1 LEU B 377      15.328 -19.223  36.682  1.00 60.13           C  
ANISOU 3294  CD1 LEU B 377     7622   7371   7854   1785    859    235       C  
ATOM   3295  CD2 LEU B 377      16.466 -20.434  34.814  1.00 53.33           C  
ANISOU 3295  CD2 LEU B 377     6788   6454   7022   1642    679    321       C  
ATOM   3296  N   GLU B 378      15.914 -23.555  39.667  1.00 39.33           N  
ANISOU 3296  N   GLU B 378     4934   5003   5006   1386    934    381       N  
ATOM   3297  CA  GLU B 378      15.913 -24.888  40.266  1.00 44.32           C  
ANISOU 3297  CA  GLU B 378     5548   5684   5606   1279    949    465       C  
ATOM   3298  C   GLU B 378      16.076 -26.012  39.245  1.00 44.07           C  
ANISOU 3298  C   GLU B 378     5505   5584   5655   1198    866    528       C  
ATOM   3299  O   GLU B 378      15.408 -27.043  39.332  1.00 43.21           O  
ANISOU 3299  O   GLU B 378     5330   5511   5577   1114    886    595       O  
ATOM   3300  CB  GLU B 378      14.636 -25.105  41.080  1.00 50.28           C  
ANISOU 3300  CB  GLU B 378     6189   6576   6339   1267   1053    493       C  
ATOM   3301  CG  GLU B 378      14.479 -24.141  42.239  1.00 54.46           C  
ANISOU 3301  CG  GLU B 378     6734   7189   6770   1342   1152    422       C  
ATOM   3302  CD  GLU B 378      13.286 -24.472  43.112  1.00 58.72           C  
ANISOU 3302  CD  GLU B 378     7153   7888   7270   1321   1267    456       C  
ATOM   3303  OE1 GLU B 378      12.244 -24.890  42.566  1.00 60.42           O  
ANISOU 3303  OE1 GLU B 378     7236   8154   7567   1297   1274    499       O  
ATOM   3304  OE2 GLU B 378      13.392 -24.311  44.346  1.00 61.38           O  
ANISOU 3304  OE2 GLU B 378     7522   8316   7484   1320   1349    439       O  
ATOM   3305  N   LEU B 379      16.964 -25.811  38.280  1.00 39.08           N  
ANISOU 3305  N   LEU B 379     4940   4853   5056   1216    778    499       N  
ATOM   3306  CA  LEU B 379      17.267 -26.849  37.308  1.00 36.85           C  
ANISOU 3306  CA  LEU B 379     4663   4500   4838   1146    703    534       C  
ATOM   3307  C   LEU B 379      18.076 -27.951  37.984  1.00 39.99           C  
ANISOU 3307  C   LEU B 379     5132   4861   5201   1082    703    598       C  
ATOM   3308  O   LEU B 379      18.835 -27.683  38.914  1.00 39.75           O  
ANISOU 3308  O   LEU B 379     5167   4850   5085   1106    723    603       O  
ATOM   3309  CB  LEU B 379      18.062 -26.265  36.138  1.00 38.55           C  
ANISOU 3309  CB  LEU B 379     4930   4639   5078   1189    621    484       C  
ATOM   3310  CG  LEU B 379      17.435 -25.082  35.396  1.00 39.20           C  
ANISOU 3310  CG  LEU B 379     4964   4738   5191   1271    611    440       C  
ATOM   3311  CD1 LEU B 379      18.354 -24.615  34.269  1.00 37.47           C  
ANISOU 3311  CD1 LEU B 379     4811   4445   4983   1294    533    412       C  
ATOM   3312  CD2 LEU B 379      16.065 -25.456  34.860  1.00 35.67           C  
ANISOU 3312  CD2 LEU B 379     4384   4365   4805   1252    611    463       C  
ATOM   3313  N   ASP B 380      17.907 -29.188  37.530  1.00 41.24           N  
ANISOU 3313  N   ASP B 380     5279   4965   5425   1001    678    648       N  
ATOM   3314  CA  ASP B 380      18.760 -30.277  37.998  1.00 44.21           C  
ANISOU 3314  CA  ASP B 380     5737   5272   5789    961    669    718       C  
ATOM   3315  C   ASP B 380      19.743 -30.704  36.904  1.00 40.46           C  
ANISOU 3315  C   ASP B 380     5322   4687   5365    971    586    686       C  
ATOM   3316  O   ASP B 380      19.776 -30.112  35.824  1.00 39.70           O  
ANISOU 3316  O   ASP B 380     5205   4581   5296    998    537    612       O  
ATOM   3317  CB  ASP B 380      17.931 -31.464  38.502  1.00 47.80           C  
ANISOU 3317  CB  ASP B 380     6161   5722   6280    860    722    809       C  
ATOM   3318  CG  ASP B 380      17.102 -32.107  37.411  1.00 52.45           C  
ANISOU 3318  CG  ASP B 380     6687   6263   6978    776    696    785       C  
ATOM   3319  OD1 ASP B 380      17.528 -32.071  36.238  1.00 52.69           O  
ANISOU 3319  OD1 ASP B 380     6736   6228   7055    793    623    716       O  
ATOM   3320  OD2 ASP B 380      16.024 -32.655  37.729  1.00 52.33           O  
ANISOU 3320  OD2 ASP B 380     6600   6290   6994    682    751    831       O  
ATOM   3321  N   ASP B 381      20.538 -31.728  37.191  1.00 38.92           N  
ANISOU 3321  N   ASP B 381     5198   4414   5176    958    574    748       N  
ATOM   3322  CA  ASP B 381      21.584 -32.172  36.275  1.00 38.07           C  
ANISOU 3322  CA  ASP B 381     5146   4210   5108    986    507    714       C  
ATOM   3323  C   ASP B 381      21.045 -32.615  34.917  1.00 40.51           C  
ANISOU 3323  C   ASP B 381     5427   4455   5511    933    472    649       C  
ATOM   3324  O   ASP B 381      21.663 -32.352  33.887  1.00 38.34           O  
ANISOU 3324  O   ASP B 381     5165   4157   5244    967    417    576       O  
ATOM   3325  CB  ASP B 381      22.408 -33.294  36.909  1.00 36.87           C  
ANISOU 3325  CB  ASP B 381     5070   3981   4958    998    510    806       C  
ATOM   3326  CG  ASP B 381      23.278 -32.802  38.044  1.00 41.00           C  
ANISOU 3326  CG  ASP B 381     5619   4591   5366   1063    516    856       C  
ATOM   3327  OD1 ASP B 381      24.041 -31.837  37.827  1.00 38.68           O  
ANISOU 3327  OD1 ASP B 381     5324   4357   5017   1117    480    786       O  
ATOM   3328  OD2 ASP B 381      23.202 -33.379  39.150  1.00 45.47           O  
ANISOU 3328  OD2 ASP B 381     6209   5175   5892   1051    555    966       O  
ATOM   3329  N   SER B 382      19.896 -33.284  34.914  1.00 38.92           N  
ANISOU 3329  N   SER B 382     5180   4239   5370    838    504    673       N  
ATOM   3330  CA  SER B 382      19.307 -33.751  33.662  1.00 43.68           C  
ANISOU 3330  CA  SER B 382     5747   4801   6050    766    467    601       C  
ATOM   3331  C   SER B 382      18.861 -32.587  32.776  1.00 43.46           C  
ANISOU 3331  C   SER B 382     5637   4878   5996    800    427    523       C  
ATOM   3332  O   SER B 382      18.937 -32.671  31.550  1.00 44.73           O  
ANISOU 3332  O   SER B 382     5790   5024   6180    786    370    448       O  
ATOM   3333  CB  SER B 382      18.153 -34.727  33.917  1.00 45.91           C  
ANISOU 3333  CB  SER B 382     5988   5055   6399    633    511    643       C  
ATOM   3334  OG  SER B 382      17.141 -34.145  34.718  1.00 48.82           O  
ANISOU 3334  OG  SER B 382     6263   5554   6731    614    568    689       O  
ATOM   3335  N   ASP B 383      18.401 -31.505  33.401  1.00 39.14           N  
ANISOU 3335  N   ASP B 383     5036   4438   5397    851    459    542       N  
ATOM   3336  CA  ASP B 383      18.050 -30.290  32.671  1.00 36.20           C  
ANISOU 3336  CA  ASP B 383     4603   4149   5003    912    427    489       C  
ATOM   3337  C   ASP B 383      19.313 -29.639  32.117  1.00 35.10           C  
ANISOU 3337  C   ASP B 383     4540   3973   4824    989    379    449       C  
ATOM   3338  O   ASP B 383      19.390 -29.312  30.933  1.00 34.35           O  
ANISOU 3338  O   ASP B 383     4430   3889   4732   1000    323    400       O  
ATOM   3339  CB  ASP B 383      17.348 -29.281  33.584  1.00 33.96           C  
ANISOU 3339  CB  ASP B 383     4262   3963   4680    968    487    513       C  
ATOM   3340  CG  ASP B 383      16.091 -29.836  34.226  1.00 37.05           C  
ANISOU 3340  CG  ASP B 383     4558   4422   5098    893    549    557       C  
ATOM   3341  OD1 ASP B 383      15.316 -30.541  33.544  1.00 40.72           O  
ANISOU 3341  OD1 ASP B 383     4950   4900   5620    802    526    548       O  
ATOM   3342  OD2 ASP B 383      15.873 -29.548  35.421  1.00 38.97           O  
ANISOU 3342  OD2 ASP B 383     4794   4716   5296    916    623    597       O  
ATOM   3343  N   LEU B 384      20.293 -29.445  32.997  1.00 30.56           N  
ANISOU 3343  N   LEU B 384     4038   3373   4200   1033    402    474       N  
ATOM   3344  CA  LEU B 384      21.550 -28.778  32.659  1.00 34.66           C  
ANISOU 3344  CA  LEU B 384     4620   3876   4674   1092    366    440       C  
ATOM   3345  C   LEU B 384      22.286 -29.442  31.496  1.00 35.86           C  
ANISOU 3345  C   LEU B 384     4801   3974   4852   1077    310    400       C  
ATOM   3346  O   LEU B 384      22.883 -28.762  30.658  1.00 34.11           O  
ANISOU 3346  O   LEU B 384     4591   3767   4602   1108    273    359       O  
ATOM   3347  CB  LEU B 384      22.462 -28.740  33.888  1.00 36.98           C  
ANISOU 3347  CB  LEU B 384     4971   4172   4908   1119    395    476       C  
ATOM   3348  CG  LEU B 384      22.503 -27.462  34.732  1.00 40.62           C  
ANISOU 3348  CG  LEU B 384     5441   4693   5300   1161    430    463       C  
ATOM   3349  CD1 LEU B 384      21.335 -26.547  34.439  1.00 42.97           C  
ANISOU 3349  CD1 LEU B 384     5682   5025   5620   1183    452    437       C  
ATOM   3350  CD2 LEU B 384      22.592 -27.795  36.216  1.00 34.78           C  
ANISOU 3350  CD2 LEU B 384     4719   3993   4501   1155    480    515       C  
ATOM   3351  N   ALA B 385      22.245 -30.770  31.455  1.00 35.74           N  
ANISOU 3351  N   ALA B 385     4802   3890   4888   1029    312    411       N  
ATOM   3352  CA  ALA B 385      22.945 -31.527  30.422  1.00 37.21           C  
ANISOU 3352  CA  ALA B 385     5022   4014   5101   1022    272    357       C  
ATOM   3353  C   ALA B 385      22.493 -31.113  29.023  1.00 38.24           C  
ANISOU 3353  C   ALA B 385     5108   4194   5229   1000    226    285       C  
ATOM   3354  O   ALA B 385      23.316 -30.912  28.129  1.00 36.82           O  
ANISOU 3354  O   ALA B 385     4949   4023   5017   1028    192    235       O  
ATOM   3355  CB  ALA B 385      22.751 -33.022  30.631  1.00 35.04           C  
ANISOU 3355  CB  ALA B 385     4781   3631   4901    968    292    375       C  
ATOM   3356  N   ILE B 386      21.184 -30.973  28.837  1.00 35.58           N  
ANISOU 3356  N   ILE B 386     4697   3908   4914    950    224    287       N  
ATOM   3357  CA  ILE B 386      20.654 -30.542  27.547  1.00 35.11           C  
ANISOU 3357  CA  ILE B 386     4580   3923   4836    933    171    235       C  
ATOM   3358  C   ILE B 386      20.913 -29.055  27.304  1.00 34.73           C  
ANISOU 3358  C   ILE B 386     4524   3944   4727   1014    155    255       C  
ATOM   3359  O   ILE B 386      21.264 -28.653  26.196  1.00 36.09           O  
ANISOU 3359  O   ILE B 386     4699   4156   4858   1028    110    223       O  
ATOM   3360  CB  ILE B 386      19.147 -30.823  27.425  1.00 37.42           C  
ANISOU 3360  CB  ILE B 386     4774   4278   5167    858    167    236       C  
ATOM   3361  CG1 ILE B 386      18.829 -32.248  27.885  1.00 33.05           C  
ANISOU 3361  CG1 ILE B 386     4238   3635   4685    757    199    232       C  
ATOM   3362  CG2 ILE B 386      18.683 -30.603  25.995  1.00 38.30           C  
ANISOU 3362  CG2 ILE B 386     4823   4481   5248    832     97    179       C  
ATOM   3363  CD1 ILE B 386      17.359 -32.595  27.803  1.00 32.43           C  
ANISOU 3363  CD1 ILE B 386     4049   3627   4644    654    199    230       C  
ATOM   3364  N   PHE B 387      20.744 -28.241  28.340  1.00 31.14           N  
ANISOU 3364  N   PHE B 387     4069   3499   4264   1064    198    306       N  
ATOM   3365  CA  PHE B 387      20.991 -26.807  28.227  1.00 29.70           C  
ANISOU 3365  CA  PHE B 387     3901   3346   4039   1137    195    323       C  
ATOM   3366  C   PHE B 387      22.416 -26.515  27.757  1.00 31.12           C  
ANISOU 3366  C   PHE B 387     4155   3497   4172   1153    174    301       C  
ATOM   3367  O   PHE B 387      22.633 -25.692  26.871  1.00 34.81           O  
ANISOU 3367  O   PHE B 387     4629   3993   4605   1176    144    301       O  
ATOM   3368  CB  PHE B 387      20.751 -26.123  29.572  1.00 32.97           C  
ANISOU 3368  CB  PHE B 387     4324   3755   4450   1181    257    357       C  
ATOM   3369  CG  PHE B 387      21.007 -24.644  29.554  1.00 40.62           C  
ANISOU 3369  CG  PHE B 387     5327   4720   5388   1251    265    362       C  
ATOM   3370  CD1 PHE B 387      20.332 -23.821  28.669  1.00 45.38           C  
ANISOU 3370  CD1 PHE B 387     5890   5355   5998   1297    237    379       C  
ATOM   3371  CD2 PHE B 387      21.916 -24.075  30.430  1.00 38.08           C  
ANISOU 3371  CD2 PHE B 387     5080   4359   5030   1267    299    353       C  
ATOM   3372  CE1 PHE B 387      20.562 -22.459  28.655  1.00 46.54           C  
ANISOU 3372  CE1 PHE B 387     6087   5466   6130   1364    251    393       C  
ATOM   3373  CE2 PHE B 387      22.149 -22.716  30.423  1.00 36.77           C  
ANISOU 3373  CE2 PHE B 387     4960   4164   4845   1314    313    348       C  
ATOM   3374  CZ  PHE B 387      21.471 -21.907  29.536  1.00 43.99           C  
ANISOU 3374  CZ  PHE B 387     5851   5082   5782   1365    292    371       C  
ATOM   3375  N   ILE B 388      23.383 -27.184  28.372  1.00 29.91           N  
ANISOU 3375  N   ILE B 388     4051   3298   4015   1143    192    292       N  
ATOM   3376  CA  ILE B 388      24.790 -26.998  28.030  1.00 32.16           C  
ANISOU 3376  CA  ILE B 388     4385   3578   4256   1157    178    270       C  
ATOM   3377  C   ILE B 388      25.086 -27.426  26.596  1.00 30.70           C  
ANISOU 3377  C   ILE B 388     4191   3416   4057   1138    136    222       C  
ATOM   3378  O   ILE B 388      25.867 -26.782  25.899  1.00 31.97           O  
ANISOU 3378  O   ILE B 388     4369   3613   4167   1147    121    212       O  
ATOM   3379  CB  ILE B 388      25.696 -27.765  29.011  1.00 33.00           C  
ANISOU 3379  CB  ILE B 388     4526   3651   4363   1166    201    280       C  
ATOM   3380  CG1 ILE B 388      25.836 -26.979  30.314  1.00 36.36           C  
ANISOU 3380  CG1 ILE B 388     4970   4090   4754   1184    236    314       C  
ATOM   3381  CG2 ILE B 388      27.053 -28.045  28.391  1.00 35.84           C  
ANISOU 3381  CG2 ILE B 388     4905   4021   4692   1179    180    245       C  
ATOM   3382  CD1 ILE B 388      26.288 -27.827  31.481  1.00 43.74           C  
ANISOU 3382  CD1 ILE B 388     5922   5012   5684   1192    257    350       C  
ATOM   3383  N   ALA B 389      24.455 -28.511  26.160  1.00 31.91           N  
ANISOU 3383  N   ALA B 389     4320   3554   4251   1100    122    189       N  
ATOM   3384  CA  ALA B 389      24.594 -28.974  24.786  1.00 34.36           C  
ANISOU 3384  CA  ALA B 389     4620   3897   4538   1073     84    123       C  
ATOM   3385  C   ALA B 389      24.057 -27.921  23.818  1.00 36.46           C  
ANISOU 3385  C   ALA B 389     4849   4255   4750   1074     46    139       C  
ATOM   3386  O   ALA B 389      24.651 -27.671  22.768  1.00 34.33           O  
ANISOU 3386  O   ALA B 389     4587   4040   4415   1073     21    112       O  
ATOM   3387  CB  ALA B 389      23.868 -30.304  24.593  1.00 31.31           C  
ANISOU 3387  CB  ALA B 389     4220   3467   4211   1012     79     72       C  
ATOM   3388  N   VAL B 390      22.934 -27.306  24.181  1.00 36.01           N  
ANISOU 3388  N   VAL B 390     4747   4221   4714   1085     44    191       N  
ATOM   3389  CA  VAL B 390      22.352 -26.236  23.374  1.00 34.44           C  
ANISOU 3389  CA  VAL B 390     4511   4102   4472   1112      8    233       C  
ATOM   3390  C   VAL B 390      23.337 -25.080  23.182  1.00 32.94           C  
ANISOU 3390  C   VAL B 390     4382   3904   4230   1153     17    272       C  
ATOM   3391  O   VAL B 390      23.508 -24.571  22.074  1.00 36.19           O  
ANISOU 3391  O   VAL B 390     4793   4380   4579   1155    -18    288       O  
ATOM   3392  CB  VAL B 390      21.041 -25.689  23.995  1.00 32.57           C  
ANISOU 3392  CB  VAL B 390     4212   3885   4279   1147     18    289       C  
ATOM   3393  CG1 VAL B 390      20.625 -24.408  23.300  1.00 34.27           C  
ANISOU 3393  CG1 VAL B 390     4407   4159   4457   1211    -12    354       C  
ATOM   3394  CG2 VAL B 390      19.927 -26.723  23.907  1.00 30.04           C  
ANISOU 3394  CG2 VAL B 390     3806   3609   3997   1084     -1    256       C  
ATOM   3395  N   ILE B 391      23.982 -24.668  24.269  1.00 36.73           N  
ANISOU 3395  N   ILE B 391     4912   4313   4729   1175     64    288       N  
ATOM   3396  CA  ILE B 391      24.941 -23.571  24.221  1.00 34.59           C  
ANISOU 3396  CA  ILE B 391     4701   4025   4417   1188     79    317       C  
ATOM   3397  C   ILE B 391      26.089 -23.884  23.265  1.00 33.39           C  
ANISOU 3397  C   ILE B 391     4565   3921   4202   1152     63    282       C  
ATOM   3398  O   ILE B 391      26.515 -23.029  22.489  1.00 30.72           O  
ANISOU 3398  O   ILE B 391     4249   3613   3808   1144     54    317       O  
ATOM   3399  CB  ILE B 391      25.522 -23.277  25.615  1.00 36.40           C  
ANISOU 3399  CB  ILE B 391     4975   4189   4667   1194    129    314       C  
ATOM   3400  CG1 ILE B 391      24.435 -22.729  26.548  1.00 37.42           C  
ANISOU 3400  CG1 ILE B 391     5095   4282   4842   1237    159    343       C  
ATOM   3401  CG2 ILE B 391      26.684 -22.296  25.512  1.00 33.23           C  
ANISOU 3401  CG2 ILE B 391     4631   3776   4219   1174    142    324       C  
ATOM   3402  CD1 ILE B 391      24.934 -22.402  27.943  1.00 34.20           C  
ANISOU 3402  CD1 ILE B 391     4731   3828   4434   1238    208    329       C  
ATOM   3403  N   ILE B 392      26.583 -25.117  23.321  1.00 28.68           N  
ANISOU 3403  N   ILE B 392     3957   3326   3614   1133     65    218       N  
ATOM   3404  CA  ILE B 392      27.714 -25.520  22.492  1.00 33.06           C  
ANISOU 3404  CA  ILE B 392     4516   3932   4112   1114     62    170       C  
ATOM   3405  C   ILE B 392      27.387 -25.426  21.005  1.00 35.08           C  
ANISOU 3405  C   ILE B 392     4750   4277   4300   1093     24    159       C  
ATOM   3406  O   ILE B 392      28.188 -24.926  20.212  1.00 33.08           O  
ANISOU 3406  O   ILE B 392     4508   4092   3971   1077     27    167       O  
ATOM   3407  CB  ILE B 392      28.177 -26.949  22.819  1.00 32.60           C  
ANISOU 3407  CB  ILE B 392     4453   3841   4091   1122     75    100       C  
ATOM   3408  CG1 ILE B 392      28.659 -27.026  24.266  1.00 36.98           C  
ANISOU 3408  CG1 ILE B 392     5028   4336   4688   1147    107    127       C  
ATOM   3409  CG2 ILE B 392      29.289 -27.376  21.873  1.00 31.34           C  
ANISOU 3409  CG2 ILE B 392     4289   3747   3873   1121     79     37       C  
ATOM   3410  CD1 ILE B 392      29.102 -28.414  24.695  1.00 35.28           C  
ANISOU 3410  CD1 ILE B 392     4815   4072   4518   1174    121     88       C  
ATOM   3411  N   LEU B 393      26.203 -25.902  20.638  1.00 34.81           N  
ANISOU 3411  N   LEU B 393     4678   4262   4285   1085    -10    143       N  
ATOM   3412  CA  LEU B 393      25.791 -25.941  19.240  1.00 30.87           C  
ANISOU 3412  CA  LEU B 393     4147   3874   3708   1059    -57    124       C  
ATOM   3413  C   LEU B 393      25.150 -24.625  18.802  1.00 31.51           C  
ANISOU 3413  C   LEU B 393     4218   4005   3747   1084    -87    234       C  
ATOM   3414  O   LEU B 393      24.047 -24.618  18.262  1.00 35.44           O  
ANISOU 3414  O   LEU B 393     4662   4574   4229   1085   -136    253       O  
ATOM   3415  CB  LEU B 393      24.826 -27.110  19.000  1.00 29.26           C  
ANISOU 3415  CB  LEU B 393     3899   3683   3536   1021    -88     46       C  
ATOM   3416  CG  LEU B 393      25.458 -28.502  18.858  1.00 32.09           C  
ANISOU 3416  CG  LEU B 393     4279   4002   3913    992    -67    -79       C  
ATOM   3417  CD1 LEU B 393      26.199 -28.634  17.531  1.00 35.85           C  
ANISOU 3417  CD1 LEU B 393     4759   4585   4277    975    -77   -149       C  
ATOM   3418  CD2 LEU B 393      26.386 -28.807  20.009  1.00 28.29           C  
ANISOU 3418  CD2 LEU B 393     3842   3407   3500   1032    -12    -73       C  
ATOM   3419  N   SER B 394      25.848 -23.517  19.040  1.00 32.16           N  
ANISOU 3419  N   SER B 394     4351   4051   3815   1103    -57    308       N  
ATOM   3420  CA  SER B 394      25.368 -22.195  18.638  1.00 36.18           C  
ANISOU 3420  CA  SER B 394     4875   4573   4297   1137    -75    425       C  
ATOM   3421  C   SER B 394      25.904 -21.808  17.259  1.00 40.17           C  
ANISOU 3421  C   SER B 394     5392   5192   4681   1107    -97    462       C  
ATOM   3422  O   SER B 394      27.115 -21.691  17.056  1.00 38.03           O  
ANISOU 3422  O   SER B 394     5157   4933   4362   1065    -61    447       O  
ATOM   3423  CB  SER B 394      25.768 -21.134  19.668  1.00 35.95           C  
ANISOU 3423  CB  SER B 394     4914   4420   4325   1161    -24    482       C  
ATOM   3424  OG  SER B 394      25.173 -21.391  20.931  1.00 37.68           O  
ANISOU 3424  OG  SER B 394     5122   4557   4639   1193     -2    456       O  
ATOM   3425  N   GLY B 395      24.994 -21.604  16.316  1.00 42.47           N  
ANISOU 3425  N   GLY B 395     5640   5585   4911   1126   -156    517       N  
ATOM   3426  CA  GLY B 395      25.375 -21.329  14.943  1.00 41.20           C  
ANISOU 3426  CA  GLY B 395     5481   5561   4611   1095   -183    558       C  
ATOM   3427  C   GLY B 395      25.844 -19.913  14.663  1.00 40.59           C  
ANISOU 3427  C   GLY B 395     5475   5450   4498   1107   -161    706       C  
ATOM   3428  O   GLY B 395      26.160 -19.584  13.520  1.00 39.88           O  
ANISOU 3428  O   GLY B 395     5391   5478   4282   1079   -179    766       O  
ATOM   3429  N   ASP B 396      25.901 -19.072  15.693  1.00 39.25           N  
ANISOU 3429  N   ASP B 396     5364   5116   4431   1142   -119    762       N  
ATOM   3430  CA  ASP B 396      26.276 -17.673  15.493  1.00 39.06           C  
ANISOU 3430  CA  ASP B 396     5427   5020   4395   1146    -92    902       C  
ATOM   3431  C   ASP B 396      27.696 -17.332  15.959  1.00 41.96           C  
ANISOU 3431  C   ASP B 396     5862   5311   4770   1062    -20    874       C  
ATOM   3432  O   ASP B 396      28.068 -16.160  16.019  1.00 44.75           O  
ANISOU 3432  O   ASP B 396     6300   5567   5137   1044     15    975       O  
ATOM   3433  CB  ASP B 396      25.253 -16.731  16.143  1.00 45.02           C  
ANISOU 3433  CB  ASP B 396     6211   5640   5252   1248    -94    996       C  
ATOM   3434  CG  ASP B 396      25.295 -16.774  17.659  1.00 49.35           C  
ANISOU 3434  CG  ASP B 396     6785   6037   5928   1262    -42    915       C  
ATOM   3435  OD1 ASP B 396      25.929 -17.692  18.215  1.00 48.15           O  
ANISOU 3435  OD1 ASP B 396     6609   5898   5786   1203    -20    792       O  
ATOM   3436  OD2 ASP B 396      24.690 -15.886  18.296  1.00 54.96           O  
ANISOU 3436  OD2 ASP B 396     7539   6619   6724   1339    -21    974       O  
ATOM   3437  N   ARG B 397      28.488 -18.350  16.283  1.00 40.22           N  
ANISOU 3437  N   ARG B 397     5602   5137   4544   1011      2    741       N  
ATOM   3438  CA  ARG B 397      29.888 -18.129  16.638  1.00 40.03           C  
ANISOU 3438  CA  ARG B 397     5610   5090   4510    929     63    710       C  
ATOM   3439  C   ARG B 397      30.647 -17.606  15.423  1.00 43.45           C  
ANISOU 3439  C   ARG B 397     6060   5631   4818    858     78    786       C  
ATOM   3440  O   ARG B 397      30.423 -18.066  14.304  1.00 42.98           O  
ANISOU 3440  O   ARG B 397     5957   5720   4653    861     44    790       O  
ATOM   3441  CB  ARG B 397      30.540 -19.420  17.139  1.00 34.62           C  
ANISOU 3441  CB  ARG B 397     4863   4452   3837    916     77    562       C  
ATOM   3442  CG  ARG B 397      29.773 -20.130  18.245  1.00 35.21           C  
ANISOU 3442  CG  ARG B 397     4917   4442   4019    978     63    494       C  
ATOM   3443  CD  ARG B 397      29.531 -19.224  19.448  1.00 31.53           C  
ANISOU 3443  CD  ARG B 397     4510   3827   3645    995     88    536       C  
ATOM   3444  NE  ARG B 397      29.070 -19.990  20.603  1.00 34.59           N  
ANISOU 3444  NE  ARG B 397     4870   4157   4114   1037     89    464       N  
ATOM   3445  CZ  ARG B 397      28.688 -19.458  21.759  1.00 35.22           C  
ANISOU 3445  CZ  ARG B 397     4986   4126   4267   1064    112    473       C  
ATOM   3446  NH1 ARG B 397      28.703 -18.141  21.926  1.00 27.81           N  
ANISOU 3446  NH1 ARG B 397     4122   3099   3346   1056    137    538       N  
ATOM   3447  NH2 ARG B 397      28.287 -20.246  22.749  1.00 33.35           N  
ANISOU 3447  NH2 ARG B 397     4720   3864   4087   1095    116    416       N  
ATOM   3448  N   PRO B 398      31.555 -16.644  15.638  1.00 43.38           N  
ANISOU 3448  N   PRO B 398     6114   5559   4812    779    131    844       N  
ATOM   3449  CA  PRO B 398      32.326 -16.083  14.523  1.00 46.72           C  
ANISOU 3449  CA  PRO B 398     6553   6084   5113    692    157    933       C  
ATOM   3450  C   PRO B 398      33.205 -17.140  13.858  1.00 44.32           C  
ANISOU 3450  C   PRO B 398     6157   5982   4700    650    172    826       C  
ATOM   3451  O   PRO B 398      33.775 -17.984  14.550  1.00 43.60           O  
ANISOU 3451  O   PRO B 398     6011   5904   4651    653    190    695       O  
ATOM   3452  CB  PRO B 398      33.207 -15.023  15.199  1.00 46.19           C  
ANISOU 3452  CB  PRO B 398     6560   5892   5099    594    219    975       C  
ATOM   3453  CG  PRO B 398      32.543 -14.737  16.513  1.00 44.96           C  
ANISOU 3453  CG  PRO B 398     6453   5543   5086    656    213    944       C  
ATOM   3454  CD  PRO B 398      31.904 -16.023  16.926  1.00 42.65           C  
ANISOU 3454  CD  PRO B 398     6077   5303   4826    752    171    827       C  
ATOM   3455  N   GLY B 399      33.295 -17.097  12.532  1.00 43.01           N  
ANISOU 3455  N   GLY B 399     5975   5974   4392    621    167    886       N  
ATOM   3456  CA  GLY B 399      34.226 -17.935  11.795  1.00 42.43           C  
ANISOU 3456  CA  GLY B 399     5821   6102   4199    577    199    788       C  
ATOM   3457  C   GLY B 399      33.755 -19.344  11.479  1.00 44.21           C  
ANISOU 3457  C   GLY B 399     5974   6426   4396    651    160    638       C  
ATOM   3458  O   GLY B 399      34.536 -20.161  10.993  1.00 47.35           O  
ANISOU 3458  O   GLY B 399     6308   6969   4715    634    195    526       O  
ATOM   3459  N   LEU B 400      32.490 -19.638  11.761  1.00 37.72           N  
ANISOU 3459  N   LEU B 400     5162   5524   3644    730     94    630       N  
ATOM   3460  CA  LEU B 400      31.914 -20.934  11.410  1.00 39.26           C  
ANISOU 3460  CA  LEU B 400     5299   5800   3816    778     53    492       C  
ATOM   3461  C   LEU B 400      31.917 -21.128   9.895  1.00 42.72           C  
ANISOU 3461  C   LEU B 400     5709   6457   4067    746     38    489       C  
ATOM   3462  O   LEU B 400      31.613 -20.202   9.145  1.00 46.05           O  
ANISOU 3462  O   LEU B 400     6160   6944   4394    724     16    641       O  
ATOM   3463  CB  LEU B 400      30.485 -21.048  11.950  1.00 39.94           C  
ANISOU 3463  CB  LEU B 400     5392   5779   4004    847    -15    507       C  
ATOM   3464  CG  LEU B 400      30.226 -21.936  13.174  1.00 42.48           C  
ANISOU 3464  CG  LEU B 400     5698   5967   4475    891    -14    391       C  
ATOM   3465  CD1 LEU B 400      31.485 -22.202  13.984  1.00 39.55           C  
ANISOU 3465  CD1 LEU B 400     5327   5542   4158    874     53    324       C  
ATOM   3466  CD2 LEU B 400      29.125 -21.361  14.051  1.00 36.12           C  
ANISOU 3466  CD2 LEU B 400     4918   5019   3787    943    -46    473       C  
ATOM   3467  N   LEU B 401      32.254 -22.335   9.451  1.00 43.76           N  
ANISOU 3467  N   LEU B 401     5787   6699   4141    749     52    317       N  
ATOM   3468  CA  LEU B 401      32.306 -22.640   8.023  1.00 43.39           C  
ANISOU 3468  CA  LEU B 401     5710   6878   3899    715     45    277       C  
ATOM   3469  C   LEU B 401      30.995 -23.223   7.491  1.00 39.96           C  
ANISOU 3469  C   LEU B 401     5255   6505   3424    738    -44    224       C  
ATOM   3470  O   LEU B 401      30.589 -22.936   6.366  1.00 41.24           O  
ANISOU 3470  O   LEU B 401     5405   6845   3420    710    -86    283       O  
ATOM   3471  CB  LEU B 401      33.464 -23.595   7.715  1.00 48.31           C  
ANISOU 3471  CB  LEU B 401     6286   7606   4465    706    121    102       C  
ATOM   3472  CG  LEU B 401      34.872 -22.997   7.602  1.00 53.62           C  
ANISOU 3472  CG  LEU B 401     6941   8356   5078    654    211    156       C  
ATOM   3473  CD1 LEU B 401      34.857 -21.770   6.702  1.00 54.17           C  
ANISOU 3473  CD1 LEU B 401     7040   8544   4999    579    209    349       C  
ATOM   3474  CD2 LEU B 401      35.443 -22.650   8.966  1.00 56.43           C  
ANISOU 3474  CD2 LEU B 401     7307   8530   5603    663    243    191       C  
ATOM   3475  N   ASN B 402      30.339 -24.052   8.296  1.00 39.92           N  
ANISOU 3475  N   ASN B 402     5240   6366   3562    778    -74    117       N  
ATOM   3476  CA  ASN B 402      29.092 -24.678   7.872  1.00 41.53           C  
ANISOU 3476  CA  ASN B 402     5412   6628   3739    779   -157     50       C  
ATOM   3477  C   ASN B 402      28.040 -24.635   8.972  1.00 42.37           C  
ANISOU 3477  C   ASN B 402     5518   6558   4022    822   -204     93       C  
ATOM   3478  O   ASN B 402      27.929 -25.564   9.769  1.00 40.84           O  
ANISOU 3478  O   ASN B 402     5322   6237   3957    834   -189    -30       O  
ATOM   3479  CB  ASN B 402      29.335 -26.124   7.430  1.00 42.30           C  
ANISOU 3479  CB  ASN B 402     5486   6787   3798    757   -138   -190       C  
ATOM   3480  CG  ASN B 402      28.109 -26.748   6.786  1.00 45.15           C  
ANISOU 3480  CG  ASN B 402     5809   7248   4096    722   -226   -275       C  
ATOM   3481  OD1 ASN B 402      27.095 -26.077   6.571  1.00 40.69           O  
ANISOU 3481  OD1 ASN B 402     5219   6745   3497    722   -307   -143       O  
ATOM   3482  ND2 ASN B 402      28.196 -28.037   6.472  1.00 43.03           N  
ANISOU 3482  ND2 ASN B 402     5537   6998   3816    694   -210   -499       N  
ATOM   3483  N   VAL B 403      27.274 -23.550   9.008  1.00 39.47           N  
ANISOU 3483  N   VAL B 403     5155   6184   3658    851   -253    274       N  
ATOM   3484  CA  VAL B 403      26.297 -23.322  10.069  1.00 41.50           C  
ANISOU 3484  CA  VAL B 403     5406   6286   4076    903   -285    332       C  
ATOM   3485  C   VAL B 403      25.139 -24.320  10.040  1.00 42.83           C  
ANISOU 3485  C   VAL B 403     5507   6494   4273    890   -350    219       C  
ATOM   3486  O   VAL B 403      24.551 -24.635  11.076  1.00 42.04           O  
ANISOU 3486  O   VAL B 403     5394   6256   4322    913   -350    195       O  
ATOM   3487  CB  VAL B 403      25.738 -21.882  10.006  1.00 44.35           C  
ANISOU 3487  CB  VAL B 403     5786   6636   4429    956   -318    553       C  
ATOM   3488  CG1 VAL B 403      24.638 -21.678  11.045  1.00 42.96           C  
ANISOU 3488  CG1 VAL B 403     5588   6325   4409   1024   -346    598       C  
ATOM   3489  CG2 VAL B 403      26.864 -20.868  10.191  1.00 44.00           C  
ANISOU 3489  CG2 VAL B 403     5822   6511   4384    947   -245    662       C  
ATOM   3490  N   LYS B 404      24.822 -24.823   8.851  1.00 43.46           N  
ANISOU 3490  N   LYS B 404     5541   6772   4201    840   -404    145       N  
ATOM   3491  CA  LYS B 404      23.649 -25.676   8.667  1.00 48.30           C  
ANISOU 3491  CA  LYS B 404     6080   7454   4818    801   -477     41       C  
ATOM   3492  C   LYS B 404      23.546 -26.858   9.639  1.00 48.20           C  
ANISOU 3492  C   LYS B 404     6073   7270   4968    774   -442   -118       C  
ATOM   3493  O   LYS B 404      22.549 -26.984  10.350  1.00 45.85           O  
ANISOU 3493  O   LYS B 404     5732   6905   4784    781   -473    -98       O  
ATOM   3494  CB  LYS B 404      23.548 -26.164   7.217  1.00 51.00           C  
ANISOU 3494  CB  LYS B 404     6382   8043   4952    729   -530    -57       C  
ATOM   3495  CG  LYS B 404      22.379 -27.103   6.971  1.00 53.29           C  
ANISOU 3495  CG  LYS B 404     6592   8418   5237    660   -609   -190       C  
ATOM   3496  CD  LYS B 404      22.071 -27.244   5.487  1.00 56.58           C  
ANISOU 3496  CD  LYS B 404     6956   9126   5418    593   -686   -241       C  
ATOM   3497  CE  LYS B 404      21.063 -28.354   5.246  1.00 56.73           C  
ANISOU 3497  CE  LYS B 404     6900   9225   5431    491   -755   -424       C  
ATOM   3498  NZ  LYS B 404      19.982 -28.331   6.268  1.00 55.77           N  
ANISOU 3498  NZ  LYS B 404     6715   8987   5487    509   -790   -362       N  
ATOM   3499  N   PRO B 405      24.571 -27.730   9.671  1.00 46.42           N  
ANISOU 3499  N   PRO B 405     5900   6979   4757    749   -372   -270       N  
ATOM   3500  CA  PRO B 405      24.499 -28.926  10.519  1.00 44.23           C  
ANISOU 3500  CA  PRO B 405     5642   6531   4631    728   -337   -412       C  
ATOM   3501  C   PRO B 405      24.458 -28.551  11.993  1.00 41.94           C  
ANISOU 3501  C   PRO B 405     5374   6044   4516    788   -300   -307       C  
ATOM   3502  O   PRO B 405      23.876 -29.271  12.803  1.00 42.82           O  
ANISOU 3502  O   PRO B 405     5479   6034   4755    769   -296   -357       O  
ATOM   3503  CB  PRO B 405      25.812 -29.663  10.214  1.00 41.72           C  
ANISOU 3503  CB  PRO B 405     5381   6188   4282    730   -260   -555       C  
ATOM   3504  CG  PRO B 405      26.353 -29.033   8.980  1.00 46.50           C  
ANISOU 3504  CG  PRO B 405     5976   7003   4689    721   -267   -525       C  
ATOM   3505  CD  PRO B 405      25.870 -27.623   8.989  1.00 45.42           C  
ANISOU 3505  CD  PRO B 405     5815   6927   4514    751   -313   -302       C  
ATOM   3506  N   ILE B 406      25.081 -27.428  12.329  1.00 38.89           N  
ANISOU 3506  N   ILE B 406     5018   5631   4128    850   -269   -165       N  
ATOM   3507  CA  ILE B 406      25.117 -26.949  13.706  1.00 35.77           C  
ANISOU 3507  CA  ILE B 406     4650   5067   3876    904   -232    -72       C  
ATOM   3508  C   ILE B 406      23.730 -26.530  14.194  1.00 40.73           C  
ANISOU 3508  C   ILE B 406     5226   5681   4570    921   -281     16       C  
ATOM   3509  O   ILE B 406      23.288 -26.943  15.266  1.00 40.12           O  
ANISOU 3509  O   ILE B 406     5143   5482   4619    927   -261      1       O  
ATOM   3510  CB  ILE B 406      26.105 -25.779  13.852  1.00 35.25           C  
ANISOU 3510  CB  ILE B 406     4630   4983   3780    944   -189     46       C  
ATOM   3511  CG1 ILE B 406      27.514 -26.239  13.465  1.00 34.23           C  
ANISOU 3511  CG1 ILE B 406     4529   4885   3592    928   -131    -43       C  
ATOM   3512  CG2 ILE B 406      26.075 -25.220  15.272  1.00 33.26           C  
ANISOU 3512  CG2 ILE B 406     4407   4568   3661    991   -155    128       C  
ATOM   3513  CD1 ILE B 406      28.532 -25.128  13.408  1.00 36.33           C  
ANISOU 3513  CD1 ILE B 406     4827   5172   3807    935    -90     63       C  
ATOM   3514  N   GLU B 407      23.043 -25.712  13.402  1.00 42.21           N  
ANISOU 3514  N   GLU B 407     5367   6005   4665    936   -343    114       N  
ATOM   3515  CA  GLU B 407      21.694 -25.280  13.747  1.00 42.40           C  
ANISOU 3515  CA  GLU B 407     5320   6048   4741    971   -393    201       C  
ATOM   3516  C   GLU B 407      20.728 -26.458  13.722  1.00 45.83           C  
ANISOU 3516  C   GLU B 407     5676   6528   5207    896   -434     79       C  
ATOM   3517  O   GLU B 407      19.803 -26.528  14.528  1.00 43.01           O  
ANISOU 3517  O   GLU B 407     5265   6124   4952    907   -438    105       O  
ATOM   3518  CB  GLU B 407      21.212 -24.188  12.793  1.00 47.20           C  
ANISOU 3518  CB  GLU B 407     5892   6808   5234   1018   -458    343       C  
ATOM   3519  CG  GLU B 407      21.774 -22.811  13.087  1.00 53.72           C  
ANISOU 3519  CG  GLU B 407     6792   7543   6074   1099   -417    502       C  
ATOM   3520  CD  GLU B 407      21.303 -21.767  12.092  1.00 66.05           C  
ANISOU 3520  CD  GLU B 407     8331   9240   7524   1154   -480    662       C  
ATOM   3521  OE1 GLU B 407      20.532 -22.122  11.174  1.00 70.40           O  
ANISOU 3521  OE1 GLU B 407     8794   9984   7972   1131   -563    649       O  
ATOM   3522  OE2 GLU B 407      21.705 -20.591  12.224  1.00 68.88           O  
ANISOU 3522  OE2 GLU B 407     8763   9513   7894   1215   -447    803       O  
ATOM   3523  N   ASP B 408      20.947 -27.384  12.794  1.00 45.20           N  
ANISOU 3523  N   ASP B 408     5593   6543   5039    811   -458    -60       N  
ATOM   3524  CA  ASP B 408      20.109 -28.573  12.700  1.00 45.00           C  
ANISOU 3524  CA  ASP B 408     5508   6548   5043    711   -492   -199       C  
ATOM   3525  C   ASP B 408      20.191 -29.396  13.982  1.00 45.13           C  
ANISOU 3525  C   ASP B 408     5566   6352   5231    693   -424   -258       C  
ATOM   3526  O   ASP B 408      19.177 -29.877  14.490  1.00 46.45           O  
ANISOU 3526  O   ASP B 408     5670   6501   5480    640   -440   -277       O  
ATOM   3527  CB  ASP B 408      20.506 -29.428  11.495  1.00 45.75           C  
ANISOU 3527  CB  ASP B 408     5617   6755   5011    622   -515   -365       C  
ATOM   3528  CG  ASP B 408      19.999 -28.861  10.177  1.00 54.57           C  
ANISOU 3528  CG  ASP B 408     6660   8134   5941    607   -607   -321       C  
ATOM   3529  OD1 ASP B 408      19.164 -27.930  10.197  1.00 56.66           O  
ANISOU 3529  OD1 ASP B 408     6847   8491   6190    664   -665   -164       O  
ATOM   3530  OD2 ASP B 408      20.436 -29.353   9.117  1.00 55.94           O  
ANISOU 3530  OD2 ASP B 408     6850   8429   5976    545   -621   -444       O  
ATOM   3531  N   ILE B 409      21.402 -29.554  14.506  1.00 40.67           N  
ANISOU 3531  N   ILE B 409     5099   5640   4713    733   -347   -278       N  
ATOM   3532  CA  ILE B 409      21.597 -30.286  15.752  1.00 38.77           C  
ANISOU 3532  CA  ILE B 409     4906   5202   4622    732   -282   -309       C  
ATOM   3533  C   ILE B 409      21.009 -29.522  16.940  1.00 38.09           C  
ANISOU 3533  C   ILE B 409     4792   5054   4627    790   -265   -170       C  
ATOM   3534  O   ILE B 409      20.362 -30.110  17.806  1.00 44.06           O  
ANISOU 3534  O   ILE B 409     5528   5727   5487    755   -245   -180       O  
ATOM   3535  CB  ILE B 409      23.087 -30.587  16.006  1.00 40.12           C  
ANISOU 3535  CB  ILE B 409     5174   5262   4809    779   -211   -351       C  
ATOM   3536  CG1 ILE B 409      23.640 -31.496  14.903  1.00 42.45           C  
ANISOU 3536  CG1 ILE B 409     5497   5606   5028    731   -212   -514       C  
ATOM   3537  CG2 ILE B 409      23.279 -31.227  17.376  1.00 29.66           C  
ANISOU 3537  CG2 ILE B 409     3895   3745   3630    797   -152   -346       C  
ATOM   3538  CD1 ILE B 409      25.137 -31.724  14.987  1.00 45.14           C  
ANISOU 3538  CD1 ILE B 409     5908   5877   5366    795   -143   -556       C  
ATOM   3539  N   GLN B 410      21.227 -28.211  16.977  1.00 33.20           N  
ANISOU 3539  N   GLN B 410     4176   4471   3968    875   -267    -45       N  
ATOM   3540  CA  GLN B 410      20.698 -27.397  18.067  1.00 35.25           C  
ANISOU 3540  CA  GLN B 410     4418   4670   4307    942   -243     71       C  
ATOM   3541  C   GLN B 410      19.171 -27.414  18.080  1.00 36.41           C  
ANISOU 3541  C   GLN B 410     4448   4907   4478    922   -290     97       C  
ATOM   3542  O   GLN B 410      18.551 -27.404  19.140  1.00 37.59           O  
ANISOU 3542  O   GLN B 410     4567   4997   4720    938   -256    134       O  
ATOM   3543  CB  GLN B 410      21.205 -25.956  17.987  1.00 36.47           C  
ANISOU 3543  CB  GLN B 410     4610   4830   4415   1030   -234    190       C  
ATOM   3544  CG  GLN B 410      21.060 -25.206  19.306  1.00 37.50           C  
ANISOU 3544  CG  GLN B 410     4763   4848   4637   1100   -182    271       C  
ATOM   3545  CD  GLN B 410      21.268 -23.712  19.173  1.00 33.44           C  
ANISOU 3545  CD  GLN B 410     4286   4328   4092   1180   -178    388       C  
ATOM   3546  OE1 GLN B 410      21.959 -23.100  19.983  1.00 42.04           O  
ANISOU 3546  OE1 GLN B 410     5448   5308   5218   1212   -123    417       O  
ATOM   3547  NE2 GLN B 410      20.670 -23.118  18.151  1.00 32.23           N  
ANISOU 3547  NE2 GLN B 410     4087   4292   3869   1210   -238    456       N  
ATOM   3548  N   ASP B 411      18.568 -27.435  16.898  1.00 37.36           N  
ANISOU 3548  N   ASP B 411     4494   5196   4506    885   -368     79       N  
ATOM   3549  CA  ASP B 411      17.118 -27.546  16.797  1.00 43.51           C  
ANISOU 3549  CA  ASP B 411     5136   6099   5295    854   -424     93       C  
ATOM   3550  C   ASP B 411      16.611 -28.793  17.516  1.00 41.56           C  
ANISOU 3550  C   ASP B 411     4863   5779   5149    744   -394     -3       C  
ATOM   3551  O   ASP B 411      15.625 -28.734  18.249  1.00 39.39           O  
ANISOU 3551  O   ASP B 411     4500   5520   4945    745   -383     43       O  
ATOM   3552  CB  ASP B 411      16.674 -27.548  15.333  1.00 53.67           C  
ANISOU 3552  CB  ASP B 411     6347   7602   6444    810   -522     68       C  
ATOM   3553  CG  ASP B 411      16.607 -26.151  14.746  1.00 68.22           C  
ANISOU 3553  CG  ASP B 411     8170   9550   8200    932   -564    222       C  
ATOM   3554  OD1 ASP B 411      16.868 -25.181  15.492  1.00 67.60           O  
ANISOU 3554  OD1 ASP B 411     8143   9358   8184   1044   -513    335       O  
ATOM   3555  OD2 ASP B 411      16.291 -26.019  13.544  1.00 77.48           O  
ANISOU 3555  OD2 ASP B 411     9282  10916   9240    913   -648    231       O  
ATOM   3556  N   ASN B 412      17.296 -29.914  17.311  1.00 42.46           N  
ANISOU 3556  N   ASN B 412     5056   5807   5271    654   -372   -133       N  
ATOM   3557  CA  ASN B 412      16.938 -31.169  17.966  1.00 43.56           C  
ANISOU 3557  CA  ASN B 412     5199   5838   5514    543   -335   -220       C  
ATOM   3558  C   ASN B 412      17.182 -31.119  19.471  1.00 41.23           C  
ANISOU 3558  C   ASN B 412     4957   5375   5333    597   -249   -145       C  
ATOM   3559  O   ASN B 412      16.409 -31.671  20.254  1.00 42.16           O  
ANISOU 3559  O   ASN B 412     5030   5454   5537    532   -221   -139       O  
ATOM   3560  CB  ASN B 412      17.713 -32.336  17.349  1.00 43.87           C  
ANISOU 3560  CB  ASN B 412     5331   5798   5540    458   -326   -377       C  
ATOM   3561  CG  ASN B 412      17.393 -32.534  15.881  1.00 59.75           C  
ANISOU 3561  CG  ASN B 412     7288   7989   7424    380   -408   -480       C  
ATOM   3562  OD1 ASN B 412      18.245 -32.960  15.100  1.00 71.70           O  
ANISOU 3562  OD1 ASN B 412     8877   9493   8871    365   -405   -588       O  
ATOM   3563  ND2 ASN B 412      16.161 -32.219  15.495  1.00 60.97           N  
ANISOU 3563  ND2 ASN B 412     7302   8330   7535    333   -483   -449       N  
ATOM   3564  N   LEU B 413      18.267 -30.462  19.869  1.00 34.60           N  
ANISOU 3564  N   LEU B 413     4209   4452   4486    705   -207    -88       N  
ATOM   3565  CA  LEU B 413      18.584 -30.310  21.282  1.00 35.71           C  
ANISOU 3565  CA  LEU B 413     4400   4460   4708    761   -132    -18       C  
ATOM   3566  C   LEU B 413      17.565 -29.410  21.974  1.00 38.95           C  
ANISOU 3566  C   LEU B 413     4722   4935   5144    814   -124     85       C  
ATOM   3567  O   LEU B 413      17.173 -29.665  23.113  1.00 36.95           O  
ANISOU 3567  O   LEU B 413     4456   4619   4962    803    -69    118       O  
ATOM   3568  CB  LEU B 413      19.999 -29.754  21.459  1.00 36.07           C  
ANISOU 3568  CB  LEU B 413     4549   4432   4724    850   -100      8       C  
ATOM   3569  CG  LEU B 413      21.130 -30.698  21.032  1.00 37.58           C  
ANISOU 3569  CG  LEU B 413     4826   4546   4907    824    -86    -89       C  
ATOM   3570  CD1 LEU B 413      22.464 -29.967  20.950  1.00 31.27           C  
ANISOU 3570  CD1 LEU B 413     4091   3738   4053    907    -67    -60       C  
ATOM   3571  CD2 LEU B 413      21.218 -31.902  21.963  1.00 33.73           C  
ANISOU 3571  CD2 LEU B 413     4386   3909   4520    783    -35   -118       C  
ATOM   3572  N   LEU B 414      17.139 -28.360  21.279  1.00 38.03           N  
ANISOU 3572  N   LEU B 414     4541   4945   4963    880   -175    139       N  
ATOM   3573  CA  LEU B 414      16.126 -27.452  21.804  1.00 38.87           C  
ANISOU 3573  CA  LEU B 414     4555   5121   5095    956   -167    232       C  
ATOM   3574  C   LEU B 414      14.803 -28.185  21.995  1.00 43.08           C  
ANISOU 3574  C   LEU B 414     4953   5743   5672    866   -179    208       C  
ATOM   3575  O   LEU B 414      14.120 -27.995  23.002  1.00 40.05           O  
ANISOU 3575  O   LEU B 414     4512   5358   5347    892   -126    257       O  
ATOM   3576  CB  LEU B 414      15.946 -26.247  20.875  1.00 40.99           C  
ANISOU 3576  CB  LEU B 414     4787   5501   5287   1053   -227    305       C  
ATOM   3577  CG  LEU B 414      17.064 -25.200  20.933  1.00 40.42           C  
ANISOU 3577  CG  LEU B 414     4837   5335   5187   1150   -198    361       C  
ATOM   3578  CD1 LEU B 414      16.983 -24.251  19.753  1.00 39.99           C  
ANISOU 3578  CD1 LEU B 414     4764   5386   5046   1216   -264    433       C  
ATOM   3579  CD2 LEU B 414      17.021 -24.432  22.251  1.00 39.14           C  
ANISOU 3579  CD2 LEU B 414     4708   5070   5095   1239   -121    419       C  
ATOM   3580  N   GLN B 415      14.447 -29.026  21.026  1.00 44.33           N  
ANISOU 3580  N   GLN B 415     5059   5988   5796    748   -243    125       N  
ATOM   3581  CA  GLN B 415      13.253 -29.858  21.141  1.00 45.90           C  
ANISOU 3581  CA  GLN B 415     5131   6273   6038    622   -256     85       C  
ATOM   3582  C   GLN B 415      13.356 -30.751  22.367  1.00 45.53           C  
ANISOU 3582  C   GLN B 415     5140   6067   6091    547   -166     70       C  
ATOM   3583  O   GLN B 415      12.399 -30.895  23.126  1.00 45.68           O  
ANISOU 3583  O   GLN B 415     5061   6132   6165    507   -129    107       O  
ATOM   3584  CB  GLN B 415      13.064 -30.723  19.894  1.00 47.30           C  
ANISOU 3584  CB  GLN B 415     5274   6542   6157    482   -336    -33       C  
ATOM   3585  CG  GLN B 415      12.653 -29.960  18.650  1.00 55.67           C  
ANISOU 3585  CG  GLN B 415     6237   7817   7100    531   -438     -9       C  
ATOM   3586  CD  GLN B 415      12.370 -30.879  17.475  1.00 63.34           C  
ANISOU 3586  CD  GLN B 415     7163   8906   7999    372   -518   -144       C  
ATOM   3587  OE1 GLN B 415      12.935 -30.712  16.392  1.00 66.66           O  
ANISOU 3587  OE1 GLN B 415     7626   9394   8308    385   -573   -183       O  
ATOM   3588  NE2 GLN B 415      11.498 -31.860  17.685  1.00 61.99           N  
ANISOU 3588  NE2 GLN B 415     6905   8765   7884    208   -520   -221       N  
ATOM   3589  N   ALA B 416      14.526 -31.351  22.552  1.00 41.32           N  
ANISOU 3589  N   ALA B 416     4763   5360   5578    532   -129     24       N  
ATOM   3590  CA  ALA B 416      14.758 -32.238  23.682  1.00 39.09           C  
ANISOU 3590  CA  ALA B 416     4554   4916   5383    474    -49     28       C  
ATOM   3591  C   ALA B 416      14.662 -31.475  24.999  1.00 41.63           C  
ANISOU 3591  C   ALA B 416     4869   5219   5730    575     23    138       C  
ATOM   3592  O   ALA B 416      14.072 -31.958  25.965  1.00 41.84           O  
ANISOU 3592  O   ALA B 416     4862   5221   5814    514     82    173       O  
ATOM   3593  CB  ALA B 416      16.111 -32.920  23.553  1.00 37.47           C  
ANISOU 3593  CB  ALA B 416     4509   4543   5187    476    -30    -31       C  
ATOM   3594  N   LEU B 417      15.239 -30.279  25.026  1.00 39.46           N  
ANISOU 3594  N   LEU B 417     4630   4956   5407    719     21    187       N  
ATOM   3595  CA  LEU B 417      15.212 -29.444  26.220  1.00 39.95           C  
ANISOU 3595  CA  LEU B 417     4698   4999   5481    819     88    268       C  
ATOM   3596  C   LEU B 417      13.780 -29.053  26.572  1.00 41.34           C  
ANISOU 3596  C   LEU B 417     4718   5312   5677    827    104    312       C  
ATOM   3597  O   LEU B 417      13.373 -29.112  27.733  1.00 40.26           O  
ANISOU 3597  O   LEU B 417     4557   5167   5573    826    180    352       O  
ATOM   3598  CB  LEU B 417      16.061 -28.189  26.008  1.00 38.70           C  
ANISOU 3598  CB  LEU B 417     4610   4824   5270    954     77    297       C  
ATOM   3599  CG  LEU B 417      16.109 -27.184  27.162  1.00 37.28           C  
ANISOU 3599  CG  LEU B 417     4454   4617   5095   1060    145    357       C  
ATOM   3600  CD1 LEU B 417      16.684 -27.836  28.418  1.00 30.19           C  
ANISOU 3600  CD1 LEU B 417     3634   3618   4219   1024    215    362       C  
ATOM   3601  CD2 LEU B 417      16.916 -25.945  26.766  1.00 30.71           C  
ANISOU 3601  CD2 LEU B 417     3696   3754   4217   1166    128    376       C  
ATOM   3602  N   GLU B 418      13.021 -28.656  25.557  1.00 44.21           N  
ANISOU 3602  N   GLU B 418     4966   5821   6011    838     32    306       N  
ATOM   3603  CA  GLU B 418      11.643 -28.229  25.749  1.00 46.56           C  
ANISOU 3603  CA  GLU B 418     5088   6280   6323    865     37    349       C  
ATOM   3604  C   GLU B 418      10.812 -29.326  26.406  1.00 47.63           C  
ANISOU 3604  C   GLU B 418     5138   6446   6515    714     83    333       C  
ATOM   3605  O   GLU B 418      10.123 -29.084  27.397  1.00 49.01           O  
ANISOU 3605  O   GLU B 418     5233   6671   6716    743    157    382       O  
ATOM   3606  CB  GLU B 418      11.020 -27.814  24.414  1.00 53.18           C  
ANISOU 3606  CB  GLU B 418     5809   7287   7111    888    -66    348       C  
ATOM   3607  CG  GLU B 418       9.623 -27.236  24.542  1.00 58.33           C  
ANISOU 3607  CG  GLU B 418     6261   8130   7774    953    -70    404       C  
ATOM   3608  CD  GLU B 418       9.119 -26.631  23.247  1.00 62.87           C  
ANISOU 3608  CD  GLU B 418     6726   8877   8284   1017   -180    431       C  
ATOM   3609  OE1 GLU B 418       9.574 -27.061  22.166  1.00 59.43           O  
ANISOU 3609  OE1 GLU B 418     6334   8458   7789    938   -261    379       O  
ATOM   3610  OE2 GLU B 418       8.263 -25.724  23.313  1.00 68.66           O  
ANISOU 3610  OE2 GLU B 418     7328   9739   9021   1155   -184    507       O  
ATOM   3611  N   LEU B 419      10.884 -30.532  25.851  1.00 47.47           N  
ANISOU 3611  N   LEU B 419     5137   6390   6508    547     47    261       N  
ATOM   3612  CA  LEU B 419      10.152 -31.669  26.395  1.00 46.76           C  
ANISOU 3612  CA  LEU B 419     4986   6302   6480    372     92    246       C  
ATOM   3613  C   LEU B 419      10.636 -31.988  27.805  1.00 47.65           C  
ANISOU 3613  C   LEU B 419     5205   6265   6633    376    200    301       C  
ATOM   3614  O   LEU B 419       9.837 -32.243  28.705  1.00 50.50           O  
ANISOU 3614  O   LEU B 419     5482   6680   7027    316    271    348       O  
ATOM   3615  CB  LEU B 419      10.306 -32.894  25.488  1.00 45.89           C  
ANISOU 3615  CB  LEU B 419     4917   6136   6385    194     36    142       C  
ATOM   3616  CG  LEU B 419       9.529 -34.150  25.891  1.00 48.23           C  
ANISOU 3616  CG  LEU B 419     5160   6413   6753    -22     76    116       C  
ATOM   3617  CD1 LEU B 419       8.035 -33.863  25.936  1.00 51.59           C  
ANISOU 3617  CD1 LEU B 419     5347   7080   7175    -75     67    145       C  
ATOM   3618  CD2 LEU B 419       9.822 -35.303  24.943  1.00 45.32           C  
ANISOU 3618  CD2 LEU B 419     4867   5950   6402   -187     23     -9       C  
ATOM   3619  N   GLN B 420      11.952 -31.967  27.990  1.00 47.05           N  
ANISOU 3619  N   GLN B 420     5308   6024   6547    445    212    299       N  
ATOM   3620  CA  GLN B 420      12.552 -32.237  29.292  1.00 43.98           C  
ANISOU 3620  CA  GLN B 420     5027   5506   6177    463    300    358       C  
ATOM   3621  C   GLN B 420      11.960 -31.351  30.386  1.00 44.05           C  
ANISOU 3621  C   GLN B 420     4958   5614   6165    554    375    430       C  
ATOM   3622  O   GLN B 420      11.549 -31.837  31.437  1.00 45.78           O  
ANISOU 3622  O   GLN B 420     5158   5832   6403    490    455    482       O  
ATOM   3623  CB  GLN B 420      14.067 -32.034  29.223  1.00 41.77           C  
ANISOU 3623  CB  GLN B 420     4916   5087   5868    559    286    346       C  
ATOM   3624  CG  GLN B 420      14.756 -31.986  30.578  1.00 43.37           C  
ANISOU 3624  CG  GLN B 420     5215   5203   6061    615    363    415       C  
ATOM   3625  CD  GLN B 420      14.771 -33.328  31.287  1.00 44.35           C  
ANISOU 3625  CD  GLN B 420     5395   5216   6238    496    415    453       C  
ATOM   3626  OE1 GLN B 420      14.546 -34.373  30.675  1.00 45.93           O  
ANISOU 3626  OE1 GLN B 420     5603   5352   6495    372    391    410       O  
ATOM   3627  NE2 GLN B 420      15.047 -33.304  32.587  1.00 41.30           N  
ANISOU 3627  NE2 GLN B 420     5058   4805   5830    531    487    535       N  
ATOM   3628  N   LEU B 421      11.919 -30.048  30.129  1.00 42.96           N  
ANISOU 3628  N   LEU B 421     4782   5556   5985    705    353    433       N  
ATOM   3629  CA  LEU B 421      11.435 -29.085  31.111  1.00 44.47           C  
ANISOU 3629  CA  LEU B 421     4916   5825   6157    818    428    480       C  
ATOM   3630  C   LEU B 421       9.942 -29.243  31.391  1.00 46.51           C  
ANISOU 3630  C   LEU B 421     4979   6254   6440    762    468    503       C  
ATOM   3631  O   LEU B 421       9.503 -29.104  32.531  1.00 45.83           O  
ANISOU 3631  O   LEU B 421     4851   6216   6345    780    564    542       O  
ATOM   3632  CB  LEU B 421      11.746 -27.659  30.655  1.00 45.71           C  
ANISOU 3632  CB  LEU B 421     5093   5997   6280    993    395    474       C  
ATOM   3633  CG  LEU B 421      13.235 -27.338  30.496  1.00 43.37           C  
ANISOU 3633  CG  LEU B 421     4976   5552   5951   1047    369    456       C  
ATOM   3634  CD1 LEU B 421      13.420 -25.937  29.936  1.00 38.52           C  
ANISOU 3634  CD1 LEU B 421     4376   4948   5312   1196    337    459       C  
ATOM   3635  CD2 LEU B 421      13.973 -27.500  31.825  1.00 39.89           C  
ANISOU 3635  CD2 LEU B 421     4644   5022   5491   1048    448    474       C  
ATOM   3636  N   LYS B 422       9.165 -29.532  30.352  1.00 44.35           N  
ANISOU 3636  N   LYS B 422     4575   6091   6185    691    395    475       N  
ATOM   3637  CA  LYS B 422       7.729 -29.735  30.513  1.00 51.18           C  
ANISOU 3637  CA  LYS B 422     5227   7148   7073    621    422    493       C  
ATOM   3638  C   LYS B 422       7.425 -30.983  31.337  1.00 52.10           C  
ANISOU 3638  C   LYS B 422     5340   7230   7225    427    498    514       C  
ATOM   3639  O   LYS B 422       6.468 -31.007  32.106  1.00 56.56           O  
ANISOU 3639  O   LYS B 422     5766   7927   7796    394    578    554       O  
ATOM   3640  CB  LYS B 422       7.034 -29.805  29.150  1.00 57.73           C  
ANISOU 3640  CB  LYS B 422     5914   8120   7901    573    310    454       C  
ATOM   3641  CG  LYS B 422       6.869 -28.451  28.480  1.00 64.04           C  
ANISOU 3641  CG  LYS B 422     6650   9020   8663    778    252    473       C  
ATOM   3642  CD  LYS B 422       6.202 -28.568  27.116  1.00 70.58           C  
ANISOU 3642  CD  LYS B 422     7333  10016   9469    728    131    445       C  
ATOM   3643  CE  LYS B 422       6.041 -27.202  26.465  1.00 71.51           C  
ANISOU 3643  CE  LYS B 422     7395  10227   9549    949     73    493       C  
ATOM   3644  NZ  LYS B 422       5.576 -27.304  25.055  1.00 74.81           N  
ANISOU 3644  NZ  LYS B 422     7694  10811   9919    906    -61    476       N  
ATOM   3645  N   LEU B 423       8.247 -32.015  31.176  1.00 50.11           N  
ANISOU 3645  N   LEU B 423     5243   6799   6999    305    478    492       N  
ATOM   3646  CA  LEU B 423       8.073 -33.255  31.923  1.00 50.79           C  
ANISOU 3646  CA  LEU B 423     5361   6809   7129    121    549    527       C  
ATOM   3647  C   LEU B 423       8.639 -33.152  33.337  1.00 51.49           C  
ANISOU 3647  C   LEU B 423     5560   6815   7189    186    653    607       C  
ATOM   3648  O   LEU B 423       8.074 -33.701  34.281  1.00 53.43           O  
ANISOU 3648  O   LEU B 423     5761   7096   7443     83    744    673       O  
ATOM   3649  CB  LEU B 423       8.742 -34.419  31.190  1.00 51.26           C  
ANISOU 3649  CB  LEU B 423     5554   6686   7236    -17    491    471       C  
ATOM   3650  CG  LEU B 423       8.112 -34.901  29.885  1.00 50.06           C  
ANISOU 3650  CG  LEU B 423     5301   6610   7109   -153    399    377       C  
ATOM   3651  CD1 LEU B 423       8.949 -36.018  29.281  1.00 51.15           C  
ANISOU 3651  CD1 LEU B 423     5609   6532   7292   -265    361    306       C  
ATOM   3652  CD2 LEU B 423       6.692 -35.371  30.129  1.00 50.68           C  
ANISOU 3652  CD2 LEU B 423     5183   6854   7220   -327    436    394       C  
ATOM   3653  N   ASN B 424       9.757 -32.446  33.476  1.00 48.18           N  
ANISOU 3653  N   ASN B 424     5279   6300   6725    346    638    603       N  
ATOM   3654  CA  ASN B 424      10.470 -32.383  34.747  1.00 44.96           C  
ANISOU 3654  CA  ASN B 424     4991   5816   6274    402    718    667       C  
ATOM   3655  C   ASN B 424      10.000 -31.240  35.644  1.00 47.06           C  
ANISOU 3655  C   ASN B 424     5178   6225   6477    533    794    688       C  
ATOM   3656  O   ASN B 424      10.170 -31.292  36.861  1.00 49.27           O  
ANISOU 3656  O   ASN B 424     5504   6508   6707    540    882    744       O  
ATOM   3657  CB  ASN B 424      11.977 -32.267  34.503  1.00 44.05           C  
ANISOU 3657  CB  ASN B 424     5062   5537   6139    490    664    645       C  
ATOM   3658  CG  ASN B 424      12.801 -32.753  35.682  1.00 49.50           C  
ANISOU 3658  CG  ASN B 424     5885   6127   6796    489    725    721       C  
ATOM   3659  OD1 ASN B 424      12.394 -33.662  36.407  1.00 49.40           O  
ANISOU 3659  OD1 ASN B 424     5870   6100   6801    373    790    796       O  
ATOM   3660  ND2 ASN B 424      13.972 -32.155  35.872  1.00 48.62           N  
ANISOU 3660  ND2 ASN B 424     5887   5953   6631    611    703    709       N  
ATOM   3661  N   HIS B 425       9.419 -30.210  35.038  1.00 47.04           N  
ANISOU 3661  N   HIS B 425     5060   6341   6472    644    763    641       N  
ATOM   3662  CA  HIS B 425       8.915 -29.057  35.782  1.00 48.99           C  
ANISOU 3662  CA  HIS B 425     5230   6710   6673    790    839    642       C  
ATOM   3663  C   HIS B 425       7.525 -28.677  35.284  1.00 52.46           C  
ANISOU 3663  C   HIS B 425     5445   7345   7144    811    836    631       C  
ATOM   3664  O   HIS B 425       7.328 -27.580  34.761  1.00 49.53           O  
ANISOU 3664  O   HIS B 425     5022   7025   6772    971    802    601       O  
ATOM   3665  CB  HIS B 425       9.855 -27.856  35.633  1.00 46.00           C  
ANISOU 3665  CB  HIS B 425     4973   6247   6259    969    807    599       C  
ATOM   3666  CG  HIS B 425      11.269 -28.132  36.042  1.00 47.20           C  
ANISOU 3666  CG  HIS B 425     5323   6237   6374    957    797    604       C  
ATOM   3667  ND1 HIS B 425      11.731 -27.915  37.323  1.00 48.47           N  
ANISOU 3667  ND1 HIS B 425     5564   6390   6465    991    878    623       N  
ATOM   3668  CD2 HIS B 425      12.328 -28.593  35.334  1.00 44.03           C  
ANISOU 3668  CD2 HIS B 425     5044   5696   5988    922    714    591       C  
ATOM   3669  CE1 HIS B 425      13.010 -28.239  37.389  1.00 49.48           C  
ANISOU 3669  CE1 HIS B 425     5847   6386   6569    977    838    628       C  
ATOM   3670  NE2 HIS B 425      13.397 -28.653  36.195  1.00 43.81           N  
ANISOU 3670  NE2 HIS B 425     5156   5584   5907    940    743    609       N  
ATOM   3671  N   PRO B 426       6.553 -29.584  35.452  1.00 56.35           N  
ANISOU 3671  N   PRO B 426     5797   7949   7664    649    873    663       N  
ATOM   3672  CA  PRO B 426       5.207 -29.406  34.901  1.00 56.50           C  
ANISOU 3672  CA  PRO B 426     5573   8182   7713    638    858    654       C  
ATOM   3673  C   PRO B 426       4.545 -28.111  35.356  1.00 58.22           C  
ANISOU 3673  C   PRO B 426     5668   8552   7903    847    924    649       C  
ATOM   3674  O   PRO B 426       3.726 -27.558  34.623  1.00 60.53           O  
ANISOU 3674  O   PRO B 426     5788   8992   8218    931    877    637       O  
ATOM   3675  CB  PRO B 426       4.443 -30.615  35.465  1.00 59.46           C  
ANISOU 3675  CB  PRO B 426     5850   8634   8109    409    928    700       C  
ATOM   3676  CG  PRO B 426       5.260 -31.057  36.649  1.00 58.13           C  
ANISOU 3676  CG  PRO B 426     5862   8324   7902    372   1016    753       C  
ATOM   3677  CD  PRO B 426       6.661 -30.855  36.185  1.00 56.07           C  
ANISOU 3677  CD  PRO B 426     5820   7848   7634    457    932    720       C  
ATOM   3678  N   GLU B 427       4.899 -27.630  36.543  1.00 59.26           N  
ANISOU 3678  N   GLU B 427     5885   8648   7981    938   1032    656       N  
ATOM   3679  CA  GLU B 427       4.237 -26.460  37.112  1.00 64.34           C  
ANISOU 3679  CA  GLU B 427     6420   9427   8600   1134   1119    635       C  
ATOM   3680  C   GLU B 427       4.986 -25.154  36.853  1.00 62.20           C  
ANISOU 3680  C   GLU B 427     6284   9029   8321   1356   1085    586       C  
ATOM   3681  O   GLU B 427       4.556 -24.091  37.297  1.00 60.44           O  
ANISOU 3681  O   GLU B 427     6007   8872   8086   1541   1159    556       O  
ATOM   3682  CB  GLU B 427       4.011 -26.651  38.614  1.00 70.17           C  
ANISOU 3682  CB  GLU B 427     7151  10239   9272   1098   1273    656       C  
ATOM   3683  CG  GLU B 427       3.189 -27.880  38.962  1.00 79.68           C  
ANISOU 3683  CG  GLU B 427     8215  11575  10483    872   1326    720       C  
ATOM   3684  CD  GLU B 427       2.675 -27.855  40.391  1.00 89.75           C  
ANISOU 3684  CD  GLU B 427     9426  12994  11682    866   1493    747       C  
ATOM   3685  OE1 GLU B 427       2.905 -26.845  41.091  1.00 91.10           O  
ANISOU 3685  OE1 GLU B 427     9652  13172  11791   1050   1566    698       O  
ATOM   3686  OE2 GLU B 427       2.037 -28.844  40.811  1.00 93.60           O  
ANISOU 3686  OE2 GLU B 427     9810  13588  12165    671   1556    814       O  
ATOM   3687  N   SER B 428       6.098 -25.235  36.130  1.00 58.02           N  
ANISOU 3687  N   SER B 428     5930   8315   7801   1336    982    576       N  
ATOM   3688  CA  SER B 428       6.899 -24.053  35.828  1.00 56.89           C  
ANISOU 3688  CA  SER B 428     5928   8036   7652   1512    947    537       C  
ATOM   3689  C   SER B 428       6.602 -23.524  34.430  1.00 56.92           C  
ANISOU 3689  C   SER B 428     5861   8062   7705   1602    835    546       C  
ATOM   3690  O   SER B 428       7.281 -23.875  33.464  1.00 55.12           O  
ANISOU 3690  O   SER B 428     5717   7742   7486   1534    727    550       O  
ATOM   3691  CB  SER B 428       8.390 -24.367  35.962  1.00 61.24           C  
ANISOU 3691  CB  SER B 428     6712   8387   8170   1444    912    525       C  
ATOM   3692  OG  SER B 428       8.705 -24.799  37.273  1.00 68.51           O  
ANISOU 3692  OG  SER B 428     7700   9300   9030   1376   1008    530       O  
ATOM   3693  N   SER B 429       5.588 -22.672  34.328  1.00 57.25           N  
ANISOU 3693  N   SER B 429     5745   8236   7772   1764    863    552       N  
ATOM   3694  CA  SER B 429       5.186 -22.115  33.043  1.00 58.06           C  
ANISOU 3694  CA  SER B 429     5760   8390   7911   1871    757    583       C  
ATOM   3695  C   SER B 429       6.334 -21.380  32.352  1.00 50.37           C  
ANISOU 3695  C   SER B 429     4991   7213   6934   1954    683    580       C  
ATOM   3696  O   SER B 429       7.049 -20.593  32.976  1.00 45.00           O  
ANISOU 3696  O   SER B 429     4473   6382   6244   2049    744    546       O  
ATOM   3697  CB  SER B 429       3.991 -21.175  33.222  1.00 64.39           C  
ANISOU 3697  CB  SER B 429     6373   9351   8742   2078    816    597       C  
ATOM   3698  OG  SER B 429       3.563 -20.651  31.977  1.00 65.61           O  
ANISOU 3698  OG  SER B 429     6431   9572   8925   2192    705    649       O  
ATOM   3699  N   GLN B 430       6.499 -21.646  31.060  1.00 48.62           N  
ANISOU 3699  N   GLN B 430     4759   7000   6713   1904    554    610       N  
ATOM   3700  CA  GLN B 430       7.499 -20.964  30.241  1.00 47.70           C  
ANISOU 3700  CA  GLN B 430     4812   6725   6588   1973    479    623       C  
ATOM   3701  C   GLN B 430       8.913 -21.055  30.814  1.00 47.42           C  
ANISOU 3701  C   GLN B 430     5011   6481   6525   1903    512    577       C  
ATOM   3702  O   GLN B 430       9.716 -20.138  30.643  1.00 47.74           O  
ANISOU 3702  O   GLN B 430     5201   6375   6563   1997    506    576       O  
ATOM   3703  CB  GLN B 430       7.112 -19.498  30.020  1.00 46.26           C  
ANISOU 3703  CB  GLN B 430     4615   6525   6437   2221    491    663       C  
ATOM   3704  CG  GLN B 430       5.834 -19.308  29.213  1.00 45.26           C  
ANISOU 3704  CG  GLN B 430     4256   6613   6330   2319    429    731       C  
ATOM   3705  CD  GLN B 430       5.899 -19.966  27.845  1.00 50.48           C  
ANISOU 3705  CD  GLN B 430     4866   7362   6953   2200    282    766       C  
ATOM   3706  OE1 GLN B 430       5.100 -20.846  27.528  1.00 57.55           O  
ANISOU 3706  OE1 GLN B 430     5577   8454   7837   2081    236    764       O  
ATOM   3707  NE2 GLN B 430       6.860 -19.547  27.031  1.00 44.83           N  
ANISOU 3707  NE2 GLN B 430     4314   6508   6210   2219    212    792       N  
ATOM   3708  N   LEU B 431       9.217 -22.161  31.486  1.00 43.22           N  
ANISOU 3708  N   LEU B 431     4506   5942   5975   1737    547    546       N  
ATOM   3709  CA  LEU B 431      10.570 -22.386  31.985  1.00 40.60           C  
ANISOU 3709  CA  LEU B 431     4374   5443   5610   1666    564    513       C  
ATOM   3710  C   LEU B 431      11.536 -22.387  30.804  1.00 36.64           C  
ANISOU 3710  C   LEU B 431     3980   4846   5097   1636    458    517       C  
ATOM   3711  O   LEU B 431      12.616 -21.804  30.868  1.00 38.13           O  
ANISOU 3711  O   LEU B 431     4325   4899   5265   1671    459    501       O  
ATOM   3712  CB  LEU B 431      10.662 -23.723  32.719  1.00 40.66           C  
ANISOU 3712  CB  LEU B 431     4379   5467   5602   1494    601    505       C  
ATOM   3713  CG  LEU B 431      11.568 -23.785  33.955  1.00 44.43           C  
ANISOU 3713  CG  LEU B 431     5001   5846   6036   1470    677    483       C  
ATOM   3714  CD1 LEU B 431      12.032 -25.216  34.213  1.00 36.59           C  
ANISOU 3714  CD1 LEU B 431     4049   4820   5033   1298    668    500       C  
ATOM   3715  CD2 LEU B 431      12.754 -22.848  33.849  1.00 41.63           C  
ANISOU 3715  CD2 LEU B 431     4813   5349   5657   1551    657    452       C  
ATOM   3716  N   PHE B 432      11.129 -23.052  29.729  1.00 36.69           N  
ANISOU 3716  N   PHE B 432     3892   4941   5108   1560    370    534       N  
ATOM   3717  CA  PHE B 432      11.906 -23.103  28.495  1.00 37.34           C  
ANISOU 3717  CA  PHE B 432     4052   4973   5165   1530    270    535       C  
ATOM   3718  C   PHE B 432      12.349 -21.705  28.072  1.00 40.37           C  
ANISOU 3718  C   PHE B 432     4521   5279   5539   1683    256    569       C  
ATOM   3719  O   PHE B 432      13.541 -21.447  27.896  1.00 40.91           O  
ANISOU 3719  O   PHE B 432     4742   5221   5582   1669    244    556       O  
ATOM   3720  CB  PHE B 432      11.077 -23.767  27.392  1.00 36.56           C  
ANISOU 3720  CB  PHE B 432     3804   5027   5061   1456    181    542       C  
ATOM   3721  CG  PHE B 432      11.810 -23.942  26.092  1.00 41.28           C  
ANISOU 3721  CG  PHE B 432     4469   5602   5613   1410     81    532       C  
ATOM   3722  CD1 PHE B 432      13.004 -24.643  26.043  1.00 36.06           C  
ANISOU 3722  CD1 PHE B 432     3950   4818   4934   1309     77    482       C  
ATOM   3723  CD2 PHE B 432      11.291 -23.428  24.913  1.00 45.08           C  
ANISOU 3723  CD2 PHE B 432     4863   6204   6062   1473     -6    575       C  
ATOM   3724  CE1 PHE B 432      13.676 -24.813  24.846  1.00 41.04           C  
ANISOU 3724  CE1 PHE B 432     4635   5445   5515   1270     -3    462       C  
ATOM   3725  CE2 PHE B 432      11.958 -23.595  23.711  1.00 44.61           C  
ANISOU 3725  CE2 PHE B 432     4863   6146   5940   1425    -92    564       C  
ATOM   3726  CZ  PHE B 432      13.152 -24.290  23.678  1.00 42.65           C  
ANISOU 3726  CZ  PHE B 432     4757   5775   5675   1321    -85    501       C  
ATOM   3727  N   ALA B 433      11.383 -20.802  27.930  1.00 39.54           N  
ANISOU 3727  N   ALA B 433     4315   5250   5459   1829    262    616       N  
ATOM   3728  CA  ALA B 433      11.666 -19.426  27.534  1.00 39.78           C  
ANISOU 3728  CA  ALA B 433     4429   5188   5496   1987    256    665       C  
ATOM   3729  C   ALA B 433      12.584 -18.717  28.529  1.00 39.34           C  
ANISOU 3729  C   ALA B 433     4548   4949   5449   2024    344    621       C  
ATOM   3730  O   ALA B 433      13.525 -18.028  28.134  1.00 39.11           O  
ANISOU 3730  O   ALA B 433     4663   4789   5407   2044    326    634       O  
ATOM   3731  CB  ALA B 433      10.368 -18.645  27.361  1.00 39.41           C  
ANISOU 3731  CB  ALA B 433     4232   5253   5487   2161    259    727       C  
ATOM   3732  N   LYS B 434      12.303 -18.883  29.817  1.00 38.59           N  
ANISOU 3732  N   LYS B 434     4437   4859   5368   2021    440    568       N  
ATOM   3733  CA  LYS B 434      13.112 -18.260  30.863  1.00 46.06           C  
ANISOU 3733  CA  LYS B 434     5537   5659   6306   2042    524    510       C  
ATOM   3734  C   LYS B 434      14.573 -18.685  30.752  1.00 42.59           C  
ANISOU 3734  C   LYS B 434     5244   5119   5820   1909    489    482       C  
ATOM   3735  O   LYS B 434      15.484 -17.867  30.880  1.00 43.11           O  
ANISOU 3735  O   LYS B 434     5454   5051   5876   1929    505    459       O  
ATOM   3736  CB  LYS B 434      12.574 -18.618  32.251  1.00 50.45           C  
ANISOU 3736  CB  LYS B 434     6035   6279   6854   2031    627    457       C  
ATOM   3737  CG  LYS B 434      11.212 -18.023  32.580  1.00 58.10           C  
ANISOU 3737  CG  LYS B 434     6863   7345   7865   2184    692    467       C  
ATOM   3738  CD  LYS B 434      10.748 -18.468  33.962  1.00 61.65           C  
ANISOU 3738  CD  LYS B 434     7255   7879   8288   2150    802    414       C  
ATOM   3739  CE  LYS B 434       9.365 -17.928  34.299  1.00 68.86           C  
ANISOU 3739  CE  LYS B 434     8005   8917   9241   2306    877    417       C  
ATOM   3740  NZ  LYS B 434       9.385 -16.467  34.589  1.00 70.22           N  
ANISOU 3740  NZ  LYS B 434     8270   8964   9447   2501    943    375       N  
ATOM   3741  N   LEU B 435      14.784 -19.972  30.512  1.00 43.07           N  
ANISOU 3741  N   LEU B 435     5264   5243   5856   1773    442    480       N  
ATOM   3742  CA  LEU B 435      16.125 -20.523  30.385  1.00 44.17           C  
ANISOU 3742  CA  LEU B 435     5518   5308   5956   1661    409    455       C  
ATOM   3743  C   LEU B 435      16.861 -19.915  29.193  1.00 42.10           C  
ANISOU 3743  C   LEU B 435     5331   4985   5680   1677    341    483       C  
ATOM   3744  O   LEU B 435      18.030 -19.534  29.301  1.00 41.01           O  
ANISOU 3744  O   LEU B 435     5317   4750   5515   1647    346    461       O  
ATOM   3745  CB  LEU B 435      16.049 -22.043  30.252  1.00 47.26           C  
ANISOU 3745  CB  LEU B 435     5846   5769   6341   1533    376    451       C  
ATOM   3746  CG  LEU B 435      17.355 -22.823  30.366  1.00 52.09           C  
ANISOU 3746  CG  LEU B 435     6560   6313   6920   1433    358    424       C  
ATOM   3747  CD1 LEU B 435      18.210 -22.273  31.504  1.00 55.90           C  
ANISOU 3747  CD1 LEU B 435     7149   6722   7370   1450    419    395       C  
ATOM   3748  CD2 LEU B 435      17.058 -24.302  30.566  1.00 50.72           C  
ANISOU 3748  CD2 LEU B 435     6330   6181   6760   1325    355    422       C  
ATOM   3749  N   LEU B 436      16.169 -19.815  28.061  1.00 38.48           N  
ANISOU 3749  N   LEU B 436     4789   4601   5231   1717    276    537       N  
ATOM   3750  CA  LEU B 436      16.755 -19.229  26.860  1.00 39.96           C  
ANISOU 3750  CA  LEU B 436     5038   4753   5391   1734    212    582       C  
ATOM   3751  C   LEU B 436      17.168 -17.786  27.108  1.00 39.38           C  
ANISOU 3751  C   LEU B 436     5083   4543   5336   1829    258    604       C  
ATOM   3752  O   LEU B 436      18.181 -17.324  26.584  1.00 38.96           O  
ANISOU 3752  O   LEU B 436     5139   4410   5254   1796    238    619       O  
ATOM   3753  CB  LEU B 436      15.783 -19.298  25.683  1.00 40.95           C  
ANISOU 3753  CB  LEU B 436     5040   5011   5510   1776    134    646       C  
ATOM   3754  CG  LEU B 436      15.415 -20.704  25.210  1.00 41.37           C  
ANISOU 3754  CG  LEU B 436     4984   5194   5539   1657     78    611       C  
ATOM   3755  CD1 LEU B 436      14.698 -20.628  23.884  1.00 45.47           C  
ANISOU 3755  CD1 LEU B 436     5399   5853   6022   1685    -15    669       C  
ATOM   3756  CD2 LEU B 436      16.655 -21.581  25.096  1.00 41.10           C  
ANISOU 3756  CD2 LEU B 436     5045   5102   5468   1527     67    550       C  
ATOM   3757  N   GLN B 437      16.379 -17.081  27.913  1.00 39.00           N  
ANISOU 3757  N   GLN B 437     5014   4466   5338   1943    325    600       N  
ATOM   3758  CA  GLN B 437      16.683 -15.700  28.270  1.00 42.32           C  
ANISOU 3758  CA  GLN B 437     5559   4728   5791   2036    383    601       C  
ATOM   3759  C   GLN B 437      17.980 -15.614  29.067  1.00 45.36           C  
ANISOU 3759  C   GLN B 437     6085   5004   6145   1933    427    520       C  
ATOM   3760  O   GLN B 437      18.726 -14.644  28.947  1.00 51.59           O  
ANISOU 3760  O   GLN B 437     7006   5657   6941   1935    444    522       O  
ATOM   3761  CB  GLN B 437      15.532 -15.081  29.069  1.00 44.88           C  
ANISOU 3761  CB  GLN B 437     5824   5053   6175   2186    459    589       C  
ATOM   3762  CG  GLN B 437      14.275 -14.818  28.247  1.00 47.68           C  
ANISOU 3762  CG  GLN B 437     6041   5508   6566   2326    416    684       C  
ATOM   3763  CD  GLN B 437      13.136 -14.252  29.078  1.00 55.13           C  
ANISOU 3763  CD  GLN B 437     6907   6471   7571   2488    501    665       C  
ATOM   3764  OE1 GLN B 437      12.376 -13.403  28.612  1.00 57.68           O  
ANISOU 3764  OE1 GLN B 437     7188   6784   7945   2662    497    740       O  
ATOM   3765  NE2 GLN B 437      13.018 -14.717  30.316  1.00 57.64           N  
ANISOU 3765  NE2 GLN B 437     7201   6822   7878   2441    582    570       N  
ATOM   3766  N   LYS B 438      18.244 -16.628  29.885  1.00 35.28           N  
ANISOU 3766  N   LYS B 438     4778   3792   4835   1837    445    455       N  
ATOM   3767  CA  LYS B 438      19.471 -16.662  30.677  1.00 42.89           C  
ANISOU 3767  CA  LYS B 438     5850   4690   5754   1739    476    384       C  
ATOM   3768  C   LYS B 438      20.716 -16.797  29.802  1.00 50.17           C  
ANISOU 3768  C   LYS B 438     6839   5587   6639   1643    414    403       C  
ATOM   3769  O   LYS B 438      21.767 -16.241  30.123  1.00 50.43           O  
ANISOU 3769  O   LYS B 438     6977   5537   6646   1586    434    363       O  
ATOM   3770  CB  LYS B 438      19.423 -17.775  31.727  1.00 46.25           C  
ANISOU 3770  CB  LYS B 438     6221   5204   6146   1673    504    336       C  
ATOM   3771  CG  LYS B 438      18.996 -17.297  33.108  1.00 50.43           C  
ANISOU 3771  CG  LYS B 438     6767   5722   6671   1723    598    272       C  
ATOM   3772  CD  LYS B 438      17.531 -16.911  33.137  1.00 60.11           C  
ANISOU 3772  CD  LYS B 438     7897   6988   7953   1853    640    294       C  
ATOM   3773  CE  LYS B 438      17.252 -15.879  34.217  1.00 65.88           C  
ANISOU 3773  CE  LYS B 438     8687   7655   8689   1940    742    216       C  
ATOM   3774  NZ  LYS B 438      17.917 -16.209  35.504  1.00 68.52           N  
ANISOU 3774  NZ  LYS B 438     9077   8013   8945   1850    792    134       N  
ATOM   3775  N   MET B 439      20.598 -17.539  28.703  1.00 52.45           N  
ANISOU 3775  N   MET B 439     7057   5957   6915   1616    342    455       N  
ATOM   3776  CA  MET B 439      21.697 -17.664  27.751  1.00 59.22           C  
ANISOU 3776  CA  MET B 439     7962   6810   7727   1537    290    473       C  
ATOM   3777  C   MET B 439      22.177 -16.281  27.348  1.00 56.53           C  
ANISOU 3777  C   MET B 439     7729   6354   7394   1561    304    509       C  
ATOM   3778  O   MET B 439      23.372 -16.055  27.157  1.00 56.73           O  
ANISOU 3778  O   MET B 439     7830   6343   7382   1475    301    496       O  
ATOM   3779  CB  MET B 439      21.261 -18.448  26.513  1.00 61.10           C  
ANISOU 3779  CB  MET B 439     8110   7156   7948   1527    216    518       C  
ATOM   3780  CG  MET B 439      21.250 -19.952  26.706  1.00 61.27           C  
ANISOU 3780  CG  MET B 439     8061   7262   7958   1455    197    471       C  
ATOM   3781  SD  MET B 439      20.424 -20.834  25.366  1.00 75.72           S  
ANISOU 3781  SD  MET B 439     9778   9219   9774   1439    117    495       S  
ATOM   3782  CE  MET B 439      21.360 -20.259  23.952  1.00139.59           C  
ANISOU 3782  CE  MET B 439    17930  17315  17794   1420     68    536       C  
ATOM   3783  N   THR B 440      21.230 -15.356  27.234  1.00 54.74           N  
ANISOU 3783  N   THR B 440     7508   6071   7220   1679    324    559       N  
ATOM   3784  CA  THR B 440      21.540 -13.967  26.926  1.00 60.10           C  
ANISOU 3784  CA  THR B 440     8307   6602   7925   1717    349    605       C  
ATOM   3785  C   THR B 440      22.370 -13.334  28.037  1.00 65.43           C  
ANISOU 3785  C   THR B 440     9101   7154   8608   1656    419    512       C  
ATOM   3786  O   THR B 440      23.309 -12.583  27.773  1.00 71.95           O  
ANISOU 3786  O   THR B 440    10037   7878   9423   1585    429    520       O  
ATOM   3787  CB  THR B 440      20.251 -13.143  26.708  1.00 64.14           C  
ANISOU 3787  CB  THR B 440     8795   7069   8506   1888    362    679       C  
ATOM   3788  OG1 THR B 440      19.648 -13.521  25.464  1.00 66.53           O  
ANISOU 3788  OG1 THR B 440     8998   7494   8785   1930    281    782       O  
ATOM   3789  CG2 THR B 440      20.558 -11.650  26.686  1.00 62.08           C  
ANISOU 3789  CG2 THR B 440     8688   6603   8295   1937    411    713       C  
ATOM   3790  N   ASP B 441      22.023 -13.646  29.280  1.00 62.06           N  
ANISOU 3790  N   ASP B 441     8646   6746   8186   1672    469    423       N  
ATOM   3791  CA  ASP B 441      22.734 -13.104  30.432  1.00 59.50           C  
ANISOU 3791  CA  ASP B 441     8422   6334   7849   1611    533    317       C  
ATOM   3792  C   ASP B 441      24.125 -13.714  30.580  1.00 57.36           C  
ANISOU 3792  C   ASP B 441     8166   6125   7502   1452    503    274       C  
ATOM   3793  O   ASP B 441      25.002 -13.134  31.222  1.00 62.38           O  
ANISOU 3793  O   ASP B 441     8892   6696   8113   1368    536    199       O  
ATOM   3794  CB  ASP B 441      21.925 -13.333  31.707  1.00 62.06           C  
ANISOU 3794  CB  ASP B 441     8702   6699   8179   1674    595    240       C  
ATOM   3795  CG  ASP B 441      20.521 -12.772  31.613  1.00 67.17           C  
ANISOU 3795  CG  ASP B 441     9309   7312   8903   1846    632    277       C  
ATOM   3796  OD1 ASP B 441      20.282 -11.891  30.758  1.00 69.71           O  
ANISOU 3796  OD1 ASP B 441     9679   7527   9279   1925    622    352       O  
ATOM   3797  OD2 ASP B 441      19.659 -13.216  32.398  1.00 66.47           O  
ANISOU 3797  OD2 ASP B 441     9132   7309   8814   1905    673    240       O  
ATOM   3798  N   LEU B 442      24.319 -14.893  29.996  1.00 48.48           N  
ANISOU 3798  N   LEU B 442     6949   5131   6341   1414    441    312       N  
ATOM   3799  CA  LEU B 442      25.633 -15.525  29.981  1.00 46.81           C  
ANISOU 3799  CA  LEU B 442     6734   4987   6063   1290    410    284       C  
ATOM   3800  C   LEU B 442      26.553 -14.767  29.038  1.00 46.75           C  
ANISOU 3800  C   LEU B 442     6798   4924   6044   1220    393    322       C  
ATOM   3801  O   LEU B 442      27.702 -14.485  29.374  1.00 47.03           O  
ANISOU 3801  O   LEU B 442     6880   4952   6039   1113    403    273       O  
ATOM   3802  CB  LEU B 442      25.533 -16.986  29.539  1.00 46.12           C  
ANISOU 3802  CB  LEU B 442     6539   5030   5953   1285    357    311       C  
ATOM   3803  CG  LEU B 442      25.166 -18.024  30.596  1.00 50.75           C  
ANISOU 3803  CG  LEU B 442     7063   5690   6530   1294    371    273       C  
ATOM   3804  CD1 LEU B 442      23.971 -17.561  31.364  1.00 63.43           C  
ANISOU 3804  CD1 LEU B 442     8663   7262   8175   1378    425    260       C  
ATOM   3805  CD2 LEU B 442      24.874 -19.355  29.937  1.00 51.22           C  
ANISOU 3805  CD2 LEU B 442     7034   5834   6593   1294    323    307       C  
ATOM   3806  N   ARG B 443      26.034 -14.444  27.855  1.00 42.48           N  
ANISOU 3806  N   ARG B 443     6255   4358   5528   1275    367    414       N  
ATOM   3807  CA  ARG B 443      26.786 -13.696  26.854  1.00 45.94           C  
ANISOU 3807  CA  ARG B 443     6760   4746   5948   1212    356    477       C  
ATOM   3808  C   ARG B 443      27.283 -12.378  27.433  1.00 50.04           C  
ANISOU 3808  C   ARG B 443     7413   5103   6497   1159    415    442       C  
ATOM   3809  O   ARG B 443      28.416 -11.968  27.180  1.00 51.99           O  
ANISOU 3809  O   ARG B 443     7712   5332   6710   1032    421    438       O  
ATOM   3810  CB  ARG B 443      25.922 -13.431  25.618  1.00 49.61           C  
ANISOU 3810  CB  ARG B 443     7208   5209   6432   1304    321    597       C  
ATOM   3811  CG  ARG B 443      25.452 -14.682  24.885  1.00 54.81           C  
ANISOU 3811  CG  ARG B 443     7741   6033   7053   1332    258    620       C  
ATOM   3812  CD  ARG B 443      26.541 -15.254  23.992  1.00 60.36           C  
ANISOU 3812  CD  ARG B 443     8421   6839   7675   1228    223    626       C  
ATOM   3813  NE  ARG B 443      26.061 -16.365  23.172  1.00 58.98           N  
ANISOU 3813  NE  ARG B 443     8142   6804   7462   1253    166    637       N  
ATOM   3814  CZ  ARG B 443      25.765 -16.267  21.879  1.00 57.35           C  
ANISOU 3814  CZ  ARG B 443     7915   6666   7210   1271    121    718       C  
ATOM   3815  NH1 ARG B 443      25.902 -15.107  21.252  1.00 59.24           N  
ANISOU 3815  NH1 ARG B 443     8232   6839   7438   1277    129    819       N  
ATOM   3816  NH2 ARG B 443      25.336 -17.329  21.211  1.00 52.07           N  
ANISOU 3816  NH2 ARG B 443     7153   6131   6500   1278     70    700       N  
ATOM   3817  N   GLN B 444      26.431 -11.720  28.214  1.00 54.69           N  
ANISOU 3817  N   GLN B 444     8053   5575   7150   1250    465    408       N  
ATOM   3818  CA  GLN B 444      26.787 -10.455  28.851  1.00 60.39           C  
ANISOU 3818  CA  GLN B 444     8917   6118   7912   1206    531    349       C  
ATOM   3819  C   GLN B 444      27.867 -10.656  29.909  1.00 59.19           C  
ANISOU 3819  C   GLN B 444     8776   6016   7698   1062    547    219       C  
ATOM   3820  O   GLN B 444      28.818  -9.880  29.992  1.00 65.29           O  
ANISOU 3820  O   GLN B 444     9641   6707   8460    931    570    181       O  
ATOM   3821  CB  GLN B 444      25.553  -9.802  29.478  1.00 72.07           C  
ANISOU 3821  CB  GLN B 444    10438   7474   9472   1361    588    325       C  
ATOM   3822  CG  GLN B 444      25.858  -8.563  30.308  1.00 81.25           C  
ANISOU 3822  CG  GLN B 444    11757   8438  10677   1321    668    227       C  
ATOM   3823  CD  GLN B 444      26.379  -7.408  29.471  1.00 88.65           C  
ANISOU 3823  CD  GLN B 444    12834   9188  11661   1264    683    304       C  
ATOM   3824  OE1 GLN B 444      27.183  -6.601  29.938  1.00 91.21           O  
ANISOU 3824  OE1 GLN B 444    13283   9381  11993   1135    729    221       O  
ATOM   3825  NE2 GLN B 444      25.921  -7.325  28.226  1.00 90.29           N  
ANISOU 3825  NE2 GLN B 444    13022   9388  11895   1349    644    466       N  
ATOM   3826  N   ILE B 445      27.708 -11.698  30.719  1.00 56.46           N  
ANISOU 3826  N   ILE B 445     8334   5812   7308   1081    534    158       N  
ATOM   3827  CA  ILE B 445      28.691 -12.042  31.741  1.00 56.42           C  
ANISOU 3827  CA  ILE B 445     8315   5896   7227    962    535     51       C  
ATOM   3828  C   ILE B 445      30.069 -12.259  31.123  1.00 52.72           C  
ANISOU 3828  C   ILE B 445     7822   5510   6700    820    492     71       C  
ATOM   3829  O   ILE B 445      31.069 -11.726  31.603  1.00 50.57           O  
ANISOU 3829  O   ILE B 445     7596   5230   6389    684    506     -2       O  
ATOM   3830  CB  ILE B 445      28.282 -13.317  32.507  1.00 60.17           C  
ANISOU 3830  CB  ILE B 445     8679   6526   7659   1017    517     28       C  
ATOM   3831  CG1 ILE B 445      27.189 -12.999  33.528  1.00 64.72           C  
ANISOU 3831  CG1 ILE B 445     9279   7050   8262   1114    579    -33       C  
ATOM   3832  CG2 ILE B 445      29.485 -13.935  33.203  1.00 58.82           C  
ANISOU 3832  CG2 ILE B 445     8463   6491   7394    901    490    -32       C  
ATOM   3833  CD1 ILE B 445      27.676 -12.175  34.697  1.00 68.45           C  
ANISOU 3833  CD1 ILE B 445     9844   7470   8695   1038    632   -165       C  
ATOM   3834  N   VAL B 446      30.113 -13.042  30.053  1.00 48.94           N  
ANISOU 3834  N   VAL B 446     7262   5122   6211    846    443    162       N  
ATOM   3835  CA  VAL B 446      31.371 -13.346  29.384  1.00 48.83           C  
ANISOU 3835  CA  VAL B 446     7204   5210   6138    732    409    182       C  
ATOM   3836  C   VAL B 446      31.995 -12.092  28.787  1.00 51.16           C  
ANISOU 3836  C   VAL B 446     7601   5392   6447    622    437    209       C  
ATOM   3837  O   VAL B 446      33.174 -11.811  29.007  1.00 50.69           O  
ANISOU 3837  O   VAL B 446     7545   5377   6340    475    442    161       O  
ATOM   3838  CB  VAL B 446      31.179 -14.400  28.285  1.00 44.19           C  
ANISOU 3838  CB  VAL B 446     6521   4732   5536    794    361    261       C  
ATOM   3839  CG1 VAL B 446      32.441 -14.534  27.451  1.00 45.02           C  
ANISOU 3839  CG1 VAL B 446     6588   4936   5581    686    342    283       C  
ATOM   3840  CG2 VAL B 446      30.793 -15.729  28.906  1.00 42.78           C  
ANISOU 3840  CG2 VAL B 446     6248   4659   5345    868    336    230       C  
ATOM   3841  N   THR B 447      31.197 -11.337  28.036  1.00 52.01           N  
ANISOU 3841  N   THR B 447     7786   5357   6618    692    455    295       N  
ATOM   3842  CA  THR B 447      31.667 -10.097  27.433  1.00 54.88           C  
ANISOU 3842  CA  THR B 447     8267   5579   7006    597    489    347       C  
ATOM   3843  C   THR B 447      32.241  -9.165  28.496  1.00 59.27           C  
ANISOU 3843  C   THR B 447     8925   6018   7577    474    541    231       C  
ATOM   3844  O   THR B 447      33.239  -8.482  28.267  1.00 62.36           O  
ANISOU 3844  O   THR B 447     9373   6371   7951    308    560    227       O  
ATOM   3845  CB  THR B 447      30.535  -9.369  26.680  1.00 59.30           C  
ANISOU 3845  CB  THR B 447     8908   5980   7644    729    503    464       C  
ATOM   3846  OG1 THR B 447      29.956 -10.250  25.710  1.00 59.07           O  
ANISOU 3846  OG1 THR B 447     8774   6083   7587    832    447    558       O  
ATOM   3847  CG2 THR B 447      31.074  -8.136  25.975  1.00 61.24           C  
ANISOU 3847  CG2 THR B 447     9284   6069   7914    626    539    545       C  
ATOM   3848  N   GLU B 448      31.605  -9.147  29.663  1.00 61.88           N  
ANISOU 3848  N   GLU B 448     9277   6302   7931    546    566    130       N  
ATOM   3849  CA  GLU B 448      32.047  -8.299  30.764  1.00 69.01           C  
ANISOU 3849  CA  GLU B 448    10281   7104   8838    435    616     -7       C  
ATOM   3850  C   GLU B 448      33.313  -8.849  31.416  1.00 67.71           C  
ANISOU 3850  C   GLU B 448    10027   7131   8567    274    583   -101       C  
ATOM   3851  O   GLU B 448      34.187  -8.090  31.830  1.00 69.58           O  
ANISOU 3851  O   GLU B 448    10329   7325   8782    100    607   -187       O  
ATOM   3852  CB  GLU B 448      30.938  -8.153  31.808  1.00 75.89           C  
ANISOU 3852  CB  GLU B 448    11192   7894   9750    572    658    -91       C  
ATOM   3853  CG  GLU B 448      31.341  -7.343  33.028  1.00 86.99           C  
ANISOU 3853  CG  GLU B 448    12701   9211  11140    461    712   -261       C  
ATOM   3854  CD  GLU B 448      30.196  -7.138  34.003  1.00 95.49           C  
ANISOU 3854  CD  GLU B 448    13820  10209  12252    608    769   -349       C  
ATOM   3855  OE1 GLU B 448      29.214  -7.910  33.945  1.00 97.60           O  
ANISOU 3855  OE1 GLU B 448    13995  10558  12531    777    754   -287       O  
ATOM   3856  OE2 GLU B 448      30.279  -6.204  34.830  1.00 98.35           O  
ANISOU 3856  OE2 GLU B 448    14307  10433  12627    548    833   -488       O  
ATOM   3857  N   HIS B 449      33.405 -10.172  31.505  1.00 63.43           N  
ANISOU 3857  N   HIS B 449     9336   6803   7961    332    529    -85       N  
ATOM   3858  CA  HIS B 449      34.564 -10.813  32.116  1.00 63.74           C  
ANISOU 3858  CA  HIS B 449     9272   7047   7900    217    490   -154       C  
ATOM   3859  C   HIS B 449      35.820 -10.581  31.281  1.00 63.83           C  
ANISOU 3859  C   HIS B 449     9250   7126   7877     58    475   -117       C  
ATOM   3860  O   HIS B 449      36.897 -10.331  31.819  1.00 65.10           O  
ANISOU 3860  O   HIS B 449     9383   7377   7973   -104    469   -198       O  
ATOM   3861  CB  HIS B 449      34.316 -12.312  32.299  1.00 62.36           C  
ANISOU 3861  CB  HIS B 449     8958   7054   7684    339    440   -121       C  
ATOM   3862  CG  HIS B 449      35.408 -13.018  33.041  1.00 64.08           C  
ANISOU 3862  CG  HIS B 449     9066   7480   7800    260    398   -179       C  
ATOM   3863  ND1 HIS B 449      35.522 -12.976  34.414  1.00 66.08           N  
ANISOU 3863  ND1 HIS B 449     9323   7793   7992    226    400   -281       N  
ATOM   3864  CD2 HIS B 449      36.435 -13.782  32.601  1.00 66.24           C  
ANISOU 3864  CD2 HIS B 449     9218   7931   8018    219    352   -144       C  
ATOM   3865  CE1 HIS B 449      36.572 -13.685  34.788  1.00 67.92           C  
ANISOU 3865  CE1 HIS B 449     9437   8235   8134    169    349   -295       C  
ATOM   3866  NE2 HIS B 449      37.144 -14.185  33.707  1.00 68.28           N  
ANISOU 3866  NE2 HIS B 449     9403   8351   8189    170    322   -214       N  
ATOM   3867  N   VAL B 450      35.672 -10.665  29.963  1.00 64.82           N  
ANISOU 3867  N   VAL B 450     9366   7228   8032     99    469      5       N  
ATOM   3868  CA  VAL B 450      36.786 -10.448  29.049  1.00 68.36           C  
ANISOU 3868  CA  VAL B 450     9779   7752   8442    -46    467     55       C  
ATOM   3869  C   VAL B 450      37.402  -9.066  29.240  1.00 73.02           C  
ANISOU 3869  C   VAL B 450    10490   8203   9051   -241    516      9       C  
ATOM   3870  O   VAL B 450      38.624  -8.922  29.288  1.00 73.05           O  
ANISOU 3870  O   VAL B 450    10435   8327   8993   -422    512    -31       O  
ATOM   3871  CB  VAL B 450      36.344 -10.610  27.585  1.00 68.92           C  
ANISOU 3871  CB  VAL B 450     9847   7801   8536     36    462    198       C  
ATOM   3872  CG1 VAL B 450      37.369  -9.992  26.647  1.00 71.02           C  
ANISOU 3872  CG1 VAL B 450    10122   8093   8769   -133    484    258       C  
ATOM   3873  CG2 VAL B 450      36.119 -12.080  27.260  1.00 66.13           C  
ANISOU 3873  CG2 VAL B 450     9355   7626   8146    172    411    224       C  
ATOM   3874  N   GLN B 451      36.549  -8.053  29.351  1.00 76.70           N  
ANISOU 3874  N   GLN B 451    11122   8413   9607   -205    565     12       N  
ATOM   3875  CA  GLN B 451      37.009  -6.683  29.542  1.00 83.32           C  
ANISOU 3875  CA  GLN B 451    12110   9064  10486   -386    622    -37       C  
ATOM   3876  C   GLN B 451      37.785  -6.538  30.848  1.00 89.82           C  
ANISOU 3876  C   GLN B 451    12913   9968  11248   -541    620   -215       C  
ATOM   3877  O   GLN B 451      38.613  -5.639  30.992  1.00 94.10           O  
ANISOU 3877  O   GLN B 451    13522  10444  11785   -760    651   -277       O  
ATOM   3878  CB  GLN B 451      35.827  -5.712  29.522  1.00 84.57           C  
ANISOU 3878  CB  GLN B 451    12454   8917  10763   -272    678     -8       C  
ATOM   3879  N   LEU B 452      37.511  -7.428  31.796  1.00 89.71           N  
ANISOU 3879  N   LEU B 452    12805  10102  11180   -437    582   -293       N  
ATOM   3880  CA  LEU B 452      38.193  -7.410  33.084  1.00 89.64           C  
ANISOU 3880  CA  LEU B 452    12759  10213  11088   -564    567   -455       C  
ATOM   3881  C   LEU B 452      39.617  -7.938  32.945  1.00 87.20           C  
ANISOU 3881  C   LEU B 452    12284  10174  10675   -719    515   -458       C  
ATOM   3882  O   LEU B 452      40.542  -7.430  33.580  1.00 87.61           O  
ANISOU 3882  O   LEU B 452    12325  10296  10667   -924    512   -572       O  
ATOM   3883  CB  LEU B 452      37.411  -8.233  34.112  1.00 91.23           C  
ANISOU 3883  CB  LEU B 452    12910  10500  11253   -394    545   -512       C  
ATOM   3884  CG  LEU B 452      37.808  -8.106  35.585  1.00 95.60           C  
ANISOU 3884  CG  LEU B 452    13458  11154  11713   -493    538   -684       C  
ATOM   3885  CD1 LEU B 452      36.628  -8.442  36.486  1.00 95.46           C  
ANISOU 3885  CD1 LEU B 452    13472  11103  11697   -313    558   -730       C  
ATOM   3886  CD2 LEU B 452      39.009  -8.984  35.914  1.00 97.54           C  
ANISOU 3886  CD2 LEU B 452    13515  11717  11830   -582    461   -695       C  
ATOM   3887  N   LEU B 453      39.787  -8.958  32.111  1.00 86.36           N  
ANISOU 3887  N   LEU B 453    12039  10227  10546   -620    474   -341       N  
ATOM   3888  CA  LEU B 453      41.106  -9.523  31.852  1.00 88.58           C  
ANISOU 3888  CA  LEU B 453    12146  10773  10736   -731    431   -331       C  
ATOM   3889  C   LEU B 453      41.991  -8.510  31.133  1.00 97.36           C  
ANISOU 3889  C   LEU B 453    13297  11838  11856   -962    471   -314       C  
ATOM   3890  O   LEU B 453      41.814  -8.251  29.942  1.00 98.96           O  
ANISOU 3890  O   LEU B 453    13547  11944  12108   -950    503   -195       O  
ATOM   3891  CB  LEU B 453      40.990 -10.803  31.025  1.00 81.28           C  
ANISOU 3891  CB  LEU B 453    11090   9992   9800   -555    395   -217       C  
ATOM   3892  CG  LEU B 453      40.167 -11.936  31.640  1.00 75.90           C  
ANISOU 3892  CG  LEU B 453    10361   9362   9116   -339    357   -215       C  
ATOM   3893  CD1 LEU B 453      40.167 -13.150  30.725  1.00 71.53           C  
ANISOU 3893  CD1 LEU B 453     9689   8931   8557   -197    328   -117       C  
ATOM   3894  CD2 LEU B 453      40.698 -12.301  33.015  1.00 77.34           C  
ANISOU 3894  CD2 LEU B 453    10463   9713   9210   -376    316   -317       C  
ATOM   3895  N   GLN B 454      42.944  -7.942  31.865  1.00101.23           N  
ANISOU 3895  N   GLN B 454    13765  12409  12289  -1183    468   -432       N  
ATOM   3896  CA  GLN B 454      43.810  -6.904  31.323  1.00103.75           C  
ANISOU 3896  CA  GLN B 454    14127  12676  12616  -1443    511   -431       C  
ATOM   3897  C   GLN B 454      44.988  -6.644  32.257  1.00109.19           C  
ANISOU 3897  C   GLN B 454    14718  13560  13209  -1681    482   -577       C  
ATOM   3898  O   GLN B 454      44.967  -7.040  33.422  1.00110.12           O  
ANISOU 3898  O   GLN B 454    14783  13796  13261  -1642    434   -688       O  
ATOM   3899  CB  GLN B 454      43.015  -5.615  31.118  1.00101.39           C  
ANISOU 3899  CB  GLN B 454    14084  12003  12437  -1487    588   -424       C  
ATOM   3900  CG  GLN B 454      42.404  -5.070  32.398  1.00100.79           C  
ANISOU 3900  CG  GLN B 454    14144  11765  12386  -1482    604   -582       C  
ATOM   3901  CD  GLN B 454      41.357  -4.007  32.140  1.00101.78           C  
ANISOU 3901  CD  GLN B 454    14518  11504  12649  -1427    681   -556       C  
ATOM   3902  OE1 GLN B 454      40.801  -3.429  33.073  1.00101.63           O  
ANISOU 3902  OE1 GLN B 454    14633  11315  12665  -1416    714   -687       O  
ATOM   3903  NE2 GLN B 454      41.080  -3.745  30.868  1.00102.85           N  
ANISOU 3903  NE2 GLN B 454    14714  11506  12856  -1381    714   -384       N  
ATOM   3904  N   VAL B 455      46.013  -5.975  31.741  1.00112.54           N  
ANISOU 3904  N   VAL B 455    15112  14032  13616  -1935    510   -572       N  
ATOM   3905  CA  VAL B 455      47.194  -5.658  32.536  1.00115.14           C  
ANISOU 3905  CA  VAL B 455    15332  14566  13850  -2195    480   -710       C  
ATOM   3906  C   VAL B 455      47.456  -4.156  32.559  1.00116.03           C  
ANISOU 3906  C   VAL B 455    15626  14439  14021  -2492    550   -787       C  
ATOM   3907  O   VAL B 455      46.969  -3.445  33.438  1.00115.99           O  
ANISOU 3907  O   VAL B 455    15789  14231  14049  -2545    571   -922       O  
ATOM   3908  CB  VAL B 455      48.443  -6.380  32.002  1.00116.66           C  
ANISOU 3908  CB  VAL B 455    15256  15125  13946  -2261    441   -652       C  
ATOM   3909  CG1 VAL B 455      49.619  -6.169  32.943  1.00119.00           C  
ANISOU 3909  CG1 VAL B 455    15403  15682  14129  -2506    392   -799       C  
ATOM   3910  CG2 VAL B 455      48.158  -7.862  31.814  1.00115.24           C  
ANISOU 3910  CG2 VAL B 455    14922  15133  13732  -1955    386   -564       C  
ATOM   3911  N   LEU B 465      53.362 -16.211  35.827  1.00 96.37           N  
ANISOU 3911  N   LEU B 465    10784  15201  10632   -964   -223   -465       N  
ATOM   3912  CA  LEU B 465      54.039 -14.950  35.558  1.00 99.02           C  
ANISOU 3912  CA  LEU B 465    11102  15583  10939  -1298   -190   -556       C  
ATOM   3913  C   LEU B 465      55.172 -15.150  34.555  1.00101.20           C  
ANISOU 3913  C   LEU B 465    11151  16098  11201  -1337   -163   -513       C  
ATOM   3914  O   LEU B 465      55.584 -14.209  33.877  1.00104.46           O  
ANISOU 3914  O   LEU B 465    11575  16488  11628  -1586   -101   -549       O  
ATOM   3915  CB  LEU B 465      54.578 -14.347  36.857  1.00101.77           C  
ANISOU 3915  CB  LEU B 465    11386  16126  11157  -1507   -267   -674       C  
ATOM   3916  CG  LEU B 465      54.993 -12.875  36.819  1.00104.77           C  
ANISOU 3916  CG  LEU B 465    11828  16461  11521  -1890   -229   -801       C  
ATOM   3917  CD1 LEU B 465      53.795 -11.989  36.515  1.00104.41           C  
ANISOU 3917  CD1 LEU B 465    12107  15967  11595  -1955   -140   -834       C  
ATOM   3918  CD2 LEU B 465      55.647 -12.469  38.132  1.00104.95           C  
ANISOU 3918  CD2 LEU B 465    11743  16741  11390  -2084   -320   -928       C  
ATOM   3919  N   HIS B 466      55.673 -16.379  34.465  1.00 98.02           N  
ANISOU 3919  N   HIS B 466    10546  15925  10772  -1089   -203   -434       N  
ATOM   3920  CA  HIS B 466      56.734 -16.698  33.516  1.00 96.95           C  
ANISOU 3920  CA  HIS B 466    10178  16038  10622  -1081   -171   -396       C  
ATOM   3921  C   HIS B 466      56.156 -17.316  32.242  1.00 88.58           C  
ANISOU 3921  C   HIS B 466     9205  14781   9670   -877    -85   -315       C  
ATOM   3922  O   HIS B 466      55.115 -17.972  32.284  1.00 85.14           O  
ANISOU 3922  O   HIS B 466     8931  14111   9309   -653    -85   -269       O  
ATOM   3923  CB  HIS B 466      57.790 -17.612  34.151  1.00103.07           C  
ANISOU 3923  CB  HIS B 466    10647  17218  11296   -937   -262   -368       C  
ATOM   3924  CG  HIS B 466      57.356 -19.037  34.296  1.00106.48           C  
ANISOU 3924  CG  HIS B 466    11072  17614  11771   -552   -294   -270       C  
ATOM   3925  ND1 HIS B 466      57.472 -19.958  33.277  1.00107.93           N  
ANISOU 3925  ND1 HIS B 466    11187  17798  12025   -319   -238   -201       N  
ATOM   3926  CD2 HIS B 466      56.823 -19.704  35.347  1.00107.46           C  
ANISOU 3926  CD2 HIS B 466    11255  17699  11877   -368   -370   -230       C  
ATOM   3927  CE1 HIS B 466      57.020 -21.128  33.690  1.00107.74           C  
ANISOU 3927  CE1 HIS B 466    11188  17711  12036    -11   -278   -126       C  
ATOM   3928  NE2 HIS B 466      56.621 -21.002  34.943  1.00107.54           N  
ANISOU 3928  NE2 HIS B 466    11238  17664  11958    -36   -359   -131       N  
ATOM   3929  N   PRO B 467      56.840 -17.105  31.107  1.00 83.58           N  
ANISOU 3929  N   PRO B 467     8459  14261   9037   -966    -11   -303       N  
ATOM   3930  CA  PRO B 467      56.367 -17.448  29.760  1.00 76.00           C  
ANISOU 3930  CA  PRO B 467     7586  13134   8157   -841     82   -246       C  
ATOM   3931  C   PRO B 467      55.631 -18.783  29.653  1.00 67.32           C  
ANISOU 3931  C   PRO B 467     6544  11911   7125   -481     69   -189       C  
ATOM   3932  O   PRO B 467      54.572 -18.843  29.030  1.00 65.66           O  
ANISOU 3932  O   PRO B 467     6543  11408   6997   -403    117   -162       O  
ATOM   3933  CB  PRO B 467      57.662 -17.503  28.949  1.00 77.97           C  
ANISOU 3933  CB  PRO B 467     7569  13713   8343   -912    129   -242       C  
ATOM   3934  CG  PRO B 467      58.547 -16.518  29.613  1.00 83.59           C  
ANISOU 3934  CG  PRO B 467     8157  14636   8969  -1227     94   -306       C  
ATOM   3935  CD  PRO B 467      58.209 -16.557  31.082  1.00 84.88           C  
ANISOU 3935  CD  PRO B 467     8374  14773   9106  -1203    -15   -346       C  
ATOM   3936  N   LEU B 468      56.182 -19.835  30.248  1.00 65.31           N  
ANISOU 3936  N   LEU B 468     6106  11873   6838   -267      5   -167       N  
ATOM   3937  CA  LEU B 468      55.650 -21.178  30.037  1.00 68.46           C  
ANISOU 3937  CA  LEU B 468     6539  12166   7307     72      5   -112       C  
ATOM   3938  C   LEU B 468      54.217 -21.354  30.548  1.00 70.34           C  
ANISOU 3938  C   LEU B 468     7044  12061   7622    165    -17    -91       C  
ATOM   3939  O   LEU B 468      53.325 -21.724  29.786  1.00 69.16           O  
ANISOU 3939  O   LEU B 468     7051  11670   7558    279     36    -70       O  
ATOM   3940  CB  LEU B 468      56.585 -22.229  30.638  1.00 73.96           C  
ANISOU 3940  CB  LEU B 468     6986  13159   7957    287    -60    -79       C  
ATOM   3941  CG  LEU B 468      56.641 -23.555  29.876  1.00 75.79           C  
ANISOU 3941  CG  LEU B 468     7158  13383   8254    604    -17    -40       C  
ATOM   3942  CD1 LEU B 468      57.983 -24.243  30.078  1.00 73.80           C  
ANISOU 3942  CD1 LEU B 468     6590  13507   7941    750    -49    -21       C  
ATOM   3943  CD2 LEU B 468      55.488 -24.465  30.279  1.00 77.47           C  
ANISOU 3943  CD2 LEU B 468     7571  13303   8559    837    -42      9       C  
ATOM   3944  N   LEU B 469      53.988 -21.092  31.831  1.00 71.38           N  
ANISOU 3944  N   LEU B 469     7220  12188   7715    112    -93   -100       N  
ATOM   3945  CA  LEU B 469      52.633 -21.199  32.365  1.00 71.26           C  
ANISOU 3945  CA  LEU B 469     7444  11870   7761    185   -106    -82       C  
ATOM   3946  C   LEU B 469      51.739 -20.100  31.793  1.00 65.23           C  
ANISOU 3946  C   LEU B 469     6902  10830   7052      0    -41   -120       C  
ATOM   3947  O   LEU B 469      50.515 -20.236  31.756  1.00 64.02           O  
ANISOU 3947  O   LEU B 469     6947  10402   6976     85    -22   -100       O  
ATOM   3948  CB  LEU B 469      52.625 -21.198  33.898  1.00 75.40           C  
ANISOU 3948  CB  LEU B 469     7955  12484   8211    176   -197    -84       C  
ATOM   3949  CG  LEU B 469      53.258 -20.036  34.663  1.00 80.04           C  
ANISOU 3949  CG  LEU B 469     8482  13241   8689   -107   -238   -167       C  
ATOM   3950  CD1 LEU B 469      52.391 -18.792  34.565  1.00 82.04           C  
ANISOU 3950  CD1 LEU B 469     8971  13217   8983   -326   -186   -238       C  
ATOM   3951  CD2 LEU B 469      53.466 -20.426  36.119  1.00 81.00           C  
ANISOU 3951  CD2 LEU B 469     8526  13541   8710    -45   -341   -153       C  
ATOM   3952  N   GLN B 470      52.360 -19.016  31.339  1.00 64.42           N  
ANISOU 3952  N   GLN B 470     6761  10805   6912   -252     -5   -167       N  
ATOM   3953  CA  GLN B 470      51.635 -17.964  30.638  1.00 68.85           C  
ANISOU 3953  CA  GLN B 470     7522  11109   7528   -418     65   -182       C  
ATOM   3954  C   GLN B 470      51.043 -18.520  29.347  1.00 65.00           C  
ANISOU 3954  C   GLN B 470     7105  10475   7115   -264    129   -126       C  
ATOM   3955  O   GLN B 470      49.965 -18.108  28.917  1.00 64.32           O  
ANISOU 3955  O   GLN B 470     7222  10119   7097   -274    165   -108       O  
ATOM   3956  CB  GLN B 470      52.555 -16.780  30.334  1.00 77.83           C  
ANISOU 3956  CB  GLN B 470     8589  12372   8610   -721     97   -227       C  
ATOM   3957  CG  GLN B 470      51.876 -15.648  29.579  1.00 85.79           C  
ANISOU 3957  CG  GLN B 470     9811  13107   9680   -893    173   -222       C  
ATOM   3958  CD  GLN B 470      52.827 -14.516  29.238  1.00 95.93           C  
ANISOU 3958  CD  GLN B 470    11030  14504  10915  -1206    214   -254       C  
ATOM   3959  OE1 GLN B 470      54.047 -14.666  29.320  1.00 99.22           O  
ANISOU 3959  OE1 GLN B 470    11212  15238  11250  -1286    196   -276       O  
ATOM   3960  NE2 GLN B 470      52.271 -13.373  28.851  1.00 97.52           N  
ANISOU 3960  NE2 GLN B 470    11438  14448  11169  -1384    271   -250       N  
ATOM   3961  N   GLU B 471      51.756 -19.461  28.733  1.00 60.26           N  
ANISOU 3961  N   GLU B 471     6331  10067   6498   -117    141   -103       N  
ATOM   3962  CA  GLU B 471      51.257 -20.146  27.546  1.00 56.39           C  
ANISOU 3962  CA  GLU B 471     5894   9469   6064     43    197    -70       C  
ATOM   3963  C   GLU B 471      50.070 -21.033  27.901  1.00 52.39           C  
ANISOU 3963  C   GLU B 471     5529   8740   5637    263    169    -45       C  
ATOM   3964  O   GLU B 471      49.054 -21.037  27.206  1.00 53.64           O  
ANISOU 3964  O   GLU B 471     5847   8679   5856    303    204    -28       O  
ATOM   3965  CB  GLU B 471      52.364 -20.976  26.889  1.00 58.72           C  
ANISOU 3965  CB  GLU B 471     5960  10033   6317    159    224    -72       C  
ATOM   3966  CG  GLU B 471      53.277 -20.171  25.982  1.00 60.22           C  
ANISOU 3966  CG  GLU B 471     6039  10402   6440    -47    290    -84       C  
ATOM   3967  CD  GLU B 471      52.521 -19.506  24.847  1.00 63.65           C  
ANISOU 3967  CD  GLU B 471     6653  10631   6900   -148    363    -59       C  
ATOM   3968  OE1 GLU B 471      51.616 -20.151  24.275  1.00 56.99           O  
ANISOU 3968  OE1 GLU B 471     5929   9614   6111     21    379    -43       O  
ATOM   3969  OE2 GLU B 471      52.832 -18.341  24.523  1.00 72.54           O  
ANISOU 3969  OE2 GLU B 471     7800  11772   7989   -402    402    -50       O  
ATOM   3970  N   ILE B 472      50.204 -21.782  28.991  1.00 51.92           N  
ANISOU 3970  N   ILE B 472     5406   8750   5572    398    103    -35       N  
ATOM   3971  CA  ILE B 472      49.143 -22.674  29.441  1.00 53.10           C  
ANISOU 3971  CA  ILE B 472     5679   8704   5794    593     78     -1       C  
ATOM   3972  C   ILE B 472      47.816 -21.939  29.617  1.00 56.77           C  
ANISOU 3972  C   ILE B 472     6369   8894   6308    505     87     -3       C  
ATOM   3973  O   ILE B 472      46.755 -22.477  29.301  1.00 60.13           O  
ANISOU 3973  O   ILE B 472     6919   9120   6808    625    103     20       O  
ATOM   3974  CB  ILE B 472      49.524 -23.381  30.755  1.00 55.34           C  
ANISOU 3974  CB  ILE B 472     5869   9115   6044    712      2     28       C  
ATOM   3975  CG1 ILE B 472      50.720 -24.310  30.531  1.00 51.49           C  
ANISOU 3975  CG1 ILE B 472     5159   8878   5528    866     -7     45       C  
ATOM   3976  CG2 ILE B 472      48.343 -24.162  31.298  1.00 57.81           C  
ANISOU 3976  CG2 ILE B 472     6331   9207   6429    873    -17     73       C  
ATOM   3977  CD1 ILE B 472      51.197 -25.010  31.787  1.00 49.99           C  
ANISOU 3977  CD1 ILE B 472     4858   8842   5296    999    -89     97       C  
ATOM   3978  N   TYR B 473      47.879 -20.706  30.112  1.00 62.79           N  
ANISOU 3978  N   TYR B 473     7178   9648   7030    293     82    -37       N  
ATOM   3979  CA  TYR B 473      46.673 -19.910  30.331  1.00 65.52           C  
ANISOU 3979  CA  TYR B 473     7732   9739   7424    217     97    -45       C  
ATOM   3980  C   TYR B 473      46.571 -18.749  29.347  1.00 69.85           C  
ANISOU 3980  C   TYR B 473     8365  10186   7987     41    157    -53       C  
ATOM   3981  O   TYR B 473      46.160 -17.647  29.715  1.00 71.46           O  
ANISOU 3981  O   TYR B 473     8694  10257   8200   -108    169    -79       O  
ATOM   3982  CB  TYR B 473      46.625 -19.385  31.769  1.00 61.91           C  
ANISOU 3982  CB  TYR B 473     7305   9299   6920    128     52    -85       C  
ATOM   3983  CG  TYR B 473      46.776 -20.466  32.815  1.00 62.78           C  
ANISOU 3983  CG  TYR B 473     7328   9530   6995    291    -11    -57       C  
ATOM   3984  CD1 TYR B 473      45.897 -21.538  32.861  1.00 61.91           C  
ANISOU 3984  CD1 TYR B 473     7282   9291   6951    498    -14      1       C  
ATOM   3985  CD2 TYR B 473      47.793 -20.412  33.760  1.00 66.30           C  
ANISOU 3985  CD2 TYR B 473     7629  10223   7338    230    -70    -81       C  
ATOM   3986  CE1 TYR B 473      46.029 -22.531  33.812  1.00 63.97           C  
ANISOU 3986  CE1 TYR B 473     7477   9645   7183    646    -67     48       C  
ATOM   3987  CE2 TYR B 473      47.931 -21.400  34.718  1.00 67.02           C  
ANISOU 3987  CE2 TYR B 473     7644  10432   7388    389   -132    -32       C  
ATOM   3988  CZ  TYR B 473      47.046 -22.457  34.737  1.00 65.94           C  
ANISOU 3988  CZ  TYR B 473     7586  10142   7325    600   -127     39       C  
ATOM   3989  OH  TYR B 473      47.173 -23.446  35.683  1.00 68.60           O  
ANISOU 3989  OH  TYR B 473     7860  10579   7625    758   -183    109       O  
ATOM   3990  N   LYS B 474      46.945 -19.002  28.097  1.00 68.75           N  
ANISOU 3990  N   LYS B 474     8167  10109   7847     63    199    -27       N  
ATOM   3991  CA  LYS B 474      46.904 -17.978  27.058  1.00 70.31           C  
ANISOU 3991  CA  LYS B 474     8437  10231   8045    -96    258     -9       C  
ATOM   3992  C   LYS B 474      45.509 -17.372  26.918  1.00 71.48           C  
ANISOU 3992  C   LYS B 474     8803  10088   8267    -96    274     20       C  
ATOM   3993  O   LYS B 474      44.508 -18.004  27.259  1.00 72.28           O  
ANISOU 3993  O   LYS B 474     8978  10062   8422     61    251     28       O  
ATOM   3994  CB  LYS B 474      47.360 -18.556  25.717  1.00 69.75           C  
ANISOU 3994  CB  LYS B 474     8273  10279   7951    -32    302     18       C  
TER    3995      LYS B 474                                                      
HETATM 3996  C1  KNA A 501      12.461   3.522  13.740  1.00 69.61           C  
ANISOU 3996  C1  KNA A 501     9154   9071   8223   1117   -227    120       C  
HETATM 3997  O1  KNA A 501      12.201   3.864  12.575  1.00 74.89           O  
ANISOU 3997  O1  KNA A 501     9864   9704   8886   1031   -214    147       O  
HETATM 3998  C2  KNA A 501      13.177   4.551  14.576  1.00 66.73           C  
ANISOU 3998  C2  KNA A 501     8818   8699   7838   1100   -270     60       C  
HETATM 3999  O2  KNA A 501      12.204   2.421  14.263  1.00 64.75           O  
ANISOU 3999  O2  KNA A 501     8483   8495   7622   1206   -210    139       O  
HETATM 4000  C3  KNA A 501      14.334   5.097  13.792  1.00 71.92           C  
ANISOU 4000  C3  KNA A 501     9462   9365   8498    951   -263     11       C  
HETATM 4001  C4  KNA A 501      15.622   5.218  14.587  1.00 75.45           C  
ANISOU 4001  C4  KNA A 501     9840   9884   8944    923   -292    -69       C  
HETATM 4002  C5  KNA A 501      16.489   6.343  14.027  1.00 78.38           C  
ANISOU 4002  C5  KNA A 501    10242  10229   9311    760   -297   -117       C  
HETATM 4003  C6  KNA A 501      17.416   5.863  12.908  1.00 80.31           C  
ANISOU 4003  C6  KNA A 501    10398  10540   9576    648   -240   -135       C  
HETATM 4004  C7  KNA A 501      16.778   6.013  11.531  1.00 77.79           C  
ANISOU 4004  C7  KNA A 501    10155  10159   9244    576   -193    -74       C  
HETATM 4005  C8  KNA A 501      17.615   6.918  10.657  1.00 76.11           C  
ANISOU 4005  C8  KNA A 501     9967   9935   9015    390   -168    -96       C  
HETATM 4006  C9  KNA A 501      18.788   6.141  10.135  1.00 76.14           C  
ANISOU 4006  C9  KNA A 501     9830  10062   9038    322   -104   -153       C  
HETATM 4007  C1  KNA A 502      19.290   7.496  19.759  1.00 74.68           C  
ANISOU 4007  C1  KNA A 502     9635  10067   8674    834   -600   -431       C  
HETATM 4008  O1  KNA A 502      20.115   7.107  20.514  1.00 77.00           O  
ANISOU 4008  O1  KNA A 502     9824  10492   8941    848   -659   -466       O  
HETATM 4009  C2  KNA A 502      19.606   8.670  18.834  1.00 70.96           C  
ANISOU 4009  C2  KNA A 502     9234   9493   8234    656   -577   -472       C  
HETATM 4010  O2  KNA A 502      17.968   7.055  19.900  1.00 75.25           O  
ANISOU 4010  O2  KNA A 502     9783  10073   8735    976   -564   -356       O  
HETATM 4011  C3  KNA A 502      20.826   8.556  17.923  1.00 65.24           C  
ANISOU 4011  C3  KNA A 502     8382   8845   7561    511   -554   -494       C  
HETATM 4012  C4  KNA A 502      20.616   8.010  16.511  1.00 61.21           C  
ANISOU 4012  C4  KNA A 502     7848   8305   7104    492   -465   -423       C  
HETATM 4013  C5  KNA A 502      21.865   7.711  15.685  1.00 59.15           C  
ANISOU 4013  C5  KNA A 502     7438   8150   6888    369   -425   -453       C  
HETATM 4014  C6  KNA A 502      21.752   7.756  14.163  1.00 58.14           C  
ANISOU 4014  C6  KNA A 502     7339   7966   6784    271   -332   -410       C  
HETATM 4015  C7  KNA A 502      23.051   7.864  13.366  1.00 54.77           C  
ANISOU 4015  C7  KNA A 502     6790   7635   6386    102   -282   -459       C  
HETATM 4016  C8  KNA A 502      22.947   8.139  11.868  1.00 52.22           C  
ANISOU 4016  C8  KNA A 502     6526   7255   6058    -28   -188   -419       C  
HETATM 4017  C9  KNA A 502      24.172   8.724  11.168  1.00 48.53           C  
ANISOU 4017  C9  KNA A 502     5983   6856   5602   -245   -137   -469       C  
HETATM 4018  C1  KNA A 503      13.562   6.239   9.636  1.00 74.73           C  
ANISOU 4018  C1  KNA A 503     9993   9599   8802    628   -196    150       C  
HETATM 4019  O1  KNA A 503      12.408   6.067   9.852  1.00 81.08           O  
ANISOU 4019  O1  KNA A 503    10825  10372   9611    730   -220    206       O  
HETATM 4020  C2  KNA A 503      14.072   7.639   9.303  1.00 69.26           C  
ANISOU 4020  C2  KNA A 503     9392   8832   8092    505   -212    152       C  
HETATM 4021  O2  KNA A 503      14.475   5.197   9.846  1.00 72.44           O  
ANISOU 4021  O2  KNA A 503     9585   9407   8534    632   -154     81       O  
HETATM 4022  C3  KNA A 503      13.119   8.816   9.493  1.00 60.85           C  
ANISOU 4022  C3  KNA A 503     8457   7633   7028    550   -266    218       C  
HETATM 4023  C4  KNA A 503      13.663  10.192   9.122  1.00 63.42           C  
ANISOU 4023  C4  KNA A 503     8892   7859   7346    418   -277    225       C  
HETATM 4024  C5  KNA A 503      15.162  10.403   9.330  1.00 66.47           C  
ANISOU 4024  C5  KNA A 503     9227   8294   7736    284   -251    129       C  
HETATM 4025  C6  KNA A 503      15.865  11.438   8.456  1.00 66.87           C  
ANISOU 4025  C6  KNA A 503     9361   8283   7765     89   -231    149       C  
HETATM 4026  C7  KNA A 503      17.346  11.213   8.162  1.00 64.17           C  
ANISOU 4026  C7  KNA A 503     8914   8052   7415    -72   -176     69       C  
HETATM 4027  C8  KNA A 503      18.167  12.414   7.696  1.00 66.45           C  
ANISOU 4027  C8  KNA A 503     9282   8271   7693   -276   -159     68       C  
HETATM 4028  C9  KNA A 503      17.646  13.220   6.508  1.00 65.18           C  
ANISOU 4028  C9  KNA A 503     9278   7998   7489   -372   -151    193       C  
HETATM 4029  C1  GOL A 504       6.825   2.366  13.119  1.00 71.37           C  
HETATM 4030  O1  GOL A 504       6.659   3.548  12.384  1.00 69.91           O  
HETATM 4031  C2  GOL A 504       8.038   1.540  12.700  1.00 69.03           C  
HETATM 4032  O2  GOL A 504       9.070   2.365  12.308  1.00 68.88           O  
HETATM 4033  C3  GOL A 504       7.704   0.577  11.574  1.00 64.09           C  
HETATM 4034  O3  GOL A 504       8.349  -0.651  11.696  1.00 53.26           O  
HETATM 4035  C1  KNA B 501      33.877 -24.771  36.957  0.80 64.26           C  
ANISOU 4035  C1  KNA B 501     8494   8228   7696   1116    174    297       C  
HETATM 4036  O1  KNA B 501      32.802 -24.809  36.320  0.80 62.86           O  
ANISOU 4036  O1  KNA B 501     8355   7926   7604   1132    205    299       O  
HETATM 4037  C2  KNA B 501      35.026 -23.976  36.334  0.80 60.52           C  
ANISOU 4037  C2  KNA B 501     7985   7819   7190   1049    148    234       C  
HETATM 4038  O2  KNA B 501      34.099 -25.323  38.057  0.80 69.61           O  
ANISOU 4038  O2  KNA B 501     9150   8994   8304   1145    160    349       O  
HETATM 4039  C3  KNA B 501      35.648 -23.020  37.354  0.80 60.15           C  
ANISOU 4039  C3  KNA B 501     7936   7887   7031    957    138    175       C  
HETATM 4040  C4  KNA B 501      36.213 -21.776  36.665  0.80 63.45           C  
ANISOU 4040  C4  KNA B 501     8369   8293   7448    845    144     91       C  
HETATM 4041  C5  KNA B 501      36.086 -20.545  37.566  0.80 67.23           C  
ANISOU 4041  C5  KNA B 501     8910   8775   7860    740    168      2       C  
HETATM 4042  C6  KNA B 501      35.346 -19.415  36.848  0.80 71.24           C  
ANISOU 4042  C6  KNA B 501     9516   9106   8446    694    219    -49       C  
HETATM 4043  C7  KNA B 501      36.168 -18.125  36.862  0.80 76.57           C  
ANISOU 4043  C7  KNA B 501    10222   9792   9079    543    224   -142       C  
HETATM 4044  C8  KNA B 501      35.434 -16.998  36.132  0.80 78.92           C  
ANISOU 4044  C8  KNA B 501    10633   9889   9465    513    278   -172       C  
HETATM 4045  C9  KNA B 501      35.865 -15.629  36.662  0.80 80.76           C  
ANISOU 4045  C9  KNA B 501    10944  10082   9658    366    305   -285       C  
HETATM 4046  O16 TCE B 502      44.407 -20.297  46.524  1.00 85.43           O  
ANISOU 4046  O16 TCE B 502    10416  13281   8762    180   -399   -216       O  
HETATM 4047  C14 TCE B 502      43.302 -20.730  46.389  0.84 85.06           C  
ANISOU 4047  C14 TCE B 502    10484  13025   8810    301   -335   -149       C  
HETATM 4048  O15 TCE B 502      42.689 -21.422  47.448  0.86 86.54           O  
ANISOU 4048  O15 TCE B 502    10700  13283   8899    406   -341    -56       O  
HETATM 4049  C5  TCE B 502      42.666 -20.788  44.986  0.74 82.24           C  
ANISOU 4049  C5  TCE B 502    10209  12362   8677    366   -259   -123       C  
HETATM 4050  C2  TCE B 502      41.151 -21.050  45.110  1.00 80.99           C  
ANISOU 4050  C2  TCE B 502    10199  11974   8598    464   -178    -84       C  
HETATM 4051  P   TCE B 502      40.580 -22.103  43.661  0.51 87.68           P  
ANISOU 4051  P   TCE B 502    11064  12578   9670    646   -139     57       P  
HETATM 4052  C3  TCE B 502      39.042 -21.345  42.917  1.00 94.29           C  
ANISOU 4052  C3  TCE B 502    12079  13082  10666    623    -28    -18       C  
HETATM 4053  C6  TCE B 502      39.100 -19.824  43.060  1.00 95.22           C  
ANISOU 4053  C6  TCE B 502    12267  13164  10747    447      4   -190       C  
HETATM 4054  C8  TCE B 502      38.218 -19.175  41.984  1.00 94.79           C  
ANISOU 4054  C8  TCE B 502    12324  12838  10853    443     79   -228       C  
HETATM 4055  O10 TCE B 502      37.080 -19.500  41.868  1.00 94.61           O  
ANISOU 4055  O10 TCE B 502    12365  12676  10906    540    127   -182       O  
HETATM 4056  O9  TCE B 502      38.784 -18.271  41.077  1.00 93.21           O  
ANISOU 4056  O9  TCE B 502    12137  12569  10708    329     86   -299       O  
HETATM 4057  C1  TCE B 502      40.198 -23.855  44.259  1.00102.86           C  
ANISOU 4057  C1  TCE B 502    12956  14542  11584    864   -163    271       C  
HETATM 4058  C4  TCE B 502      40.021 -24.798  43.036  1.00 71.40           C  
ANISOU 4058  C4  TCE B 502     8968  10385   7776    999   -144    365       C  
HETATM 4059  C11 TCE B 502      38.612 -24.601  42.429  0.90 69.48           C  
ANISOU 4059  C11 TCE B 502     8856   9875   7667   1000    -59    337       C  
HETATM 4060  O12 TCE B 502      37.922 -25.545  42.193  1.00 67.57           O  
ANISOU 4060  O12 TCE B 502     8648   9512   7513   1109    -34    434       O  
HETATM 4061  O13 TCE B 502      38.178 -23.305  42.080  0.92 71.32           O  
ANISOU 4061  O13 TCE B 502     9165  10008   7927    875    -11    198       O  
HETATM 4062  C1  GOL B 503      41.420 -27.430   7.963  1.00 59.97           C  
HETATM 4063  O1  GOL B 503      42.173 -26.255   8.170  1.00 52.85           O  
HETATM 4064  C2  GOL B 503      41.671 -28.412   9.103  1.00 66.06           C  
HETATM 4065  O2  GOL B 503      42.702 -27.931   9.941  1.00 65.30           O  
HETATM 4066  C3  GOL B 503      42.050 -29.779   8.542  1.00 64.39           C  
HETATM 4067  O3  GOL B 503      40.896 -30.436   8.061  1.00 66.74           O  
HETATM 4068  C1  GOL B 504      30.230 -28.057  37.652  1.00 70.58           C  
HETATM 4069  O1  GOL B 504      28.984 -28.535  38.123  1.00 62.92           O  
HETATM 4070  C2  GOL B 504      31.444 -28.810  38.193  1.00 75.96           C  
HETATM 4071  O2  GOL B 504      32.481 -27.887  38.171  1.00 77.70           O  
HETATM 4072  C3  GOL B 504      31.830 -30.001  37.326  1.00 78.89           C  
HETATM 4073  O3  GOL B 504      32.848 -30.782  37.913  1.00 79.31           O  
HETATM 4074  O   HOH A 601      -1.955  -1.576  30.148  1.00 37.60           O  
ANISOU 4074  O   HOH A 601     4701   5262   4323   1505    263    118       O  
HETATM 4075  O   HOH A 602      11.968 -11.129  10.692  1.00 40.14           O  
ANISOU 4075  O   HOH A 602     5235   4999   5017    352     57    -41       O  
HETATM 4076  O   HOH A 603      11.389  -6.238  12.309  1.00 30.90           O  
ANISOU 4076  O   HOH A 603     4094   3812   3836    365     24    -29       O  
HETATM 4077  O   HOH A 604      11.920  -8.279  10.591  1.00 37.77           O  
ANISOU 4077  O   HOH A 604     4954   4696   4702    341     38    -33       O  
HETATM 4078  O   HOH A 605      -1.384 -16.366  20.530  1.00 37.33           O  
ANISOU 4078  O   HOH A 605     4327   4939   4916    407    101    439       O  
HETATM 4079  O   HOH A 606      16.589   2.195  25.810  1.00 39.32           O  
ANISOU 4079  O   HOH A 606     5548   4664   4729    625   -257   -114       O  
HETATM 4080  O   HOH A 607      11.401   0.961  38.714  1.00 47.24           O  
ANISOU 4080  O   HOH A 607     6675   5928   5344   1507    -63   -239       O  
HETATM 4081  O   HOH A 608      18.153  -4.986  30.821  1.00 44.00           O  
ANISOU 4081  O   HOH A 608     5913   5465   5342    700     36    -98       O  
HETATM 4082  O   HOH A 609      11.772 -10.520   6.612  1.00 38.65           O  
ANISOU 4082  O   HOH A 609     5106   4800   4781    330      8    -51       O  
HETATM 4083  O   HOH A 610      24.383   0.408   0.099  1.00 45.57           O  
ANISOU 4083  O   HOH A 610     5851   6138   5325    -51    -37    443       O  
HETATM 4084  O   HOH A 611      -0.258   1.086  11.205  1.00 36.59           O  
ANISOU 4084  O   HOH A 611     4830   4510   4565    662   -161    -11       O  
HETATM 4085  O   HOH A 612      -0.535 -10.922  16.968  1.00 35.27           O  
ANISOU 4085  O   HOH A 612     4250   4580   4570    506     71    233       O  
HETATM 4086  O   HOH A 613      -8.434   0.695  20.122  1.00 46.61           O  
ANISOU 4086  O   HOH A 613     5675   6354   5681   1305     74    202       O  
HETATM 4087  O   HOH A 614       6.081  -3.826  38.820  1.00 44.94           O  
ANISOU 4087  O   HOH A 614     5917   6068   5090   1573    297    -11       O  
HETATM 4088  O   HOH A 615       0.819  -8.733  36.735  1.00 49.27           O  
ANISOU 4088  O   HOH A 615     5959   6954   5807   1392    503    323       O  
HETATM 4089  O   HOH A 616       4.044  -2.784  40.183  1.00 43.80           O  
ANISOU 4089  O   HOH A 616     5764   6050   4825   1801    332      6       O  
HETATM 4090  O   HOH A 617       3.905  -6.239   2.217  1.00 45.92           O  
ANISOU 4090  O   HOH A 617     6063   5603   5782    296   -181    -17       O  
HETATM 4091  O   HOH A 618     -10.175  -3.851  16.027  1.00 54.77           O  
ANISOU 4091  O   HOH A 618     6476   7375   6957    910     30    382       O  
HETATM 4092  O   HOH A 619      25.986   5.253  10.396  1.00 49.09           O  
ANISOU 4092  O   HOH A 619     6471   6181   6000   -227   -392    440       O  
HETATM 4093  O   HOH A 620       8.163 -21.732  17.199  1.00 41.76           O  
ANISOU 4093  O   HOH A 620     5308   5136   5424    307     -4    122       O  
HETATM 4094  O   HOH A 621       1.383   6.292  17.831  1.00 44.30           O  
ANISOU 4094  O   HOH A 621     6080   5415   5337   1022   -259   -133       O  
HETATM 4095  O   HOH A 622       0.416  -5.257   9.074  1.00 40.13           O  
ANISOU 4095  O   HOH A 622     5143   4979   5125    447   -102     53       O  
HETATM 4096  O   HOH A 623      -4.339  -3.024  31.349  1.00 51.45           O  
ANISOU 4096  O   HOH A 623     6251   7240   6057   1587    369    260       O  
HETATM 4097  O   HOH A 624      10.729 -18.474   9.662  1.00 52.84           O  
ANISOU 4097  O   HOH A 624     6896   6505   6675    362    -38    -55       O  
HETATM 4098  O   HOH A 625      18.157  -2.620  13.489  1.00 50.09           O  
ANISOU 4098  O   HOH A 625     6581   6263   6189    242    -42     37       O  
HETATM 4099  O   HOH A 626       4.749  -8.161   3.801  1.00 45.27           O  
ANISOU 4099  O   HOH A 626     5947   5539   5715    303   -140    -18       O  
HETATM 4100  O   HOH A 627      -0.473  -5.541  36.268  1.00 45.70           O  
ANISOU 4100  O   HOH A 627     5597   6509   5257   1591    458    245       O  
HETATM 4101  O   HOH A 628      11.642   5.260  37.552  1.00 53.41           O  
ANISOU 4101  O   HOH A 628     7735   6491   6069   1566   -323   -336       O  
HETATM 4102  O   HOH A 629      26.945   3.019   9.334  1.00 48.22           O  
ANISOU 4102  O   HOH A 629     6241   6225   5856   -190   -253    453       O  
HETATM 4103  O   HOH A 630      27.793  20.793  25.462  1.00 61.80           O  
ANISOU 4103  O   HOH A 630     9504   6381   7595   -233  -2072    315       O  
HETATM 4104  O   HOH A 631       7.109 -22.114  14.332  1.00 53.30           O  
ANISOU 4104  O   HOH A 631     6825   6529   6897    273    -97    108       O  
HETATM 4105  O   HOH A 632       9.630  -8.407  43.271  1.00 60.11           O  
ANISOU 4105  O   HOH A 632     7783   8037   7017   1478    407     55       O  
HETATM 4106  O   HOH A 633       8.814   1.028  -4.625  1.00 55.93           O  
ANISOU 4106  O   HOH A 633     7532   6903   6816    152   -267     65       O  
HETATM 4107  O   HOH A 634       8.197 -15.176  38.252  1.00 56.17           O  
ANISOU 4107  O   HOH A 634     6926   7558   6858    978    481    280       O  
HETATM 4108  O   HOH A 635       7.630 -24.324  25.573  1.00 61.05           O  
ANISOU 4108  O   HOH A 635     7563   7735   7899    322    119    329       O  
HETATM 4109  O   HOH A 636      -7.261   3.086  20.986  1.00 45.47           O  
ANISOU 4109  O   HOH A 636     5714   6121   5442   1437     21     90       O  
HETATM 4110  O   HOH A 637       8.188  -3.234  12.577  1.00 36.94           O  
ANISOU 4110  O   HOH A 637     4892   4539   4606    433    -41    -31       O  
HETATM 4111  O   HOH A 638       5.685  -8.271   6.295  1.00 44.28           O  
ANISOU 4111  O   HOH A 638     5784   5444   5595    325    -85    -13       O  
HETATM 4112  O   HOH A 639       3.667  -8.045   8.108  1.00 39.33           O  
ANISOU 4112  O   HOH A 639     5092   4839   5012    357    -79     20       O  
HETATM 4113  O   HOH A 640      17.633 -11.010   5.465  1.00 62.56           O  
ANISOU 4113  O   HOH A 640     8120   7987   7663    357     94    -34       O  
HETATM 4114  O   HOH A 641      11.802  -3.108  29.366  1.00 39.41           O  
ANISOU 4114  O   HOH A 641     5311   4943   4720    890     64    -98       O  
HETATM 4115  O   HOH A 642      11.152 -22.913  20.010  1.00 51.93           O  
ANISOU 4115  O   HOH A 642     6611   6447   6673    356     66     91       O  
HETATM 4116  O   HOH A 643      25.259   4.383  -1.906  1.00 58.95           O  
ANISOU 4116  O   HOH A 643     7553   7850   6994   -253   -174    646       O  
HETATM 4117  O   HOH A 644      15.116  -6.254  37.773  1.00 55.91           O  
ANISOU 4117  O   HOH A 644     7435   7118   6690   1071    158   -101       O  
HETATM 4118  O   HOH A 645      18.299  -7.773   2.078  1.00 56.42           O  
ANISOU 4118  O   HOH A 645     7354   7276   6805    293     67     40       O  
HETATM 4119  O   HOH A 646      15.938 -12.193  36.002  1.00 61.57           O  
ANISOU 4119  O   HOH A 646     7919   7908   7567    835    300      0       O  
HETATM 4120  O   HOH A 647       6.764 -10.897   6.620  1.00 43.98           O  
ANISOU 4120  O   HOH A 647     5745   5407   5561    318    -69    -21       O  
HETATM 4121  O   HOH A 648       1.845  -4.413  40.758  1.00 66.48           O  
ANISOU 4121  O   HOH A 648     8439   9131   7690   1845    457    139       O  
HETATM 4122  O   HOH A 649       3.346   5.185   6.612  1.00 53.36           O  
ANISOU 4122  O   HOH A 649     7208   6432   6633    470   -342    -45       O  
HETATM 4123  O   HOH A 650      -9.142  -9.863  21.318  1.00 61.82           O  
ANISOU 4123  O   HOH A 650     7123   8464   7900    791    189    613       O  
HETATM 4124  O   HOH A 651      -2.430 -12.483  15.484  1.00 58.87           O  
ANISOU 4124  O   HOH A 651     7173   7565   7629    424      9    310       O  
HETATM 4125  O   HOH A 652      16.359  -7.988   4.484  1.00 51.09           O  
ANISOU 4125  O   HOH A 652     6684   6502   6225    291     46      0       O  
HETATM 4126  O   HOH A 653      24.539   1.223  -2.539  1.00 66.64           O  
ANISOU 4126  O   HOH A 653     8512   8886   7922    -80    -39    520       O  
HETATM 4127  O   HOH A 654      24.648  -7.585   4.744  1.00 62.02           O  
ANISOU 4127  O   HOH A 654     7896   8218   7450    260    162    172       O  
HETATM 4128  O   HOH A 655       1.423   8.041  15.338  1.00 61.12           O  
ANISOU 4128  O   HOH A 655     8300   7444   7480    946   -364   -144       O  
HETATM 4129  O   HOH A 656       1.788 -21.401  24.277  1.00 54.21           O  
ANISOU 4129  O   HOH A 656     6492   7031   7076    320    120    494       O  
HETATM 4130  O   HOH A 657       8.885 -11.693   4.961  1.00 70.71           O  
ANISOU 4130  O   HOH A 657     9186   8797   8883    322    -64    -53       O  
HETATM 4131  O   HOH A 658      -7.268  -4.750  13.659  1.00 59.05           O  
ANISOU 4131  O   HOH A 658     7185   7702   7550    714    -33    276       O  
HETATM 4132  O   HOH A 659      -7.298   3.302  23.581  1.00 44.43           O  
ANISOU 4132  O   HOH A 659     5583   6080   5218   1604     73     89       O  
HETATM 4133  O   HOH A 660       0.516 -22.465  26.550  1.00 73.57           O  
ANISOU 4133  O   HOH A 660     8825   9591   9536    315    153    633       O  
HETATM 4134  O   HOH A 661      12.497  -8.587   4.892  1.00 66.85           O  
ANISOU 4134  O   HOH A 661     8702   8391   8307    306     -4    -38       O  
HETATM 4135  O   HOH A 662       3.964   8.821  15.005  1.00 55.46           O  
ANISOU 4135  O   HOH A 662     7677   6629   6765    827   -435   -148       O  
HETATM 4136  O   HOH A 663      25.226  -0.502  17.688  1.00 61.89           O  
ANISOU 4136  O   HOH A 663     8063   7783   7668     89   -171    172       O  
HETATM 4137  O   HOH A 664       0.741  -9.551  10.012  1.00 35.22           O  
ANISOU 4137  O   HOH A 664     4447   4373   4562    377    -75    102       O  
HETATM 4138  O   HOH A 665      13.162   3.884  -5.931  1.00 41.60           O  
ANISOU 4138  O   HOH A 665     5713   5199   4893     13   -281    225       O  
HETATM 4139  O   HOH A 666       7.202   5.609  -0.556  1.00 44.00           O  
ANISOU 4139  O   HOH A 666     6091   5246   5383    176   -393     56       O  
HETATM 4140  O   HOH A 667      -1.243 -14.028  12.188  1.00 57.00           O  
ANISOU 4140  O   HOH A 667     7055   7180   7423    308    -92    247       O  
HETATM 4141  O   HOH A 668       4.433   6.541   3.129  1.00 64.70           O  
ANISOU 4141  O   HOH A 668     8721   7815   8048    341   -419    -12       O  
HETATM 4142  O   HOH A 669      27.638  18.192  25.017  1.00 70.65           O  
ANISOU 4142  O   HOH A 669    10389   7723   8732   -194  -1773    298       O  
HETATM 4143  O   HOH A 670       3.864   9.144   3.637  1.00 67.84           O  
ANISOU 4143  O   HOH A 670     9218   8133   8423    387   -523    -24       O  
HETATM 4144  O   HOH A 671       4.675   5.457   0.819  1.00 62.09           O  
ANISOU 4144  O   HOH A 671     8365   7512   7715    275   -397      8       O  
HETATM 4145  O   HOH A 672       2.711   8.426  18.813  1.00 66.77           O  
ANISOU 4145  O   HOH A 672     9093   8152   8125   1069   -370   -184       O  
HETATM 4146  O   HOH A 673      19.332 -20.860  15.731  1.00 64.31           O  
ANISOU 4146  O   HOH A 673     8301   8112   8023    495    152   -105       O  
HETATM 4147  O   HOH A 674       6.659   8.058  -1.909  1.00 61.45           O  
ANISOU 4147  O   HOH A 674     8385   7391   7573    145   -496     81       O  
HETATM 4148  O   HOH A 675      -6.191  -8.013  15.301  1.00 57.15           O  
ANISOU 4148  O   HOH A 675     6873   7486   7356    617     16    340       O  
HETATM 4149  O   HOH A 676       1.143  -9.238   6.949  1.00 58.42           O  
ANISOU 4149  O   HOH A 676     7468   7246   7484    332   -136     62       O  
HETATM 4150  O   HOH A 677       1.088   2.989  -5.170  1.00 50.53           O  
ANISOU 4150  O   HOH A 677     6884   6051   6264    245   -435      6       O  
HETATM 4151  O   HOH A 678      15.256   2.179  -6.700  1.00 40.95           O  
ANISOU 4151  O   HOH A 678     5569   5251   4740     32   -193    258       O  
HETATM 4152  O   HOH A 679      19.172  -2.865  26.916  1.00 59.76           O  
ANISOU 4152  O   HOH A 679     7934   7399   7374    544    -61    -74       O  
HETATM 4153  O   HOH A 680      15.479 -12.012   4.320  1.00 64.16           O  
ANISOU 4153  O   HOH A 680     8367   8123   7888    373     50    -66       O  
HETATM 4154  O   HOH A 681      14.058  -6.329   0.170  1.00 59.17           O  
ANISOU 4154  O   HOH A 681     7785   7488   7209    267    -31      8       O  
HETATM 4155  O   HOH A 682      18.839  -0.351  27.444  1.00 72.97           O  
ANISOU 4155  O   HOH A 682     9722   8992   9012    582   -172    -94       O  
HETATM 4156  O   HOH A 683      -9.660  -6.466  17.256  1.00 70.32           O  
ANISOU 4156  O   HOH A 683     8360   9383   8973    815     72    460       O  
HETATM 4157  O   HOH A 684      35.089  18.608  25.440  1.00 65.33           O  
ANISOU 4157  O   HOH A 684     9489   7125   8208   -778  -2068    746       O  
HETATM 4158  O   HOH A 685      11.609  -6.747  43.316  1.00 67.74           O  
ANISOU 4158  O   HOH A 685     8908   8863   7967   1475    300    -45       O  
HETATM 4159  O   HOH A 686       8.425 -18.850   8.165  1.00 69.25           O  
ANISOU 4159  O   HOH A 686     8991   8528   8792    326   -121    -34       O  
HETATM 4160  O   HOH A 687      36.717  17.035  26.779  1.00 64.89           O  
ANISOU 4160  O   HOH A 687     9310   7174   8171   -791  -1989    772       O  
HETATM 4161  O   HOH A 688      28.877  -3.064   4.752  1.00 51.57           O  
ANISOU 4161  O   HOH A 688     6434   7062   6100     26     88    449       O  
HETATM 4162  O   HOH A 689       6.646 -23.964  28.137  1.00 73.41           O  
ANISOU 4162  O   HOH A 689     9036   9407   9448    359    186    414       O  
HETATM 4163  O   HOH A 690       5.647  -7.062  -0.153  1.00 60.64           O  
ANISOU 4163  O   HOH A 690     7991   7467   7581    278   -187    -39       O  
HETATM 4164  O   HOH A 691      14.931 -10.542  37.887  1.00 66.85           O  
ANISOU 4164  O   HOH A 691     8640   8604   8154    971    294    -12       O  
HETATM 4165  O   HOH A 692      18.704 -21.209  18.323  1.00 68.30           O  
ANISOU 4165  O   HOH A 692     8774   8601   8575    478    166    -78       O  
HETATM 4166  O   HOH A 693      17.527 -12.950  33.824  1.00 60.24           O  
ANISOU 4166  O   HOH A 693     7739   7693   7455    718    278    -15       O  
HETATM 4167  O   HOH A 694      29.053  11.093  -1.082  1.00 61.77           O  
ANISOU 4167  O   HOH A 694     7905   8147   7417   -729   -558   1080       O  
HETATM 4168  O   HOH A 695      33.506  19.552  27.367  1.00 70.43           O  
ANISOU 4168  O   HOH A 695    10390   7573   8799   -587  -2186    576       O  
HETATM 4169  O   HOH A 696      26.150   1.514   7.212  1.00 46.47           O  
ANISOU 4169  O   HOH A 696     5979   6084   5593   -126   -150    423       O  
HETATM 4170  O   HOH A 697      12.200  -7.622   1.349  1.00 58.68           O  
ANISOU 4170  O   HOH A 697     7722   7362   7213    290    -46    -31       O  
HETATM 4171  O   HOH A 698       0.745 -20.269  34.079  1.00 73.83           O  
ANISOU 4171  O   HOH A 698     8732   9971   9350    646    429    713       O  
HETATM 4172  O   HOH A 699      12.535 -11.562  32.267  1.00 75.77           O  
ANISOU 4172  O   HOH A 699     9642   9726   9421    788    298     35       O  
HETATM 4173  O   HOH A 700       4.371   9.924  17.435  1.00 57.26           O  
ANISOU 4173  O   HOH A 700     8003   6821   6932    948   -486   -189       O  
HETATM 4174  O   HOH A 701      24.717  -9.989   8.858  1.00 65.88           O  
ANISOU 4174  O   HOH A 701     8381   8631   8020    320    189     87       O  
HETATM 4175  O   HOH A 702      15.368  -5.282  41.093  1.00 71.68           O  
ANISOU 4175  O   HOH A 702     9547   9120   8568   1251    128   -138       O  
HETATM 4176  O   HOH A 703      -0.644   4.689   8.904  1.00 50.39           O  
ANISOU 4176  O   HOH A 703     6728   6148   6272    674   -296    -50       O  
HETATM 4177  O   HOH A 704      -3.186  -6.370  36.340  1.00 62.43           O  
ANISOU 4177  O   HOH A 704     7521   8828   7372   1641    533    390       O  
HETATM 4178  O   HOH A 705      23.906  -9.615   3.349  1.00 66.01           O  
ANISOU 4178  O   HOH A 705     8438   8728   7913    355    188    109       O  
HETATM 4179  O   HOH A 706      10.562   8.014  38.363  1.00 71.63           O  
ANISOU 4179  O   HOH A 706    10255   8712   8249   1787   -471   -417       O  
HETATM 4180  O   HOH A 707      15.019   8.039  33.857  1.00 62.99           O  
ANISOU 4180  O   HOH A 707     9102   7412   7421   1196   -612   -320       O  
HETATM 4181  O   HOH A 708      21.764 -10.677   2.613  1.00 60.46           O  
ANISOU 4181  O   HOH A 708     7808   7934   7230    394    159     38       O  
HETATM 4182  O   HOH A 709      12.807 -11.570  35.135  1.00 73.10           O  
ANISOU 4182  O   HOH A 709     9323   9429   9022    887    326     41       O  
HETATM 4183  O   HOH A 710      -4.748   3.332  19.935  1.00 58.88           O  
ANISOU 4183  O   HOH A 710     7547   7647   7176   1286    -40     17       O  
HETATM 4184  O   HOH A 711      21.635  18.865  27.294  1.00 63.36           O  
ANISOU 4184  O   HOH A 711     9763   6685   7627    409  -1696    -68       O  
HETATM 4185  O   HOH A 712      29.585  -5.230  24.134  1.00 68.11           O  
ANISOU 4185  O   HOH A 712     8738   8671   8470    191    -58    137       O  
HETATM 4186  O   HOH A 713      30.657  -8.853  22.744  1.00 78.30           O  
ANISOU 4186  O   HOH A 713     9904  10106   9740    248     91    131       O  
HETATM 4187  O   HOH A 714       1.864   1.101   7.611  1.00 41.72           O  
ANISOU 4187  O   HOH A 714     5560   5070   5222    492   -213    -24       O  
HETATM 4188  O   HOH A 715       3.122   9.042  23.332  1.00 46.42           O  
ANISOU 4188  O   HOH A 715     6618   5596   5423   1317   -376   -243       O  
HETATM 4189  O   HOH A 716       7.508  14.101  17.872  1.00 69.76           O  
ANISOU 4189  O   HOH A 716     9919   8126   8461    868   -805   -214       O  
HETATM 4190  O   HOH A 717      33.615  14.610  16.492  1.00 74.14           O  
ANISOU 4190  O   HOH A 717     9958   8910   9302   -842  -1334    906       O  
HETATM 4191  O   HOH A 718      29.117  -4.815  19.032  1.00 72.69           O  
ANISOU 4191  O   HOH A 718     9247   9350   9021    123    -14    202       O  
HETATM 4192  O   HOH A 719      12.563 -11.957   2.133  1.00 65.03           O  
ANISOU 4192  O   HOH A 719     8533   8153   8022    361    -30    -81       O  
HETATM 4193  O   HOH A 720      25.032  -6.431  15.061  1.00 66.74           O  
ANISOU 4193  O   HOH A 720     8520   8587   8250    211     81    112       O  
HETATM 4194  O   HOH A 721      19.671  19.210  25.468  1.00 74.89           O  
ANISOU 4194  O   HOH A 721    11199   8176   9081    460  -1631    -91       O  
HETATM 4195  O   HOH A 722      -2.361 -16.817  12.348  1.00 63.59           O  
ANISOU 4195  O   HOH A 722     7838   7995   8328    221   -161    339       O  
HETATM 4196  O   HOH A 723      36.222  18.624  19.224  1.00 76.39           O  
ANISOU 4196  O   HOH A 723    10501   8870   9655  -1115  -1891   1088       O  
HETATM 4197  O   HOH A 724      13.655 -13.556   3.961  1.00 72.87           O  
ANISOU 4197  O   HOH A 724     9502   9158   9026    386      4    -92       O  
HETATM 4198  O   HOH A 725      -7.090 -10.660  25.150  1.00 61.28           O  
ANISOU 4198  O   HOH A 725     7077   8460   7748    883    301    603       O  
HETATM 4199  O   HOH A 726      30.388  13.020   6.810  1.00 67.86           O  
ANISOU 4199  O   HOH A 726     8884   8522   8376   -806   -890    985       O  
HETATM 4200  O   HOH A 727      -3.456  -6.742   8.701  1.00 68.39           O  
ANISOU 4200  O   HOH A 727     8583   8618   8783    441   -139    154       O  
HETATM 4201  O   HOH A 728       6.369  -0.036  -4.626  1.00 45.35           O  
ANISOU 4201  O   HOH A 728     6189   5515   5527    196   -288     20       O  
HETATM 4202  O   HOH A 729      26.710  14.108  -4.867  1.00 78.18           O  
ANISOU 4202  O   HOH A 729    10130  10119   9454   -828   -700   1156       O  
HETATM 4203  O   HOH A 730       1.502  -5.329  -6.400  1.00 63.00           O  
ANISOU 4203  O   HOH A 730     8411   7663   7862    248   -379    -38       O  
HETATM 4204  O   HOH A 731      15.798   2.049  36.988  1.00 64.74           O  
ANISOU 4204  O   HOH A 731     9007   7914   7675   1201   -255   -257       O  
HETATM 4205  O   HOH A 732      31.625   4.680  -0.023  1.00 71.91           O  
ANISOU 4205  O   HOH A 732     8914   9805   8605   -430   -163    963       O  
HETATM 4206  O   HOH A 733       9.449   5.748   9.833  1.00 59.07           O  
ANISOU 4206  O   HOH A 733     8003   7124   7315    359   -354    -22       O  
HETATM 4207  O   HOH A 734      23.354  18.875   4.477  1.00 65.45           O  
ANISOU 4207  O   HOH A 734     9125   7668   8074   -720  -1276    784       O  
HETATM 4208  O   HOH A 735      23.156  18.400  24.631  1.00 58.00           O  
ANISOU 4208  O   HOH A 735     8897   6097   7042    137  -1646     87       O  
HETATM 4209  O   HOH A 736       9.754   1.753  16.366  1.00 52.37           O  
ANISOU 4209  O   HOH A 736     7025   6396   6475    539   -165    -71       O  
HETATM 4210  O   HOH A 737      27.428  -7.235  25.643  1.00 93.20           O  
ANISOU 4210  O   HOH A 737    11940  11820  11652    312     27     46       O  
HETATM 4211  O   HOH A 738       5.481  12.984  11.601  1.00 82.89           O  
ANISOU 4211  O   HOH A 738    11389   9879  10228    656   -702   -126       O  
HETATM 4212  O   HOH A 739      -9.224 -23.097  23.822  1.00 63.43           O  
ANISOU 4212  O   HOH A 739     7052   8596   8454     96    -33   1169       O  
HETATM 4213  O   HOH A 740       8.974  10.450  -2.398  1.00 67.61           O  
ANISOU 4213  O   HOH A 740     9236   8138   8314     29   -589    166       O  
HETATM 4214  O   HOH A 741      28.809   3.404  29.850  1.00 90.85           O  
ANISOU 4214  O   HOH A 741    12129  11080  11311    196   -615     93       O  
HETATM 4215  O   HOH A 742       7.057  12.668  -3.645  1.00 74.77           O  
ANISOU 4215  O   HOH A 742    10245   8945   9218     44   -710    159       O  
HETATM 4216  O   HOH A 743       1.069   9.619  21.917  1.00 73.79           O  
ANISOU 4216  O   HOH A 743    10048   9097   8891   1370   -378   -234       O  
HETATM 4217  O   HOH A 744      -5.649  -4.710  34.004  1.00 85.08           O  
ANISOU 4217  O   HOH A 744    10335  11737  10255   1692    494    405       O  
HETATM 4218  O   HOH A 745       3.076  12.058  21.631  1.00 68.24           O  
ANISOU 4218  O   HOH A 745     9570   8195   8164   1314   -567   -285       O  
HETATM 4219  O   HOH A 746      -6.100 -17.510  14.600  1.00 83.28           O  
ANISOU 4219  O   HOH A 746    10087  10659  10897    196   -158    567       O  
HETATM 4220  O   HOH A 747       9.852  12.590   8.223  1.00 80.17           O  
ANISOU 4220  O   HOH A 747    10993   9537   9930    282   -722     21       O  
HETATM 4221  O   HOH A 748      21.562 -16.946  22.584  1.00 72.23           O  
ANISOU 4221  O   HOH A 748     9207   9189   9051    471    242    -53       O  
HETATM 4222  O   HOH A 749      11.581  -5.492  -6.885  1.00 80.10           O  
ANISOU 4222  O   HOH A 749    10578  10116   9739    284   -138      5       O  
HETATM 4223  O   HOH A 750      10.120 -18.708   2.552  1.00 81.14           O  
ANISOU 4223  O   HOH A 750    10674  10014  10141    407   -184   -134       O  
HETATM 4224  O   HOH A 751      23.731  15.175  25.795  1.00 76.19           O  
ANISOU 4224  O   HOH A 751    10982   8604   9362    186  -1372     64       O  
HETATM 4225  O   HOH A 752      -1.215 -19.273  32.768  1.00 78.22           O  
ANISOU 4225  O   HOH A 752     9218  10582   9921    656    416    756       O  
HETATM 4226  O   HOH A 753      13.136 -12.958  39.286  1.00 78.15           O  
ANISOU 4226  O   HOH A 753     9953  10155   9586   1003    390     82       O  
HETATM 4227  O   HOH A 754      33.633   5.155   8.556  1.00 96.24           O  
ANISOU 4227  O   HOH A 754    12075  12590  11903   -514   -371    876       O  
HETATM 4228  O   HOH A 755      26.387 -11.288  15.414  1.00 75.96           O  
ANISOU 4228  O   HOH A 755     9623   9851   9388    335    203     57       O  
HETATM 4229  O   HOH A 756      -5.769 -20.561  14.318  1.00 67.70           O  
ANISOU 4229  O   HOH A 756     8149   8588   8987     70   -264    619       O  
HETATM 4230  O   HOH A 757      26.158   4.572  35.370  1.00 91.97           O  
ANISOU 4230  O   HOH A 757    12582  11050  11314    561   -715   -105       O  
HETATM 4231  O   HOH A 758      -1.869  -1.643  41.075  1.00 84.71           O  
ANISOU 4231  O   HOH A 758    10726  11640   9820   2216    478    155       O  
HETATM 4232  O   HOH A 759      -0.389 -12.694   9.665  1.00 72.72           O  
ANISOU 4232  O   HOH A 759     9149   9103   9379    304   -126    165       O  
HETATM 4233  O   HOH A 760      25.410  17.134  25.827  1.00 72.44           O  
ANISOU 4233  O   HOH A 760    10627   7991   8906     39  -1614    148       O  
HETATM 4234  O   HOH A 761      34.152   3.308   6.855  1.00 98.78           O  
ANISOU 4234  O   HOH A 761    12284  13094  12155   -431   -218    887       O  
HETATM 4235  O   HOH A 762      29.245  -4.279  16.319  1.00 82.08           O  
ANISOU 4235  O   HOH A 762    10400  10604  10182     78     -4    255       O  
HETATM 4236  O   HOH A 763      32.297  21.985  19.548  1.00 88.20           O  
ANISOU 4236  O   HOH A 763    12465   9949  11099   -934  -2174    867       O  
HETATM 4237  O   HOH A 764      20.528  21.595   0.806  1.00103.87           O  
ANISOU 4237  O   HOH A 764    14157  12401  12907   -748  -1420    803       O  
HETATM 4238  O   HOH A 765      -1.961 -14.959  34.768  1.00 85.09           O  
ANISOU 4238  O   HOH A 765    10118  11615  10598    994    529    667       O  
HETATM 4239  O   HOH A 766      -4.106 -13.218  33.361  1.00 74.63           O  
ANISOU 4239  O   HOH A 766     8737  10358   9261   1066    518    685       O  
HETATM 4240  O   HOH A 767      -1.315 -12.112  35.020  1.00 78.51           O  
ANISOU 4240  O   HOH A 767     9415  10750   9667   1163    530    527       O  
HETATM 4241  O   HOH A 768      -2.256 -10.568   8.747  1.00 82.26           O  
ANISOU 4241  O   HOH A 768    10331  10335  10587    336   -148    179       O  
HETATM 4242  O   HOH A 769      18.516  22.278  -0.946  1.00 87.18           O  
ANISOU 4242  O   HOH A 769    12112  10240  10773   -696  -1432    757       O  
HETATM 4243  O   HOH A 770      24.053  -9.533  15.074  1.00 87.87           O  
ANISOU 4243  O   HOH A 770    11185  11273  10929    302    156     45       O  
HETATM 4244  O   HOH A 771      -4.809  -0.935  40.029  1.00 68.65           O  
ANISOU 4244  O   HOH A 771     8553   9773   7757   2335    520    234       O  
HETATM 4245  O   HOH B 601      29.523 -22.700  20.991  1.00 29.35           O  
ANISOU 4245  O   HOH B 601     3746   3939   3467    652    294   -101       O  
HETATM 4246  O   HOH B 602      21.681 -24.132  38.575  1.00 33.77           O  
ANISOU 4246  O   HOH B 602     4304   4351   4175    648    352     82       O  
HETATM 4247  O   HOH B 603      35.284 -22.493  12.140  1.00 38.75           O  
ANISOU 4247  O   HOH B 603     4803   5631   4289    931    412    -27       O  
HETATM 4248  O   HOH B 604       8.725 -21.453  27.165  1.00 42.11           O  
ANISOU 4248  O   HOH B 604     5161   5415   5424    433    225    265       O  
HETATM 4249  O   HOH B 605       9.005 -24.794  29.919  1.00 37.42           O  
ANISOU 4249  O   HOH B 605     4532   4830   4855    393    219    367       O  
HETATM 4250  O   HOH B 606      18.829 -23.508  38.123  1.00 38.31           O  
ANISOU 4250  O   HOH B 606     4834   4962   4761    643    369    138       O  
HETATM 4251  O   HOH B 607      23.995 -24.503  37.155  1.00 34.04           O  
ANISOU 4251  O   HOH B 607     4363   4355   4216    632    326     25       O  
HETATM 4252  O   HOH B 608      38.801 -33.724  26.563  1.00 53.62           O  
ANISOU 4252  O   HOH B 608     6895   7117   6360   1170    256   -233       O  
HETATM 4253  O   HOH B 609      27.934 -21.564   6.490  1.00 40.53           O  
ANISOU 4253  O   HOH B 609     5309   5548   4542    858    267   -143       O  
HETATM 4254  O   HOH B 610      44.589 -27.063  35.046  1.00 39.14           O  
ANISOU 4254  O   HOH B 610     4710   5492   4669    854    288     12       O  
HETATM 4255  O   HOH B 611      21.594 -20.176  45.143  1.00 44.73           O  
ANISOU 4255  O   HOH B 611     5775   5832   5387    876    396     77       O  
HETATM 4256  O   HOH B 612      46.937 -25.817  34.084  1.00 45.72           O  
ANISOU 4256  O   HOH B 612     5410   6486   5476    835    291     98       O  
HETATM 4257  O   HOH B 613      26.376 -28.269  36.828  1.00 38.67           O  
ANISOU 4257  O   HOH B 613     4984   4897   4813    642    284      2       O  
HETATM 4258  O   HOH B 614      42.153 -27.062  28.758  1.00 43.51           O  
ANISOU 4258  O   HOH B 614     5286   6102   5144    914    354    -25       O  
HETATM 4259  O   HOH B 615      20.672 -32.456  39.996  1.00 45.24           O  
ANISOU 4259  O   HOH B 615     5773   5693   5722    538    241    244       O  
HETATM 4260  O   HOH B 616      11.659 -23.676  38.132  1.00 56.71           O  
ANISOU 4260  O   HOH B 616     6964   7460   7124    627    414    381       O  
HETATM 4261  O   HOH B 617      36.210 -35.354  31.895  1.00 56.66           O  
ANISOU 4261  O   HOH B 617     7378   7249   6903   1014    179   -208       O  
HETATM 4262  O   HOH B 618       9.694 -30.652  22.006  1.00 55.59           O  
ANISOU 4262  O   HOH B 618     7137   6727   7259    217   -173    257       O  
HETATM 4263  O   HOH B 619      38.716 -24.724  20.987  1.00 50.78           O  
ANISOU 4263  O   HOH B 619     6242   7080   5973    896    396    -25       O  
HETATM 4264  O   HOH B 620      30.080 -15.452  24.861  1.00 42.63           O  
ANISOU 4264  O   HOH B 620     5367   5606   5223    444    244      8       O  
HETATM 4265  O   HOH B 621      18.644 -35.115  30.494  1.00 42.53           O  
ANISOU 4265  O   HOH B 621     5598   5090   5473    431    -35    147       O  
HETATM 4266  O   HOH B 622      19.078 -34.788  37.351  1.00 47.13           O  
ANISOU 4266  O   HOH B 622     6052   5825   6033    446    116    284       O  
HETATM 4267  O   HOH B 623      38.773 -22.952  14.424  1.00 49.21           O  
ANISOU 4267  O   HOH B 623     5987   7117   5594    971    460     42       O  
HETATM 4268  O   HOH B 624      36.671 -19.051  14.600  1.00 51.41           O  
ANISOU 4268  O   HOH B 624     6254   7285   5995    712    414    113       O  
HETATM 4269  O   HOH B 625      29.701 -12.906  24.932  1.00 46.69           O  
ANISOU 4269  O   HOH B 625     5904   6088   5748    385    192     34       O  
HETATM 4270  O   HOH B 626      29.566 -37.383  37.630  1.00 49.59           O  
ANISOU 4270  O   HOH B 626     6563   6088   6192    747     91    -34       O  
HETATM 4271  O   HOH B 627      25.793 -41.412  27.140  1.00 53.21           O  
ANISOU 4271  O   HOH B 627     7367   6223   6627    802   -280   -165       O  
HETATM 4272  O   HOH B 628      38.404 -25.020  23.562  1.00 44.67           O  
ANISOU 4272  O   HOH B 628     5493   6212   5268    850    371    -40       O  
HETATM 4273  O   HOH B 629      27.035 -42.365  32.958  1.00 52.63           O  
ANISOU 4273  O   HOH B 629     7208   6185   6604    745   -212    -62       O  
HETATM 4274  O   HOH B 630      20.518 -30.672  41.992  1.00 50.29           O  
ANISOU 4274  O   HOH B 630     6377   6417   6316    591    315    258       O  
HETATM 4275  O   HOH B 631      13.616 -34.646  26.217  1.00 46.26           O  
ANISOU 4275  O   HOH B 631     6054   5483   6041    279   -183    240       O  
HETATM 4276  O   HOH B 632      24.407 -18.453  26.108  1.00 50.25           O  
ANISOU 4276  O   HOH B 632     6407   6433   6254    511    270    -54       O  
HETATM 4277  O   HOH B 633      40.751 -24.826  13.989  1.00 53.04           O  
ANISOU 4277  O   HOH B 633     6443   7736   5974   1147    496     29       O  
HETATM 4278  O   HOH B 634      38.232 -20.146  24.891  1.00 55.71           O  
ANISOU 4278  O   HOH B 634     6817   7597   6754    613    331     73       O  
HETATM 4279  O   HOH B 635      18.908 -23.617  15.610  1.00 59.97           O  
ANISOU 4279  O   HOH B 635     7807   7497   7482    524     96   -123       O  
HETATM 4280  O   HOH B 636      47.701 -22.607  25.753  1.00 56.27           O  
ANISOU 4280  O   HOH B 636     6508   8205   6665    812    401    277       O  
HETATM 4281  O   HOH B 637      19.707 -31.819  44.301  1.00 46.67           O  
ANISOU 4281  O   HOH B 637     5890   5998   5843    591    330    353       O  
HETATM 4282  O   HOH B 638      21.469 -32.910  46.189  1.00 60.22           O  
ANISOU 4282  O   HOH B 638     7650   7698   7534    622    324    341       O  
HETATM 4283  O   HOH B 639      34.405 -19.014  25.435  1.00 45.12           O  
ANISOU 4283  O   HOH B 639     5592   6070   5481    547    299     18       O  
HETATM 4284  O   HOH B 640       9.107 -14.462  32.621  1.00 61.50           O  
ANISOU 4284  O   HOH B 640     7663   8042   7661    776    370    178       O  
HETATM 4285  O   HOH B 641       7.116 -34.173  22.042  1.00 70.95           O  
ANISOU 4285  O   HOH B 641     9103   8540   9314     55   -398    426       O  
HETATM 4286  O   HOH B 642      22.403 -36.455  39.180  1.00 53.45           O  
ANISOU 4286  O   HOH B 642     6932   6584   6791    522    104    216       O  
HETATM 4287  O   HOH B 643      21.392 -18.745  47.670  1.00 57.82           O  
ANISOU 4287  O   HOH B 643     7494   7522   6952    999    398     67       O  
HETATM 4288  O   HOH B 644      28.689 -17.706  12.430  1.00 53.85           O  
ANISOU 4288  O   HOH B 644     6818   7206   6437    586    302    -23       O  
HETATM 4289  O   HOH B 645      41.448 -34.293  27.944  1.00 61.46           O  
ANISOU 4289  O   HOH B 645     7823   8213   7318   1249    278   -219       O  
HETATM 4290  O   HOH B 646      39.781 -20.973  16.165  1.00 70.67           O  
ANISOU 4290  O   HOH B 646     8604   9865   8383    829    454    133       O  
HETATM 4291  O   HOH B 647      33.027 -38.221  24.436  1.00 61.84           O  
ANISOU 4291  O   HOH B 647     8302   7735   7457   1162      1   -333       O  
HETATM 4292  O   HOH B 648      37.255 -19.828  10.248  1.00 58.90           O  
ANISOU 4292  O   HOH B 648     7196   8419   6766    875    471    124       O  
HETATM 4293  O   HOH B 649      20.215 -26.145  46.664  1.00 58.63           O  
ANISOU 4293  O   HOH B 649     7425   7641   7212    789    443    252       O  
HETATM 4294  O   HOH B 650       7.951 -23.886  21.485  1.00 62.13           O  
ANISOU 4294  O   HOH B 650     7801   7766   8039    295     35    230       O  
HETATM 4295  O   HOH B 651      37.594 -38.448  20.277  1.00 61.88           O  
ANISOU 4295  O   HOH B 651     8284   8044   7183   1544     84   -425       O  
HETATM 4296  O   HOH B 652       5.777 -35.383  34.245  1.00 72.06           O  
ANISOU 4296  O   HOH B 652     8801   9131   9447     13    -83    909       O  
HETATM 4297  O   HOH B 653      18.224 -29.115  41.617  1.00 53.74           O  
ANISOU 4297  O   HOH B 653     6751   6918   6749    591    351    307       O  
HETATM 4298  O   HOH B 654      30.054 -14.537  52.412  1.00 55.83           O  
ANISOU 4298  O   HOH B 654     7594   7022   6597   1047     64   -117       O  
HETATM 4299  O   HOH B 655      41.469 -21.956  18.521  1.00 59.11           O  
ANISOU 4299  O   HOH B 655     7096   8424   6940    855    453    139       O  
HETATM 4300  O   HOH B 656      22.038 -20.741  16.809  1.00 61.33           O  
ANISOU 4300  O   HOH B 656     7894   7804   7604    529    201   -109       O  
HETATM 4301  O   HOH B 657      10.533 -25.887  39.409  1.00 68.37           O  
ANISOU 4301  O   HOH B 657     8370   8983   8625    578    412    510       O  
HETATM 4302  O   HOH B 658      38.250 -33.135  35.678  1.00 60.28           O  
ANISOU 4302  O   HOH B 658     7718   7796   7392    946    240   -147       O  
HETATM 4303  O   HOH B 659      40.354 -34.563  20.334  1.00 56.14           O  
ANISOU 4303  O   HOH B 659     7247   7652   6432   1474    284   -295       O  
HETATM 4304  O   HOH B 660      39.857 -32.126  33.599  1.00 51.27           O  
ANISOU 4304  O   HOH B 660     6504   6774   6201    986    270   -145       O  
HETATM 4305  O   HOH B 661      31.622 -10.987  34.679  1.00 61.90           O  
ANISOU 4305  O   HOH B 661     7993   7854   7672    450     37      5       O  
HETATM 4306  O   HOH B 662      29.603 -18.131   9.571  1.00 59.79           O  
ANISOU 4306  O   HOH B 662     7569   8068   7081    667    326    -15       O  
HETATM 4307  O   HOH B 663      31.970 -26.734  33.584  1.00 50.95           O  
ANISOU 4307  O   HOH B 663     6499   6560   6299    696    288    -84       O  
HETATM 4308  O   HOH B 664      35.281 -24.122  41.723  1.00 55.72           O  
ANISOU 4308  O   HOH B 664     7120   7170   6882    704    248    -46       O  
HETATM 4309  O   HOH B 665      38.860 -20.290  29.471  1.00 78.01           O  
ANISOU 4309  O   HOH B 665     9674  10323   9641    585    283     61       O  
HETATM 4310  O   HOH B 666      40.626 -21.838  28.045  1.00 70.03           O  
ANISOU 4310  O   HOH B 666     8598   9437   8574    669    324     73       O  
HETATM 4311  O   HOH B 667      22.598 -20.247  20.300  1.00 58.79           O  
ANISOU 4311  O   HOH B 667     7529   7490   7320    512    234    -85       O  
HETATM 4312  O   HOH B 668      36.727 -30.904   8.585  1.00 54.37           O  
ANISOU 4312  O   HOH B 668     7131   7610   5918   1595    321   -307       O  
HETATM 4313  O   HOH B 669      18.993 -18.461  44.432  1.00 64.62           O  
ANISOU 4313  O   HOH B 669     8272   8400   7880    929    417     97       O  
HETATM 4314  O   HOH B 670      43.363 -23.548  17.195  1.00 70.85           O  
ANISOU 4314  O   HOH B 670     8526  10086   8308   1025    506    148       O  
HETATM 4315  O   HOH B 671      37.703 -35.726  34.518  1.00 61.01           O  
ANISOU 4315  O   HOH B 671     7903   7817   7462   1023    187   -191       O  
HETATM 4316  O   HOH B 672      38.906 -21.338  12.107  1.00 60.86           O  
ANISOU 4316  O   HOH B 672     7408   8705   7012    946    487    111       O  
HETATM 4317  O   HOH B 673      17.875 -25.623  11.162  1.00 56.57           O  
ANISOU 4317  O   HOH B 673     7531   6974   6989    585    -37   -185       O  
HETATM 4318  O   HOH B 674      29.820 -27.275  10.769  1.00 37.04           O  
ANISOU 4318  O   HOH B 674     4960   4996   4118   1042    217   -256       O  
HETATM 4319  O   HOH B 675      38.686 -34.068  31.742  1.00 71.24           O  
ANISOU 4319  O   HOH B 675     9125   9239   8705   1056    235   -195       O  
HETATM 4320  O   HOH B 676      30.502 -29.326   9.220  1.00 40.99           O  
ANISOU 4320  O   HOH B 676     5564   5503   4509   1213    176   -322       O  
HETATM 4321  O   HOH B 677      28.538 -18.110  37.647  1.00 57.58           O  
ANISOU 4321  O   HOH B 677     7398   7350   7129    629    251    -45       O  
HETATM 4322  O   HOH B 678      28.966 -31.679   8.774  1.00 58.42           O  
ANISOU 4322  O   HOH B 678     7943   7532   6720   1269     45   -400       O  
HETATM 4323  O   HOH B 679      47.306 -21.398  37.884  1.00 66.63           O  
ANISOU 4323  O   HOH B 679     8082   9008   8226    591    138    189       O  
HETATM 4324  O   HOH B 680      39.977 -32.527  21.918  1.00 63.22           O  
ANISOU 4324  O   HOH B 680     8047   8545   7428   1297    319   -227       O  
HETATM 4325  O   HOH B 681      40.979 -31.262  24.039  1.00 59.12           O  
ANISOU 4325  O   HOH B 681     7428   8067   6967   1201    348   -166       O  
HETATM 4326  O   HOH B 682      16.783 -37.132  31.476  1.00 70.68           O  
ANISOU 4326  O   HOH B 682     9163   8593   9098    338   -130    267       O  
HETATM 4327  O   HOH B 683      29.564 -36.313  18.386  1.00 44.75           O  
ANISOU 4327  O   HOH B 683     6217   5534   5251   1128    -50   -365       O  
HETATM 4328  O   HOH B 684      10.856 -33.408  38.816  1.00 73.66           O  
ANISOU 4328  O   HOH B 684     9090   9435   9465    290    175    686       O  
HETATM 4329  O   HOH B 685      40.956 -28.458  40.811  1.00 67.50           O  
ANISOU 4329  O   HOH B 685     8518   8789   8341    818    241    -58       O  
HETATM 4330  O   HOH B 686      27.473 -18.981   7.258  1.00 54.99           O  
ANISOU 4330  O   HOH B 686     7067   7381   6446    715    282    -76       O  
HETATM 4331  O   HOH B 687      44.386 -14.444  31.880  1.00 64.94           O  
ANISOU 4331  O   HOH B 687     7853   8785   8036    300     64    330       O  
HETATM 4332  O   HOH B 688      27.824 -11.754  50.410  1.00 74.97           O  
ANISOU 4332  O   HOH B 688    10061   9420   9004   1073     32   -143       O  
HETATM 4333  O   HOH B 689      24.733 -18.914  23.327  1.00 55.27           O  
ANISOU 4333  O   HOH B 689     7043   7087   6870    507    265    -65       O  
HETATM 4334  O   HOH B 690      27.636 -38.474  39.556  1.00 62.43           O  
ANISOU 4334  O   HOH B 690     8193   7668   7860    673     62     61       O  
HETATM 4335  O   HOH B 691      14.332 -35.884  34.892  1.00 72.26           O  
ANISOU 4335  O   HOH B 691     9174   8958   9323    273    -15    455       O  
HETATM 4336  O   HOH B 692      11.250 -36.206  34.626  1.00 71.87           O  
ANISOU 4336  O   HOH B 692     9030   8942   9337    163    -64    615       O  
HETATM 4337  O   HOH B 693      33.460 -14.178  54.764  1.00 55.53           O  
ANISOU 4337  O   HOH B 693     7652   6905   6541   1034    -77   -139       O  
HETATM 4338  O   HOH B 694      37.604 -22.634  58.476  1.00 57.29           O  
ANISOU 4338  O   HOH B 694     7712   7233   6824   1011     60    -62       O  
HETATM 4339  O   HOH B 695      43.927  -9.125  35.052  1.00 74.59           O  
ANISOU 4339  O   HOH B 695     9280   9730   9330     92   -246    380       O  
HETATM 4340  O   HOH B 696      39.519 -22.149  60.267  1.00 74.88           O  
ANISOU 4340  O   HOH B 696    10002   9422   9025   1029    -30    -76       O  
HETATM 4341  O   HOH B 697      45.151 -22.446  18.813  1.00 68.98           O  
ANISOU 4341  O   HOH B 697     8170   9929   8110    940    501    244       O  
HETATM 4342  O   HOH B 698      11.711 -14.997  33.375  1.00 66.62           O  
ANISOU 4342  O   HOH B 698     8376   8633   8304    751    360    125       O  
HETATM 4343  O   HOH B 699      24.986 -11.052  36.520  1.00 65.55           O  
ANISOU 4343  O   HOH B 699     8549   8270   8088    655    130    -72       O  
HETATM 4344  O   HOH B 700      45.358 -28.798  50.211  1.00 65.70           O  
ANISOU 4344  O   HOH B 700     8367   8501   8096    861    102    -26       O  
HETATM 4345  O   HOH B 701      42.794 -28.200  50.728  1.00 70.79           O  
ANISOU 4345  O   HOH B 701     9079   9082   8735    848    127    -38       O  
HETATM 4346  O   HOH B 702      22.365 -12.557  46.538  1.00 57.39           O  
ANISOU 4346  O   HOH B 702     7644   7333   6828   1072    224    -77       O  
HETATM 4347  O   HOH B 703       6.563 -41.087  21.267  1.00 74.01           O  
ANISOU 4347  O   HOH B 703     9792   8527   9803   -119   -895    535       O  
HETATM 4348  O   HOH B 704       7.496 -33.998  19.010  1.00 72.39           O  
ANISOU 4348  O   HOH B 704     9408   8630   9465     94   -475    314       O  
HETATM 4349  O   HOH B 705      49.800 -20.085  39.324  1.00 64.99           O  
ANISOU 4349  O   HOH B 705     7799   8853   8040    512     45    284       O  
HETATM 4350  O   HOH B 706      20.128 -13.541  47.623  1.00 68.12           O  
ANISOU 4350  O   HOH B 706     8947   8794   8143   1164    314    -25       O  
HETATM 4351  O   HOH B 707      40.112 -27.277  50.583  1.00 66.19           O  
ANISOU 4351  O   HOH B 707     8540   8463   8148    835    160    -40       O  
HETATM 4352  O   HOH B 708      39.502 -24.832  61.967  1.00 73.89           O  
ANISOU 4352  O   HOH B 708     9867   9326   8879   1076     30    -51       O  
HETATM 4353  O   HOH B 709      35.427 -39.387  32.229  1.00 70.13           O  
ANISOU 4353  O   HOH B 709     9260   8781   8606   1090     44   -250       O  
HETATM 4354  O   HOH B 710      17.112 -20.475  44.514  1.00 68.01           O  
ANISOU 4354  O   HOH B 710     8608   8896   8338    900    467    194       O  
HETATM 4355  O   HOH B 711      35.034 -30.247   6.327  1.00 71.36           O  
ANISOU 4355  O   HOH B 711     9358   9714   8042   1581    288   -326       O  
HETATM 4356  O   HOH B 712      29.996 -15.540  20.384  1.00 59.97           O  
ANISOU 4356  O   HOH B 712     7536   7882   7368    447    269     24       O  
HETATM 4357  O   HOH B 713      50.920 -17.010  36.163  1.00 78.19           O  
ANISOU 4357  O   HOH B 713     9319  10674   9716    348      0    458       O  
HETATM 4358  O   HOH B 714      31.788 -44.707  32.040  1.00 73.40           O  
ANISOU 4358  O   HOH B 714     9983   8820   9086   1042   -264   -236       O  
HETATM 4359  O   HOH B 715       7.267 -42.026  19.227  1.00 78.58           O  
ANISOU 4359  O   HOH B 715    10545   8966  10344    -64  -1022    428       O  
HETATM 4360  O   HOH B 716      17.409 -12.111  28.174  1.00 73.95           O  
ANISOU 4360  O   HOH B 716     9463   9381   9254    577    229    -30       O  
HETATM 4361  O   HOH B 717      23.896 -12.635  50.220  1.00 80.62           O  
ANISOU 4361  O   HOH B 717    10692  10262   9676   1186    185   -100       O  
HETATM 4362  O   HOH B 718      35.220 -34.176  10.588  1.00 78.90           O  
ANISOU 4362  O   HOH B 718    10448  10422   9109   1622    163   -426       O  
HETATM 4363  O   HOH B 719      49.939 -20.070  53.438  1.00 92.56           O  
ANISOU 4363  O   HOH B 719    11803  11840  11525    609   -290    111       O  
HETATM 4364  O   HOH B 720      49.611 -30.676  53.508  1.00 87.90           O  
ANISOU 4364  O   HOH B 720    11155  11352  10892    935     13     -8       O  
HETATM 4365  O   HOH B 721      29.490  -4.002  46.957  1.00 87.32           O  
ANISOU 4365  O   HOH B 721    11897  10689  10591    920   -394   -196       O  
HETATM 4366  O   HOH B 722      10.653 -35.550  37.985  1.00 85.77           O  
ANISOU 4366  O   HOH B 722    10665  10866  11056    196     59    731       O  
HETATM 4367  O   HOH B 723      49.188 -29.540  50.811  1.00 73.07           O  
ANISOU 4367  O   HOH B 723     9208   9530   9026    893     48      6       O  
HETATM 4368  O   HOH B 724       7.079 -28.424  38.782  1.00 60.27           O  
ANISOU 4368  O   HOH B 724     7192   8015   7694    427    348    748       O  
HETATM 4369  O   HOH B 725      42.088 -22.957   8.162  1.00 83.90           O  
ANISOU 4369  O   HOH B 725    10222  12024   9634   1273    603    170       O  
HETATM 4370  O   HOH B 726      31.748  -5.801  44.044  1.00 83.62           O  
ANISOU 4370  O   HOH B 726    11207  10305  10259    683   -321   -105       O  
HETATM 4371  O   HOH B 727      20.920 -11.638  42.212  1.00 83.14           O  
ANISOU 4371  O   HOH B 727    10834  10578  10178    954    224    -71       O  
HETATM 4372  O   HOH B 728      14.825 -39.230  29.639  1.00 73.37           O  
ANISOU 4372  O   HOH B 728     9580   8794   9503    239   -318    332       O  
HETATM 4373  O   HOH B 729      42.896 -31.031  45.295  1.00 92.79           O  
ANISOU 4373  O   HOH B 729    11775  11947  11533    895    197    -65       O  
HETATM 4374  O   HOH B 730       2.415 -28.639  31.983  1.00 69.50           O  
ANISOU 4374  O   HOH B 730     8279   9075   9055    188    128    848       O  
HETATM 4375  O   HOH B 731      20.097  -9.863  32.372  1.00 76.07           O  
ANISOU 4375  O   HOH B 731     9840   9615   9448    656    169    -64       O  
HETATM 4376  O   HOH B 732      32.071 -16.091  22.937  1.00 66.85           O  
ANISOU 4376  O   HOH B 732     8373   8781   8246    457    269     39       O  
HETATM 4377  O   HOH B 733      43.466  -8.299  48.352  1.00 84.84           O  
ANISOU 4377  O   HOH B 733    11178  10519  10538    371   -609    110       O  
HETATM 4378  O   HOH B 734      18.114 -22.182  11.407  1.00 83.63           O  
ANISOU 4378  O   HOH B 734    10855  10500  10421    532     61   -149       O  
HETATM 4379  O   HOH B 735      33.174 -13.219  23.934  1.00 85.56           O  
ANISOU 4379  O   HOH B 735    10727  11148  10633    359    202    107       O  
HETATM 4380  O   HOH B 736      53.353 -14.589  31.522  1.00 78.31           O  
ANISOU 4380  O   HOH B 736     9036  11030   9690    198      7    743       O  
HETATM 4381  O   HOH B 737      35.693 -36.772  13.305  1.00 88.16           O  
ANISOU 4381  O   HOH B 737    11707  11457  10335   1662     81   -475       O  
HETATM 4382  O   HOH B 738      39.818 -23.236   6.490  1.00 76.98           O  
ANISOU 4382  O   HOH B 738     9492  11013   8745   1295    563     83       O  
HETATM 4383  O   HOH B 739       4.951 -26.703  31.153  1.00 71.43           O  
ANISOU 4383  O   HOH B 739     8658   9247   9234    296    183    628       O  
HETATM 4384  O   HOH B 740      22.317  -8.942  31.963  1.00 76.91           O  
ANISOU 4384  O   HOH B 740     9975   9691   9556    594    112    -67       O  
CONECT 3996 3997 3998 3999                                                      
CONECT 3997 3996                                                                
CONECT 3998 3996 4000                                                           
CONECT 3999 3996                                                                
CONECT 4000 3998 4001                                                           
CONECT 4001 4000 4002                                                           
CONECT 4002 4001 4003                                                           
CONECT 4003 4002 4004                                                           
CONECT 4004 4003 4005                                                           
CONECT 4005 4004 4006                                                           
CONECT 4006 4005                                                                
CONECT 4007 4008 4009 4010                                                      
CONECT 4008 4007                                                                
CONECT 4009 4007 4011                                                           
CONECT 4010 4007                                                                
CONECT 4011 4009 4012                                                           
CONECT 4012 4011 4013                                                           
CONECT 4013 4012 4014                                                           
CONECT 4014 4013 4015                                                           
CONECT 4015 4014 4016                                                           
CONECT 4016 4015 4017                                                           
CONECT 4017 4016                                                                
CONECT 4018 4019 4020 4021                                                      
CONECT 4019 4018                                                                
CONECT 4020 4018 4022                                                           
CONECT 4021 4018                                                                
CONECT 4022 4020 4023                                                           
CONECT 4023 4022 4024                                                           
CONECT 4024 4023 4025                                                           
CONECT 4025 4024 4026                                                           
CONECT 4026 4025 4027                                                           
CONECT 4027 4026 4028                                                           
CONECT 4028 4027                                                                
CONECT 4029 4030 4031                                                           
CONECT 4030 4029                                                                
CONECT 4031 4029 4032 4033                                                      
CONECT 4032 4031                                                                
CONECT 4033 4031 4034                                                           
CONECT 4034 4033                                                                
CONECT 4035 4036 4037 4038                                                      
CONECT 4036 4035                                                                
CONECT 4037 4035 4039                                                           
CONECT 4038 4035                                                                
CONECT 4039 4037 4040                                                           
CONECT 4040 4039 4041                                                           
CONECT 4041 4040 4042                                                           
CONECT 4042 4041 4043                                                           
CONECT 4043 4042 4044                                                           
CONECT 4044 4043 4045                                                           
CONECT 4045 4044                                                                
CONECT 4046 4047                                                                
CONECT 4047 4046 4048 4049                                                      
CONECT 4048 4047                                                                
CONECT 4049 4047 4050                                                           
CONECT 4050 4049 4051                                                           
CONECT 4051 4050 4052 4057                                                      
CONECT 4052 4051 4053                                                           
CONECT 4053 4052 4054                                                           
CONECT 4054 4053 4055 4056                                                      
CONECT 4055 4054                                                                
CONECT 4056 4054                                                                
CONECT 4057 4051 4058                                                           
CONECT 4058 4057 4059                                                           
CONECT 4059 4058 4060 4061                                                      
CONECT 4060 4059                                                                
CONECT 4061 4059                                                                
CONECT 4062 4063 4064                                                           
CONECT 4063 4062                                                                
CONECT 4064 4062 4065 4066                                                      
CONECT 4065 4064                                                                
CONECT 4066 4064 4067                                                           
CONECT 4067 4066                                                                
CONECT 4068 4069 4070                                                           
CONECT 4069 4068                                                                
CONECT 4070 4068 4071 4072                                                      
CONECT 4071 4070                                                                
CONECT 4072 4070 4073                                                           
CONECT 4073 4072                                                                
MASTER      464    0    8   27    8    0   16    6 4352    2   78   44          
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.