CNRS Nantes University UFIP UFIP
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***  P53  ***

elNémo ID: 20051000561962982

Job options:

ID        	=	 20051000561962982
JOBID     	=	 P53
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 P53

HEADER    DNA BINDING PROTEIN                     08-AUG-19   6SI1              
TITLE     P53 CANCER MUTANT Y220H                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELLULAR TUMOR ANTIGEN P53;                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: DNA-BINDING DOMAIN;                                        
COMPND   5 SYNONYM: ANTIGEN NY-CO-13,PHOSPHOPROTEIN P53,TUMOR SUPPRESSOR P53;   
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TP53, P53;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    P53, TRANSCRIPTION FACTOR, TUMOR SUPPRESSOR, CANCER THERAPY,          
KEYWDS   2 ONCOGENIC MUTANT, PROTEIN MISFOLDING, DNA-BINDING DOMAIN, MUTANT P53 
KEYWDS   3 RESCUE, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC,    
KEYWDS   4 DNA BINDING PROTEIN                                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.C.JOERGER,A.KRAEMER,S.KNAPP,STRUCTURAL GENOMICS CONSORTIUM (SGC)    
REVDAT   2   01-APR-20 6SI1    1       JRNL                                     
REVDAT   1   19-FEB-20 6SI1    0                                                
JRNL        AUTH   M.R.BAUER,A.KRAMER,G.SETTANNI,R.N.JONES,X.NI,R.KHAN TAREQUE, 
JRNL        AUTH 2 A.R.FERSHT,J.SPENCER,A.C.JOERGER                             
JRNL        TITL   TARGETING CAVITY-CREATING P53 CANCER MUTATIONS WITH          
JRNL        TITL 2 SMALL-MOLECULE STABILIZERS: THE Y220X PARADIGM.              
JRNL        REF    ACS CHEM.BIOL.                V.  15   657 2020              
JRNL        REFN                   ESSN 1554-8937                               
JRNL        PMID   31990523                                                     
JRNL        DOI    10.1021/ACSCHEMBIO.9B00748                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.44 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10.1_2155                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.44                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.78                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 86178                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.153                           
REMARK   3   R VALUE            (WORKING SET) : 0.152                           
REMARK   3   FREE R VALUE                     : 0.179                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4296                            
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 47.7770 -  4.4733    1.00     3000   161  0.1755 0.1851        
REMARK   3     2  4.4733 -  3.5509    0.96     2719   157  0.1475 0.1777        
REMARK   3     3  3.5509 -  3.1021    1.00     2861   140  0.1560 0.1447        
REMARK   3     4  3.1021 -  2.8186    1.00     2829   134  0.1608 0.2017        
REMARK   3     5  2.8186 -  2.6165    1.00     2807   143  0.1653 0.1954        
REMARK   3     6  2.6165 -  2.4623    1.00     2824   124  0.1613 0.1818        
REMARK   3     7  2.4623 -  2.3390    1.00     2774   145  0.1563 0.1597        
REMARK   3     8  2.3390 -  2.2372    1.00     2787   139  0.1522 0.1665        
REMARK   3     9  2.2372 -  2.1510    0.96     2676   140  0.1451 0.1938        
REMARK   3    10  2.1510 -  2.0768    0.96     2692   130  0.1446 0.1600        
REMARK   3    11  2.0768 -  2.0119    0.99     2756   137  0.1422 0.1667        
REMARK   3    12  2.0119 -  1.9544    0.99     2719   159  0.1385 0.1978        
REMARK   3    13  1.9544 -  1.9029    0.99     2743   136  0.1317 0.1549        
REMARK   3    14  1.9029 -  1.8565    0.99     2743   147  0.1346 0.1642        
REMARK   3    15  1.8565 -  1.8143    0.99     2718   150  0.1369 0.1857        
REMARK   3    16  1.8143 -  1.7757    0.98     2708   151  0.1362 0.1798        
REMARK   3    17  1.7757 -  1.7401    0.98     2722   156  0.1359 0.1783        
REMARK   3    18  1.7401 -  1.7073    0.98     2681   140  0.1366 0.1803        
REMARK   3    19  1.7073 -  1.6768    0.99     2745   143  0.1307 0.1476        
REMARK   3    20  1.6768 -  1.6484    0.98     2695   150  0.1270 0.1561        
REMARK   3    21  1.6484 -  1.6218    0.98     2676   143  0.1247 0.1652        
REMARK   3    22  1.6218 -  1.5968    0.98     2721   153  0.1280 0.1755        
REMARK   3    23  1.5968 -  1.5734    0.97     2612   143  0.1354 0.1932        
REMARK   3    24  1.5734 -  1.5512    0.93     2606   133  0.1378 0.2035        
REMARK   3    25  1.5512 -  1.5302    0.98     2699   155  0.1449 0.1881        
REMARK   3    26  1.5302 -  1.5104    0.98     2659   133  0.1458 0.1939        
REMARK   3    27  1.5104 -  1.4915    0.97     2670   151  0.1664 0.2131        
REMARK   3    28  1.4915 -  1.4735    0.98     2664   139  0.1859 0.2358        
REMARK   3    29  1.4735 -  1.4564    0.97     2681   138  0.2118 0.2537        
REMARK   3    30  1.4564 -  1.4400    0.97     2695   126  0.2466 0.2848        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.140            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.680           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 13.45                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.79                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           3247                                  
REMARK   3   ANGLE     :  0.832           4433                                  
REMARK   3   CHIRALITY :  0.082            486                                  
REMARK   3   PLANARITY :  0.007            588                                  
REMARK   3   DIHEDRAL  : 14.853           1227                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 6SI1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 09-AUG-19.                  
REMARK 100 THE DEPOSITION ID IS D_1292103749.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-JUN-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000031                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.27                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 86307                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.440                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.780                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 5.500                              
REMARK 200  R MERGE                    (I) : 0.08600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.44                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.47                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.63500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 2J1X                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN SOLUTION: 6 MG/ML PROTEIN IN     
REMARK 280  25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR     
REMARK 280  BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000,   
REMARK 280  5 MM DTT., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       32.38100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.43950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.38550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.43950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       32.38100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.38550            
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                                                    
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 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     SER A    94                                                      
REMARK 465     SER A    95                                                      
REMARK 465     GLY A   293                                                      
REMARK 465     GLU A   294                                                      
REMARK 465     PRO A   295                                                      
REMARK 465     HIS A   296                                                      
REMARK 465     HIS A   297                                                      
REMARK 465     GLU A   298                                                      
REMARK 465     LEU A   299                                                      
REMARK 465     PRO A   300                                                      
REMARK 465     PRO A   301                                                      
REMARK 465     GLY A   302                                                      
REMARK 465     SER A   303                                                      
REMARK 465     THR A   304                                                      
REMARK 465     LYS A   305                                                      
REMARK 465     ARG A   306                                                      
REMARK 465     ALA A   307                                                      
REMARK 465     LEU A   308                                                      
REMARK 465     PRO A   309                                                      
REMARK 465     ASN A   310                                                      
REMARK 465     ASN A   311                                                      
REMARK 465     THR A   312                                                      
REMARK 465     LYS B   292                                                      
REMARK 465     GLY B   293                                                      
REMARK 465     GLU B   294                                                      
REMARK 465     PRO B   295                                                      
REMARK 465     HIS B   296                                                      
REMARK 465     HIS B   297                                                      
REMARK 465     GLU B   298                                                      
REMARK 465     LEU B   299                                                      
REMARK 465     PRO B   300                                                      
REMARK 465     PRO B   301                                                      
REMARK 465     GLY B   302                                                      
REMARK 465     SER B   303                                                      
REMARK 465     THR B   304                                                      
REMARK 465     LYS B   305                                                      
REMARK 465     ARG B   306                                                      
REMARK 465     ALA B   307                                                      
REMARK 465     LEU B   308                                                      
REMARK 465     PRO B   309                                                      
REMARK 465     ASN B   310                                                      
REMARK 465     ASN B   311                                                      
REMARK 465     THR B   312                                                      
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 120    CG   CD   CE   NZ                                   
REMARK 470     ARG A 209    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 224    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 280    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU A 287    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 290    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 291    CG   CD   CE   NZ                                   
REMARK 470     LYS A 292    CG   CD   CE   NZ                                   
REMARK 470     LYS B 101    CD   CE   NZ                                        
REMARK 470     LYS B 120    CG   CD   CE   NZ                                   
REMARK 470     ARG B 202    NE   CZ   NH1  NH2                                  
REMARK 470     ARG B 209    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 221    CD   OE1  OE2                                       
REMARK 470     GLU B 224    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 280    CD   NE   CZ   NH1  NH2                             
REMARK 470     ARG B 290    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 291    CG   CD   CE   NZ                                   
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    LEU A 188      -45.08   -134.33                                   
REMARK 500    ARG A 248       -3.70     76.94                                   
REMARK 500    ARG B 248       -3.73     72.02                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 176   SG                                                     
REMARK 620 2 HIS A 179   ND1 105.9                                              
REMARK 620 3 CYS A 238   SG  110.6 105.4                                        
REMARK 620 4 CYS A 242   SG  110.7 106.0 117.4                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B 401  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 176   SG                                                     
REMARK 620 2 HIS B 179   ND1 103.3                                              
REMARK 620 3 CYS B 238   SG  111.3 109.4                                        
REMARK 620 4 CYS B 242   SG  111.1 105.7 115.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EPE A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 402                 
DBREF  6SI1 A   94   312  UNP    P04637   P53_HUMAN       94    312             
DBREF  6SI1 B   94   312  UNP    P04637   P53_HUMAN       94    312             
SEQADV 6SI1 LEU A  133  UNP  P04637    MET   133 ENGINEERED MUTATION            
SEQADV 6SI1 ALA A  203  UNP  P04637    VAL   203 ENGINEERED MUTATION            
SEQADV 6SI1 HIS A  220  UNP  P04637    TYR   220 ENGINEERED MUTATION            
SEQADV 6SI1 TYR A  239  UNP  P04637    ASN   239 ENGINEERED MUTATION            
SEQADV 6SI1 ASP A  268  UNP  P04637    ASN   268 ENGINEERED MUTATION            
SEQADV 6SI1 LEU B  133  UNP  P04637    MET   133 ENGINEERED MUTATION            
SEQADV 6SI1 ALA B  203  UNP  P04637    VAL   203 ENGINEERED MUTATION            
SEQADV 6SI1 HIS B  220  UNP  P04637    TYR   220 ENGINEERED MUTATION            
SEQADV 6SI1 TYR B  239  UNP  P04637    ASN   239 ENGINEERED MUTATION            
SEQADV 6SI1 ASP B  268  UNP  P04637    ASN   268 ENGINEERED MUTATION            
SEQRES   1 A  219  SER SER SER VAL PRO SER GLN LYS THR TYR GLN GLY SER          
SEQRES   2 A  219  TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY THR ALA          
SEQRES   3 A  219  LYS SER VAL THR CYS THR TYR SER PRO ALA LEU ASN LYS          
SEQRES   4 A  219  LEU PHE CYS GLN LEU ALA LYS THR CYS PRO VAL GLN LEU          
SEQRES   5 A  219  TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG VAL ARG          
SEQRES   6 A  219  ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET THR GLU          
SEQRES   7 A  219  VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS SER ASP          
SEQRES   8 A  219  SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL          
SEQRES   9 A  219  GLU GLY ASN LEU ARG ALA GLU TYR LEU ASP ASP ARG ASN          
SEQRES  10 A  219  THR PHE ARG HIS SER VAL VAL VAL PRO HIS GLU PRO PRO          
SEQRES  11 A  219  GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR ASN TYR          
SEQRES  12 A  219  MET CYS TYR SER SER CYS MET GLY GLY MET ASN ARG ARG          
SEQRES  13 A  219  PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER SER GLY          
SEQRES  14 A  219  ASN LEU LEU GLY ARG ASP SER PHE GLU VAL ARG VAL CYS          
SEQRES  15 A  219  ALA CYS PRO GLY ARG ASP ARG ARG THR GLU GLU GLU ASN          
SEQRES  16 A  219  LEU ARG LYS LYS GLY GLU PRO HIS HIS GLU LEU PRO PRO          
SEQRES  17 A  219  GLY SER THR LYS ARG ALA LEU PRO ASN ASN THR                  
SEQRES   1 B  219  SER SER SER VAL PRO SER GLN LYS THR TYR GLN GLY SER          
SEQRES   2 B  219  TYR GLY PHE ARG LEU GLY PHE LEU HIS SER GLY THR ALA          
SEQRES   3 B  219  LYS SER VAL THR CYS THR TYR SER PRO ALA LEU ASN LYS          
SEQRES   4 B  219  LEU PHE CYS GLN LEU ALA LYS THR CYS PRO VAL GLN LEU          
SEQRES   5 B  219  TRP VAL ASP SER THR PRO PRO PRO GLY THR ARG VAL ARG          
SEQRES   6 B  219  ALA MET ALA ILE TYR LYS GLN SER GLN HIS MET THR GLU          
SEQRES   7 B  219  VAL VAL ARG ARG CYS PRO HIS HIS GLU ARG CYS SER ASP          
SEQRES   8 B  219  SER ASP GLY LEU ALA PRO PRO GLN HIS LEU ILE ARG VAL          
SEQRES   9 B  219  GLU GLY ASN LEU ARG ALA GLU TYR LEU ASP ASP ARG ASN          
SEQRES  10 B  219  THR PHE ARG HIS SER VAL VAL VAL PRO HIS GLU PRO PRO          
SEQRES  11 B  219  GLU VAL GLY SER ASP CYS THR THR ILE HIS TYR ASN TYR          
SEQRES  12 B  219  MET CYS TYR SER SER CYS MET GLY GLY MET ASN ARG ARG          
SEQRES  13 B  219  PRO ILE LEU THR ILE ILE THR LEU GLU ASP SER SER GLY          
SEQRES  14 B  219  ASN LEU LEU GLY ARG ASP SER PHE GLU VAL ARG VAL CYS          
SEQRES  15 B  219  ALA CYS PRO GLY ARG ASP ARG ARG THR GLU GLU GLU ASN          
SEQRES  16 B  219  LEU ARG LYS LYS GLY GLU PRO HIS HIS GLU LEU PRO PRO          
SEQRES  17 B  219  GLY SER THR LYS ARG ALA LEU PRO ASN ASN THR                  
HET     ZN  A 401       1                                                       
HET    EDO  A 402       4                                                       
HET    GOL  A 403       6                                                       
HET    EPE  A 404      15                                                       
HET     ZN  B 401       1                                                       
HET    GOL  B 402       6                                                       
HETNAM      ZN ZINC ION                                                         
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     GOL GLYCEROL                                                         
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     EPE HEPES                                                            
FORMUL   3   ZN    2(ZN 2+)                                                     
FORMUL   4  EDO    C2 H6 O2                                                     
FORMUL   5  GOL    2(C3 H8 O3)                                                  
FORMUL   6  EPE    C8 H18 N2 O4 S                                               
FORMUL   9  HOH   *516(H2 O)                                                    
HELIX    1 AA1 GLN A  165  MET A  169  5                                   5    
HELIX    2 AA2 HIS A  178  CYS A  182  5                                   5    
HELIX    3 AA3 CYS A  277  LYS A  292  1                                  16    
HELIX    4 AA4 HIS B  178  CYS B  182  5                                   5    
HELIX    5 AA5 CYS B  277  LYS B  291  1                                  15    
SHEET    1 AA1 4 ARG A 110  GLY A 112  0                                        
SHEET    2 AA1 4 CYS A 141  TRP A 146 -1  O  GLN A 144   N  GLY A 112           
SHEET    3 AA1 4 THR A 230  TYR A 236 -1  O  THR A 230   N  LEU A 145           
SHEET    4 AA1 4 ILE A 195  VAL A 197 -1  N  ARG A 196   O  ASN A 235           
SHEET    1 AA2 7 CYS A 124  SER A 127  0                                        
SHEET    2 AA2 7 LYS A 132  CYS A 135 -1  O  PHE A 134   N  THR A 125           
SHEET    3 AA2 7 LEU A 264  VAL A 274  1  O  GLU A 271   N  LEU A 133           
SHEET    4 AA2 7 ILE A 251  GLU A 258 -1  N  LEU A 257   O  LEU A 265           
SHEET    5 AA2 7 ARG A 156  TYR A 163 -1  N  MET A 160   O  ILE A 254           
SHEET    6 AA2 7 HIS A 214  PRO A 219 -1  O  VAL A 218   N  VAL A 157           
SHEET    7 AA2 7 GLU A 204  ASP A 207 -1  N  GLU A 204   O  VAL A 217           
SHEET    1 AA3 4 ARG B 110  GLY B 112  0                                        
SHEET    2 AA3 4 CYS B 141  TRP B 146 -1  O  TRP B 146   N  ARG B 110           
SHEET    3 AA3 4 THR B 230  TYR B 236 -1  O  THR B 230   N  LEU B 145           
SHEET    4 AA3 4 ILE B 195  VAL B 197 -1  N  ARG B 196   O  ASN B 235           
SHEET    1 AA4 7 CYS B 124  SER B 127  0                                        
SHEET    2 AA4 7 LYS B 132  CYS B 135 -1  O  LYS B 132   N  SER B 127           
SHEET    3 AA4 7 LEU B 264  VAL B 274  1  O  GLU B 271   N  LEU B 133           
SHEET    4 AA4 7 ILE B 251  GLU B 258 -1  N  THR B 253   O  PHE B 270           
SHEET    5 AA4 7 ARG B 156  TYR B 163 -1  N  MET B 160   O  ILE B 254           
SHEET    6 AA4 7 HIS B 214  PRO B 219 -1  O  VAL B 218   N  VAL B 157           
SHEET    7 AA4 7 GLU B 204  ASP B 207 -1  N  GLU B 204   O  VAL B 217           
LINK         SG  CYS A 176                ZN    ZN A 401     1555   1555  2.33  
LINK         ND1 HIS A 179                ZN    ZN A 401     1555   1555  1.99  
LINK         SG  CYS A 238                ZN    ZN A 401     1555   1555  2.31  
LINK         SG  CYS A 242                ZN    ZN A 401     1555   1555  2.30  
LINK         SG  CYS B 176                ZN    ZN B 401     1555   1555  2.31  
LINK         ND1 HIS B 179                ZN    ZN B 401     1555   1555  2.05  
LINK         SG  CYS B 238                ZN    ZN B 401     1555   1555  2.30  
LINK         SG  CYS B 242                ZN    ZN B 401     1555   1555  2.31  
SITE     1 AC1  4 CYS A 176  HIS A 179  CYS A 238  CYS A 242                    
SITE     1 AC2  4 ASN A 131  SER A 269  HOH A 535  HOH A 619                    
SITE     1 AC3  6 ARG A 174  GLN A 192  ASP A 207  PHE A 212                    
SITE     2 AC3  6 HIS A 214  HOH A 586                                          
SITE     1 AC4  7 LYS A 101  TYR A 103  LEU A 264  ARG A 267                    
SITE     2 AC4  7 HOH A 501  HOH A 524  LEU B 201                               
SITE     1 AC5  4 CYS B 176  HIS B 179  CYS B 238  CYS B 242                    
SITE     1 AC6  6 ARG B 174  GLN B 192  ASP B 207  PHE B 212                    
SITE     2 AC6  6 HIS B 214  HOH B 590                                          
CRYST1   64.762   70.771  104.879  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015441  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014130  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009535        0.00000                         
ATOM      1  N   SER A  96     113.891  74.735 -37.400  1.00 31.29           N  
ANISOU    1  N   SER A  96     3950   3999   3942    586    680    -89       N  
ATOM      2  CA  SER A  96     113.504  73.967 -36.224  1.00 28.50           C  
ANISOU    2  CA  SER A  96     3507   3646   3675    524    746   -172       C  
ATOM      3  C   SER A  96     112.832  74.858 -35.187  1.00 24.79           C  
ANISOU    3  C   SER A  96     2943   3104   3371    428    551   -125       C  
ATOM      4  O   SER A  96     112.293  74.361 -34.199  1.00 24.08           O  
ANISOU    4  O   SER A  96     2910   2851   3389    182    388      5       O  
ATOM      5  CB  SER A  96     114.710  73.251 -35.605  1.00 31.30           C  
ANISOU    5  CB  SER A  96     3933   4097   3863    241    786   -345       C  
ATOM      6  OG  SER A  96     115.628  74.172 -35.035  1.00 34.00           O  
ANISOU    6  OG  SER A  96     4308   4571   4040    289    880   -417       O  
ATOM      7  N   VAL A  97     112.883  76.170 -35.413  1.00 21.95           N  
ANISOU    7  N   VAL A  97     2470   2769   3100    404    352    -47       N  
ATOM      8  CA  VAL A  97     112.199  77.143 -34.561  1.00 19.70           C  
ANISOU    8  CA  VAL A  97     2141   2418   2926    219     43     74       C  
ATOM      9  C   VAL A  97     111.489  78.179 -35.426  1.00 18.61           C  
ANISOU    9  C   VAL A  97     1847   2503   2719    129    275     17       C  
ATOM     10  O   VAL A  97     112.139  78.899 -36.195  1.00 19.92           O  
ANISOU   10  O   VAL A  97     1931   2841   2799    204    449     70       O  
ATOM     11  CB  VAL A  97     113.171  77.829 -33.589  1.00 21.19           C  
ANISOU   11  CB  VAL A  97     2476   2521   3056    377   -307    196       C  
ATOM     12  CG1 VAL A  97     112.433  78.866 -32.789  1.00 23.45           C  
ANISOU   12  CG1 VAL A  97     2914   2777   3218    505   -483    243       C  
ATOM     13  CG2 VAL A  97     113.838  76.814 -32.668  1.00 20.82           C  
ANISOU   13  CG2 VAL A  97     2523   2304   3083    298   -382    309       C  
ATOM     14  N   PRO A  98     110.171  78.300 -35.330  1.00 18.22           N  
ANISOU   14  N   PRO A  98     1872   2495   2557    286    147    191       N  
ATOM     15  CA  PRO A  98     109.470  79.323 -36.112  1.00 17.94           C  
ANISOU   15  CA  PRO A  98     1802   2478   2535    533    135    299       C  
ATOM     16  C   PRO A  98     109.876  80.718 -35.663  1.00 17.89           C  
ANISOU   16  C   PRO A  98     1972   2316   2509    486    203    462       C  
ATOM     17  O   PRO A  98     110.073  80.971 -34.473  1.00 17.85           O  
ANISOU   17  O   PRO A  98     2220   2214   2349    313     49    219       O  
ATOM     18  CB  PRO A  98     107.993  79.054 -35.795  1.00 19.47           C  
ANISOU   18  CB  PRO A  98     1884   2779   2736    371      3    394       C  
ATOM     19  CG  PRO A  98     107.961  77.630 -35.292  1.00 20.82           C  
ANISOU   19  CG  PRO A  98     2141   3035   2735    169     20    344       C  
ATOM     20  CD  PRO A  98     109.245  77.453 -34.564  1.00 19.08           C  
ANISOU   20  CD  PRO A  98     1909   2752   2588     98    193    365       C  
ATOM     21  N   SER A  99     109.993  81.629 -36.625  1.00 18.20           N  
ANISOU   21  N   SER A  99     2204   2079   2634    686    482    570       N  
ATOM     22  CA  SER A  99     110.343  83.000 -36.293  1.00 19.06           C  
ANISOU   22  CA  SER A  99     2435   2099   2710    611    521    752       C  
ATOM     23  C   SER A  99     109.208  83.658 -35.521  1.00 18.38           C  
ANISOU   23  C   SER A  99     2301   2003   2678    412    708    683       C  
ATOM     24  O   SER A  99     108.027  83.399 -35.761  1.00 18.22           O  
ANISOU   24  O   SER A  99     2214   1976   2734    547    706    673       O  
ATOM     25  CB  SER A  99     110.595  83.811 -37.562  1.00 20.33           C  
ANISOU   25  CB  SER A  99     2932   1947   2847    617    621    904       C  
ATOM     26  OG  SER A  99     110.782  85.190 -37.252  1.00 22.91           O  
ANISOU   26  OG  SER A  99     3241   2442   3022    569    595    692       O  
ATOM     27  N   GLN A 100     109.581  84.529 -34.588  1.00 18.22           N  
ANISOU   27  N   GLN A 100     2209   2002   2714    278    640    769       N  
ATOM     28  CA  GLN A 100     108.611  85.330 -33.855  1.00 17.70           C  
ANISOU   28  CA  GLN A 100     1959   2026   2741    264    708    743       C  
ATOM     29  C   GLN A 100     108.805  86.820 -34.096  1.00 17.64           C  
ANISOU   29  C   GLN A 100     2008   1986   2706    219    844    777       C  
ATOM     30  O   GLN A 100     108.263  87.639 -33.348  1.00 19.76           O  
ANISOU   30  O   GLN A 100     2523   2137   2848    340    990    711       O  
ATOM     31  CB  GLN A 100     108.686  85.029 -32.361  1.00 18.86           C  
ANISOU   31  CB  GLN A 100     2053   2277   2837    282    332    741       C  
ATOM     32  CG  GLN A 100     110.064  85.290 -31.776  1.00 19.39           C  
ANISOU   32  CG  GLN A 100     2065   2349   2954    120    320    785       C  
ATOM     33  CD  GLN A 100     110.100  85.033 -30.289  1.00 20.03           C  
ANISOU   33  CD  GLN A 100     2318   2211   3083    133    160    923       C  
ATOM     34  OE1 GLN A 100     110.455  83.938 -29.840  1.00 21.96           O  
ANISOU   34  OE1 GLN A 100     2707   2209   3426     91     -3    756       O  
ATOM     35  NE2 GLN A 100     109.719  86.038 -29.512  1.00 19.45           N  
ANISOU   35  NE2 GLN A 100     2325   2093   2973    103    427    939       N  
ATOM     36  N   LYS A 101     109.566  87.195 -35.118  1.00 16.68           N  
ANISOU   36  N   LYS A 101     1835   1926   2578   -140    507    741       N  
ATOM     37  CA  LYS A 101     109.866  88.605 -35.325  1.00 16.62           C  
ANISOU   37  CA  LYS A 101     1880   1834   2599     84    468    726       C  
ATOM     38  C   LYS A 101     108.632  89.355 -35.805  1.00 15.48           C  
ANISOU   38  C   LYS A 101     1800   1727   2355     34    293    340       C  
ATOM     39  O   LYS A 101     107.979  88.955 -36.774  1.00 15.20           O  
ANISOU   39  O   LYS A 101     1866   1603   2306   -147    157    240       O  
ATOM     40  CB  LYS A 101     110.995  88.767 -36.335  1.00 18.27           C  
ANISOU   40  CB  LYS A 101     2050   1966   2927     36    631    899       C  
ATOM     41  CG  LYS A 101     111.396  90.223 -36.532  1.00 21.76           C  
ANISOU   41  CG  LYS A 101     2725   2263   3280    365    360    904       C  
ATOM     42  CD  LYS A 101     112.465  90.374 -37.583  1.00 26.08           C  
ANISOU   42  CD  LYS A 101     3443   2765   3701    336     37    620       C  
ATOM     43  CE  LYS A 101     112.767  91.843 -37.835  1.00 28.64           C  
ANISOU   43  CE  LYS A 101     4016   2927   3938    350   -188    475       C  
ATOM     44  NZ  LYS A 101     113.024  92.559 -36.557  1.00 30.63           N1+
ANISOU   44  NZ  LYS A 101     4410   3133   4095    398   -111    422       N1+
ATOM     45  N   THR A 102     108.314  90.446 -35.119  1.00 13.64           N  
ANISOU   45  N   THR A 102     1630   1421   2131    -86    320    417       N  
ATOM     46  CA  THR A 102     107.193  91.273 -35.523  1.00 13.05           C  
ANISOU   46  CA  THR A 102     1877   1217   1865   -146     81    434       C  
ATOM     47  C   THR A 102     107.485  91.870 -36.886  1.00 12.38           C  
ANISOU   47  C   THR A 102     1594   1255   1853   -355    -84    326       C  
ATOM     48  O   THR A 102     108.576  92.396 -37.130  1.00 14.96           O  
ANISOU   48  O   THR A 102     1882   1592   2209   -524   -241    491       O  
ATOM     49  CB  THR A 102     106.971  92.371 -34.492  1.00 14.37           C  
ANISOU   49  CB  THR A 102     2232   1349   1880   -222    -66    459       C  
ATOM     50  OG1 THR A 102     106.655  91.761 -33.232  1.00 16.19           O  
ANISOU   50  OG1 THR A 102     2424   1795   1932   -277     18    582       O  
ATOM     51  CG2 THR A 102     105.832  93.269 -34.914  1.00 15.64           C  
ANISOU   51  CG2 THR A 102     2525   1404   2012   -263   -106     78       C  
ATOM     52  N   TYR A 103     106.510  91.775 -37.778  1.00 12.33           N  
ANISOU   52  N   TYR A 103     1715   1308   1661   -306   -178     97       N  
ATOM     53  CA  TYR A 103     106.701  92.216 -39.152  1.00 12.59           C  
ANISOU   53  CA  TYR A 103     1830   1390   1562    -81    -65    100       C  
ATOM     54  C   TYR A 103     105.357  92.714 -39.659  1.00 11.68           C  
ANISOU   54  C   TYR A 103     1813   1146   1480    -31     73    221       C  
ATOM     55  O   TYR A 103     104.453  91.915 -39.901  1.00 12.00           O  
ANISOU   55  O   TYR A 103     1770   1132   1657   -238    -83    192       O  
ATOM     56  CB  TYR A 103     107.210  91.055 -39.994  1.00 14.26           C  
ANISOU   56  CB  TYR A 103     2020   1712   1686    225     99     33       C  
ATOM     57  CG  TYR A 103     107.286  91.337 -41.466  1.00 16.48           C  
ANISOU   57  CG  TYR A 103     2337   2212   1713    395    356     42       C  
ATOM     58  CD1 TYR A 103     108.017  92.414 -41.954  1.00 17.95           C  
ANISOU   58  CD1 TYR A 103     2627   2537   1656    295    565     99       C  
ATOM     59  CD2 TYR A 103     106.641  90.515 -42.373  1.00 18.01           C  
ANISOU   59  CD2 TYR A 103     2584   2596   1663    605    275   -181       C  
ATOM     60  CE1 TYR A 103     108.087  92.667 -43.313  1.00 20.07           C  
ANISOU   60  CE1 TYR A 103     2980   3058   1588    458    434     71       C  
ATOM     61  CE2 TYR A 103     106.719  90.747 -43.723  1.00 19.85           C  
ANISOU   61  CE2 TYR A 103     2798   3100   1644    793    187   -239       C  
ATOM     62  CZ  TYR A 103     107.435  91.820 -44.190  1.00 20.72           C  
ANISOU   62  CZ  TYR A 103     3083   3209   1581    646    314    -26       C  
ATOM     63  OH  TYR A 103     107.488  92.045 -45.547  1.00 23.63           O  
ANISOU   63  OH  TYR A 103     3669   3654   1655    735    234     62       O  
ATOM     64  N   GLN A 104     105.214  94.026 -39.812  1.00 12.61           N  
ANISOU   64  N   GLN A 104     2149   1148   1494    121    200    248       N  
ATOM     65  CA  GLN A 104     103.932  94.530 -40.284  1.00 12.38           C  
ANISOU   65  CA  GLN A 104     2283    922   1497   -118    215     32       C  
ATOM     66  C   GLN A 104     103.723  94.233 -41.758  1.00 12.37           C  
ANISOU   66  C   GLN A 104     2245   1048   1407   -224    305    -31       C  
ATOM     67  O   GLN A 104     102.583  94.041 -42.189  1.00 13.23           O  
ANISOU   67  O   GLN A 104     2263   1280   1485   -163    180     50       O  
ATOM     68  CB  GLN A 104     103.817  96.025 -40.036  1.00 12.99           C  
ANISOU   68  CB  GLN A 104     2634    744   1558   -276    397      5       C  
ATOM     69  CG  GLN A 104     103.669  96.359 -38.573  1.00 14.75           C  
ANISOU   69  CG  GLN A 104     3122    900   1581    -37    418   -158       C  
ATOM     70  CD  GLN A 104     102.881  97.631 -38.353  1.00 17.64           C  
ANISOU   70  CD  GLN A 104     3475   1413   1813    156    363   -139       C  
ATOM     71  OE1 GLN A 104     102.638  98.387 -39.292  1.00 21.39           O  
ANISOU   71  OE1 GLN A 104     4049   1870   2211    203    349   -160       O  
ATOM     72  NE2 GLN A 104     102.457  97.863 -37.114  1.00 18.79           N  
ANISOU   72  NE2 GLN A 104     3346   2011   1781     69    159   -112       N  
ATOM     73  N   GLY A 105     104.798  94.209 -42.544  1.00 13.38           N  
ANISOU   73  N   GLY A 105     2495   1125   1465    -22    348    166       N  
ATOM     74  CA  GLY A 105     104.661  93.946 -43.963  1.00 13.98           C  
ANISOU   74  CA  GLY A 105     2481   1381   1451    -24    211    101       C  
ATOM     75  C   GLY A 105     103.943  95.063 -44.716  1.00 14.18           C  
ANISOU   75  C   GLY A 105     2483   1426   1479   -182    269     95       C  
ATOM     76  O   GLY A 105     103.645  96.139 -44.194  1.00 15.35           O  
ANISOU   76  O   GLY A 105     2626   1611   1596   -325    248     84       O  
ATOM     77  N   SER A 106     103.659  94.767 -45.983  1.00 14.38           N  
ANISOU   77  N   SER A 106     2549   1524   1392     11    289    186       N  
ATOM     78  CA  SER A 106     103.097  95.762 -46.889  1.00 15.81           C  
ANISOU   78  CA  SER A 106     2866   1707   1435    135    372    296       C  
ATOM     79  C   SER A 106     101.708  96.219 -46.486  1.00 14.53           C  
ANISOU   79  C   SER A 106     2810   1318   1393     59    226    217       C  
ATOM     80  O   SER A 106     101.288  97.318 -46.881  1.00 16.01           O  
ANISOU   80  O   SER A 106     2910   1483   1689    107     87    225       O  
ATOM     81  CB  SER A 106     103.005  95.167 -48.292  1.00 18.98           C  
ANISOU   81  CB  SER A 106     3240   2518   1452    830    677    249       C  
ATOM     82  OG  SER A 106     104.276  94.724 -48.731  1.00 23.92           O  
ANISOU   82  OG  SER A 106     3915   3169   2006    774    394    318       O  
ATOM     83  N   TYR A 107     100.980  95.404 -45.730  1.00 12.97           N  
ANISOU   83  N   TYR A 107     2493   1188   1249   -124    410    -48       N  
ATOM     84  CA  TYR A 107      99.603  95.710 -45.383  1.00 12.95           C  
ANISOU   84  CA  TYR A 107     2360   1243   1319    -79    272    -67       C  
ATOM     85  C   TYR A 107      99.459  96.311 -43.997  1.00 13.25           C  
ANISOU   85  C   TYR A 107     2611   1007   1416    -15    271    -34       C  
ATOM     86  O   TYR A 107      98.335  96.585 -43.581  1.00 15.02           O  
ANISOU   86  O   TYR A 107     2521   1516   1670    267    228   -227       O  
ATOM     87  CB  TYR A 107      98.712  94.471 -45.562  1.00 12.88           C  
ANISOU   87  CB  TYR A 107     2462   1263   1167   -233    348   -109       C  
ATOM     88  CG  TYR A 107      98.850  93.973 -46.969  1.00 14.15           C  
ANISOU   88  CG  TYR A 107     2578   1526   1272    -36    186    -83       C  
ATOM     89  CD1 TYR A 107      98.263  94.668 -48.011  1.00 15.43           C  
ANISOU   89  CD1 TYR A 107     2769   1786   1307   -370     97    189       C  
ATOM     90  CD2 TYR A 107      99.624  92.863 -47.270  1.00 15.96           C  
ANISOU   90  CD2 TYR A 107     2692   1867   1505   -241    134   -394       C  
ATOM     91  CE1 TYR A 107      98.418  94.271 -49.299  1.00 16.61           C  
ANISOU   91  CE1 TYR A 107     2794   2235   1280   -414    141   -134       C  
ATOM     92  CE2 TYR A 107      99.784  92.448 -48.577  1.00 17.06           C  
ANISOU   92  CE2 TYR A 107     2770   2235   1478   -184    105   -464       C  
ATOM     93  CZ  TYR A 107      99.173  93.158 -49.588  1.00 18.01           C  
ANISOU   93  CZ  TYR A 107     3020   2523   1300   -299    330   -486       C  
ATOM     94  OH  TYR A 107      99.322  92.776 -50.898  1.00 21.08           O  
ANISOU   94  OH  TYR A 107     3553   3207   1248   -535    292   -613       O  
ATOM     95  N   GLY A 108     100.562  96.535 -43.285  1.00 11.83           N  
ANISOU   95  N   GLY A 108     2532    658   1304    -48    252     76       N  
ATOM     96  CA  GLY A 108     100.487  97.137 -41.960  1.00 11.84           C  
ANISOU   96  CA  GLY A 108     2451    736   1311    -71    475     25       C  
ATOM     97  C   GLY A 108      99.800  96.235 -40.964  1.00 11.95           C  
ANISOU   97  C   GLY A 108     2294    855   1391    111    243    -51       C  
ATOM     98  O   GLY A 108      98.965  96.701 -40.174  1.00 13.14           O  
ANISOU   98  O   GLY A 108     2476   1030   1486    -50    230   -267       O  
ATOM     99  N   PHE A 109     100.137  94.952 -40.987  1.00 11.30           N  
ANISOU   99  N   PHE A 109     2252    633   1408   -168    120    184       N  
ATOM    100  CA  PHE A 109      99.458  93.958 -40.173  1.00 11.05           C  
ANISOU  100  CA  PHE A 109     2222    625   1351     74     95    226       C  
ATOM    101  C   PHE A 109      99.912  94.041 -38.725  1.00 11.02           C  
ANISOU  101  C   PHE A 109     1895    972   1322     25    105     79       C  
ATOM    102  O   PHE A 109     101.114  94.052 -38.441  1.00 11.99           O  
ANISOU  102  O   PHE A 109     1974   1245   1335     -8     93     31       O  
ATOM    103  CB  PHE A 109      99.789  92.572 -40.709  1.00 11.99           C  
ANISOU  103  CB  PHE A 109     2218    776   1563    222    175     19       C  
ATOM    104  CG  PHE A 109      99.227  91.454 -39.879  1.00 11.38           C  
ANISOU  104  CG  PHE A 109     2176    767   1382     -2    134    111       C  
ATOM    105  CD1 PHE A 109      97.870  91.196 -39.881  1.00 12.12           C  
ANISOU  105  CD1 PHE A 109     2309    988   1309     91    168     43       C  
ATOM    106  CD2 PHE A 109     100.060  90.655 -39.105  1.00 11.73           C  
ANISOU  106  CD2 PHE A 109     2190    968   1299    104    281     19       C  
ATOM    107  CE1 PHE A 109      97.344  90.156 -39.124  1.00 13.38           C  
ANISOU  107  CE1 PHE A 109     2416   1284   1383     22    172    188       C  
ATOM    108  CE2 PHE A 109      99.548  89.618 -38.348  1.00 12.01           C  
ANISOU  108  CE2 PHE A 109     2113   1039   1411     82     83    145       C  
ATOM    109  CZ  PHE A 109      98.182  89.367 -38.353  1.00 12.48           C  
ANISOU  109  CZ  PHE A 109     2255   1015   1471    171    105     71       C  
ATOM    110  N   ARG A 110      98.949  94.044 -37.810  1.00 10.24           N  
ANISOU  110  N   ARG A 110     1751    948   1192     53    122    151       N  
ATOM    111  CA  ARG A 110      99.261  93.932 -36.393  1.00 10.18           C  
ANISOU  111  CA  ARG A 110     1878    901   1090   -203     25     85       C  
ATOM    112  C   ARG A 110      98.020  93.483 -35.653  1.00 10.85           C  
ANISOU  112  C   ARG A 110     2015    915   1193   -154    -93    205       C  
ATOM    113  O   ARG A 110      96.900  93.608 -36.151  1.00 11.22           O  
ANISOU  113  O   ARG A 110     1783   1040   1438      4   -124    238       O  
ATOM    114  CB  ARG A 110      99.791  95.244 -35.808  1.00 10.67           C  
ANISOU  114  CB  ARG A 110     1906    838   1311    208   -109    -43       C  
ATOM    115  CG  ARG A 110      98.763  96.364 -35.667  1.00 11.84           C  
ANISOU  115  CG  ARG A 110     2209   1024   1267    285    -71    142       C  
ATOM    116  CD  ARG A 110      98.519  97.100 -36.969  1.00 12.72           C  
ANISOU  116  CD  ARG A 110     2472    955   1408    530   -131    275       C  
ATOM    117  NE  ARG A 110      97.661  98.256 -36.754  1.00 12.90           N  
ANISOU  117  NE  ARG A 110     2649    961   1292    534   -175    204       N  
ATOM    118  CZ  ARG A 110      97.267  99.065 -37.726  1.00 14.79           C  
ANISOU  118  CZ  ARG A 110     3166   1100   1352    708    115    167       C  
ATOM    119  NH1 ARG A 110      97.658  98.832 -38.970  1.00 17.42           N1+
ANISOU  119  NH1 ARG A 110     3744   1480   1394    527    291    208       N1+
ATOM    120  NH2 ARG A 110      96.484 100.102 -37.459  1.00 16.72           N  
ANISOU  120  NH2 ARG A 110     3453   1196   1704    812    202     55       N  
ATOM    121  N   LEU A 111      98.234  92.954 -34.453  1.00 10.53           N  
ANISOU  121  N   LEU A 111     1969    896   1136    -89     66    262       N  
ATOM    122  CA  LEU A 111      97.128  92.463 -33.651  1.00 10.31           C  
ANISOU  122  CA  LEU A 111     1779    921   1216    131     72    198       C  
ATOM    123  C   LEU A 111      96.553  93.571 -32.779  1.00  9.96           C  
ANISOU  123  C   LEU A 111     1671    765   1348   -129     98     93       C  
ATOM    124  O   LEU A 111      97.169  94.612 -32.553  1.00 12.62           O  
ANISOU  124  O   LEU A 111     1953   1115   1728   -295    235    -48       O  
ATOM    125  CB  LEU A 111      97.623  91.343 -32.747  1.00  9.89           C  
ANISOU  125  CB  LEU A 111     1904    712   1141    355    -14    137       C  
ATOM    126  CG  LEU A 111      98.274  90.185 -33.491  1.00  9.67           C  
ANISOU  126  CG  LEU A 111     1763    633   1279    310   -117   -113       C  
ATOM    127  CD1 LEU A 111      98.874  89.225 -32.475  1.00  9.93           C  
ANISOU  127  CD1 LEU A 111     1893    557   1322    245   -155     62       C  
ATOM    128  CD2 LEU A 111      97.275  89.470 -34.414  1.00 11.37           C  
ANISOU  128  CD2 LEU A 111     1957   1030   1333      0   -262   -271       C  
ATOM    129  N   GLY A 112      95.361  93.312 -32.258  1.00  9.90           N  
ANISOU  129  N   GLY A 112     1721    820   1220   -120    362    -64       N  
ATOM    130  CA  GLY A 112      94.785  94.156 -31.236  1.00 10.37           C  
ANISOU  130  CA  GLY A 112     1879    765   1296    -62    235   -102       C  
ATOM    131  C   GLY A 112      94.027  93.292 -30.254  1.00 10.67           C  
ANISOU  131  C   GLY A 112     1779    961   1315    126    -55   -121       C  
ATOM    132  O   GLY A 112      93.585  92.191 -30.580  1.00 11.16           O  
ANISOU  132  O   GLY A 112     1834   1140   1268    106    -95   -107       O  
ATOM    133  N   PHE A 113      93.878  93.813 -29.041  1.00 10.68           N  
ANISOU  133  N   PHE A 113     1796    973   1287    208    111   -129       N  
ATOM    134  CA  PHE A 113      93.207  93.094 -27.974  1.00 11.34           C  
ANISOU  134  CA  PHE A 113     1811   1198   1300    437    -70   -191       C  
ATOM    135  C   PHE A 113      92.194  93.993 -27.293  1.00 12.57           C  
ANISOU  135  C   PHE A 113     1873   1404   1498    374    -58   -529       C  
ATOM    136  O   PHE A 113      92.392  95.204 -27.180  1.00 13.65           O  
ANISOU  136  O   PHE A 113     2204   1308   1673    368      0   -506       O  
ATOM    137  CB  PHE A 113      94.208  92.572 -26.950  1.00 10.82           C  
ANISOU  137  CB  PHE A 113     1822   1093   1198    510   -233   -122       C  
ATOM    138  CG  PHE A 113      95.192  91.633 -27.544  1.00 10.25           C  
ANISOU  138  CG  PHE A 113     1858    863   1172    386   -320   -292       C  
ATOM    139  CD1 PHE A 113      96.341  92.113 -28.141  1.00 11.03           C  
ANISOU  139  CD1 PHE A 113     1826   1081   1284    422   -111   -184       C  
ATOM    140  CD2 PHE A 113      94.944  90.270 -27.562  1.00 11.75           C  
ANISOU  140  CD2 PHE A 113     2296    870   1297    435   -342   -332       C  
ATOM    141  CE1 PHE A 113      97.241  91.248 -28.728  1.00 12.15           C  
ANISOU  141  CE1 PHE A 113     2102   1187   1326    482   -176   -385       C  
ATOM    142  CE2 PHE A 113      95.846  89.397 -28.129  1.00 12.45           C  
ANISOU  142  CE2 PHE A 113     2366   1030   1335    500   -120   -278       C  
ATOM    143  CZ  PHE A 113      97.003  89.885 -28.714  1.00 12.67           C  
ANISOU  143  CZ  PHE A 113     2248   1247   1319    383   -371   -358       C  
ATOM    144  N   LEU A 114      91.106  93.381 -26.844  1.00 13.91           N  
ANISOU  144  N   LEU A 114     1923   1907   1456    314     47   -450       N  
ATOM    145  CA  LEU A 114      90.112  94.109 -26.080  1.00 14.41           C  
ANISOU  145  CA  LEU A 114     1860   1861   1755    456     33   -344       C  
ATOM    146  C   LEU A 114      90.684  94.529 -24.728  1.00 14.13           C  
ANISOU  146  C   LEU A 114     1893   1684   1791    334    -20   -279       C  
ATOM    147  O   LEU A 114      91.744  94.073 -24.298  1.00 16.22           O  
ANISOU  147  O   LEU A 114     2183   1977   2003    646     16   -556       O  
ATOM    148  CB  LEU A 114      88.878  93.238 -25.862  1.00 16.12           C  
ANISOU  148  CB  LEU A 114     2201   1779   2143    239   -285   -344       C  
ATOM    149  CG  LEU A 114      88.203  92.748 -27.136  1.00 19.43           C  
ANISOU  149  CG  LEU A 114     2706   2262   2415    150   -254   -365       C  
ATOM    150  CD1 LEU A 114      87.059  91.833 -26.777  1.00 20.53           C  
ANISOU  150  CD1 LEU A 114     2844   2318   2637     14   -105   -373       C  
ATOM    151  CD2 LEU A 114      87.726  93.939 -27.946  1.00 20.97           C  
ANISOU  151  CD2 LEU A 114     2992   2622   2354     82   -486   -359       C  
ATOM    152  N   HIS A 115      89.957  95.411 -24.051  1.00 14.40           N  
ANISOU  152  N   HIS A 115     2241   1456   1773    217   -103   -358       N  
ATOM    153  CA  HIS A 115      90.330  95.887 -22.719  1.00 13.92           C  
ANISOU  153  CA  HIS A 115     2135   1235   1918     13   -234   -415       C  
ATOM    154  C   HIS A 115      89.345  95.307 -21.716  1.00 15.18           C  
ANISOU  154  C   HIS A 115     2130   1442   2195     65    145   -381       C  
ATOM    155  O   HIS A 115      88.361  95.945 -21.343  1.00 18.13           O  
ANISOU  155  O   HIS A 115     2512   1752   2623    275    345   -369       O  
ATOM    156  CB  HIS A 115      90.360  97.395 -22.690  1.00 14.97           C  
ANISOU  156  CB  HIS A 115     2441   1087   2161     36   -294   -358       C  
ATOM    157  CG  HIS A 115      91.329  97.969 -23.665  1.00 16.96           C  
ANISOU  157  CG  HIS A 115     2689   1247   2510   -159    -44   -297       C  
ATOM    158  ND1 HIS A 115      92.654  98.184 -23.358  1.00 19.16           N  
ANISOU  158  ND1 HIS A 115     3277   1314   2688    189    126   -300       N  
ATOM    159  CD2 HIS A 115      91.185  98.291 -24.971  1.00 18.40           C  
ANISOU  159  CD2 HIS A 115     2978   1429   2584   -487    -21     46       C  
ATOM    160  CE1 HIS A 115      93.274  98.657 -24.425  1.00 17.14           C  
ANISOU  160  CE1 HIS A 115     2943   1072   2499    152     87     35       C  
ATOM    161  NE2 HIS A 115      92.408  98.720 -25.419  1.00 19.67           N  
ANISOU  161  NE2 HIS A 115     3379   1315   2778   -220     30    -90       N  
ATOM    162  N   SER A 116      89.642  94.098 -21.256  1.00 14.80           N  
ANISOU  162  N   SER A 116     2271   1363   1989     26    231   -392       N  
ATOM    163  CA  SER A 116      88.699  93.313 -20.478  1.00 15.76           C  
ANISOU  163  CA  SER A 116     2367   1625   1998     -2    301   -376       C  
ATOM    164  C   SER A 116      88.854  93.502 -18.978  1.00 16.38           C  
ANISOU  164  C   SER A 116     2311   1811   2099    104    391   -597       C  
ATOM    165  O   SER A 116      87.989  93.048 -18.223  1.00 17.83           O  
ANISOU  165  O   SER A 116     2315   2215   2245     17    469   -378       O  
ATOM    166  CB  SER A 116      88.855  91.834 -20.831  1.00 18.13           C  
ANISOU  166  CB  SER A 116     3062   1778   2050   -253    157   -320       C  
ATOM    167  OG  SER A 116      88.617  91.631 -22.218  1.00 22.00           O  
ANISOU  167  OG  SER A 116     3734   2331   2293   -156    -48   -323       O  
ATOM    168  N   GLY A 117      89.926  94.146 -18.532  1.00 16.89           N  
ANISOU  168  N   GLY A 117     2430   1845   2143    121    364   -492       N  
ATOM    169  CA  GLY A 117      90.126  94.385 -17.120  1.00 16.92           C  
ANISOU  169  CA  GLY A 117     2649   1833   1947    -25    320   -497       C  
ATOM    170  C   GLY A 117      90.640  93.155 -16.405  1.00 16.94           C  
ANISOU  170  C   GLY A 117     2771   1908   1758    -40    324   -386       C  
ATOM    171  O   GLY A 117      90.940  92.125 -17.002  1.00 16.35           O  
ANISOU  171  O   GLY A 117     2693   1883   1635     48    373   -247       O  
ATOM    172  N   THR A 118      90.747  93.272 -15.079  1.00 17.91           N  
ANISOU  172  N   THR A 118     2774   2284   1748    -57    466   -272       N  
ATOM    173  CA  THR A 118      91.385  92.223 -14.290  1.00 19.85           C  
ANISOU  173  CA  THR A 118     3157   2493   1891    -23    570   -388       C  
ATOM    174  C   THR A 118      90.514  91.723 -13.144  1.00 21.33           C  
ANISOU  174  C   THR A 118     3461   2681   1965    -97    625   -409       C  
ATOM    175  O   THR A 118      91.047  91.204 -12.157  1.00 21.63           O  
ANISOU  175  O   THR A 118     3571   2711   1936   -135    486   -231       O  
ATOM    176  CB  THR A 118      92.745  92.679 -13.761  1.00 22.18           C  
ANISOU  176  CB  THR A 118     3446   2879   2103     38    442   -558       C  
ATOM    177  OG1 THR A 118      92.565  93.834 -12.933  1.00 22.73           O  
ANISOU  177  OG1 THR A 118     3533   2962   2140    130    455   -774       O  
ATOM    178  CG2 THR A 118      93.679  93.023 -14.913  1.00 23.69           C  
ANISOU  178  CG2 THR A 118     3563   3224   2214    -45    388   -544       C  
ATOM    179  N   ALA A 119      89.196  91.866 -13.247  1.00 21.09           N  
ANISOU  179  N   ALA A 119     3322   2685   2008   -387    800   -456       N  
ATOM    180  CA  ALA A 119      88.319  91.326 -12.219  1.00 22.98           C  
ANISOU  180  CA  ALA A 119     3701   2997   2033   -572    888   -423       C  
ATOM    181  C   ALA A 119      88.538  89.823 -12.084  1.00 23.53           C  
ANISOU  181  C   ALA A 119     4000   2991   1950   -782    850   -451       C  
ATOM    182  O   ALA A 119      88.904  89.136 -13.044  1.00 23.84           O  
ANISOU  182  O   ALA A 119     3937   3138   1983   -886    711   -437       O  
ATOM    183  CB  ALA A 119      86.858  91.617 -12.564  1.00 23.84           C  
ANISOU  183  CB  ALA A 119     3758   3096   2205   -572    910   -438       C  
ATOM    184  N   LYS A 120      88.333  89.314 -10.864  1.00 25.84           N  
ANISOU  184  N   LYS A 120     4461   3262   2096   -732    737   -283       N  
ATOM    185  CA  LYS A 120      88.536  87.890 -10.609  1.00 26.88           C  
ANISOU  185  CA  LYS A 120     4628   3399   2185   -825    686   -228       C  
ATOM    186  C   LYS A 120      87.731  87.016 -11.563  1.00 27.85           C  
ANISOU  186  C   LYS A 120     4594   3549   2439   -845    739   -174       C  
ATOM    187  O   LYS A 120      88.150  85.898 -11.886  1.00 27.60           O  
ANISOU  187  O   LYS A 120     4613   3377   2499   -905    727   -166       O  
ATOM    188  CB  LYS A 120      88.176  87.561  -9.157  1.00 27.15           C  
ANISOU  188  CB  LYS A 120     4727   3483   2105   -873    553   -158       C  
ATOM    189  N   SER A 121      86.591  87.513 -12.043  1.00 27.53           N  
ANISOU  189  N   SER A 121     4204   3704   2553   -829    804   -269       N  
ATOM    190  CA  SER A 121      85.712  86.737 -12.906  1.00 27.73           C  
ANISOU  190  CA  SER A 121     4065   3802   2668   -833    767   -485       C  
ATOM    191  C   SER A 121      86.107  86.769 -14.378  1.00 25.82           C  
ANISOU  191  C   SER A 121     3740   3518   2553   -860    804   -560       C  
ATOM    192  O   SER A 121      85.482  86.063 -15.176  1.00 26.93           O  
ANISOU  192  O   SER A 121     3848   3760   2626   -948    879   -646       O  
ATOM    193  CB  SER A 121      84.280  87.253 -12.772  1.00 30.04           C  
ANISOU  193  CB  SER A 121     4379   4098   2939   -560    628   -538       C  
ATOM    194  OG  SER A 121      84.207  88.611 -13.175  1.00 32.33           O  
ANISOU  194  OG  SER A 121     4627   4470   3188   -359    640   -566       O  
ATOM    195  N   VAL A 122      87.113  87.554 -14.767  1.00 22.43           N  
ANISOU  195  N   VAL A 122     3230   2986   2307   -716    796   -601       N  
ATOM    196  CA  VAL A 122      87.408  87.720 -16.187  1.00 19.71           C  
ANISOU  196  CA  VAL A 122     2860   2536   2093   -526    459   -508       C  
ATOM    197  C   VAL A 122      87.944  86.414 -16.767  1.00 18.59           C  
ANISOU  197  C   VAL A 122     2508   2546   2010   -456    210   -502       C  
ATOM    198  O   VAL A 122      88.701  85.680 -16.119  1.00 20.06           O  
ANISOU  198  O   VAL A 122     2906   2716   2001   -600     92   -492       O  
ATOM    199  CB  VAL A 122      88.351  88.919 -16.410  1.00 19.53           C  
ANISOU  199  CB  VAL A 122     2865   2497   2058   -377    391   -194       C  
ATOM    200  CG1 VAL A 122      89.808  88.562 -16.112  1.00 19.32           C  
ANISOU  200  CG1 VAL A 122     2780   2445   2117   -502    388    -38       C  
ATOM    201  CG2 VAL A 122      88.190  89.479 -17.817  1.00 19.84           C  
ANISOU  201  CG2 VAL A 122     2994   2557   1986    -89    242   -316       C  
ATOM    202  N   THR A 123      87.526  86.095 -17.989  1.00 15.92           N  
ANISOU  202  N   THR A 123     1865   2242   1942   -559    106   -533       N  
ATOM    203  CA  THR A 123      87.910  84.827 -18.594  1.00 14.13           C  
ANISOU  203  CA  THR A 123     1703   1897   1769   -307    123   -279       C  
ATOM    204  C   THR A 123      89.045  84.967 -19.591  1.00 13.48           C  
ANISOU  204  C   THR A 123     1809   1578   1733   -232     90   -132       C  
ATOM    205  O   THR A 123      89.669  83.961 -19.943  1.00 13.39           O  
ANISOU  205  O   THR A 123     1879   1426   1783   -256    -47   -152       O  
ATOM    206  CB  THR A 123      86.718  84.195 -19.320  1.00 15.86           C  
ANISOU  206  CB  THR A 123     1806   2326   1893   -472    154   -145       C  
ATOM    207  OG1 THR A 123      86.301  85.063 -20.378  1.00 15.93           O  
ANISOU  207  OG1 THR A 123     1697   2523   1833   -285     67   -245       O  
ATOM    208  CG2 THR A 123      85.564  83.974 -18.365  1.00 17.28           C  
ANISOU  208  CG2 THR A 123     2069   2479   2017   -710    214    -76       C  
ATOM    209  N   CYS A 124      89.311  86.183 -20.053  1.00 13.02           N  
ANISOU  209  N   CYS A 124     1687   1547   1715   -357    171    -96       N  
ATOM    210  CA  CYS A 124      90.374  86.447 -21.006  1.00 12.68           C  
ANISOU  210  CA  CYS A 124     1711   1319   1788   -266    -27   -110       C  
ATOM    211  C   CYS A 124      90.764  87.894 -20.794  1.00 12.36           C  
ANISOU  211  C   CYS A 124     1699   1113   1883    -51    -89    -73       C  
ATOM    212  O   CYS A 124      89.889  88.765 -20.765  1.00 13.89           O  
ANISOU  212  O   CYS A 124     1856   1285   2136    257    -58    -31       O  
ATOM    213  CB  CYS A 124      89.864  86.278 -22.438  1.00 13.26           C  
ANISOU  213  CB  CYS A 124     1901   1376   1762   -161    252    -49       C  
ATOM    214  SG  CYS A 124      91.151  86.491 -23.676  1.00 15.38           S  
ANISOU  214  SG  CYS A 124     2463   1583   1798   -218    107   -266       S  
ATOM    215  N   THR A 125      92.055  88.150 -20.637  1.00 11.65           N  
ANISOU  215  N   THR A 125     1565   1067   1793   -109    -37     24       N  
ATOM    216  CA  THR A 125      92.501  89.522 -20.461  1.00 11.17           C  
ANISOU  216  CA  THR A 125     1483   1085   1678   -101    183   -190       C  
ATOM    217  C   THR A 125      93.930  89.677 -20.967  1.00  9.62           C  
ANISOU  217  C   THR A 125     1619    492   1543    113    242     87       C  
ATOM    218  O   THR A 125      94.787  88.799 -20.776  1.00 10.50           O  
ANISOU  218  O   THR A 125     1895    532   1564     89    325     48       O  
ATOM    219  CB  THR A 125      92.339  89.986 -19.004  1.00 12.96           C  
ANISOU  219  CB  THR A 125     1831   1370   1724    -90    233   -328       C  
ATOM    220  OG1 THR A 125      92.645  91.379 -18.908  1.00 13.31           O  
ANISOU  220  OG1 THR A 125     2038   1255   1764   -174    285   -267       O  
ATOM    221  CG2 THR A 125      93.237  89.178 -18.062  1.00 13.19           C  
ANISOU  221  CG2 THR A 125     1893   1528   1589    -66     22   -229       C  
ATOM    222  N   TYR A 126      94.175  90.801 -21.615  1.00 10.08           N  
ANISOU  222  N   TYR A 126     1628    889   1313   -139    132   -144       N  
ATOM    223  CA  TYR A 126      95.438  91.048 -22.278  1.00  9.94           C  
ANISOU  223  CA  TYR A 126     1446   1082   1249    -44    163    -58       C  
ATOM    224  C   TYR A 126      96.207  92.139 -21.552  1.00  9.29           C  
ANISOU  224  C   TYR A 126     1412    859   1260    120     40    -16       C  
ATOM    225  O   TYR A 126      95.656  93.209 -21.267  1.00 11.40           O  
ANISOU  225  O   TYR A 126     1860    934   1536    115     96   -175       O  
ATOM    226  CB  TYR A 126      95.214  91.453 -23.729  1.00  9.42           C  
ANISOU  226  CB  TYR A 126     1400    956   1222    127    131     19       C  
ATOM    227  CG  TYR A 126      96.505  91.827 -24.386  1.00  8.91           C  
ANISOU  227  CG  TYR A 126     1315    900   1170    159     31    -80       C  
ATOM    228  CD1 TYR A 126      97.438  90.855 -24.724  1.00  9.12           C  
ANISOU  228  CD1 TYR A 126     1429    978   1058     19     -7    -51       C  
ATOM    229  CD2 TYR A 126      96.815  93.160 -24.630  1.00  9.15           C  
ANISOU  229  CD2 TYR A 126     1391    802   1283     48    -73    -89       C  
ATOM    230  CE1 TYR A 126      98.644  91.196 -25.300  1.00  9.40           C  
ANISOU  230  CE1 TYR A 126     1626    972    974    -25    133     57       C  
ATOM    231  CE2 TYR A 126      98.007  93.513 -25.215  1.00  9.64           C  
ANISOU  231  CE2 TYR A 126     1490   1073   1101    206    -81   -193       C  
ATOM    232  CZ  TYR A 126      98.918  92.529 -25.543  1.00  9.40           C  
ANISOU  232  CZ  TYR A 126     1550   1002   1018    202    138     72       C  
ATOM    233  OH  TYR A 126     100.110  92.880 -26.103  1.00 11.37           O  
ANISOU  233  OH  TYR A 126     1684   1522   1113     92    177     62       O  
ATOM    234  N   SER A 127      97.482  91.870 -21.273  1.00  9.14           N  
ANISOU  234  N   SER A 127     1357    806   1308   -131    -70     40       N  
ATOM    235  CA  SER A 127      98.361  92.843 -20.646  1.00  9.82           C  
ANISOU  235  CA  SER A 127     1719    654   1358   -228   -138     23       C  
ATOM    236  C   SER A 127      99.267  93.463 -21.692  1.00  9.90           C  
ANISOU  236  C   SER A 127     1960    558   1242     84    -72   -111       C  
ATOM    237  O   SER A 127     100.212  92.798 -22.145  1.00 10.93           O  
ANISOU  237  O   SER A 127     1983    774   1395     11     21    -81       O  
ATOM    238  CB  SER A 127      99.216  92.153 -19.599  1.00 10.48           C  
ANISOU  238  CB  SER A 127     1824    823   1336    -45   -430    117       C  
ATOM    239  OG  SER A 127     100.221  93.040 -19.145  1.00 12.13           O  
ANISOU  239  OG  SER A 127     2007   1065   1535   -214   -316    -92       O  
ATOM    240  N   PRO A 128      99.063  94.727 -22.068  1.00 11.54           N  
ANISOU  240  N   PRO A 128     2111    807   1467   -129   -195    -40       N  
ATOM    241  CA  PRO A 128     100.036  95.380 -22.953  1.00 11.75           C  
ANISOU  241  CA  PRO A 128     2074    825   1566   -356   -153     77       C  
ATOM    242  C   PRO A 128     101.421  95.485 -22.351  1.00 11.94           C  
ANISOU  242  C   PRO A 128     2056    920   1562   -145   -186    136       C  
ATOM    243  O   PRO A 128     102.414  95.346 -23.071  1.00 14.32           O  
ANISOU  243  O   PRO A 128     2317   1165   1957   -199   -207    100       O  
ATOM    244  CB  PRO A 128      99.432  96.775 -23.165  1.00 13.35           C  
ANISOU  244  CB  PRO A 128     2384    735   1955   -230   -335    285       C  
ATOM    245  CG  PRO A 128      97.999  96.626 -22.891  1.00 14.68           C  
ANISOU  245  CG  PRO A 128     2713    971   1893     13    -64    225       C  
ATOM    246  CD  PRO A 128      97.854  95.543 -21.868  1.00 11.89           C  
ANISOU  246  CD  PRO A 128     2269    686   1561     17   -198    147       C  
ATOM    247  N   ALA A 129     101.523  95.729 -21.043  1.00 12.32           N  
ANISOU  247  N   ALA A 129     2056   1042   1581    -85   -369     51       N  
ATOM    248  CA  ALA A 129     102.844  95.893 -20.450  1.00 13.57           C  
ANISOU  248  CA  ALA A 129     2184   1192   1781    -19   -354   -169       C  
ATOM    249  C   ALA A 129     103.661  94.615 -20.549  1.00 13.71           C  
ANISOU  249  C   ALA A 129     2128   1011   2069   -100   -148      2       C  
ATOM    250  O   ALA A 129     104.887  94.673 -20.687  1.00 16.67           O  
ANISOU  250  O   ALA A 129     2228   1506   2598   -125    -89    192       O  
ATOM    251  CB  ALA A 129     102.723  96.337 -18.996  1.00 14.73           C  
ANISOU  251  CB  ALA A 129     2452   1466   1679    -42   -480   -351       C  
ATOM    252  N   LEU A 130     103.002  93.460 -20.505  1.00 12.21           N  
ANISOU  252  N   LEU A 130     2032    839   1768     77   -264     -3       N  
ATOM    253  CA  LEU A 130     103.673  92.174 -20.585  1.00 13.21           C  
ANISOU  253  CA  LEU A 130     2421    902   1698    264    -98   -105       C  
ATOM    254  C   LEU A 130     103.599  91.560 -21.978  1.00 13.82           C  
ANISOU  254  C   LEU A 130     2499   1133   1618     33   -125   -158       C  
ATOM    255  O   LEU A 130     104.219  90.518 -22.206  1.00 14.98           O  
ANISOU  255  O   LEU A 130     2736   1201   1754    293     -7    -47       O  
ATOM    256  CB  LEU A 130     103.023  91.197 -19.602  1.00 13.10           C  
ANISOU  256  CB  LEU A 130     2353    972   1651     39   -251   -173       C  
ATOM    257  CG  LEU A 130     103.100  91.551 -18.118  1.00 14.45           C  
ANISOU  257  CG  LEU A 130     2393   1395   1702    -88   -360    -91       C  
ATOM    258  CD1 LEU A 130     102.112  90.714 -17.327  1.00 15.43           C  
ANISOU  258  CD1 LEU A 130     2789   1401   1673    -19   -241    124       C  
ATOM    259  CD2 LEU A 130     104.516  91.354 -17.575  1.00 16.82           C  
ANISOU  259  CD2 LEU A 130     2570   1875   1947     66   -604    -59       C  
ATOM    260  N   ASN A 131     102.860  92.175 -22.902  1.00 12.95           N  
ANISOU  260  N   ASN A 131     2143   1212   1565   -218   -365   -182       N  
ATOM    261  CA  ASN A 131     102.458  91.550 -24.171  1.00 10.45           C  
ANISOU  261  CA  ASN A 131     1805    806   1360   -431     21   -243       C  
ATOM    262  C   ASN A 131     102.031  90.107 -23.948  1.00 10.13           C  
ANISOU  262  C   ASN A 131     1699    761   1390   -126    -36    -62       C  
ATOM    263  O   ASN A 131     102.581  89.169 -24.522  1.00 10.85           O  
ANISOU  263  O   ASN A 131     1811    817   1496      9    100     -6       O  
ATOM    264  CB  ASN A 131     103.544  91.627 -25.245  1.00 11.11           C  
ANISOU  264  CB  ASN A 131     1827    960   1435   -254    214   -193       C  
ATOM    265  CG  ASN A 131     103.059  91.115 -26.585  1.00 10.79           C  
ANISOU  265  CG  ASN A 131     1754    835   1510   -334     75   -106       C  
ATOM    266  OD1 ASN A 131     101.876  91.221 -26.918  1.00 11.80           O  
ANISOU  266  OD1 ASN A 131     1779   1168   1535   -160   -120    -39       O  
ATOM    267  ND2 ASN A 131     103.967  90.532 -27.352  1.00 10.79           N  
ANISOU  267  ND2 ASN A 131     1879    913   1307   -135    197   -124       N  
ATOM    268  N   LYS A 132     101.046  89.941 -23.076  1.00  9.88           N  
ANISOU  268  N   LYS A 132     1599    812   1342    -29    -85    -32       N  
ATOM    269  CA  LYS A 132     100.704  88.616 -22.590  1.00  8.76           C  
ANISOU  269  CA  LYS A 132     1453    581   1294     80   -147    199       C  
ATOM    270  C   LYS A 132      99.204  88.513 -22.421  1.00  9.19           C  
ANISOU  270  C   LYS A 132     1566    661   1265   -105    -46     34       C  
ATOM    271  O   LYS A 132      98.592  89.361 -21.769  1.00 10.35           O  
ANISOU  271  O   LYS A 132     1752    730   1453    -29   -114   -129       O  
ATOM    272  CB  LYS A 132     101.392  88.335 -21.251  1.00  9.48           C  
ANISOU  272  CB  LYS A 132     1743    672   1188    120   -370    291       C  
ATOM    273  CG  LYS A 132     101.174  86.926 -20.715  1.00  9.91           C  
ANISOU  273  CG  LYS A 132     1667    792   1308    278   -232    427       C  
ATOM    274  CD  LYS A 132     102.197  86.631 -19.625  1.00 12.32           C  
ANISOU  274  CD  LYS A 132     1947   1088   1647    100   -194    656       C  
ATOM    275  CE  LYS A 132     102.043  85.232 -19.081  1.00 14.87           C  
ANISOU  275  CE  LYS A 132     2400   1297   1954    166   -244    678       C  
ATOM    276  NZ  LYS A 132     103.141  84.928 -18.133  1.00 17.45           N1+
ANISOU  276  NZ  LYS A 132     2490   1827   2312    459   -391    450       N1+
ATOM    277  N   LEU A 133      98.623  87.490 -23.039  1.00  9.17           N  
ANISOU  277  N   LEU A 133     1457    736   1290   -185   -109     34       N  
ATOM    278  CA  LEU A 133      97.214  87.177 -22.896  1.00  9.92           C  
ANISOU  278  CA  LEU A 133     1508    993   1268   -358   -238     92       C  
ATOM    279  C   LEU A 133      97.073  86.161 -21.773  1.00  9.93           C  
ANISOU  279  C   LEU A 133     1449    859   1466   -107     -5    284       C  
ATOM    280  O   LEU A 133      97.817  85.179 -21.728  1.00 11.80           O  
ANISOU  280  O   LEU A 133     1668   1155   1662    223    143    305       O  
ATOM    281  CB  LEU A 133      96.706  86.559 -24.194  1.00 11.13           C  
ANISOU  281  CB  LEU A 133     1548   1312   1368   -116   -295    -70       C  
ATOM    282  CG  LEU A 133      95.201  86.349 -24.263  1.00 12.84           C  
ANISOU  282  CG  LEU A 133     1670   1618   1591     29   -524   -298       C  
ATOM    283  CD1 LEU A 133      94.479  87.704 -24.339  1.00 15.61           C  
ANISOU  283  CD1 LEU A 133     2127   2013   1792    349   -514   -129       C  
ATOM    284  CD2 LEU A 133      94.862  85.467 -25.459  1.00 16.41           C  
ANISOU  284  CD2 LEU A 133     2194   2225   1815   -116   -443   -668       C  
ATOM    285  N   PHE A 134      96.145  86.413 -20.859  1.00  9.29           N  
ANISOU  285  N   PHE A 134     1262    876   1390   -282     50    391       N  
ATOM    286  CA  PHE A 134      95.807  85.478 -19.801  1.00 11.04           C  
ANISOU  286  CA  PHE A 134     1443   1293   1460   -166     13     76       C  
ATOM    287  C   PHE A 134      94.392  84.988 -20.057  1.00 10.04           C  
ANISOU  287  C   PHE A 134     1575    869   1372   -368     92     20       C  
ATOM    288  O   PHE A 134      93.476  85.798 -20.232  1.00 11.26           O  
ANISOU  288  O   PHE A 134     1628   1127   1525    -12     55    192       O  
ATOM    289  CB  PHE A 134      95.829  86.199 -18.456  1.00 11.02           C  
ANISOU  289  CB  PHE A 134     1507   1214   1466   -166    132   -160       C  
ATOM    290  CG  PHE A 134      97.173  86.742 -18.073  1.00 11.23           C  
ANISOU  290  CG  PHE A 134     1590   1242   1434   -194    155    -74       C  
ATOM    291  CD1 PHE A 134      97.651  87.926 -18.619  1.00 11.62           C  
ANISOU  291  CD1 PHE A 134     1616   1291   1508   -101    182    -53       C  
ATOM    292  CD2 PHE A 134      97.952  86.073 -17.144  1.00 12.49           C  
ANISOU  292  CD2 PHE A 134     1914   1283   1548      1    -76   -206       C  
ATOM    293  CE1 PHE A 134      98.893  88.423 -18.246  1.00 10.26           C  
ANISOU  293  CE1 PHE A 134     1457   1006   1437    -70   -142    -66       C  
ATOM    294  CE2 PHE A 134      99.183  86.557 -16.768  1.00 12.74           C  
ANISOU  294  CE2 PHE A 134     1869   1254   1718   -160   -176    -27       C  
ATOM    295  CZ  PHE A 134      99.661  87.732 -17.318  1.00 12.51           C  
ANISOU  295  CZ  PHE A 134     1805   1247   1700   -309    -30    106       C  
ATOM    296  N   CYS A 135      94.197  83.673 -20.077  1.00 11.14           N  
ANISOU  296  N   CYS A 135     1817    917   1497   -493     21     79       N  
ATOM    297  CA  CYS A 135      92.859  83.188 -20.388  1.00 11.47           C  
ANISOU  297  CA  CYS A 135     1935    874   1551   -418    -45    135       C  
ATOM    298  C   CYS A 135      92.574  81.902 -19.642  1.00 12.20           C  
ANISOU  298  C   CYS A 135     1840    939   1855   -294   -126    111       C  
ATOM    299  O   CYS A 135      93.483  81.178 -19.232  1.00 14.11           O  
ANISOU  299  O   CYS A 135     2037   1283   2039   -154    -30    433       O  
ATOM    300  CB  CYS A 135      92.677  82.975 -21.889  1.00 12.43           C  
ANISOU  300  CB  CYS A 135     2224   1015   1483    102   -165   -152       C  
ATOM    301  SG  CYS A 135      93.786  81.727 -22.565  1.00 15.53           S  
ANISOU  301  SG  CYS A 135     2832   1575   1495    204   -265   -184       S  
ATOM    302  N   GLN A 136      91.287  81.646 -19.454  1.00 13.66           N  
ANISOU  302  N   GLN A 136     2100   1084   2004   -573    -47     99       N  
ATOM    303  CA  GLN A 136      90.833  80.380 -18.919  1.00 14.11           C  
ANISOU  303  CA  GLN A 136     2055   1234   2072   -592    191     94       C  
ATOM    304  C   GLN A 136      90.817  79.311 -20.004  1.00 13.48           C  
ANISOU  304  C   GLN A 136     1941   1105   2078   -245    147    264       C  
ATOM    305  O   GLN A 136      90.820  79.593 -21.205  1.00 14.23           O  
ANISOU  305  O   GLN A 136     2313   1011   2084   -248     25    350       O  
ATOM    306  CB  GLN A 136      89.440  80.531 -18.310  1.00 15.82           C  
ANISOU  306  CB  GLN A 136     2063   1686   2262   -703    328   -129       C  
ATOM    307  CG  GLN A 136      89.459  81.356 -17.040  1.00 19.01           C  
ANISOU  307  CG  GLN A 136     2435   2331   2458   -679    380   -398       C  
ATOM    308  CD  GLN A 136      88.087  81.583 -16.453  1.00 22.62           C  
ANISOU  308  CD  GLN A 136     2755   3149   2691   -701    448   -437       C  
ATOM    309  OE1 GLN A 136      87.075  81.338 -17.099  1.00 25.46           O  
ANISOU  309  OE1 GLN A 136     3054   3722   2898   -565    533   -367       O  
ATOM    310  NE2 GLN A 136      88.047  82.060 -15.219  1.00 24.62           N  
ANISOU  310  NE2 GLN A 136     3090   3456   2809   -522    553   -503       N  
ATOM    311  N   LEU A 137      90.781  78.067 -19.551  1.00 13.50           N  
ANISOU  311  N   LEU A 137     1815   1132   2183   -326    -41    232       N  
ATOM    312  CA  LEU A 137      90.802  76.922 -20.441  1.00 12.59           C  
ANISOU  312  CA  LEU A 137     1677    976   2128   -265     21    269       C  
ATOM    313  C   LEU A 137      89.563  76.894 -21.323  1.00 12.08           C  
ANISOU  313  C   LEU A 137     1659    956   1976   -193    116    138       C  
ATOM    314  O   LEU A 137      88.434  76.960 -20.831  1.00 13.01           O  
ANISOU  314  O   LEU A 137     1656   1301   1986   -150     64    106       O  
ATOM    315  CB  LEU A 137      90.829  75.671 -19.571  1.00 13.73           C  
ANISOU  315  CB  LEU A 137     1938   1147   2130   -267    -25    330       C  
ATOM    316  CG  LEU A 137      90.752  74.350 -20.298  1.00 14.79           C  
ANISOU  316  CG  LEU A 137     2286   1232   2101    -45    210    173       C  
ATOM    317  CD1 LEU A 137      92.053  74.119 -20.982  1.00 15.45           C  
ANISOU  317  CD1 LEU A 137     2266   1652   1951   -346    333   -191       C  
ATOM    318  CD2 LEU A 137      90.448  73.256 -19.291  1.00 17.20           C  
ANISOU  318  CD2 LEU A 137     2785   1454   2297   -339    504    388       C  
ATOM    319  N   ALA A 138      89.777  76.810 -22.637  1.00 12.54           N  
ANISOU  319  N   ALA A 138     1722    943   2098    -51    174    182       N  
ATOM    320  CA  ALA A 138      88.711  76.607 -23.613  1.00 14.23           C  
ANISOU  320  CA  ALA A 138     1970   1039   2396    203      4    202       C  
ATOM    321  C   ALA A 138      87.729  77.774 -23.674  1.00 16.86           C  
ANISOU  321  C   ALA A 138     2133   1615   2659    241   -270     20       C  
ATOM    322  O   ALA A 138      86.595  77.609 -24.124  1.00 22.12           O  
ANISOU  322  O   ALA A 138     2631   2304   3468    513   -808   -338       O  
ATOM    323  CB  ALA A 138      87.980  75.266 -23.410  1.00 14.41           C  
ANISOU  323  CB  ALA A 138     2089    949   2439   -109   -165     64       C  
ATOM    324  N   LYS A 139      88.133  78.957 -23.236  1.00 13.24           N  
ANISOU  324  N   LYS A 139     1887   1137   2008    246     26    154       N  
ATOM    325  CA  LYS A 139      87.270  80.122 -23.305  1.00 12.94           C  
ANISOU  325  CA  LYS A 139     1903   1237   1777    104    104    229       C  
ATOM    326  C   LYS A 139      87.656  80.995 -24.493  1.00 12.05           C  
ANISOU  326  C   LYS A 139     1655   1169   1755    303    345    209       C  
ATOM    327  O   LYS A 139      88.785  80.957 -24.989  1.00 13.56           O  
ANISOU  327  O   LYS A 139     1753   1570   1830    403    349    115       O  
ATOM    328  CB  LYS A 139      87.351  80.934 -22.005  1.00 16.53           C  
ANISOU  328  CB  LYS A 139     2671   1730   1881    140    215    266       C  
ATOM    329  CG  LYS A 139      86.864  80.197 -20.765  1.00 20.52           C  
ANISOU  329  CG  LYS A 139     3066   2567   2164    178    346    476       C  
ATOM    330  CD  LYS A 139      85.383  79.908 -20.835  1.00 24.61           C  
ANISOU  330  CD  LYS A 139     3665   3238   2449     87    422    704       C  
ATOM    331  CE  LYS A 139      84.809  79.684 -19.446  1.00 28.34           C  
ANISOU  331  CE  LYS A 139     4146   3862   2760     96    409    492       C  
ATOM    332  NZ  LYS A 139      85.632  78.730 -18.680  1.00 31.17           N1+
ANISOU  332  NZ  LYS A 139     4571   4301   2972    -30    368    429       N1+
ATOM    333  N   THR A 140      86.690  81.791 -24.943  1.00 11.58           N  
ANISOU  333  N   THR A 140     1684   1018   1697    328    118    328       N  
ATOM    334  CA  THR A 140      86.884  82.641 -26.112  1.00 10.46           C  
ANISOU  334  CA  THR A 140     1466    850   1657     98    129    268       C  
ATOM    335  C   THR A 140      87.970  83.678 -25.868  1.00 11.04           C  
ANISOU  335  C   THR A 140     1471   1185   1539     12    145    -34       C  
ATOM    336  O   THR A 140      87.919  84.441 -24.899  1.00 13.13           O  
ANISOU  336  O   THR A 140     1906   1521   1559   -181    188    -85       O  
ATOM    337  CB  THR A 140      85.567  83.343 -26.429  1.00 10.96           C  
ANISOU  337  CB  THR A 140     1620    767   1777    107   -154    275       C  
ATOM    338  OG1 THR A 140      84.555  82.359 -26.656  1.00 12.66           O  
ANISOU  338  OG1 THR A 140     1737   1142   1932   -180   -152    289       O  
ATOM    339  CG2 THR A 140      85.699  84.232 -27.661  1.00 13.44           C  
ANISOU  339  CG2 THR A 140     2046   1175   1884    176   -186    360       C  
ATOM    340  N   CYS A 141      88.950  83.715 -26.767  1.00  9.85           N  
ANISOU  340  N   CYS A 141     1432    879   1433    -43    256     36       N  
ATOM    341  CA  CYS A 141      89.993  84.739 -26.744  1.00  9.69           C  
ANISOU  341  CA  CYS A 141     1478    793   1411    -12     59    182       C  
ATOM    342  C   CYS A 141      89.880  85.548 -28.018  1.00 10.35           C  
ANISOU  342  C   CYS A 141     1624    925   1382   -121     73   -121       C  
ATOM    343  O   CYS A 141      90.325  85.088 -29.087  1.00 10.84           O  
ANISOU  343  O   CYS A 141     1790    917   1412   -102    165   -288       O  
ATOM    344  CB  CYS A 141      91.373  84.094 -26.681  1.00 11.96           C  
ANISOU  344  CB  CYS A 141     1867   1183   1493    226     11    327       C  
ATOM    345  SG  CYS A 141      91.616  83.110 -25.229  1.00 13.58           S  
ANISOU  345  SG  CYS A 141     2138   1470   1551     64    -91    198       S  
ATOM    346  N   PRO A 142      89.310  86.751 -27.966  1.00 10.73           N  
ANISOU  346  N   PRO A 142     1776    962   1339     46    206   -138       N  
ATOM    347  CA  PRO A 142      89.185  87.556 -29.186  1.00 11.58           C  
ANISOU  347  CA  PRO A 142     1831   1164   1404     45    207     50       C  
ATOM    348  C   PRO A 142      90.521  88.211 -29.496  1.00 11.52           C  
ANISOU  348  C   PRO A 142     1976   1039   1361   -439    117     -8       C  
ATOM    349  O   PRO A 142      91.127  88.858 -28.642  1.00 14.62           O  
ANISOU  349  O   PRO A 142     2446   1533   1574   -387    -25   -222       O  
ATOM    350  CB  PRO A 142      88.131  88.609 -28.818  1.00 13.18           C  
ANISOU  350  CB  PRO A 142     2143   1184   1679    398    165     88       C  
ATOM    351  CG  PRO A 142      87.492  88.109 -27.560  1.00 13.92           C  
ANISOU  351  CG  PRO A 142     2231   1464   1593    620    365    104       C  
ATOM    352  CD  PRO A 142      88.556  87.330 -26.847  1.00 12.01           C  
ANISOU  352  CD  PRO A 142     1859   1226   1477    341    329   -202       C  
ATOM    353  N   VAL A 143      90.988  88.018 -30.718  1.00  9.50           N  
ANISOU  353  N   VAL A 143     1638    787   1186   -162    -22    -12       N  
ATOM    354  CA  VAL A 143      92.219  88.628 -31.186  1.00 10.15           C  
ANISOU  354  CA  VAL A 143     1616    861   1379   -179    -48    144       C  
ATOM    355  C   VAL A 143      91.862  89.422 -32.426  1.00 10.59           C  
ANISOU  355  C   VAL A 143     1676   1050   1298   -244   -260      2       C  
ATOM    356  O   VAL A 143      91.341  88.863 -33.398  1.00 11.79           O  
ANISOU  356  O   VAL A 143     1809   1174   1497   -400   -328   -151       O  
ATOM    357  CB  VAL A 143      93.292  87.575 -31.493  1.00 10.50           C  
ANISOU  357  CB  VAL A 143     1564    983   1441   -106    -32    135       C  
ATOM    358  CG1 VAL A 143      94.526  88.254 -32.069  1.00 12.44           C  
ANISOU  358  CG1 VAL A 143     1698   1255   1772    -41     -7    151       C  
ATOM    359  CG2 VAL A 143      93.646  86.797 -30.218  1.00 12.10           C  
ANISOU  359  CG2 VAL A 143     1911   1271   1414     67   -277      8       C  
ATOM    360  N   GLN A 144      92.107  90.722 -32.385  1.00 10.56           N  
ANISOU  360  N   GLN A 144     1736   1056   1222   -176   -233     99       N  
ATOM    361  CA  GLN A 144      91.806  91.566 -33.526  1.00 10.41           C  
ANISOU  361  CA  GLN A 144     1761    836   1360    222   -135     31       C  
ATOM    362  C   GLN A 144      92.958  91.552 -34.511  1.00 10.11           C  
ANISOU  362  C   GLN A 144     1721    738   1381    222   -210   -113       C  
ATOM    363  O   GLN A 144      94.132  91.478 -34.133  1.00 10.70           O  
ANISOU  363  O   GLN A 144     1653    875   1536    191   -105    -73       O  
ATOM    364  CB  GLN A 144      91.575  93.004 -33.085  1.00 11.52           C  
ANISOU  364  CB  GLN A 144     1950    925   1504    457     36   -137       C  
ATOM    365  CG  GLN A 144      90.498  93.141 -32.053  1.00 12.76           C  
ANISOU  365  CG  GLN A 144     2071   1152   1625    425    352   -287       C  
ATOM    366  CD  GLN A 144      90.370  94.549 -31.574  1.00 14.68           C  
ANISOU  366  CD  GLN A 144     2427   1501   1649    254    294   -322       C  
ATOM    367  OE1 GLN A 144      91.346  95.311 -31.556  1.00 15.08           O  
ANISOU  367  OE1 GLN A 144     2688   1414   1627    215    429    -82       O  
ATOM    368  NE2 GLN A 144      89.164  94.919 -31.186  1.00 18.71           N  
ANISOU  368  NE2 GLN A 144     2743   2237   2127    437    298   -345       N  
ATOM    369  N   LEU A 145      92.606  91.641 -35.788  1.00 11.24           N  
ANISOU  369  N   LEU A 145     2074    879   1318    342   -130    -56       N  
ATOM    370  CA  LEU A 145      93.571  91.762 -36.864  1.00 11.23           C  
ANISOU  370  CA  LEU A 145     2113    855   1299    401   -133      7       C  
ATOM    371  C   LEU A 145      93.375  93.132 -37.485  1.00 11.71           C  
ANISOU  371  C   LEU A 145     2115    917   1419    113   -253    240       C  
ATOM    372  O   LEU A 145      92.287  93.442 -37.983  1.00 14.16           O  
ANISOU  372  O   LEU A 145     2107   1281   1991    182   -311    306       O  
ATOM    373  CB  LEU A 145      93.338  90.686 -37.919  1.00 12.26           C  
ANISOU  373  CB  LEU A 145     2172    997   1491    146   -359   -259       C  
ATOM    374  CG  LEU A 145      93.178  89.257 -37.404  1.00 13.22           C  
ANISOU  374  CG  LEU A 145     2222   1188   1614    241   -370   -191       C  
ATOM    375  CD1 LEU A 145      92.861  88.341 -38.582  1.00 15.82           C  
ANISOU  375  CD1 LEU A 145     2607   1590   1813     91   -452   -428       C  
ATOM    376  CD2 LEU A 145      94.428  88.792 -36.683  1.00 13.53           C  
ANISOU  376  CD2 LEU A 145     2264   1208   1670    366   -247    118       C  
ATOM    377  N   TRP A 146      94.417  93.944 -37.441  1.00 10.43           N  
ANISOU  377  N   TRP A 146     2026    652   1285     27    -31     94       N  
ATOM    378  CA  TRP A 146      94.398  95.289 -37.986  1.00 10.05           C  
ANISOU  378  CA  TRP A 146     1826    698   1296     38    -88    268       C  
ATOM    379  C   TRP A 146      95.332  95.343 -39.180  1.00 11.73           C  
ANISOU  379  C   TRP A 146     2012   1058   1388    200    -45    402       C  
ATOM    380  O   TRP A 146      96.440  94.801 -39.132  1.00 12.82           O  
ANISOU  380  O   TRP A 146     1972   1413   1484    284   -168    293       O  
ATOM    381  CB  TRP A 146      94.873  96.292 -36.935  1.00 11.02           C  
ANISOU  381  CB  TRP A 146     1875    763   1551   -265   -120   -159       C  
ATOM    382  CG  TRP A 146      93.905  96.449 -35.822  1.00 11.72           C  
ANISOU  382  CG  TRP A 146     1936    933   1586    272   -101    -42       C  
ATOM    383  CD1 TRP A 146      93.852  95.730 -34.656  1.00 12.15           C  
ANISOU  383  CD1 TRP A 146     1971    996   1648    159    -65   -163       C  
ATOM    384  CD2 TRP A 146      92.823  97.380 -35.767  1.00 11.82           C  
ANISOU  384  CD2 TRP A 146     1920    840   1732    352    -79    -19       C  
ATOM    385  NE1 TRP A 146      92.802  96.163 -33.884  1.00 12.53           N  
ANISOU  385  NE1 TRP A 146     2044    940   1775    341    -30   -247       N  
ATOM    386  CE2 TRP A 146      92.157  97.177 -34.543  1.00 12.71           C  
ANISOU  386  CE2 TRP A 146     1993   1009   1828    343    -69   -260       C  
ATOM    387  CE3 TRP A 146      92.350  98.363 -36.638  1.00 13.49           C  
ANISOU  387  CE3 TRP A 146     2284    895   1945    417     -9    -49       C  
ATOM    388  CZ2 TRP A 146      91.046  97.920 -34.170  1.00 13.62           C  
ANISOU  388  CZ2 TRP A 146     2219    954   2002    183   -116   -174       C  
ATOM    389  CZ3 TRP A 146      91.246  99.095 -36.266  1.00 14.27           C  
ANISOU  389  CZ3 TRP A 146     2310    962   2149    326    -33   -182       C  
ATOM    390  CH2 TRP A 146      90.607  98.872 -35.046  1.00 14.49           C  
ANISOU  390  CH2 TRP A 146     2342   1049   2113    250   -201   -143       C  
ATOM    391  N   VAL A 147      94.875  95.986 -40.252  1.00 12.56           N  
ANISOU  391  N   VAL A 147     2189   1137   1444    164     97    429       N  
ATOM    392  CA  VAL A 147      95.701  96.230 -41.425  1.00 12.26           C  
ANISOU  392  CA  VAL A 147     2229   1065   1364    273    217    202       C  
ATOM    393  C   VAL A 147      95.474  97.666 -41.865  1.00 13.50           C  
ANISOU  393  C   VAL A 147     2516   1161   1454    508    112     34       C  
ATOM    394  O   VAL A 147      94.410  98.247 -41.628  1.00 15.40           O  
ANISOU  394  O   VAL A 147     2642   1576   1632    522    263    232       O  
ATOM    395  CB  VAL A 147      95.395  95.265 -42.593  1.00 12.84           C  
ANISOU  395  CB  VAL A 147     2107   1347   1426    475   -176     98       C  
ATOM    396  CG1 VAL A 147      95.848  93.835 -42.262  1.00 13.60           C  
ANISOU  396  CG1 VAL A 147     2360   1154   1655    605   -210     95       C  
ATOM    397  CG2 VAL A 147      93.909  95.292 -42.934  1.00 15.12           C  
ANISOU  397  CG2 VAL A 147     2117   1979   1650    508    -30    106       C  
ATOM    398  N   ASP A 148      96.492  98.237 -42.509  1.00 14.12           N  
ANISOU  398  N   ASP A 148     2776   1150   1440    263     98    244       N  
ATOM    399  CA  ASP A 148      96.367  99.563 -43.104  1.00 15.32           C  
ANISOU  399  CA  ASP A 148     3026   1167   1628    505   -104    270       C  
ATOM    400  C   ASP A 148      95.729  99.499 -44.483  1.00 15.75           C  
ANISOU  400  C   ASP A 148     3231   1123   1630    562   -197    205       C  
ATOM    401  O   ASP A 148      95.121 100.480 -44.926  1.00 18.25           O  
ANISOU  401  O   ASP A 148     3554   1572   1810    659   -396    331       O  
ATOM    402  CB  ASP A 148      97.742 100.213 -43.251  1.00 16.33           C  
ANISOU  402  CB  ASP A 148     3220   1395   1591     67     -9    175       C  
ATOM    403  CG  ASP A 148      98.368 100.554 -41.929  1.00 18.46           C  
ANISOU  403  CG  ASP A 148     3599   1651   1765    -14    143    257       C  
ATOM    404  OD1 ASP A 148      97.619 100.876 -40.993  1.00 18.36           O  
ANISOU  404  OD1 ASP A 148     3705   1568   1704     -2    180    157       O  
ATOM    405  OD2 ASP A 148      99.607 100.515 -41.825  1.00 20.75           O1-
ANISOU  405  OD2 ASP A 148     3748   2071   2065   -100     62    193       O1-
ATOM    406  N   SER A 149      95.887  98.381 -45.186  1.00 15.89           N  
ANISOU  406  N   SER A 149     3291   1136   1610    232   -133    161       N  
ATOM    407  CA  SER A 149      95.254  98.211 -46.482  1.00 17.27           C  
ANISOU  407  CA  SER A 149     3513   1301   1749    -45      6     63       C  
ATOM    408  C   SER A 149      94.867  96.748 -46.622  1.00 16.58           C  
ANISOU  408  C   SER A 149     3376   1207   1718     32    -98   -148       C  
ATOM    409  O   SER A 149      95.375  95.881 -45.908  1.00 16.59           O  
ANISOU  409  O   SER A 149     3399   1375   1528    391   -149     20       O  
ATOM    410  CB  SER A 149      96.159  98.651 -47.638  1.00 20.01           C  
ANISOU  410  CB  SER A 149     3769   1761   2074    -58    206    308       C  
ATOM    411  OG  SER A 149      97.428  98.037 -47.557  1.00 22.09           O  
ANISOU  411  OG  SER A 149     4011   2058   2324     96    373    351       O  
ATOM    412  N   THR A 150      93.959  96.484 -47.544  1.00 17.93           N  
ANISOU  412  N   THR A 150     3265   1546   1999    123   -134   -346       N  
ATOM    413  CA  THR A 150      93.366  95.156 -47.639  1.00 17.47           C  
ANISOU  413  CA  THR A 150     3005   1431   2199    437    -98   -376       C  
ATOM    414  C   THR A 150      94.317  94.211 -48.363  1.00 16.05           C  
ANISOU  414  C   THR A 150     2976   1249   1874    515     18    -23       C  
ATOM    415  O   THR A 150      94.713  94.496 -49.500  1.00 17.71           O  
ANISOU  415  O   THR A 150     3242   1579   1908    350    -38      4       O  
ATOM    416  CB  THR A 150      92.054  95.240 -48.397  1.00 19.75           C  
ANISOU  416  CB  THR A 150     2975   1721   2807    628   -226   -667       C  
ATOM    417  OG1 THR A 150      91.202  96.198 -47.755  1.00 23.60           O  
ANISOU  417  OG1 THR A 150     3433   2224   3310    874   -450   -866       O  
ATOM    418  CG2 THR A 150      91.364  93.879 -48.421  1.00 21.29           C  
ANISOU  418  CG2 THR A 150     3069   2039   2979    287    -97   -603       C  
ATOM    419  N   PRO A 151      94.699  93.090 -47.762  1.00 14.59           N  
ANISOU  419  N   PRO A 151     2894   1120   1531    385     95     88       N  
ATOM    420  CA  PRO A 151      95.526  92.124 -48.482  1.00 14.44           C  
ANISOU  420  CA  PRO A 151     2839   1181   1468    377     78    -80       C  
ATOM    421  C   PRO A 151      94.708  91.390 -49.528  1.00 14.55           C  
ANISOU  421  C   PRO A 151     2594   1351   1585    221     10      4       C  
ATOM    422  O   PRO A 151      93.467  91.408 -49.491  1.00 15.90           O  
ANISOU  422  O   PRO A 151     2672   1584   1785    293    145   -241       O  
ATOM    423  CB  PRO A 151      96.007  91.169 -47.379  1.00 15.07           C  
ANISOU  423  CB  PRO A 151     3084   1250   1392    368     84    -19       C  
ATOM    424  CG  PRO A 151      95.055  91.337 -46.270  1.00 17.83           C  
ANISOU  424  CG  PRO A 151     3313   1756   1705    577    344    149       C  
ATOM    425  CD  PRO A 151      94.468  92.705 -46.358  1.00 15.91           C  
ANISOU  425  CD  PRO A 151     3223   1245   1578    261    240    210       C  
ATOM    426  N   PRO A 152      95.375  90.741 -50.476  1.00 14.09           N  
ANISOU  426  N   PRO A 152     2888    960   1505    158     13    -23       N  
ATOM    427  CA  PRO A 152      94.684  90.147 -51.624  1.00 13.98           C  
ANISOU  427  CA  PRO A 152     2849   1082   1379     51    -36   -156       C  
ATOM    428  C   PRO A 152      93.743  89.026 -51.222  1.00 13.84           C  
ANISOU  428  C   PRO A 152     2598   1290   1372    193   -185    110       C  
ATOM    429  O   PRO A 152      93.920  88.388 -50.174  1.00 14.18           O  
ANISOU  429  O   PRO A 152     2477   1356   1554     80    -56     85       O  
ATOM    430  CB  PRO A 152      95.842  89.594 -52.472  1.00 15.18           C  
ANISOU  430  CB  PRO A 152     3097   1401   1269    119    146   -158       C  
ATOM    431  CG  PRO A 152      97.017  90.427 -52.097  1.00 16.27           C  
ANISOU  431  CG  PRO A 152     3346   1471   1366    125     81    -65       C  
ATOM    432  CD  PRO A 152      96.839  90.726 -50.641  1.00 14.70           C  
ANISOU  432  CD  PRO A 152     3035   1116   1435    245    270     -1       C  
ATOM    433  N   PRO A 153      92.757  88.722 -52.067  1.00 15.05           N  
ANISOU  433  N   PRO A 153     2734   1495   1488    367   -410    155       N  
ATOM    434  CA  PRO A 153      91.942  87.521 -51.850  1.00 14.26           C  
ANISOU  434  CA  PRO A 153     2569   1417   1431    318   -521     36       C  
ATOM    435  C   PRO A 153      92.834  86.293 -51.781  1.00 13.43           C  
ANISOU  435  C   PRO A 153     2425   1252   1427    182   -423    112       C  
ATOM    436  O   PRO A 153      93.782  86.150 -52.552  1.00 14.13           O  
ANISOU  436  O   PRO A 153     2425   1346   1599    261    -94    105       O  
ATOM    437  CB  PRO A 153      91.047  87.467 -53.095  1.00 15.63           C  
ANISOU  437  CB  PRO A 153     2729   1695   1516    442   -744      2       C  
ATOM    438  CG  PRO A 153      91.047  88.853 -53.641  1.00 16.74           C  
ANISOU  438  CG  PRO A 153     2954   1701   1704    389   -597    -98       C  
ATOM    439  CD  PRO A 153      92.383  89.443 -53.296  1.00 16.23           C  
ANISOU  439  CD  PRO A 153     2868   1696   1604    478   -613    228       C  
ATOM    440  N   GLY A 154      92.527  85.405 -50.841  1.00 12.89           N  
ANISOU  440  N   GLY A 154     2374   1106   1419     61   -460    241       N  
ATOM    441  CA  GLY A 154      93.334  84.228 -50.614  1.00 12.31           C  
ANISOU  441  CA  GLY A 154     2193   1115   1368    160   -554     90       C  
ATOM    442  C   GLY A 154      94.338  84.375 -49.495  1.00 11.38           C  
ANISOU  442  C   GLY A 154     2126    977   1222    -34   -345    199       C  
ATOM    443  O   GLY A 154      94.988  83.388 -49.128  1.00 12.98           O  
ANISOU  443  O   GLY A 154     2345   1183   1405    100   -173     44       O  
ATOM    444  N   THR A 155      94.472  85.573 -48.936  1.00 11.84           N  
ANISOU  444  N   THR A 155     2291   1174   1033   -129   -168     45       N  
ATOM    445  CA  THR A 155      95.297  85.757 -47.753  1.00 10.94           C  
ANISOU  445  CA  THR A 155     2190    947   1021    -38   -161     76       C  
ATOM    446  C   THR A 155      94.715  84.954 -46.602  1.00 11.33           C  
ANISOU  446  C   THR A 155     2127   1107   1073     66   -157     98       C  
ATOM    447  O   THR A 155      93.496  84.814 -46.478  1.00 11.87           O  
ANISOU  447  O   THR A 155     2084   1273   1155    309   -147     90       O  
ATOM    448  CB  THR A 155      95.328  87.248 -47.409  1.00 11.20           C  
ANISOU  448  CB  THR A 155     2372    833   1048     21    -66   -106       C  
ATOM    449  OG1 THR A 155      95.906  87.963 -48.507  1.00 12.01           O  
ANISOU  449  OG1 THR A 155     2431    889   1245    104    254     -1       O  
ATOM    450  CG2 THR A 155      96.166  87.512 -46.176  1.00 11.47           C  
ANISOU  450  CG2 THR A 155     2287    894   1176    102   -340    -31       C  
ATOM    451  N   ARG A 156      95.595  84.400 -45.768  1.00 10.68           N  
ANISOU  451  N   ARG A 156     2052   1080    925    -43   -169    230       N  
ATOM    452  CA  ARG A 156      95.174  83.594 -44.635  1.00 10.18           C  
ANISOU  452  CA  ARG A 156     1958    897   1012   -121   -183    132       C  
ATOM    453  C   ARG A 156      95.877  84.068 -43.372  1.00  9.71           C  
ANISOU  453  C   ARG A 156     1998    694    997      4   -114     33       C  
ATOM    454  O   ARG A 156      96.855  84.823 -43.415  1.00 10.59           O  
ANISOU  454  O   ARG A 156     2100    799   1124   -230    -90    -55       O  
ATOM    455  CB  ARG A 156      95.433  82.107 -44.888  1.00 11.81           C  
ANISOU  455  CB  ARG A 156     2327    994   1167   -388   -168    -31       C  
ATOM    456  CG  ARG A 156      94.677  81.597 -46.094  1.00 13.33           C  
ANISOU  456  CG  ARG A 156     2746   1039   1279   -347   -253   -153       C  
ATOM    457  CD  ARG A 156      94.342  80.135 -45.964  1.00 13.87           C  
ANISOU  457  CD  ARG A 156     2836    939   1495   -321    -18   -277       C  
ATOM    458  NE  ARG A 156      95.528  79.297 -46.020  1.00 14.05           N  
ANISOU  458  NE  ARG A 156     2938    908   1492   -194    287   -116       N  
ATOM    459  CZ  ARG A 156      95.505  77.987 -45.821  1.00 14.66           C  
ANISOU  459  CZ  ARG A 156     2995    982   1594   -244    248    -78       C  
ATOM    460  NH1 ARG A 156      94.357  77.390 -45.509  1.00 15.61           N1+
ANISOU  460  NH1 ARG A 156     3208   1148   1575   -446    265     88       N1+
ATOM    461  NH2 ARG A 156      96.628  77.287 -45.911  1.00 16.59           N  
ANISOU  461  NH2 ARG A 156     3292   1137   1874      4     26    -92       N  
ATOM    462  N   VAL A 157      95.352  83.618 -42.236  1.00  9.85           N  
ANISOU  462  N   VAL A 157     1908    915    919      4     93    -19       N  
ATOM    463  CA  VAL A 157      95.864  84.005 -40.925  1.00  9.65           C  
ANISOU  463  CA  VAL A 157     1978    773    914    156    -63    -51       C  
ATOM    464  C   VAL A 157      96.097  82.726 -40.138  1.00  9.34           C  
ANISOU  464  C   VAL A 157     1825    689   1036     95    -18    186       C  
ATOM    465  O   VAL A 157      95.147  81.975 -39.880  1.00  9.93           O  
ANISOU  465  O   VAL A 157     1687    895   1192   -184    -21     93       O  
ATOM    466  CB  VAL A 157      94.868  84.893 -40.167  1.00 10.37           C  
ANISOU  466  CB  VAL A 157     1909    953   1079    287     25    -41       C  
ATOM    467  CG1 VAL A 157      95.485  85.356 -38.860  1.00 11.62           C  
ANISOU  467  CG1 VAL A 157     1994   1179   1240    128   -278   -345       C  
ATOM    468  CG2 VAL A 157      94.430  86.072 -41.030  1.00 12.18           C  
ANISOU  468  CG2 VAL A 157     2258    925   1444    429     65    210       C  
ATOM    469  N   ARG A 158      97.349  82.477 -39.758  1.00  9.66           N  
ANISOU  469  N   ARG A 158     1867    782   1021    205   -206     75       N  
ATOM    470  CA  ARG A 158      97.734  81.247 -39.080  1.00  9.50           C  
ANISOU  470  CA  ARG A 158     1839    748   1024    242   -187    -17       C  
ATOM    471  C   ARG A 158      98.133  81.556 -37.646  1.00  8.95           C  
ANISOU  471  C   ARG A 158     1702    659   1038     17   -123    119       C  
ATOM    472  O   ARG A 158      98.765  82.580 -37.380  1.00 10.10           O  
ANISOU  472  O   ARG A 158     1978    661   1198   -134     32     49       O  
ATOM    473  CB  ARG A 158      98.918  80.588 -39.793  1.00  9.99           C  
ANISOU  473  CB  ARG A 158     1938    632   1227    404     36    -47       C  
ATOM    474  CG  ARG A 158      99.313  79.243 -39.198  1.00 11.19           C  
ANISOU  474  CG  ARG A 158     2233    761   1259    496     64    -77       C  
ATOM    475  CD  ARG A 158     100.444  78.612 -39.987  1.00 11.67           C  
ANISOU  475  CD  ARG A 158     2149   1020   1264    643    213   -145       C  
ATOM    476  NE  ARG A 158     100.092  78.496 -41.398  1.00 11.86           N  
ANISOU  476  NE  ARG A 158     2285   1016   1205    324    200   -150       N  
ATOM    477  CZ  ARG A 158      99.396  77.498 -41.936  1.00 11.92           C  
ANISOU  477  CZ  ARG A 158     2626    791   1111    343    372     84       C  
ATOM    478  NH1 ARG A 158      98.983  76.472 -41.194  1.00 13.17           N1+
ANISOU  478  NH1 ARG A 158     2708    925   1369    106    200    273       N1+
ATOM    479  NH2 ARG A 158      99.103  77.532 -43.227  1.00 14.51           N  
ANISOU  479  NH2 ARG A 158     2848   1560   1106    527    303    238       N  
ATOM    480  N   ALA A 159      97.770  80.662 -36.724  1.00  9.04           N  
ANISOU  480  N   ALA A 159     1588    790   1056     15   -145    161       N  
ATOM    481  CA  ALA A 159      98.203  80.750 -35.339  1.00  8.11           C  
ANISOU  481  CA  ALA A 159     1275    760   1045    175    -34    184       C  
ATOM    482  C   ALA A 159      98.985  79.495 -34.988  1.00  8.70           C  
ANISOU  482  C   ALA A 159     1343    852   1111     35   -192    141       C  
ATOM    483  O   ALA A 159      98.581  78.384 -35.341  1.00 10.02           O  
ANISOU  483  O   ALA A 159     1556    947   1303   -102   -179      3       O  
ATOM    484  CB  ALA A 159      97.013  80.876 -34.392  1.00  9.48           C  
ANISOU  484  CB  ALA A 159     1463   1007   1132     85    245     28       C  
ATOM    485  N   MET A 160     100.096  79.681 -34.287  1.00  8.88           N  
ANISOU  485  N   MET A 160     1311    937   1125    195   -242    247       N  
ATOM    486  CA  MET A 160     100.935  78.575 -33.852  1.00  9.44           C  
ANISOU  486  CA  MET A 160     1313   1077   1196    390   -212     23       C  
ATOM    487  C   MET A 160     101.514  78.943 -32.496  1.00  8.78           C  
ANISOU  487  C   MET A 160     1443    729   1163    271   -177     52       C  
ATOM    488  O   MET A 160     101.858  80.105 -32.262  1.00 10.46           O  
ANISOU  488  O   MET A 160     1826    609   1539    161   -499     93       O  
ATOM    489  CB  MET A 160     102.080  78.373 -34.848  1.00 10.86           C  
ANISOU  489  CB  MET A 160     1543   1215   1367    554    -43     25       C  
ATOM    490  CG  MET A 160     103.023  77.241 -34.497  1.00 12.34           C  
ANISOU  490  CG  MET A 160     1754   1409   1524    322    -15    134       C  
ATOM    491  SD  MET A 160     104.426  77.170 -35.623  1.00 15.19           S  
ANISOU  491  SD  MET A 160     1840   2067   1863    239    128    -67       S  
ATOM    492  CE  MET A 160     103.657  76.572 -37.123  1.00 15.65           C  
ANISOU  492  CE  MET A 160     1959   2167   1821    554    -21   -263       C  
ATOM    493  N   ALA A 161     101.634  77.959 -31.610  1.00  8.97           N  
ANISOU  493  N   ALA A 161     1471    942    996    283   -242    225       N  
ATOM    494  CA  ALA A 161     102.272  78.170 -30.321  1.00  8.83           C  
ANISOU  494  CA  ALA A 161     1223    895   1237    313   -280    164       C  
ATOM    495  C   ALA A 161     103.685  77.614 -30.338  1.00 10.08           C  
ANISOU  495  C   ALA A 161     1430    846   1553    -41   -303     39       C  
ATOM    496  O   ALA A 161     103.940  76.562 -30.929  1.00 11.58           O  
ANISOU  496  O   ALA A 161     1787    901   1714     72   -228     21       O  
ATOM    497  CB  ALA A 161     101.490  77.483 -29.206  1.00 10.12           C  
ANISOU  497  CB  ALA A 161     1373   1117   1355    161   -101    327       C  
ATOM    498  N   ILE A 162     104.599  78.329 -29.686  1.00  9.30           N  
ANISOU  498  N   ILE A 162     1392    674   1469     67   -303    122       N  
ATOM    499  CA  ILE A 162     105.935  77.825 -29.407  1.00  9.60           C  
ANISOU  499  CA  ILE A 162     1267    855   1524    310   -296     70       C  
ATOM    500  C   ILE A 162     106.252  78.107 -27.944  1.00  8.95           C  
ANISOU  500  C   ILE A 162     1154    653   1594    129   -329     85       C  
ATOM    501  O   ILE A 162     105.664  78.992 -27.319  1.00 10.56           O  
ANISOU  501  O   ILE A 162     1494    680   1837    239   -214     11       O  
ATOM    502  CB  ILE A 162     107.019  78.435 -30.320  1.00 11.65           C  
ANISOU  502  CB  ILE A 162     1749    945   1733    129    -23     83       C  
ATOM    503  CG1 ILE A 162     107.135  79.945 -30.098  1.00 12.45           C  
ANISOU  503  CG1 ILE A 162     1609   1232   1890   -239    162    207       C  
ATOM    504  CG2 ILE A 162     106.726  78.120 -31.779  1.00 12.67           C  
ANISOU  504  CG2 ILE A 162     1950   1235   1629    118    -64    -28       C  
ATOM    505  CD1 ILE A 162     108.398  80.545 -30.706  1.00 14.16           C  
ANISOU  505  CD1 ILE A 162     1673   1697   2010   -276     68    399       C  
ATOM    506  N   TYR A 163     107.188  77.340 -27.394  1.00 10.07           N  
ANISOU  506  N   TYR A 163     1175   1006   1646     -9   -344    167       N  
ATOM    507  CA  TYR A 163     107.669  77.663 -26.058  1.00 10.05           C  
ANISOU  507  CA  TYR A 163     1217    864   1737    -27   -516    -74       C  
ATOM    508  C   TYR A 163     108.480  78.944 -26.101  1.00 11.28           C  
ANISOU  508  C   TYR A 163     1457    950   1878     80   -322    -65       C  
ATOM    509  O   TYR A 163     109.237  79.189 -27.042  1.00 13.17           O  
ANISOU  509  O   TYR A 163     1708   1303   1993     35   -185     52       O  
ATOM    510  CB  TYR A 163     108.487  76.515 -25.458  1.00 10.25           C  
ANISOU  510  CB  TYR A 163     1390    722   1784    220   -354     92       C  
ATOM    511  CG  TYR A 163     107.567  75.406 -25.057  1.00 10.91           C  
ANISOU  511  CG  TYR A 163     1523    825   1795   -224   -289     24       C  
ATOM    512  CD1 TYR A 163     106.650  75.597 -24.031  1.00 11.87           C  
ANISOU  512  CD1 TYR A 163     1768    996   1747   -218   -296     43       C  
ATOM    513  CD2 TYR A 163     107.555  74.198 -25.740  1.00 10.62           C  
ANISOU  513  CD2 TYR A 163     1497    704   1833   -185   -350    107       C  
ATOM    514  CE1 TYR A 163     105.760  74.615 -23.686  1.00 12.45           C  
ANISOU  514  CE1 TYR A 163     2104    759   1869     70   -219    144       C  
ATOM    515  CE2 TYR A 163     106.666  73.205 -25.400  1.00 11.36           C  
ANISOU  515  CE2 TYR A 163     1745    747   1824     42   -291    236       C  
ATOM    516  CZ  TYR A 163     105.772  73.419 -24.372  1.00 12.03           C  
ANISOU  516  CZ  TYR A 163     2052    718   1802     91   -241    188       C  
ATOM    517  OH  TYR A 163     104.870  72.451 -24.038  1.00 13.94           O  
ANISOU  517  OH  TYR A 163     2310   1179   1807    -91     -2    195       O  
ATOM    518  N   LYS A 164     108.295  79.777 -25.079  1.00 10.98           N  
ANISOU  518  N   LYS A 164     1551    687   1934   -186   -397   -174       N  
ATOM    519  CA  LYS A 164     108.962  81.066 -25.048  1.00 11.73           C  
ANISOU  519  CA  LYS A 164     1679    688   2089    -53   -209   -250       C  
ATOM    520  C   LYS A 164     110.426  80.948 -24.651  1.00 12.43           C  
ANISOU  520  C   LYS A 164     1564   1025   2134     51   -280   -154       C  
ATOM    521  O   LYS A 164     111.261  81.723 -25.134  1.00 13.65           O  
ANISOU  521  O   LYS A 164     1596   1247   2343    -91   -203    -70       O  
ATOM    522  CB  LYS A 164     108.217  81.993 -24.092  1.00 13.06           C  
ANISOU  522  CB  LYS A 164     2119    674   2170   -127    111   -362       C  
ATOM    523  CG  LYS A 164     108.828  83.369 -23.996  1.00 16.08           C  
ANISOU  523  CG  LYS A 164     2540    959   2612   -271    423   -536       C  
ATOM    524  CD  LYS A 164     108.009  84.252 -23.104  1.00 20.03           C  
ANISOU  524  CD  LYS A 164     3049   1285   3275   -346    643   -770       C  
ATOM    525  CE  LYS A 164     108.625  85.638 -23.041  1.00 23.14           C  
ANISOU  525  CE  LYS A 164     3538   1580   3672   -478    799   -970       C  
ATOM    526  NZ  LYS A 164     107.815  86.554 -22.200  1.00 27.79           N1+
ANISOU  526  NZ  LYS A 164     4170   2266   4124   -456    989  -1027       N1+
ATOM    527  N   GLN A 165     110.763  80.004 -23.782  1.00 13.19           N  
ANISOU  527  N   GLN A 165     1614   1294   2104    165   -476   -152       N  
ATOM    528  CA  GLN A 165     112.143  79.858 -23.341  1.00 13.47           C  
ANISOU  528  CA  GLN A 165     1525   1370   2225    -20   -248    -82       C  
ATOM    529  C   GLN A 165     112.961  79.160 -24.417  1.00 13.19           C  
ANISOU  529  C   GLN A 165     1359   1242   2410      5    -82     -2       C  
ATOM    530  O   GLN A 165     112.542  78.129 -24.948  1.00 13.65           O  
ANISOU  530  O   GLN A 165     1590   1215   2382   -104   -249    133       O  
ATOM    531  CB  GLN A 165     112.191  79.046 -22.054  1.00 15.71           C  
ANISOU  531  CB  GLN A 165     1921   1969   2078    121   -316     21       C  
ATOM    532  CG  GLN A 165     111.508  79.733 -20.896  1.00 19.00           C  
ANISOU  532  CG  GLN A 165     2379   2569   2273     20   -639   -176       C  
ATOM    533  CD  GLN A 165     111.186  78.774 -19.774  1.00 22.81           C  
ANISOU  533  CD  GLN A 165     3049   3132   2484    151   -988    -30       C  
ATOM    534  OE1 GLN A 165     110.324  77.909 -19.910  1.00 21.28           O  
ANISOU  534  OE1 GLN A 165     2954   2710   2422    534  -1020   -140       O  
ATOM    535  NE2 GLN A 165     111.885  78.917 -18.659  1.00 26.62           N  
ANISOU  535  NE2 GLN A 165     3617   3774   2723   -116  -1155     64       N  
ATOM    536  N   SER A 166     114.143  79.710 -24.707  1.00 15.20           N  
ANISOU  536  N   SER A 166     1467   1641   2666     28    114    123       N  
ATOM    537  CA ASER A 166     114.946  79.209 -25.819  0.44 15.20           C  
ANISOU  537  CA ASER A 166     1588   1534   2652     26     -3    146       C  
ATOM    538  CA BSER A 166     114.953  79.211 -25.816  0.56 15.68           C  
ANISOU  538  CA BSER A 166     1615   1623   2719    -31    -21     52       C  
ATOM    539  C   SER A 166     115.286  77.733 -25.653  1.00 14.78           C  
ANISOU  539  C   SER A 166     1528   1449   2638     57   -102     99       C  
ATOM    540  O   SER A 166     115.327  76.990 -26.638  1.00 15.13           O  
ANISOU  540  O   SER A 166     1784   1527   2438    -36    -42      3       O  
ATOM    541  CB ASER A 166     116.219  80.041 -25.976  0.44 15.65           C  
ANISOU  541  CB ASER A 166     1836   1461   2651    -14    -47    385       C  
ATOM    542  CB BSER A 166     116.238  80.025 -25.922  0.56 17.13           C  
ANISOU  542  CB BSER A 166     1911   1725   2873   -208    -95    135       C  
ATOM    543  OG ASER A 166     115.917  81.349 -26.430  0.44 16.36           O  
ANISOU  543  OG ASER A 166     2040   1508   2669      5    -77    464       O  
ATOM    544  OG BSER A 166     116.926  80.011 -24.685  0.56 18.90           O  
ANISOU  544  OG BSER A 166     2140   1997   3042   -287   -147     47       O  
ATOM    545  N   GLN A 167     115.534  77.287 -24.418  1.00 14.57           N  
ANISOU  545  N   GLN A 167     1276   1493   2769     59   -253     75       N  
ATOM    546  CA  GLN A 167     115.910  75.892 -24.196  1.00 15.34           C  
ANISOU  546  CA  GLN A 167     1503   1563   2761    209   -515     66       C  
ATOM    547  C   GLN A 167     114.767  74.914 -24.433  1.00 15.14           C  
ANISOU  547  C   GLN A 167     1549   1387   2818    263   -320     17       C  
ATOM    548  O   GLN A 167     115.006  73.700 -24.432  1.00 17.07           O  
ANISOU  548  O   GLN A 167     1907   1540   3039    241   -231    -72       O  
ATOM    549  CB  GLN A 167     116.482  75.698 -22.788  1.00 18.12           C  
ANISOU  549  CB  GLN A 167     2020   2098   2765    387   -547    145       C  
ATOM    550  CG  GLN A 167     115.467  75.864 -21.667  1.00 21.75           C  
ANISOU  550  CG  GLN A 167     2366   2903   2995    484   -295    110       C  
ATOM    551  CD  GLN A 167     115.361  77.298 -21.158  1.00 25.30           C  
ANISOU  551  CD  GLN A 167     2829   3645   3139    519   -259     71       C  
ATOM    552  OE1 GLN A 167     115.602  78.257 -21.892  1.00 25.71           O  
ANISOU  552  OE1 GLN A 167     2635   3971   3164    634   -303     41       O  
ATOM    553  NE2 GLN A 167     114.987  77.446 -19.891  1.00 28.03           N  
ANISOU  553  NE2 GLN A 167     3306   4079   3265    459   -233    -25       N  
ATOM    554  N   HIS A 168     113.545  75.404 -24.629  1.00 13.08           N  
ANISOU  554  N   HIS A 168     1157   1330   2481     48   -237    144       N  
ATOM    555  CA  HIS A 168     112.401  74.563 -24.949  1.00 13.15           C  
ANISOU  555  CA  HIS A 168     1305   1288   2402     -7   -150    219       C  
ATOM    556  C   HIS A 168     111.839  74.829 -26.330  1.00 13.12           C  
ANISOU  556  C   HIS A 168     1427   1239   2317    107   -164    190       C  
ATOM    557  O   HIS A 168     110.861  74.189 -26.713  1.00 13.00           O  
ANISOU  557  O   HIS A 168     1589   1150   2202     65   -321    -75       O  
ATOM    558  CB  HIS A 168     111.281  74.767 -23.921  1.00 14.30           C  
ANISOU  558  CB  HIS A 168     1511   1608   2315     87   -177    375       C  
ATOM    559  CG  HIS A 168     111.684  74.389 -22.538  1.00 15.58           C  
ANISOU  559  CG  HIS A 168     1839   1797   2283     19   -376    454       C  
ATOM    560  ND1 HIS A 168     112.058  73.106 -22.209  1.00 16.84           N  
ANISOU  560  ND1 HIS A 168     2279   1702   2418    272   -399    567       N  
ATOM    561  CD2 HIS A 168     111.802  75.121 -21.406  1.00 16.57           C  
ANISOU  561  CD2 HIS A 168     2130   1943   2222    -60   -306    419       C  
ATOM    562  CE1 HIS A 168     112.385  73.062 -20.929  1.00 17.33           C  
ANISOU  562  CE1 HIS A 168     2290   2006   2287     81   -416    551       C  
ATOM    563  NE2 HIS A 168     112.232  74.270 -20.418  1.00 18.13           N  
ANISOU  563  NE2 HIS A 168     2370   2208   2309    -62   -416    485       N  
ATOM    564  N   MET A 169     112.445  75.735 -27.094  1.00 14.37           N  
ANISOU  564  N   MET A 169     1794   1275   2393     75   -136    389       N  
ATOM    565  CA  MET A 169     111.806  76.229 -28.307  1.00 15.64           C  
ANISOU  565  CA  MET A 169     2006   1366   2570   -119    -82    394       C  
ATOM    566  C   MET A 169     111.675  75.169 -29.385  1.00 15.04           C  
ANISOU  566  C   MET A 169     1685   1566   2466     69    -19    284       C  
ATOM    567  O   MET A 169     110.796  75.286 -30.243  1.00 15.03           O  
ANISOU  567  O   MET A 169     1612   1808   2290    277    -27    308       O  
ATOM    568  CB  MET A 169     112.583  77.401 -28.868  1.00 20.27           C  
ANISOU  568  CB  MET A 169     2889   1596   3218   -298    327    345       C  
ATOM    569  CG  MET A 169     112.061  78.692 -28.412  1.00 25.03           C  
ANISOU  569  CG  MET A 169     3862   1763   3886   -364   1129    353       C  
ATOM    570  SD  MET A 169     112.628  79.971 -29.508  1.00 29.22           S  
ANISOU  570  SD  MET A 169     4929   1781   4390   -226   1913    306       S  
ATOM    571  CE  MET A 169     112.135  81.366 -28.526  1.00 28.81           C  
ANISOU  571  CE  MET A 169     4814   1742   4391    107   1718   -174       C  
ATOM    572  N   THR A 170     112.557  74.171 -29.402  1.00 14.92           N  
ANISOU  572  N   THR A 170     1565   1587   2517    103    -60    138       N  
ATOM    573  CA  THR A 170     112.452  73.144 -30.426  1.00 15.85           C  
ANISOU  573  CA  THR A 170     1665   1714   2643    324    143     27       C  
ATOM    574  C   THR A 170     111.396  72.100 -30.107  1.00 15.95           C  
ANISOU  574  C   THR A 170     1791   1743   2526    101    324     -9       C  
ATOM    575  O   THR A 170     111.115  71.259 -30.965  1.00 18.08           O  
ANISOU  575  O   THR A 170     2157   2040   2672    -15    260   -292       O  
ATOM    576  CB  THR A 170     113.800  72.457 -30.669  1.00 18.71           C  
ANISOU  576  CB  THR A 170     1872   2252   2986    203    253    205       C  
ATOM    577  OG1 THR A 170     114.232  71.807 -29.472  1.00 20.64           O  
ANISOU  577  OG1 THR A 170     2178   2563   3102    391     24    295       O  
ATOM    578  CG2 THR A 170     114.843  73.471 -31.093  1.00 19.69           C  
ANISOU  578  CG2 THR A 170     1744   2565   3172   -104    385    141       C  
ATOM    579  N   GLU A 171     110.804  72.126 -28.913  1.00 13.64           N  
ANISOU  579  N   GLU A 171     1500   1385   2299    120    209    104       N  
ATOM    580  CA  GLU A 171     109.787  71.144 -28.562  1.00 13.48           C  
ANISOU  580  CA  GLU A 171     1676   1177   2270    208   -146     97       C  
ATOM    581  C   GLU A 171     108.425  71.601 -29.072  1.00 11.90           C  
ANISOU  581  C   GLU A 171     1514    958   2049    383    -66    143       C  
ATOM    582  O   GLU A 171     108.017  72.742 -28.844  1.00 12.60           O  
ANISOU  582  O   GLU A 171     1729    960   2100    339    -68    -36       O  
ATOM    583  CB  GLU A 171     109.728  70.957 -27.047  1.00 15.05           C  
ANISOU  583  CB  GLU A 171     2005   1307   2408    125   -169    124       C  
ATOM    584  CG  GLU A 171     108.719  69.900 -26.622  1.00 17.33           C  
ANISOU  584  CG  GLU A 171     2263   1749   2571    -24   -276     85       C  
ATOM    585  CD  GLU A 171     108.710  69.649 -25.125  1.00 19.95           C  
ANISOU  585  CD  GLU A 171     2707   2196   2678   -179   -357    -34       C  
ATOM    586  OE1 GLU A 171     109.759  69.850 -24.470  1.00 22.27           O  
ANISOU  586  OE1 GLU A 171     3153   2512   2796    -80   -405   -142       O  
ATOM    587  OE2 GLU A 171     107.648  69.244 -24.606  1.00 20.56           O1-
ANISOU  587  OE2 GLU A 171     2721   2477   2613   -149   -158     45       O1-
ATOM    588  N   VAL A 172     107.709  70.698 -29.745  1.00 11.97           N  
ANISOU  588  N   VAL A 172     1658   1030   1859     37   -144    109       N  
ATOM    589  CA  VAL A 172     106.371  71.016 -30.228  1.00 10.96           C  
ANISOU  589  CA  VAL A 172     1476    879   1810    123    -65     36       C  
ATOM    590  C   VAL A 172     105.457  71.280 -29.040  1.00 10.61           C  
ANISOU  590  C   VAL A 172     1431    945   1656    314    -30    -11       C  
ATOM    591  O   VAL A 172     105.393  70.478 -28.099  1.00 12.26           O  
ANISOU  591  O   VAL A 172     1734   1148   1776     92    -85    183       O  
ATOM    592  CB  VAL A 172     105.828  69.859 -31.083  1.00 12.27           C  
ANISOU  592  CB  VAL A 172     1675   1087   1900    292     98    -76       C  
ATOM    593  CG1 VAL A 172     104.347  70.098 -31.431  1.00 12.25           C  
ANISOU  593  CG1 VAL A 172     1584   1136   1933    224     56   -164       C  
ATOM    594  CG2 VAL A 172     106.679  69.659 -32.330  1.00 13.68           C  
ANISOU  594  CG2 VAL A 172     2008   1149   2040    454    292    -99       C  
ATOM    595  N   VAL A 173     104.740  72.404 -29.075  1.00  9.96           N  
ANISOU  595  N   VAL A 173     1307    883   1596    243     94    -58       N  
ATOM    596  CA  VAL A 173     103.710  72.679 -28.080  1.00  9.72           C  
ANISOU  596  CA  VAL A 173     1482    750   1462    176    123   -175       C  
ATOM    597  C   VAL A 173     102.487  71.855 -28.444  1.00  8.94           C  
ANISOU  597  C   VAL A 173     1333    663   1401     89    -95    185       C  
ATOM    598  O   VAL A 173     101.948  71.983 -29.549  1.00 10.39           O  
ANISOU  598  O   VAL A 173     1585   1068   1294    -84   -181    242       O  
ATOM    599  CB  VAL A 173     103.347  74.170 -28.038  1.00  9.81           C  
ANISOU  599  CB  VAL A 173     1434    744   1550     21    207    -25       C  
ATOM    600  CG1 VAL A 173     102.191  74.390 -27.054  1.00 10.83           C  
ANISOU  600  CG1 VAL A 173     1569   1005   1542    277    178    -15       C  
ATOM    601  CG2 VAL A 173     104.546  75.026 -27.648  1.00 10.23           C  
ANISOU  601  CG2 VAL A 173     1423    845   1620   -234   -142    117       C  
ATOM    602  N   ARG A 174     102.025  71.029 -27.510  1.00  9.76           N  
ANISOU  602  N   ARG A 174     1561    542   1608    -95    -88    138       N  
ATOM    603  CA  ARG A 174     100.879  70.172 -27.772  1.00  9.63           C  
ANISOU  603  CA  ARG A 174     1445    576   1637    -77    101     68       C  
ATOM    604  C   ARG A 174     100.067  70.039 -26.496  1.00  9.92           C  
ANISOU  604  C   ARG A 174     1279    898   1592    -33     -6    202       C  
ATOM    605  O   ARG A 174     100.522  70.390 -25.407  1.00 11.60           O  
ANISOU  605  O   ARG A 174     1591   1160   1658   -115   -180     88       O  
ATOM    606  CB  ARG A 174     101.320  68.783 -28.228  1.00 10.84           C  
ANISOU  606  CB  ARG A 174     1776    626   1718    150    -51     70       C  
ATOM    607  CG  ARG A 174     102.215  68.107 -27.214  1.00 10.94           C  
ANISOU  607  CG  ARG A 174     1772    693   1691    406   -195    232       C  
ATOM    608  CD  ARG A 174     102.532  66.662 -27.585  1.00 12.69           C  
ANISOU  608  CD  ARG A 174     2255    828   1738    216    158    341       C  
ATOM    609  NE  ARG A 174     103.190  66.540 -28.893  1.00 14.35           N  
ANISOU  609  NE  ARG A 174     2511   1211   1733    262     67    227       N  
ATOM    610  CZ  ARG A 174     102.562  66.244 -30.029  1.00 15.83           C  
ANISOU  610  CZ  ARG A 174     2659   1462   1894    216     72     37       C  
ATOM    611  NH1 ARG A 174     103.255  66.140 -31.158  1.00 16.87           N1+
ANISOU  611  NH1 ARG A 174     2963   1451   1996    215    336      8       N1+
ATOM    612  NH2 ARG A 174     101.244  66.036 -30.032  1.00 15.28           N  
ANISOU  612  NH2 ARG A 174     2464   1388   1954    366   -305    121       N  
ATOM    613  N   ARG A 175      98.860  69.512 -26.635  1.00  9.82           N  
ANISOU  613  N   ARG A 175     1411    879   1440    -12     94    202       N  
ATOM    614  CA  ARG A 175      98.076  69.223 -25.449  1.00 10.35           C  
ANISOU  614  CA  ARG A 175     1589    901   1440    -46    -19    266       C  
ATOM    615  C   ARG A 175      98.683  68.079 -24.656  1.00 10.90           C  
ANISOU  615  C   ARG A 175     1832    826   1485    -67    -64     -5       C  
ATOM    616  O   ARG A 175      99.362  67.197 -25.194  1.00 11.50           O  
ANISOU  616  O   ARG A 175     2130    743   1495   -175    114     70       O  
ATOM    617  CB  ARG A 175      96.637  68.897 -25.818  1.00 10.27           C  
ANISOU  617  CB  ARG A 175     1773    596   1533    -41   -143    368       C  
ATOM    618  CG  ARG A 175      95.926  70.108 -26.395  1.00 11.17           C  
ANISOU  618  CG  ARG A 175     1757    807   1681     99   -142    236       C  
ATOM    619  CD  ARG A 175      94.512  69.733 -26.740  1.00 13.58           C  
ANISOU  619  CD  ARG A 175     1704   1581   1875    302    116    117       C  
ATOM    620  NE  ARG A 175      93.596  69.883 -25.625  1.00 14.63           N  
ANISOU  620  NE  ARG A 175     2214   1403   1943    -50   -151    328       N  
ATOM    621  CZ  ARG A 175      92.371  69.375 -25.616  1.00 13.06           C  
ANISOU  621  CZ  ARG A 175     1817   1410   1737   -593   -439    545       C  
ATOM    622  NH1 ARG A 175      91.954  68.589 -26.618  1.00 13.83           N1+
ANISOU  622  NH1 ARG A 175     2000   1620   1636   -160   -486    562       N1+
ATOM    623  NH2 ARG A 175      91.575  69.629 -24.599  1.00 14.84           N  
ANISOU  623  NH2 ARG A 175     2180   1545   1913   -120   -370    334       N  
ATOM    624  N   CYS A 176      98.393  68.091 -23.364  1.00 11.10           N  
ANISOU  624  N   CYS A 176     2151    663   1405   -353    -97     71       N  
ATOM    625  CA  CYS A 176      98.993  67.177 -22.423  1.00 11.61           C  
ANISOU  625  CA  CYS A 176     2274    777   1360    -55   -200    150       C  
ATOM    626  C   CYS A 176      98.374  65.789 -22.571  1.00 11.75           C  
ANISOU  626  C   CYS A 176     2174    870   1421   -109   -193    -45       C  
ATOM    627  O   CYS A 176      97.387  65.610 -23.299  1.00 12.12           O  
ANISOU  627  O   CYS A 176     2212    728   1666   -231   -125    -53       O  
ATOM    628  CB  CYS A 176      98.808  67.724 -21.008  1.00 11.95           C  
ANISOU  628  CB  CYS A 176     2289    850   1400    105    -42      1       C  
ATOM    629  SG  CYS A 176      97.120  67.563 -20.370  1.00 12.51           S  
ANISOU  629  SG  CYS A 176     2452    868   1432   -208    -51    171       S  
ATOM    630  N   PRO A 177      98.948  64.775 -21.906  1.00 12.43           N  
ANISOU  630  N   PRO A 177     2433    868   1423     -9   -269     69       N  
ATOM    631  CA  PRO A 177      98.439  63.407 -22.089  1.00 13.67           C  
ANISOU  631  CA  PRO A 177     2745    931   1520   -125   -127    225       C  
ATOM    632  C   PRO A 177      97.019  63.222 -21.616  1.00 13.16           C  
ANISOU  632  C   PRO A 177     2744    867   1389   -358    -59    114       C  
ATOM    633  O   PRO A 177      96.343  62.308 -22.097  1.00 14.17           O  
ANISOU  633  O   PRO A 177     2884   1109   1391   -625     52     16       O  
ATOM    634  CB  PRO A 177      99.417  62.542 -21.282  1.00 13.77           C  
ANISOU  634  CB  PRO A 177     2574    973   1684     75   -236    102       C  
ATOM    635  CG  PRO A 177     100.647  63.374 -21.151  1.00 14.96           C  
ANISOU  635  CG  PRO A 177     2880    902   1901    -29   -295    -11       C  
ATOM    636  CD  PRO A 177     100.190  64.789 -21.106  1.00 13.00           C  
ANISOU  636  CD  PRO A 177     2449    811   1681     72   -369      7       C  
ATOM    637  N   HIS A 178      96.538  64.063 -20.701  1.00 13.30           N  
ANISOU  637  N   HIS A 178     2624    946   1484   -135   -107    208       N  
ATOM    638  CA  HIS A 178      95.138  64.005 -20.313  1.00 13.13           C  
ANISOU  638  CA  HIS A 178     2727    815   1448    -31    -34    254       C  
ATOM    639  C   HIS A 178      94.248  64.662 -21.357  1.00 13.32           C  
ANISOU  639  C   HIS A 178     2768    796   1497     62    -70    170       C  
ATOM    640  O   HIS A 178      93.277  64.060 -21.827  1.00 14.22           O  
ANISOU  640  O   HIS A 178     2634   1111   1657    -62   -329    257       O  
ATOM    641  CB  HIS A 178      94.920  64.703 -18.976  1.00 14.70           C  
ANISOU  641  CB  HIS A 178     2762   1297   1525     84     43    220       C  
ATOM    642  CG  HIS A 178      93.480  64.961 -18.694  1.00 15.16           C  
ANISOU  642  CG  HIS A 178     2869   1207   1684    189    350    202       C  
ATOM    643  ND1 HIS A 178      92.570  63.942 -18.510  1.00 17.09           N  
ANISOU  643  ND1 HIS A 178     3112   1519   1864    280    458    255       N  
ATOM    644  CD2 HIS A 178      92.778  66.115 -18.617  1.00 16.63           C  
ANISOU  644  CD2 HIS A 178     2962   1454   1903    344    553    217       C  
ATOM    645  CE1 HIS A 178      91.372  64.459 -18.303  1.00 18.28           C  
ANISOU  645  CE1 HIS A 178     3122   1694   2129    282    556    238       C  
ATOM    646  NE2 HIS A 178      91.471  65.776 -18.368  1.00 18.84           N  
ANISOU  646  NE2 HIS A 178     3277   1718   2163    -27    618    251       N  
ATOM    647  N   HIS A 179      94.539  65.915 -21.701  1.00 13.30           N  
ANISOU  647  N   HIS A 179     2690    902   1463    257     17    197       N  
ATOM    648  CA  HIS A 179      93.594  66.645 -22.529  1.00 12.22           C  
ANISOU  648  CA  HIS A 179     2494    708   1441    138     35    243       C  
ATOM    649  C   HIS A 179      93.547  66.118 -23.952  1.00 12.60           C  
ANISOU  649  C   HIS A 179     2517    843   1427    134     31    121       C  
ATOM    650  O   HIS A 179      92.495  66.196 -24.593  1.00 13.18           O  
ANISOU  650  O   HIS A 179     2450   1042   1515    451   -168    115       O  
ATOM    651  CB  HIS A 179      93.910  68.134 -22.501  1.00 11.92           C  
ANISOU  651  CB  HIS A 179     2460    663   1406    112    196    162       C  
ATOM    652  CG  HIS A 179      93.379  68.815 -21.284  1.00 12.90           C  
ANISOU  652  CG  HIS A 179     2462    995   1444    212    253    -89       C  
ATOM    653  ND1 HIS A 179      94.192  69.394 -20.334  1.00 13.32           N  
ANISOU  653  ND1 HIS A 179     2332   1255   1476    336     57   -127       N  
ATOM    654  CD2 HIS A 179      92.110  68.955 -20.834  1.00 13.57           C  
ANISOU  654  CD2 HIS A 179     2340   1167   1650    232     94     -4       C  
ATOM    655  CE1 HIS A 179      93.442  69.896 -19.367  1.00 13.85           C  
ANISOU  655  CE1 HIS A 179     2285   1460   1519    174    160     54       C  
ATOM    656  NE2 HIS A 179      92.175  69.643 -19.646  1.00 14.76           N  
ANISOU  656  NE2 HIS A 179     2641   1357   1612     81     43     -9       N  
ATOM    657  N   GLU A 180      94.649  65.560 -24.462  1.00 11.51           N  
ANISOU  657  N   GLU A 180     2174    784   1416    168    139    101       N  
ATOM    658  CA  GLU A 180      94.555  65.007 -25.812  1.00 11.99           C  
ANISOU  658  CA  GLU A 180     2206    737   1614    104     82     29       C  
ATOM    659  C   GLU A 180      93.642  63.789 -25.874  1.00 12.04           C  
ANISOU  659  C   GLU A 180     2194    701   1682     58   -103     17       C  
ATOM    660  O   GLU A 180      93.247  63.392 -26.979  1.00 14.50           O  
ANISOU  660  O   GLU A 180     2749   1095   1667     21   -157     10       O  
ATOM    661  CB  GLU A 180      95.933  64.659 -26.388  1.00 12.87           C  
ANISOU  661  CB  GLU A 180     2258    815   1815     23    167    296       C  
ATOM    662  CG  GLU A 180      96.560  63.408 -25.786  1.00 14.74           C  
ANISOU  662  CG  GLU A 180     2650   1037   1913    207    240    309       C  
ATOM    663  CD  GLU A 180      97.802  62.938 -26.532  1.00 15.46           C  
ANISOU  663  CD  GLU A 180     2850   1145   1878     69    247    282       C  
ATOM    664  OE1 GLU A 180      98.282  63.644 -27.437  1.00 15.16           O  
ANISOU  664  OE1 GLU A 180     2794   1192   1773    -15    254     75       O  
ATOM    665  OE2 GLU A 180      98.297  61.838 -26.223  1.00 18.53           O1-
ANISOU  665  OE2 GLU A 180     3242   1678   2121    463    457    639       O1-
ATOM    666  N   ARG A 181      93.278  63.214 -24.722  1.00 12.14           N  
ANISOU  666  N   ARG A 181     1910    770   1935     22   -124    163       N  
ATOM    667  CA  ARG A 181      92.421  62.036 -24.635  1.00 13.14           C  
ANISOU  667  CA  ARG A 181     1964    924   2106    -77   -129     88       C  
ATOM    668  C   ARG A 181      91.050  62.312 -24.035  1.00 15.77           C  
ANISOU  668  C   ARG A 181     2249   1309   2434     20     66     76       C  
ATOM    669  O   ARG A 181      90.339  61.362 -23.699  1.00 18.17           O  
ANISOU  669  O   ARG A 181     2717   1470   2718   -410    250    -21       O  
ATOM    670  CB  ARG A 181      93.096  60.957 -23.789  1.00 13.68           C  
ANISOU  670  CB  ARG A 181     2197    935   2067   -108    -81     93       C  
ATOM    671  CG  ARG A 181      94.369  60.453 -24.389  1.00 13.11           C  
ANISOU  671  CG  ARG A 181     2177    816   1987     97     63    215       C  
ATOM    672  CD  ARG A 181      94.975  59.347 -23.567  1.00 12.16           C  
ANISOU  672  CD  ARG A 181     2133    751   1735    144    -82    124       C  
ATOM    673  NE  ARG A 181      94.165  58.134 -23.550  1.00 11.46           N  
ANISOU  673  NE  ARG A 181     2027    828   1499    -23    190    153       N  
ATOM    674  CZ  ARG A 181      93.593  57.619 -22.465  1.00 11.41           C  
ANISOU  674  CZ  ARG A 181     1940    936   1458   -297   -168    275       C  
ATOM    675  NH1 ARG A 181      93.723  58.221 -21.293  1.00 11.67           N1+
ANISOU  675  NH1 ARG A 181     1892   1194   1347    -70   -395    236       N1+
ATOM    676  NH2 ARG A 181      92.913  56.479 -22.550  1.00 11.30           N  
ANISOU  676  NH2 ARG A 181     1972    784   1539    -27   -164     99       N  
ATOM    677  N  ACYS A 182      90.653  63.566 -23.874  0.68 16.35           N  
ANISOU  677  N  ACYS A 182     2247   1400   2564    206     45   -120       N  
ATOM    678  N  BCYS A 182      90.662  63.582 -23.903  0.32 17.45           N  
ANISOU  678  N  BCYS A 182     2308   1621   2701    193     86    -76       N  
ATOM    679  CA ACYS A 182      89.404  63.820 -23.167  0.68 18.71           C  
ANISOU  679  CA ACYS A 182     2522   1570   3019    187    124   -270       C  
ATOM    680  CA BCYS A 182      89.426  63.934 -23.213  0.32 19.86           C  
ANISOU  680  CA BCYS A 182     2502   1938   3104    279    147   -228       C  
ATOM    681  C  ACYS A 182      88.186  63.939 -24.086  0.68 21.71           C  
ANISOU  681  C  ACYS A 182     2828   1830   3590    214      2   -155       C  
ATOM    682  C  BCYS A 182      88.182  63.758 -24.065  0.32 22.27           C  
ANISOU  682  C  BCYS A 182     2767   2128   3567    308    -65   -194       C  
ATOM    683  O  ACYS A 182      87.102  64.284 -23.604  0.68 22.63           O  
ANISOU  683  O  ACYS A 182     2852   1932   3814     -7    176     36       O  
ATOM    684  O  BCYS A 182      87.075  63.747 -23.515  0.32 22.55           O  
ANISOU  684  O  BCYS A 182     2724   2156   3688    301    -20   -229       O  
ATOM    685  CB ACYS A 182      89.532  65.024 -22.226  0.68 19.20           C  
ANISOU  685  CB ACYS A 182     2823   1608   2864    -34    105   -171       C  
ATOM    686  CB BCYS A 182      89.472  65.388 -22.756  0.32 20.05           C  
ANISOU  686  CB BCYS A 182     2557   2036   3024    307    335   -265       C  
ATOM    687  SG ACYS A 182      89.664  66.596 -23.054  0.68 19.45           S  
ANISOU  687  SG ACYS A 182     3007   1749   2633   -209     -1   -131       S  
ATOM    688  SG BCYS A 182      90.297  65.608 -21.202  0.32 20.39           S  
ANISOU  688  SG BCYS A 182     2589   2236   2923    299    416   -345       S  
ATOM    689  N   SER A 183      88.334  63.650 -25.383  1.00 24.37           N  
ANISOU  689  N   SER A 183     3023   2356   3882    337   -374     43       N  
ATOM    690  CA  SER A 183      87.194  63.544 -26.306  1.00 27.55           C  
ANISOU  690  CA  SER A 183     3390   2549   4530   -139   -668     87       C  
ATOM    691  C   SER A 183      86.365  64.827 -26.345  1.00 28.73           C  
ANISOU  691  C   SER A 183     3254   2891   4770   -260   -704    128       C  
ATOM    692  O   SER A 183      85.139  64.792 -26.476  1.00 30.87           O  
ANISOU  692  O   SER A 183     3458   3139   5132   -400   -719    215       O  
ATOM    693  CB  SER A 183      86.311  62.317 -26.037  1.00 30.33           C  
ANISOU  693  CB  SER A 183     4047   2587   4888   -233   -674     21       C  
ATOM    694  OG  SER A 183      87.075  61.124 -26.025  1.00 32.63           O  
ANISOU  694  OG  SER A 183     4480   2762   5158   -245   -591    -91       O  
ATOM    695  N   ASP A 184      87.038  65.970 -26.225  1.00 26.42           N  
ANISOU  695  N   ASP A 184     2865   2567   4606   -507   -547    164       N  
ATOM    696  CA  ASP A 184      86.391  67.270 -26.341  1.00 25.43           C  
ANISOU  696  CA  ASP A 184     2542   2642   4479   -315   -474    234       C  
ATOM    697  C   ASP A 184      86.468  67.833 -27.752  1.00 26.83           C  
ANISOU  697  C   ASP A 184     2818   2765   4611   -199   -656    167       C  
ATOM    698  O   ASP A 184      86.498  69.058 -27.932  1.00 24.87           O  
ANISOU  698  O   ASP A 184     2509   2364   4577   -395   -721    447       O  
ATOM    699  CB  ASP A 184      86.953  68.246 -25.308  1.00 23.09           C  
ANISOU  699  CB  ASP A 184     2102   2470   4202   -470   -291    296       C  
ATOM    700  CG  ASP A 184      88.438  68.490 -25.481  1.00 22.16           C  
ANISOU  700  CG  ASP A 184     2176   2279   3967   -349   -258    197       C  
ATOM    701  OD1 ASP A 184      89.021  68.017 -26.475  1.00 20.68           O  
ANISOU  701  OD1 ASP A 184     2297   1790   3768   -302   -368    283       O  
ATOM    702  OD2 ASP A 184      89.024  69.156 -24.606  1.00 23.30           O1-
ANISOU  702  OD2 ASP A 184     2417   2503   3932   -372    -61   -201       O1-
ATOM    703  N   SER A 185      86.507  66.956 -28.751  1.00 30.39           N  
ANISOU  703  N   SER A 185     3547   3284   4717    174   -689    -49       N  
ATOM    704  CA  SER A 185      86.573  67.362 -30.145  1.00 32.57           C  
ANISOU  704  CA  SER A 185     4005   3604   4765    278   -804     11       C  
ATOM    705  C   SER A 185      85.441  68.317 -30.490  1.00 32.99           C  
ANISOU  705  C   SER A 185     3925   3812   4798    -97   -863    103       C  
ATOM    706  O   SER A 185      84.305  68.151 -30.038  1.00 33.72           O  
ANISOU  706  O   SER A 185     3989   3891   4932   -627   -955    116       O  
ATOM    707  CB  SER A 185      86.449  66.114 -31.021  1.00 34.74           C  
ANISOU  707  CB  SER A 185     4507   3859   4835    167   -815    -62       C  
ATOM    708  OG  SER A 185      86.112  66.455 -32.353  1.00 36.04           O  
ANISOU  708  OG  SER A 185     4813   3978   4904    156   -680     49       O  
ATOM    709  N   ASP A 186      85.762  69.332 -31.286  1.00 32.07           N  
ANISOU  709  N   ASP A 186     3702   3821   4663   -196   -906    162       N  
ATOM    710  CA  ASP A 186      84.743  70.139 -31.938  1.00 32.61           C  
ANISOU  710  CA  ASP A 186     3923   3855   4613   -197   -676    161       C  
ATOM    711  C   ASP A 186      84.407  69.623 -33.328  1.00 33.66           C  
ANISOU  711  C   ASP A 186     4120   4167   4503   -264   -754    150       C  
ATOM    712  O   ASP A 186      83.713  70.312 -34.081  1.00 34.90           O  
ANISOU  712  O   ASP A 186     4347   4316   4596    -83   -881    263       O  
ATOM    713  CB  ASP A 186      85.163  71.611 -31.994  1.00 32.63           C  
ANISOU  713  CB  ASP A 186     4045   3718   4636   -130   -470    181       C  
ATOM    714  CG  ASP A 186      86.433  71.832 -32.795  1.00 31.98           C  
ANISOU  714  CG  ASP A 186     3980   3550   4622   -176   -466    110       C  
ATOM    715  OD1 ASP A 186      86.991  70.861 -33.346  1.00 31.13           O  
ANISOU  715  OD1 ASP A 186     3915   3317   4595   -288   -340    -84       O  
ATOM    716  OD2 ASP A 186      86.877  72.995 -32.875  1.00 31.94           O1-
ANISOU  716  OD2 ASP A 186     4055   3488   4594   -102   -435    221       O1-
ATOM    717  N   GLY A 187      84.891  68.433 -33.683  1.00 33.04           N  
ANISOU  717  N   GLY A 187     4079   4220   4254   -492   -761     12       N  
ATOM    718  CA  GLY A 187      84.674  67.869 -34.995  1.00 32.96           C  
ANISOU  718  CA  GLY A 187     4287   4261   3974   -570   -863    -96       C  
ATOM    719  C   GLY A 187      85.671  68.291 -36.053  1.00 32.13           C  
ANISOU  719  C   GLY A 187     4432   4145   3632   -533  -1049   -127       C  
ATOM    720  O   GLY A 187      85.615  67.771 -37.175  1.00 33.89           O  
ANISOU  720  O   GLY A 187     4777   4369   3732   -562  -1170   -222       O  
ATOM    721  N   LEU A 188      86.586  69.206 -35.738  1.00 28.47           N  
ANISOU  721  N   LEU A 188     3923   3693   3200   -431  -1246    -19       N  
ATOM    722  CA  LEU A 188      87.517  69.713 -36.737  1.00 26.15           C  
ANISOU  722  CA  LEU A 188     3826   3244   2868   -308  -1078    -19       C  
ATOM    723  C   LEU A 188      88.943  69.758 -36.202  1.00 20.66           C  
ANISOU  723  C   LEU A 188     3174   2360   2315   -345   -849   -128       C  
ATOM    724  O   LEU A 188      89.884  69.344 -36.884  1.00 21.15           O  
ANISOU  724  O   LEU A 188     3361   2581   2093   -352   -694   -199       O  
ATOM    725  CB  LEU A 188      87.082  71.103 -37.202  1.00 29.21           C  
ANISOU  725  CB  LEU A 188     4354   3647   3096   -337  -1038    174       C  
ATOM    726  CG  LEU A 188      87.867  71.729 -38.354  1.00 31.81           C  
ANISOU  726  CG  LEU A 188     4843   3907   3338   -460   -904    132       C  
ATOM    727  CD1 LEU A 188      88.014  70.753 -39.509  1.00 32.53           C  
ANISOU  727  CD1 LEU A 188     5075   3961   3324   -477   -762     48       C  
ATOM    728  CD2 LEU A 188      87.191  73.019 -38.820  1.00 32.84           C  
ANISOU  728  CD2 LEU A 188     5005   4017   3455   -391  -1007     89       C  
ATOM    729  N   ALA A 189      89.117  70.249 -34.991  1.00 16.89           N  
ANISOU  729  N   ALA A 189     2711   1685   2024    -65   -776     -8       N  
ATOM    730  CA  ALA A 189      90.462  70.344 -34.447  1.00 14.35           C  
ANISOU  730  CA  ALA A 189     2416   1169   1866    -42   -502    -99       C  
ATOM    731  C   ALA A 189      90.943  68.964 -34.021  1.00 13.39           C  
ANISOU  731  C   ALA A 189     2354   1018   1718   -144   -344    -51       C  
ATOM    732  O   ALA A 189      90.207  68.243 -33.330  1.00 14.56           O  
ANISOU  732  O   ALA A 189     2376   1372   1784   -267   -275    -62       O  
ATOM    733  CB  ALA A 189      90.476  71.271 -33.241  1.00 13.69           C  
ANISOU  733  CB  ALA A 189     2323   1117   1760    -58   -353   -190       C  
ATOM    734  N   PRO A 190      92.149  68.561 -34.405  1.00 12.43           N  
ANISOU  734  N   PRO A 190     2371    831   1520   -118   -235    107       N  
ATOM    735  CA  PRO A 190      92.719  67.335 -33.858  1.00 12.33           C  
ANISOU  735  CA  PRO A 190     2365    843   1476   -171   -305    181       C  
ATOM    736  C   PRO A 190      92.828  67.457 -32.353  1.00 11.59           C  
ANISOU  736  C   PRO A 190     2151    666   1585   -173   -186     68       C  
ATOM    737  O   PRO A 190      93.094  68.548 -31.827  1.00 11.62           O  
ANISOU  737  O   PRO A 190     2053    603   1760      5   -211    107       O  
ATOM    738  CB  PRO A 190      94.113  67.274 -34.498  1.00 14.00           C  
ANISOU  738  CB  PRO A 190     2519   1213   1587     63   -100     76       C  
ATOM    739  CG  PRO A 190      94.009  68.120 -35.730  1.00 14.41           C  
ANISOU  739  CG  PRO A 190     2578   1325   1572    -40     -6     79       C  
ATOM    740  CD  PRO A 190      93.071  69.231 -35.336  1.00 13.44           C  
ANISOU  740  CD  PRO A 190     2457   1057   1592    -68    -49     65       C  
ATOM    741  N   PRO A 191      92.621  66.363 -31.627  1.00 12.49           N  
ANISOU  741  N   PRO A 191     2302    837   1606   -569   -250     43       N  
ATOM    742  CA  PRO A 191      92.637  66.447 -30.160  1.00 12.46           C  
ANISOU  742  CA  PRO A 191     2206    915   1613   -511   -361    215       C  
ATOM    743  C   PRO A 191      93.977  66.847 -29.578  1.00 11.73           C  
ANISOU  743  C   PRO A 191     2088    732   1637   -200   -343    142       C  
ATOM    744  O   PRO A 191      94.016  67.275 -28.421  1.00 11.44           O  
ANISOU  744  O   PRO A 191     2101    671   1575   -178   -190    132       O  
ATOM    745  CB  PRO A 191      92.229  65.036 -29.725  1.00 14.76           C  
ANISOU  745  CB  PRO A 191     2828   1036   1744   -616   -261    339       C  
ATOM    746  CG  PRO A 191      92.561  64.168 -30.891  1.00 15.58           C  
ANISOU  746  CG  PRO A 191     3138   1037   1745   -298   -384    345       C  
ATOM    747  CD  PRO A 191      92.296  65.009 -32.107  1.00 13.83           C  
ANISOU  747  CD  PRO A 191     2622    989   1644   -637   -528     93       C  
ATOM    748  N   GLN A 192      95.067  66.741 -30.343  1.00 10.51           N  
ANISOU  748  N   GLN A 192     1647    673   1672    -41   -388    125       N  
ATOM    749  CA  GLN A 192      96.379  67.133 -29.843  1.00 10.36           C  
ANISOU  749  CA  GLN A 192     1810    524   1602    150   -221    117       C  
ATOM    750  C   GLN A 192      96.629  68.633 -29.906  1.00 10.41           C  
ANISOU  750  C   GLN A 192     1926    494   1534     33    -47    104       C  
ATOM    751  O   GLN A 192      97.569  69.102 -29.257  1.00 10.67           O  
ANISOU  751  O   GLN A 192     1974    525   1556    -37   -215     88       O  
ATOM    752  CB  GLN A 192      97.484  66.451 -30.650  1.00 11.47           C  
ANISOU  752  CB  GLN A 192     2135    717   1506    204    -15   -122       C  
ATOM    753  CG  GLN A 192      97.395  64.912 -30.676  1.00 11.57           C  
ANISOU  753  CG  GLN A 192     2192    632   1570     15    -88   -285       C  
ATOM    754  CD  GLN A 192      96.644  64.379 -31.885  1.00 12.75           C  
ANISOU  754  CD  GLN A 192     2280    909   1655    250   -131   -137       C  
ATOM    755  OE1 GLN A 192      95.664  64.962 -32.335  1.00 14.98           O  
ANISOU  755  OE1 GLN A 192     2540   1307   1846    610   -423   -346       O  
ATOM    756  NE2 GLN A 192      97.113  63.259 -32.419  1.00 12.80           N  
ANISOU  756  NE2 GLN A 192     2386    887   1591    -21    124    -85       N  
ATOM    757  N   HIS A 193      95.845  69.381 -30.684  1.00  9.93           N  
ANISOU  757  N   HIS A 193     1885    482   1406     -5    -78     82       N  
ATOM    758  CA  HIS A 193      96.134  70.794 -30.916  1.00  8.99           C  
ANISOU  758  CA  HIS A 193     1786    459   1171     35    -91     76       C  
ATOM    759  C   HIS A 193      95.738  71.668 -29.740  1.00  9.74           C  
ANISOU  759  C   HIS A 193     1652    821   1228   -181   -111    -43       C  
ATOM    760  O   HIS A 193      94.590  71.649 -29.289  1.00 11.53           O  
ANISOU  760  O   HIS A 193     1922   1052   1407   -241    -10    -63       O  
ATOM    761  CB  HIS A 193      95.417  71.296 -32.163  1.00  9.15           C  
ANISOU  761  CB  HIS A 193     1840    505   1133    115   -252     70       C  
ATOM    762  CG  HIS A 193      96.096  70.910 -33.435  1.00 10.01           C  
ANISOU  762  CG  HIS A 193     1873    662   1269    -51   -125   -175       C  
ATOM    763  ND1 HIS A 193      96.192  71.765 -34.511  1.00 10.39           N  
ANISOU  763  ND1 HIS A 193     1769    882   1297    -76   -102     -6       N  
ATOM    764  CD2 HIS A 193      96.701  69.758 -33.811  1.00 11.11           C  
ANISOU  764  CD2 HIS A 193     2083    810   1327    181    -26    -95       C  
ATOM    765  CE1 HIS A 193      96.840  71.163 -35.492  1.00  9.88           C  
ANISOU  765  CE1 HIS A 193     1664    974   1115    238    -38    -85       C  
ATOM    766  NE2 HIS A 193      97.156  69.941 -35.096  1.00 10.97           N  
ANISOU  766  NE2 HIS A 193     2006    986   1176     94    -65    144       N  
ATOM    767  N   LEU A 194      96.688  72.484 -29.290  1.00  8.49           N  
ANISOU  767  N   LEU A 194     1395    611   1219     47   -289   -265       N  
ATOM    768  CA  LEU A 194      96.425  73.418 -28.204  1.00  8.97           C  
ANISOU  768  CA  LEU A 194     1414    741   1253     71   -105   -172       C  
ATOM    769  C   LEU A 194      95.478  74.523 -28.641  1.00  8.72           C  
ANISOU  769  C   LEU A 194     1377    727   1209      6    -83     27       C  
ATOM    770  O   LEU A 194      94.557  74.887 -27.901  1.00  9.77           O  
ANISOU  770  O   LEU A 194     1548    756   1409    102    -14    129       O  
ATOM    771  CB  LEU A 194      97.739  74.022 -27.716  1.00  9.89           C  
ANISOU  771  CB  LEU A 194     1755    886   1117   -455   -187   -116       C  
ATOM    772  CG  LEU A 194      97.581  75.130 -26.670  1.00 10.25           C  
ANISOU  772  CG  LEU A 194     1795    867   1231   -461     89   -125       C  
ATOM    773  CD1 LEU A 194      97.077  74.534 -25.361  1.00 11.53           C  
ANISOU  773  CD1 LEU A 194     1741   1386   1254   -486    104     99       C  
ATOM    774  CD2 LEU A 194      98.877  75.882 -26.460  1.00 10.99           C  
ANISOU  774  CD2 LEU A 194     1848    972   1358   -271     46   -147       C  
ATOM    775  N   ILE A 195      95.715  75.110 -29.819  1.00  8.65           N  
ANISOU  775  N   ILE A 195     1424    747   1115     69   -117    199       N  
ATOM    776  CA  ILE A 195      94.962  76.277 -30.264  1.00  8.63           C  
ANISOU  776  CA  ILE A 195     1510    542   1227    121   -311    -49       C  
ATOM    777  C   ILE A 195      93.871  75.851 -31.228  1.00  8.61           C  
ANISOU  777  C   ILE A 195     1562    478   1232    211   -122     75       C  
ATOM    778  O   ILE A 195      94.146  75.220 -32.254  1.00 10.07           O  
ANISOU  778  O   ILE A 195     1615    903   1307    265      7   -206       O  
ATOM    779  CB  ILE A 195      95.869  77.317 -30.936  1.00  8.75           C  
ANISOU  779  CB  ILE A 195     1551    464   1309    107   -152     15       C  
ATOM    780  CG1 ILE A 195      97.004  77.738 -30.006  1.00  9.66           C  
ANISOU  780  CG1 ILE A 195     1451    674   1547   -100   -291     25       C  
ATOM    781  CG2 ILE A 195      95.047  78.533 -31.327  1.00  9.73           C  
ANISOU  781  CG2 ILE A 195     1618    550   1529    321     -4    114       C  
ATOM    782  CD1 ILE A 195      97.978  78.696 -30.686  1.00 11.15           C  
ANISOU  782  CD1 ILE A 195     1624    875   1739   -135   -187    233       C  
ATOM    783  N   ARG A 196      92.646  76.249 -30.928  1.00  9.47           N  
ANISOU  783  N   ARG A 196     1525    760   1313    -27   -142    -15       N  
ATOM    784  CA  ARG A 196      91.531  76.099 -31.840  1.00 10.03           C  
ANISOU  784  CA  ARG A 196     1570    912   1328     79   -330     59       C  
ATOM    785  C   ARG A 196      90.996  77.466 -32.215  1.00 10.23           C  
ANISOU  785  C   ARG A 196     1645    878   1363      7   -385    -68       C  
ATOM    786  O   ARG A 196      91.161  78.446 -31.486  1.00 11.03           O  
ANISOU  786  O   ARG A 196     1795    972   1425    282   -330   -191       O  
ATOM    787  CB  ARG A 196      90.389  75.320 -31.198  1.00 10.65           C  
ANISOU  787  CB  ARG A 196     1772    760   1517   -258   -234     79       C  
ATOM    788  CG  ARG A 196      90.773  73.928 -30.783  1.00 11.26           C  
ANISOU  788  CG  ARG A 196     1830    765   1685   -239   -241    275       C  
ATOM    789  CD  ARG A 196      89.583  73.178 -30.235  1.00 12.38           C  
ANISOU  789  CD  ARG A 196     1940    953   1811   -164   -214    302       C  
ATOM    790  NE  ARG A 196      89.995  71.875 -29.739  1.00 12.86           N  
ANISOU  790  NE  ARG A 196     1979   1013   1894   -366   -332    442       N  
ATOM    791  CZ  ARG A 196      89.197  71.040 -29.091  1.00 15.78           C  
ANISOU  791  CZ  ARG A 196     2200   1544   2253   -471   -319    415       C  
ATOM    792  NH1 ARG A 196      87.943  71.385 -28.836  1.00 17.77           N1+
ANISOU  792  NH1 ARG A 196     2194   2151   2406   -514   -200    328       N1+
ATOM    793  NH2 ARG A 196      89.666  69.867 -28.686  1.00 16.75           N  
ANISOU  793  NH2 ARG A 196     2448   1458   2460   -449   -435    463       N  
ATOM    794  N   VAL A 197      90.363  77.520 -33.379  1.00 10.46           N  
ANISOU  794  N   VAL A 197     1523   1111   1342    139   -600     18       N  
ATOM    795  CA  VAL A 197      89.550  78.663 -33.769  1.00 11.05           C  
ANISOU  795  CA  VAL A 197     1762    903   1532    306   -297    127       C  
ATOM    796  C   VAL A 197      88.096  78.297 -33.548  1.00 12.88           C  
ANISOU  796  C   VAL A 197     1876   1120   1897    -12   -237    -34       C  
ATOM    797  O   VAL A 197      87.648  77.219 -33.959  1.00 14.09           O  
ANISOU  797  O   VAL A 197     2019   1136   2199   -189   -235   -360       O  
ATOM    798  CB  VAL A 197      89.802  79.059 -35.231  1.00 11.69           C  
ANISOU  798  CB  VAL A 197     2009    995   1440    210   -132    269       C  
ATOM    799  CG1 VAL A 197      88.766  80.087 -35.708  1.00 12.45           C  
ANISOU  799  CG1 VAL A 197     2124   1062   1542    404   -144    311       C  
ATOM    800  CG2 VAL A 197      91.194  79.626 -35.368  1.00 12.51           C  
ANISOU  800  CG2 VAL A 197     1856   1333   1566     22    -48    -11       C  
ATOM    801  N   GLU A 198      87.364  79.191 -32.898  1.00 12.68           N  
ANISOU  801  N   GLU A 198     1587   1310   1922    144    -52    -74       N  
ATOM    802  CA  GLU A 198      85.947  79.025 -32.625  1.00 15.58           C  
ANISOU  802  CA  GLU A 198     1993   1733   2193     53    283    -27       C  
ATOM    803  C   GLU A 198      85.120  79.586 -33.768  1.00 15.08           C  
ANISOU  803  C   GLU A 198     1738   1720   2272   -127    208     38       C  
ATOM    804  O   GLU A 198      85.409  80.669 -34.276  1.00 16.58           O  
ANISOU  804  O   GLU A 198     2098   1663   2539   -158     86    280       O  
ATOM    805  CB  GLU A 198      85.606  79.869 -31.402  1.00 20.29           C  
ANISOU  805  CB  GLU A 198     2781   2433   2494     99    383   -167       C  
ATOM    806  CG  GLU A 198      85.387  79.114 -30.170  1.00 23.29           C  
ANISOU  806  CG  GLU A 198     3115   2933   2800    370    277   -186       C  
ATOM    807  CD  GLU A 198      84.741  79.970 -29.125  1.00 20.95           C  
ANISOU  807  CD  GLU A 198     2721   2534   2704    736    150   -198       C  
ATOM    808  OE1 GLU A 198      85.393  80.929 -28.674  1.00 18.42           O  
ANISOU  808  OE1 GLU A 198     2135   2377   2487    515     17   -183       O  
ATOM    809  OE2 GLU A 198      83.579  79.691 -28.774  1.00 22.67           O1-
ANISOU  809  OE2 GLU A 198     2972   2767   2874    703    -75   -175       O1-
ATOM    810  N   GLY A 199      84.064  78.867 -34.134  1.00 16.42           N  
ANISOU  810  N   GLY A 199     1872   2032   2336     57    -85     -5       N  
ATOM    811  CA  GLY A 199      83.029  79.436 -34.984  1.00 17.55           C  
ANISOU  811  CA  GLY A 199     2010   2343   2316    133     47    283       C  
ATOM    812  C   GLY A 199      83.492  79.852 -36.361  1.00 19.47           C  
ANISOU  812  C   GLY A 199     2371   2614   2411    304   -101    415       C  
ATOM    813  O   GLY A 199      83.035  80.874 -36.887  1.00 22.00           O  
ANISOU  813  O   GLY A 199     2686   3070   2603    634    -70    588       O  
ATOM    814  N   ASN A 200      84.394  79.082 -36.961  1.00 17.67           N  
ANISOU  814  N   ASN A 200     2125   2384   2205   -124   -220    -54       N  
ATOM    815  CA  ASN A 200      84.819  79.333 -38.335  1.00 16.33           C  
ANISOU  815  CA  ASN A 200     2004   2080   2120   -255   -401    -64       C  
ATOM    816  C   ASN A 200      84.952  77.985 -39.033  1.00 17.36           C  
ANISOU  816  C   ASN A 200     2054   2275   2267   -277   -331    -92       C  
ATOM    817  O   ASN A 200      85.933  77.267 -38.832  1.00 17.16           O  
ANISOU  817  O   ASN A 200     2048   2256   2216   -235   -326    -15       O  
ATOM    818  CB  ASN A 200      86.119  80.116 -38.389  1.00 16.14           C  
ANISOU  818  CB  ASN A 200     2291   1814   2029   -118   -416      2       C  
ATOM    819  CG  ASN A 200      86.421  80.619 -39.781  1.00 16.06           C  
ANISOU  819  CG  ASN A 200     2443   1720   1940    -59   -618    -87       C  
ATOM    820  OD1 ASN A 200      86.036  79.995 -40.779  1.00 18.28           O  
ANISOU  820  OD1 ASN A 200     2938   1861   2146   -265   -683   -307       O  
ATOM    821  ND2 ASN A 200      87.092  81.755 -39.863  1.00 16.06           N  
ANISOU  821  ND2 ASN A 200     2195   1787   2118    111   -474    -80       N  
ATOM    822  N   LEU A 201      83.964  77.655 -39.864  1.00 18.46           N  
ANISOU  822  N   LEU A 201     2120   2497   2395   -255   -430   -499       N  
ATOM    823  CA  LEU A 201      83.966  76.383 -40.572  1.00 20.76           C  
ANISOU  823  CA  LEU A 201     2251   2876   2759   -343   -456   -643       C  
ATOM    824  C   LEU A 201      85.081  76.276 -41.599  1.00 19.91           C  
ANISOU  824  C   LEU A 201     2365   2419   2781   -194   -342   -532       C  
ATOM    825  O   LEU A 201      85.339  75.172 -42.090  1.00 20.90           O  
ANISOU  825  O   LEU A 201     2712   2327   2902   -277   -170   -538       O  
ATOM    826  CB  LEU A 201      82.620  76.173 -41.261  1.00 24.74           C  
ANISOU  826  CB  LEU A 201     2416   3880   3104   -535   -475   -737       C  
ATOM    827  CG  LEU A 201      81.423  76.417 -40.352  1.00 29.68           C  
ANISOU  827  CG  LEU A 201     3000   4761   3516   -517   -410   -559       C  
ATOM    828  CD1 LEU A 201      80.107  76.426 -41.152  1.00 30.88           C  
ANISOU  828  CD1 LEU A 201     2960   5014   3758   -619   -473   -655       C  
ATOM    829  CD2 LEU A 201      81.420  75.381 -39.212  1.00 31.70           C  
ANISOU  829  CD2 LEU A 201     3339   5058   3646   -480   -350   -384       C  
ATOM    830  N   ARG A 202      85.725  77.385 -41.953  1.00 16.94           N  
ANISOU  830  N   ARG A 202     1851   1976   2612     10   -526   -257       N  
ATOM    831  CA  ARG A 202      86.828  77.372 -42.900  1.00 16.65           C  
ANISOU  831  CA  ARG A 202     2005   1928   2392     66   -489    -74       C  
ATOM    832  C   ARG A 202      88.183  77.249 -42.219  1.00 15.16           C  
ANISOU  832  C   ARG A 202     1934   1808   2019    -49   -313   -124       C  
ATOM    833  O   ARG A 202      89.215  77.301 -42.898  1.00 15.98           O  
ANISOU  833  O   ARG A 202     2091   1880   2102     86   -328    -91       O  
ATOM    834  CB  ARG A 202      86.770  78.596 -43.810  1.00 19.96           C  
ANISOU  834  CB  ARG A 202     2400   2325   2858     95   -832    162       C  
ATOM    835  CG  ARG A 202      85.551  78.583 -44.720  1.00 24.01           C  
ANISOU  835  CG  ARG A 202     3079   2726   3319    191  -1114    173       C  
ATOM    836  CD  ARG A 202      85.686  79.584 -45.850  1.00 28.31           C  
ANISOU  836  CD  ARG A 202     3733   3276   3746     93  -1187    105       C  
ATOM    837  NE  ARG A 202      85.659  80.954 -45.353  1.00 32.35           N  
ANISOU  837  NE  ARG A 202     4238   3865   4189    138  -1244    197       N  
ATOM    838  CZ  ARG A 202      85.941  82.022 -46.092  1.00 35.35           C  
ANISOU  838  CZ  ARG A 202     4720   4290   4420     65  -1246    159       C  
ATOM    839  NH1 ARG A 202      86.282  81.879 -47.367  1.00 36.17           N1+
ANISOU  839  NH1 ARG A 202     4867   4507   4369     12  -1477    202       N1+
ATOM    840  NH2 ARG A 202      85.889  83.232 -45.552  1.00 36.18           N  
ANISOU  840  NH2 ARG A 202     4886   4289   4571    166  -1126    -11       N  
ATOM    841  N   ALA A 203      88.204  77.076 -40.898  1.00 14.48           N  
ANISOU  841  N   ALA A 203     2098   1488   1917    -39   -373      5       N  
ATOM    842  CA  ALA A 203      89.459  76.819 -40.220  1.00 14.32           C  
ANISOU  842  CA  ALA A 203     2077   1474   1890    108   -171   -127       C  
ATOM    843  C   ALA A 203      90.042  75.498 -40.695  1.00 14.15           C  
ANISOU  843  C   ALA A 203     2071   1219   2088   -124   -214     -5       C  
ATOM    844  O   ALA A 203      89.325  74.508 -40.881  1.00 15.70           O  
ANISOU  844  O   ALA A 203     2041   1435   2489   -392   -235    -91       O  
ATOM    845  CB  ALA A 203      89.236  76.755 -38.710  1.00 14.98           C  
ANISOU  845  CB  ALA A 203     2097   1840   1755    100    -35      8       C  
ATOM    846  N   GLU A 204      91.350  75.494 -40.905  1.00 12.19           N  
ANISOU  846  N   GLU A 204     1923    915   1793     72   -257     50       N  
ATOM    847  CA AGLU A 204      92.077  74.282 -41.235  0.63 11.50           C  
ANISOU  847  CA AGLU A 204     1826    864   1679    -56   -287    103       C  
ATOM    848  CA BGLU A 204      92.101  74.300 -41.260  0.37 12.24           C  
ANISOU  848  CA BGLU A 204     1927   1033   1689     52   -230     66       C  
ATOM    849  C   GLU A 204      93.173  74.084 -40.204  1.00 11.02           C  
ANISOU  849  C   GLU A 204     1767    852   1569    -48   -314    -50       C  
ATOM    850  O   GLU A 204      93.799  75.046 -39.749  1.00 11.94           O  
ANISOU  850  O   GLU A 204     2004    889   1643   -195   -390     67       O  
ATOM    851  CB AGLU A 204      92.676  74.347 -42.638  0.63 12.37           C  
ANISOU  851  CB AGLU A 204     1982   1065   1654    -81   -420    -20       C  
ATOM    852  CB BGLU A 204      92.780  74.473 -42.625  0.37 14.08           C  
ANISOU  852  CB BGLU A 204     2212   1436   1702    164   -180     36       C  
ATOM    853  CG AGLU A 204      91.627  74.527 -43.725  0.63 12.91           C  
ANISOU  853  CG AGLU A 204     2204   1169   1534    -84   -568    -50       C  
ATOM    854  CG BGLU A 204      93.722  73.342 -43.011  0.37 15.62           C  
ANISOU  854  CG BGLU A 204     2603   1652   1679    217   -119     47       C  
ATOM    855  CD AGLU A 204      92.229  74.687 -45.102  0.63 15.84           C  
ANISOU  855  CD AGLU A 204     2661   1576   1782   -297   -625     55       C  
ATOM    856  CD BGLU A 204      94.724  73.743 -44.084  0.37 16.50           C  
ANISOU  856  CD BGLU A 204     2839   1814   1616    345   -117   -114       C  
ATOM    857  OE1AGLU A 204      93.463  74.561 -45.227  0.63 17.49           O  
ANISOU  857  OE1AGLU A 204     2938   1835   1874   -265   -592    102       O  
ATOM    858  OE1BGLU A 204      94.353  74.503 -44.999  0.37 17.63           O  
ANISOU  858  OE1BGLU A 204     3134   1906   1658    250   -120   -117       O  
ATOM    859  OE2AGLU A 204      91.469  74.943 -46.057  0.63 18.02           O1-
ANISOU  859  OE2AGLU A 204     3100   1814   1933   -262   -745    -19       O1-
ATOM    860  OE2BGLU A 204      95.888  73.305 -44.008  0.37 15.60           O1-
ANISOU  860  OE2BGLU A 204     2681   1764   1483    421    -56   -142       O1-
ATOM    861  N   TYR A 205      93.386  72.828 -39.830  1.00 11.56           N  
ANISOU  861  N   TYR A 205     2018    942   1432    280   -129     44       N  
ATOM    862  CA  TYR A 205      94.366  72.456 -38.827  1.00 10.94           C  
ANISOU  862  CA  TYR A 205     1967    688   1501    196    -94    -53       C  
ATOM    863  C   TYR A 205      95.483  71.691 -39.506  1.00 12.41           C  
ANISOU  863  C   TYR A 205     2014    999   1703    358    -39   -192       C  
ATOM    864  O   TYR A 205      95.225  70.729 -40.234  1.00 15.51           O  
ANISOU  864  O   TYR A 205     2423   1341   2129    269     20   -705       O  
ATOM    865  CB  TYR A 205      93.717  71.605 -37.739  1.00 10.80           C  
ANISOU  865  CB  TYR A 205     1780    772   1550    -24    -53    -49       C  
ATOM    866  CG  TYR A 205      92.776  72.410 -36.901  1.00 10.44           C  
ANISOU  866  CG  TYR A 205     1811    701   1454     35   -112     31       C  
ATOM    867  CD1 TYR A 205      91.469  72.629 -37.309  1.00 10.77           C  
ANISOU  867  CD1 TYR A 205     1652    928   1512    112    -89      9       C  
ATOM    868  CD2 TYR A 205      93.208  72.994 -35.719  1.00 10.78           C  
ANISOU  868  CD2 TYR A 205     1971    561   1564     40   -267     -2       C  
ATOM    869  CE1 TYR A 205      90.603  73.405 -36.551  1.00 10.04           C  
ANISOU  869  CE1 TYR A 205     1698    557   1560     13   -110   -103       C  
ATOM    870  CE2 TYR A 205      92.362  73.756 -34.954  1.00 10.62           C  
ANISOU  870  CE2 TYR A 205     1721    627   1687    128   -141   -119       C  
ATOM    871  CZ  TYR A 205      91.060  73.963 -35.372  1.00 10.98           C  
ANISOU  871  CZ  TYR A 205     1812    717   1644     54   -163   -264       C  
ATOM    872  OH  TYR A 205      90.231  74.731 -34.587  1.00 11.86           O  
ANISOU  872  OH  TYR A 205     2031    851   1625    173    -79   -286       O  
ATOM    873  N   LEU A 206      96.713  72.130 -39.284  1.00 12.28           N  
ANISOU  873  N   LEU A 206     1949   1089   1627    224     57   -185       N  
ATOM    874  CA  LEU A 206      97.878  71.548 -39.929  1.00 12.29           C  
ANISOU  874  CA  LEU A 206     2010   1068   1590    118     11   -168       C  
ATOM    875  C   LEU A 206      98.744  70.857 -38.888  1.00 12.11           C  
ANISOU  875  C   LEU A 206     2165    870   1568    117     15   -130       C  
ATOM    876  O   LEU A 206      99.076  71.458 -37.859  1.00 11.95           O  
ANISOU  876  O   LEU A 206     2148    959   1432     36     63   -163       O  
ATOM    877  CB  LEU A 206      98.703  72.640 -40.617  1.00 13.00           C  
ANISOU  877  CB  LEU A 206     2082   1174   1683     -2    239    -95       C  
ATOM    878  CG  LEU A 206      99.993  72.176 -41.301  1.00 15.40           C  
ANISOU  878  CG  LEU A 206     2628   1398   1826    155    515   -275       C  
ATOM    879  CD1 LEU A 206      99.671  71.259 -42.461  1.00 16.56           C  
ANISOU  879  CD1 LEU A 206     2817   1602   1871    232    564   -640       C  
ATOM    880  CD2 LEU A 206     100.827  73.369 -41.777  1.00 15.65           C  
ANISOU  880  CD2 LEU A 206     2661   1496   1790     97    722    242       C  
ATOM    881  N   ASP A 207      99.105  69.597 -39.169  1.00 14.27           N  
ANISOU  881  N   ASP A 207     2532   1033   1856    409    280   -150       N  
ATOM    882  CA  ASP A 207     100.226  68.912 -38.535  1.00 15.42           C  
ANISOU  882  CA  ASP A 207     2616   1218   2024     98    435   -130       C  
ATOM    883  C   ASP A 207     101.354  69.001 -39.555  1.00 15.52           C  
ANISOU  883  C   ASP A 207     2609   1295   1995    304    468    -17       C  
ATOM    884  O   ASP A 207     101.296  68.352 -40.605  1.00 16.50           O  
ANISOU  884  O   ASP A 207     2800   1339   2130    309    464   -188       O  
ATOM    885  CB  ASP A 207      99.911  67.431 -38.310  1.00 17.39           C  
ANISOU  885  CB  ASP A 207     3085   1199   2323     12    811     70       C  
ATOM    886  CG  ASP A 207      98.874  67.177 -37.237  1.00 21.93           C  
ANISOU  886  CG  ASP A 207     3985   1527   2819   -269    888    -52       C  
ATOM    887  OD1 ASP A 207      98.695  68.003 -36.337  1.00 21.85           O  
ANISOU  887  OD1 ASP A 207     4058   1329   2916    -99    885    -90       O  
ATOM    888  OD2 ASP A 207      98.253  66.091 -37.282  1.00 25.73           O1-
ANISOU  888  OD2 ASP A 207     4533   2120   3124   -526    825    -90       O1-
ATOM    889  N   ASP A 208     102.363  69.814 -39.273  1.00 15.33           N  
ANISOU  889  N   ASP A 208     2428   1398   1999    396    535    313       N  
ATOM    890  CA  ASP A 208     103.415  70.020 -40.261  1.00 16.82           C  
ANISOU  890  CA  ASP A 208     2616   1612   2161    497    583    -78       C  
ATOM    891  C   ASP A 208     104.157  68.713 -40.488  1.00 18.23           C  
ANISOU  891  C   ASP A 208     2886   1769   2272    532    459   -331       C  
ATOM    892  O   ASP A 208     104.616  68.079 -39.537  1.00 19.14           O  
ANISOU  892  O   ASP A 208     2982   1983   2308    786    395   -449       O  
ATOM    893  CB  ASP A 208     104.384  71.099 -39.790  1.00 18.20           C  
ANISOU  893  CB  ASP A 208     2816   1786   2315    371    687     75       C  
ATOM    894  CG  ASP A 208     105.342  71.535 -40.883  1.00 20.39           C  
ANISOU  894  CG  ASP A 208     3127   2109   2510    441    830     51       C  
ATOM    895  OD1 ASP A 208     106.282  70.778 -41.199  1.00 22.29           O  
ANISOU  895  OD1 ASP A 208     3445   2284   2740    507    889   -103       O  
ATOM    896  OD2 ASP A 208     105.155  72.643 -41.425  1.00 22.27           O1-
ANISOU  896  OD2 ASP A 208     3472   2505   2485    489    872    140       O1-
ATOM    897  N   ARG A 209     104.266  68.299 -41.752  1.00 20.08           N  
ANISOU  897  N   ARG A 209     3113   2103   2415    719    549   -591       N  
ATOM    898  CA  ARG A 209     104.845  66.990 -42.028  1.00 22.29           C  
ANISOU  898  CA  ARG A 209     3441   2391   2636    742    415   -901       C  
ATOM    899  C   ARG A 209     106.338  66.940 -41.732  1.00 24.08           C  
ANISOU  899  C   ARG A 209     3508   2733   2909    901    645   -888       C  
ATOM    900  O   ARG A 209     106.886  65.847 -41.562  1.00 25.36           O  
ANISOU  900  O   ARG A 209     3742   2817   3076   1020    681   -886       O  
ATOM    901  CB  ARG A 209     104.562  66.566 -43.472  1.00 23.35           C  
ANISOU  901  CB  ARG A 209     3852   2421   2599    707    287  -1071       C  
ATOM    902  N   ASN A 210     107.000  68.093 -41.642  1.00 25.06           N  
ANISOU  902  N   ASN A 210     3421   3101   2999    741    865   -735       N  
ATOM    903  CA  ASN A 210     108.435  68.152 -41.391  1.00 27.30           C  
ANISOU  903  CA  ASN A 210     3651   3414   3307    748    765   -595       C  
ATOM    904  C   ASN A 210     108.776  68.516 -39.952  1.00 26.00           C  
ANISOU  904  C   ASN A 210     3192   3216   3470    779    508   -565       C  
ATOM    905  O   ASN A 210     109.644  67.880 -39.345  1.00 26.76           O  
ANISOU  905  O   ASN A 210     3092   3374   3701    971    329   -609       O  
ATOM    906  CB  ASN A 210     109.093  69.137 -42.361  1.00 30.79           C  
ANISOU  906  CB  ASN A 210     4269   3968   3461    707    870   -489       C  
ATOM    907  CG  ASN A 210     108.948  68.706 -43.799  1.00 34.41           C  
ANISOU  907  CG  ASN A 210     4951   4469   3654    555    847   -325       C  
ATOM    908  OD1 ASN A 210     109.112  67.530 -44.121  1.00 36.02           O  
ANISOU  908  OD1 ASN A 210     5255   4682   3750    451    949   -367       O  
ATOM    909  ND2 ASN A 210     108.624  69.650 -44.674  1.00 35.94           N  
ANISOU  909  ND2 ASN A 210     5182   4758   3716    546    743   -140       N  
ATOM    910  N   THR A 211     108.112  69.525 -39.387  1.00 22.61           N  
ANISOU  910  N   THR A 211     2628   2656   3306    673    672   -581       N  
ATOM    911  CA  THR A 211     108.424  69.964 -38.032  1.00 21.35           C  
ANISOU  911  CA  THR A 211     2442   2408   3263    618    298   -489       C  
ATOM    912  C   THR A 211     107.518  69.349 -36.983  1.00 19.64           C  
ANISOU  912  C   THR A 211     2295   2123   3047    698    149   -491       C  
ATOM    913  O   THR A 211     107.830  69.437 -35.791  1.00 20.57           O  
ANISOU  913  O   THR A 211     2279   2382   3155    778     50   -463       O  
ATOM    914  CB  THR A 211     108.280  71.481 -37.911  1.00 21.45           C  
ANISOU  914  CB  THR A 211     2376   2391   3383    414    368   -311       C  
ATOM    915  OG1 THR A 211     106.891  71.828 -37.982  1.00 20.47           O  
ANISOU  915  OG1 THR A 211     2135   2294   3347    271    247   -262       O  
ATOM    916  CG2 THR A 211     109.033  72.170 -39.031  1.00 22.34           C  
ANISOU  916  CG2 THR A 211     2463   2606   3419     94    577   -253       C  
ATOM    917  N   PHE A 212     106.396  68.760 -37.393  1.00 17.92           N  
ANISOU  917  N   PHE A 212     2103   1862   2844    628     36   -439       N  
ATOM    918  CA  PHE A 212     105.390  68.184 -36.508  1.00 17.30           C  
ANISOU  918  CA  PHE A 212     2275   1582   2716   1047    109   -336       C  
ATOM    919  C   PHE A 212     104.671  69.235 -35.683  1.00 15.27           C  
ANISOU  919  C   PHE A 212     2230   1273   2297    760     13   -313       C  
ATOM    920  O   PHE A 212     103.872  68.892 -34.803  1.00 15.77           O  
ANISOU  920  O   PHE A 212     2535   1416   2042    622     90   -186       O  
ATOM    921  CB  PHE A 212     105.944  67.057 -35.625  1.00 19.78           C  
ANISOU  921  CB  PHE A 212     2712   1706   3099   1164     97   -377       C  
ATOM    922  CG  PHE A 212     106.720  66.035 -36.388  1.00 23.71           C  
ANISOU  922  CG  PHE A 212     3312   2146   3552   1390    199   -498       C  
ATOM    923  CD1 PHE A 212     106.078  65.184 -37.269  1.00 25.68           C  
ANISOU  923  CD1 PHE A 212     3671   2395   3693   1429    280   -568       C  
ATOM    924  CD2 PHE A 212     108.090  65.943 -36.248  1.00 26.27           C  
ANISOU  924  CD2 PHE A 212     3726   2421   3836   1395    252   -606       C  
ATOM    925  CE1 PHE A 212     106.788  64.243 -37.989  1.00 27.38           C  
ANISOU  925  CE1 PHE A 212     3954   2625   3826   1586    326   -642       C  
ATOM    926  CE2 PHE A 212     108.811  65.000 -36.958  1.00 27.99           C  
ANISOU  926  CE2 PHE A 212     3984   2660   3993   1476    263   -748       C  
ATOM    927  CZ  PHE A 212     108.158  64.153 -37.835  1.00 28.42           C  
ANISOU  927  CZ  PHE A 212     4056   2797   3947   1486    309   -759       C  
ATOM    928  N   ARG A 213     104.916  70.510 -35.951  1.00 13.94           N  
ANISOU  928  N   ARG A 213     1923   1192   2182    490   -271   -496       N  
ATOM    929  CA  ARG A 213     104.223  71.545 -35.208  1.00 12.63           C  
ANISOU  929  CA  ARG A 213     1661    962   2176    265    -71   -502       C  
ATOM    930  C   ARG A 213     102.790  71.664 -35.680  1.00 11.93           C  
ANISOU  930  C   ARG A 213     1655    960   1918    321    -62   -122       C  
ATOM    931  O   ARG A 213     102.454  71.327 -36.817  1.00 13.45           O  
ANISOU  931  O   ARG A 213     1885   1271   1956    390     67   -164       O  
ATOM    932  CB  ARG A 213     104.925  72.878 -35.375  1.00 14.12           C  
ANISOU  932  CB  ARG A 213     1638   1267   2460     46   -104   -529       C  
ATOM    933  CG  ARG A 213     106.242  72.877 -34.664  1.00 15.96           C  
ANISOU  933  CG  ARG A 213     1633   1772   2660     63   -144   -467       C  
ATOM    934  CD  ARG A 213     106.816  74.235 -34.660  1.00 16.76           C  
ANISOU  934  CD  ARG A 213     1849   1989   2530    -72   -316   -467       C  
ATOM    935  NE  ARG A 213     108.200  74.221 -34.236  1.00 16.49           N  
ANISOU  935  NE  ARG A 213     1838   2007   2419    139   -226   -264       N  
ATOM    936  CZ  ARG A 213     108.589  74.352 -32.973  1.00 14.70           C  
ANISOU  936  CZ  ARG A 213     1701   1610   2274    239    -19   -115       C  
ATOM    937  NH1 ARG A 213     107.686  74.495 -32.008  1.00 13.59           N1+
ANISOU  937  NH1 ARG A 213     1613   1173   2376   -101    122     26       N1+
ATOM    938  NH2 ARG A 213     109.880  74.361 -32.683  1.00 16.47           N  
ANISOU  938  NH2 ARG A 213     1814   2017   2425    304    -58    -96       N  
ATOM    939  N   HIS A 214     101.943  72.138 -34.778  1.00 10.64           N  
ANISOU  939  N   HIS A 214     1494    839   1709    214     -3    169       N  
ATOM    940  CA  HIS A 214     100.526  72.309 -35.033  1.00 10.20           C  
ANISOU  940  CA  HIS A 214     1594    743   1537     82     72    286       C  
ATOM    941  C   HIS A 214     100.236  73.764 -35.321  1.00  9.66           C  
ANISOU  941  C   HIS A 214     1665    631   1373     93   -160    245       C  
ATOM    942  O   HIS A 214     100.843  74.664 -34.738  1.00 10.49           O  
ANISOU  942  O   HIS A 214     1858    701   1425      2   -165    -94       O  
ATOM    943  CB  HIS A 214      99.732  71.941 -33.793  1.00  9.78           C  
ANISOU  943  CB  HIS A 214     1695    571   1450   -107     82    360       C  
ATOM    944  CG  HIS A 214     100.024  70.570 -33.287  1.00 10.08           C  
ANISOU  944  CG  HIS A 214     1746    511   1574    122    -44    256       C  
ATOM    945  ND1 HIS A 214      99.710  70.175 -32.006  1.00 11.43           N  
ANISOU  945  ND1 HIS A 214     1994    760   1589    -19   -334    446       N  
ATOM    946  CD2 HIS A 214     100.596  69.500 -33.888  1.00 11.92           C  
ANISOU  946  CD2 HIS A 214     2058    752   1721     66     16    197       C  
ATOM    947  CE1 HIS A 214     100.083  68.920 -31.838  1.00 12.00           C  
ANISOU  947  CE1 HIS A 214     2143    705   1712    415     38    159       C  
ATOM    948  NE2 HIS A 214     100.615  68.486 -32.966  1.00 13.03           N  
ANISOU  948  NE2 HIS A 214     2222   1033   1696    278      7    168       N  
ATOM    949  N   SER A 215      99.260  73.990 -36.189  1.00  9.08           N  
ANISOU  949  N   SER A 215     1590    545   1316    292   -110    147       N  
ATOM    950  CA  SER A 215      98.785  75.343 -36.385  1.00  8.78           C  
ANISOU  950  CA  SER A 215     1523    462   1351    219    -61    147       C  
ATOM    951  C   SER A 215      97.357  75.279 -36.883  1.00  9.11           C  
ANISOU  951  C   SER A 215     1668    533   1261    178    -95     -4       C  
ATOM    952  O   SER A 215      96.875  74.234 -37.341  1.00  9.87           O  
ANISOU  952  O   SER A 215     1819    676   1255    -13   -184    -42       O  
ATOM    953  CB  SER A 215      99.675  76.113 -37.364  1.00 10.42           C  
ANISOU  953  CB  SER A 215     1989    662   1306    -51    216     36       C  
ATOM    954  OG  SER A 215      99.736  75.458 -38.615  1.00 10.61           O  
ANISOU  954  OG  SER A 215     1979    859   1192     59     46     25       O  
ATOM    955  N   VAL A 216      96.679  76.414 -36.767  1.00  9.16           N  
ANISOU  955  N   VAL A 216     1663    671   1147    213    125    102       N  
ATOM    956  CA  VAL A 216      95.320  76.559 -37.255  1.00  9.20           C  
ANISOU  956  CA  VAL A 216     1675    672   1148     66   -115    226       C  
ATOM    957  C   VAL A 216      95.277  77.816 -38.105  1.00  8.54           C  
ANISOU  957  C   VAL A 216     1573    541   1129      6   -197    158       C  
ATOM    958  O   VAL A 216      95.796  78.864 -37.702  1.00  9.39           O  
ANISOU  958  O   VAL A 216     1704    607   1257   -238   -107     81       O  
ATOM    959  CB  VAL A 216      94.288  76.584 -36.106  1.00  8.74           C  
ANISOU  959  CB  VAL A 216     1456    713   1154     83   -115    -67       C  
ATOM    960  CG1 VAL A 216      94.593  77.685 -35.075  1.00 10.16           C  
ANISOU  960  CG1 VAL A 216     1778    916   1167    139   -154   -152       C  
ATOM    961  CG2 VAL A 216      92.872  76.674 -36.656  1.00 10.33           C  
ANISOU  961  CG2 VAL A 216     1567    921   1438     76    -83     98       C  
ATOM    962  N   VAL A 217      94.696  77.703 -39.290  1.00  9.28           N  
ANISOU  962  N   VAL A 217     1622    618   1285    160   -278    226       N  
ATOM    963  CA  VAL A 217      94.722  78.784 -40.261  1.00  9.66           C  
ANISOU  963  CA  VAL A 217     1675    759   1235    270   -175    143       C  
ATOM    964  C   VAL A 217      93.310  79.023 -40.770  1.00  9.62           C  
ANISOU  964  C   VAL A 217     1589    741   1325    175   -182   -119       C  
ATOM    965  O   VAL A 217      92.547  78.073 -40.990  1.00 11.57           O  
ANISOU  965  O   VAL A 217     1938    938   1519   -246   -425    -63       O  
ATOM    966  CB  VAL A 217      95.708  78.462 -41.412  1.00 10.68           C  
ANISOU  966  CB  VAL A 217     2016    719   1323    219     87    -13       C  
ATOM    967  CG1 VAL A 217      95.333  77.168 -42.137  1.00 11.49           C  
ANISOU  967  CG1 VAL A 217     2189    667   1508   -171   -107    -82       C  
ATOM    968  CG2 VAL A 217      95.810  79.622 -42.386  1.00 12.24           C  
ANISOU  968  CG2 VAL A 217     2159   1007   1486    411     51    131       C  
ATOM    969  N   VAL A 218      92.963  80.294 -40.954  1.00  9.52           N  
ANISOU  969  N   VAL A 218     1524    774   1318    293   -225    -58       N  
ATOM    970  CA  VAL A 218      91.654  80.674 -41.483  1.00 10.56           C  
ANISOU  970  CA  VAL A 218     1719    959   1333    165   -226     57       C  
ATOM    971  C   VAL A 218      91.857  81.678 -42.607  1.00 10.96           C  
ANISOU  971  C   VAL A 218     1745   1077   1341    -25   -238    229       C  
ATOM    972  O   VAL A 218      92.880  82.378 -42.665  1.00 11.38           O  
ANISOU  972  O   VAL A 218     1846   1123   1355   -127   -229     34       O  
ATOM    973  CB  VAL A 218      90.747  81.291 -40.393  1.00 11.41           C  
ANISOU  973  CB  VAL A 218     1869   1100   1368    130      9   -177       C  
ATOM    974  CG1 VAL A 218      90.420  80.278 -39.315  1.00 12.67           C  
ANISOU  974  CG1 VAL A 218     2242   1206   1366      5    149    268       C  
ATOM    975  CG2 VAL A 218      91.387  82.538 -39.798  1.00 13.01           C  
ANISOU  975  CG2 VAL A 218     1808   1522   1612    471   -147   -287       C  
ATOM    976  N   PRO A 219      90.882  81.801 -43.499  1.00 12.14           N  
ANISOU  976  N   PRO A 219     1878   1269   1466   -114   -361    308       N  
ATOM    977  CA  PRO A 219      90.948  82.870 -44.497  1.00 13.31           C  
ANISOU  977  CA  PRO A 219     2193   1431   1434     44   -299    383       C  
ATOM    978  C   PRO A 219      90.885  84.233 -43.827  1.00 13.78           C  
ANISOU  978  C   PRO A 219     2114   1491   1630    134   -186    356       C  
ATOM    979  O   PRO A 219      90.173  84.429 -42.840  1.00 14.52           O  
ANISOU  979  O   PRO A 219     2221   1681   1613    136     54    421       O  
ATOM    980  CB  PRO A 219      89.698  82.630 -45.350  1.00 14.02           C  
ANISOU  980  CB  PRO A 219     2154   1632   1540   -118   -536    456       C  
ATOM    981  CG  PRO A 219      89.351  81.194 -45.125  1.00 13.98           C  
ANISOU  981  CG  PRO A 219     2362   1444   1507    -99   -453    334       C  
ATOM    982  CD  PRO A 219      89.701  80.941 -43.693  1.00 12.50           C  
ANISOU  982  CD  PRO A 219     1959   1291   1498   -378   -738    195       C  
ATOM    983  N   HIS A 220      91.652  85.172 -44.361  1.00 13.64           N  
ANISOU  983  N   HIS A 220     2079   1391   1714    149   -125    207       N  
ATOM    984  CA  HIS A 220      91.517  86.554 -43.942  1.00 14.67           C  
ANISOU  984  CA  HIS A 220     2125   1330   2119    201     -4    263       C  
ATOM    985  C   HIS A 220      90.315  87.166 -44.642  1.00 17.20           C  
ANISOU  985  C   HIS A 220     2386   1634   2515    407   -165     78       C  
ATOM    986  O   HIS A 220      90.143  87.006 -45.853  1.00 18.40           O  
ANISOU  986  O   HIS A 220     2744   1843   2405    537   -280     47       O  
ATOM    987  CB  HIS A 220      92.761  87.356 -44.291  1.00 15.45           C  
ANISOU  987  CB  HIS A 220     2392   1149   2331    115      7    224       C  
ATOM    988  CG  HIS A 220      92.666  88.778 -43.860  1.00 17.69           C  
ANISOU  988  CG  HIS A 220     2762   1353   2605    231     28    384       C  
ATOM    989  ND1 HIS A 220      92.323  89.794 -44.723  1.00 19.83           N  
ANISOU  989  ND1 HIS A 220     3183   1549   2802     18    160    517       N  
ATOM    990  CD2 HIS A 220      92.798  89.345 -42.640  1.00 19.20           C  
ANISOU  990  CD2 HIS A 220     3070   1474   2749     88    -46    365       C  
ATOM    991  CE1 HIS A 220      92.278  90.934 -44.059  1.00 21.23           C  
ANISOU  991  CE1 HIS A 220     3466   1697   2903    -26    160    311       C  
ATOM    992  NE2 HIS A 220      92.564  90.690 -42.792  1.00 20.21           N  
ANISOU  992  NE2 HIS A 220     3397   1401   2880    255     44    333       N  
ATOM    993  N   GLU A 221      89.480  87.855 -43.881  1.00 21.38           N  
ANISOU  993  N   GLU A 221     2846   2077   3199    546   -219   -190       N  
ATOM    994  CA  GLU A 221      88.339  88.518 -44.473  1.00 27.05           C  
ANISOU  994  CA  GLU A 221     3659   2688   3931    811   -159   -356       C  
ATOM    995  C   GLU A 221      88.427  90.014 -44.210  1.00 28.62           C  
ANISOU  995  C   GLU A 221     3993   2695   4188    991   -160   -525       C  
ATOM    996  O   GLU A 221      88.893  90.421 -43.145  1.00 29.66           O  
ANISOU  996  O   GLU A 221     4054   2950   4267   1384    -97   -548       O  
ATOM    997  CB  GLU A 221      87.038  87.979 -43.871  1.00 32.68           C  
ANISOU  997  CB  GLU A 221     4408   3545   4463    779    -88   -352       C  
ATOM    998  CG  GLU A 221      86.737  86.546 -44.274  1.00 38.32           C  
ANISOU  998  CG  GLU A 221     5178   4416   4967    729     10   -181       C  
ATOM    999  CD  GLU A 221      86.125  85.757 -43.137  1.00 43.43           C  
ANISOU  999  CD  GLU A 221     5910   5256   5336    648     73   -263       C  
ATOM   1000  OE1 GLU A 221      86.138  86.251 -41.993  1.00 45.16           O  
ANISOU 1000  OE1 GLU A 221     6149   5587   5424    672    162   -365       O  
ATOM   1001  OE2 GLU A 221      85.632  84.644 -43.388  1.00 45.24           O1-
ANISOU 1001  OE2 GLU A 221     6150   5539   5500    538     48   -204       O1-
ATOM   1002  N   PRO A 222      88.017  90.850 -45.159  1.00 30.41           N  
ANISOU 1002  N   PRO A 222     4590   2579   4385    808    -39   -476       N  
ATOM   1003  CA  PRO A 222      87.946  92.280 -44.883  1.00 30.94           C  
ANISOU 1003  CA  PRO A 222     4708   2528   4519    847     18   -373       C  
ATOM   1004  C   PRO A 222      86.926  92.555 -43.800  1.00 30.37           C  
ANISOU 1004  C   PRO A 222     4398   2512   4628    849    -28   -164       C  
ATOM   1005  O   PRO A 222      85.984  91.766 -43.594  1.00 28.94           O  
ANISOU 1005  O   PRO A 222     4127   2206   4664    816   -100    -78       O  
ATOM   1006  CB  PRO A 222      87.506  92.875 -46.229  1.00 32.55           C  
ANISOU 1006  CB  PRO A 222     5088   2772   4507    769    124   -375       C  
ATOM   1007  CG  PRO A 222      87.904  91.854 -47.246  1.00 33.39           C  
ANISOU 1007  CG  PRO A 222     5264   2952   4469    620     69   -398       C  
ATOM   1008  CD  PRO A 222      87.753  90.534 -46.572  1.00 32.26           C  
ANISOU 1008  CD  PRO A 222     5053   2784   4422    760    -23   -449       C  
ATOM   1009  N   PRO A 223      87.081  93.657 -43.061  1.00 30.84           N  
ANISOU 1009  N   PRO A 223     4338   2636   4743   1033    -26   -121       N  
ATOM   1010  CA  PRO A 223      86.087  94.009 -42.039  1.00 32.44           C  
ANISOU 1010  CA  PRO A 223     4317   3012   4998    943   -123    -16       C  
ATOM   1011  C   PRO A 223      84.686  94.154 -42.612  1.00 34.18           C  
ANISOU 1011  C   PRO A 223     4169   3393   5424   1002   -407      8       C  
ATOM   1012  O   PRO A 223      84.495  94.525 -43.773  1.00 33.87           O  
ANISOU 1012  O   PRO A 223     4109   3369   5391   1137   -614    -12       O  
ATOM   1013  CB  PRO A 223      86.597  95.349 -41.496  1.00 32.18           C  
ANISOU 1013  CB  PRO A 223     4447   2932   4849   1054    -46   -191       C  
ATOM   1014  CG  PRO A 223      88.070  95.299 -41.713  1.00 32.03           C  
ANISOU 1014  CG  PRO A 223     4453   2945   4771   1018    -95   -234       C  
ATOM   1015  CD  PRO A 223      88.272  94.524 -42.997  1.00 31.73           C  
ANISOU 1015  CD  PRO A 223     4453   2860   4742   1116    -63   -294       C  
ATOM   1016  N   GLU A 224      83.700  93.858 -41.767  1.00 35.52           N  
ANISOU 1016  N   GLU A 224     3886   3754   5856    873   -580     -8       N  
ATOM   1017  CA  GLU A 224      82.305  94.078 -42.107  1.00 37.07           C  
ANISOU 1017  CA  GLU A 224     3777   4070   6238    776   -829    -74       C  
ATOM   1018  C   GLU A 224      81.996  95.573 -42.117  1.00 38.01           C  
ANISOU 1018  C   GLU A 224     3656   4231   6555    989   -950   -176       C  
ATOM   1019  O   GLU A 224      82.782  96.406 -41.655  1.00 38.07           O  
ANISOU 1019  O   GLU A 224     3623   4209   6634    970   -916   -184       O  
ATOM   1020  CB  GLU A 224      81.397  93.375 -41.099  1.00 37.59           C  
ANISOU 1020  CB  GLU A 224     3758   4255   6270    488   -891    -81       C  
ATOM   1021  N   VAL A 225      80.818  95.909 -42.645  1.00 39.30           N  
ANISOU 1021  N   VAL A 225     3799   4416   6716   1025  -1086   -178       N  
ATOM   1022  CA  VAL A 225      80.408  97.305 -42.717  1.00 40.58           C  
ANISOU 1022  CA  VAL A 225     3983   4556   6879   1075  -1032   -302       C  
ATOM   1023  C   VAL A 225      80.309  97.882 -41.313  1.00 40.95           C  
ANISOU 1023  C   VAL A 225     4201   4404   6954   1060   -973   -410       C  
ATOM   1024  O   VAL A 225      79.679  97.297 -40.421  1.00 40.95           O  
ANISOU 1024  O   VAL A 225     4315   4252   6991   1015  -1131   -323       O  
ATOM   1025  CB  VAL A 225      79.086  97.429 -43.487  1.00 41.33           C  
ANISOU 1025  CB  VAL A 225     4023   4736   6944   1180  -1060   -328       C  
ATOM   1026  CG1 VAL A 225      78.511  98.813 -43.313  1.00 41.39           C  
ANISOU 1026  CG1 VAL A 225     4076   4675   6975   1223  -1086   -269       C  
ATOM   1027  CG2 VAL A 225      79.308  97.132 -44.961  1.00 42.17           C  
ANISOU 1027  CG2 VAL A 225     4154   4891   6977   1026  -1049   -403       C  
ATOM   1028  N   GLY A 226      80.947  99.031 -41.104  1.00 41.34           N  
ANISOU 1028  N   GLY A 226     4384   4394   6928   1137   -872   -492       N  
ATOM   1029  CA  GLY A 226      80.955  99.671 -39.808  1.00 41.28           C  
ANISOU 1029  CA  GLY A 226     4480   4361   6841   1022   -825   -484       C  
ATOM   1030  C   GLY A 226      82.016  99.179 -38.850  1.00 40.47           C  
ANISOU 1030  C   GLY A 226     4423   4243   6711    752   -709   -515       C  
ATOM   1031  O   GLY A 226      82.083  99.678 -37.720  1.00 41.83           O  
ANISOU 1031  O   GLY A 226     4634   4430   6830    795   -825   -588       O  
ATOM   1032  N   SER A 227      82.836  98.214 -39.248  1.00 37.59           N  
ANISOU 1032  N   SER A 227     4048   3815   6419    367   -510   -245       N  
ATOM   1033  CA  SER A 227      83.929  97.737 -38.420  1.00 35.58           C  
ANISOU 1033  CA  SER A 227     3929   3442   6147    120   -201     16       C  
ATOM   1034  C   SER A 227      85.257  98.153 -39.035  1.00 31.62           C  
ANISOU 1034  C   SER A 227     3546   2786   5682    187   -304    147       C  
ATOM   1035  O   SER A 227      85.379  98.292 -40.255  1.00 30.45           O  
ANISOU 1035  O   SER A 227     3299   2639   5630    159   -388    135       O  
ATOM   1036  CB  SER A 227      83.882  96.217 -38.263  1.00 37.01           C  
ANISOU 1036  CB  SER A 227     4100   3707   6254   -209      9     86       C  
ATOM   1037  OG  SER A 227      82.751  95.829 -37.504  1.00 37.59           O  
ANISOU 1037  OG  SER A 227     4045   3974   6265   -267    153     56       O  
ATOM   1038  N   ASP A 228      86.251  98.358 -38.174  1.00 29.20           N  
ANISOU 1038  N   ASP A 228     3496   2355   5242    339   -377    271       N  
ATOM   1039  CA  ASP A 228      87.569  98.781 -38.613  1.00 27.78           C  
ANISOU 1039  CA  ASP A 228     3531   2189   4836    455   -536    353       C  
ATOM   1040  C   ASP A 228      88.599  97.667 -38.565  1.00 23.72           C  
ANISOU 1040  C   ASP A 228     3253   1766   3992    265   -478    447       C  
ATOM   1041  O   ASP A 228      89.728  97.870 -39.020  1.00 24.23           O  
ANISOU 1041  O   ASP A 228     3291   1995   3919    407   -416    414       O  
ATOM   1042  CB  ASP A 228      88.059  99.965 -37.768  1.00 31.11           C  
ANISOU 1042  CB  ASP A 228     4120   2471   5230    773   -692    335       C  
ATOM   1043  CG  ASP A 228      87.162 101.173 -37.896  1.00 35.15           C  
ANISOU 1043  CG  ASP A 228     4785   3008   5563    729   -764    349       C  
ATOM   1044  OD1 ASP A 228      86.669 101.429 -39.015  1.00 36.43           O1-
ANISOU 1044  OD1 ASP A 228     4869   3319   5652    582   -936    441       O1-
ATOM   1045  OD2 ASP A 228      86.944 101.857 -36.872  1.00 36.57           O  
ANISOU 1045  OD2 ASP A 228     5092   3065   5740    803   -656    296       O  
ATOM   1046  N   CYS A 229      88.244  96.508 -38.021  1.00 19.96           N  
ANISOU 1046  N   CYS A 229     3031   1275   3278    340   -354    517       N  
ATOM   1047  CA  CYS A 229      89.150  95.377 -37.965  1.00 18.41           C  
ANISOU 1047  CA  CYS A 229     3021   1242   2733    180   -448    252       C  
ATOM   1048  C   CYS A 229      88.323  94.109 -38.086  1.00 18.74           C  
ANISOU 1048  C   CYS A 229     2996   1615   2508    200   -443    192       C  
ATOM   1049  O   CYS A 229      87.092  94.142 -38.105  1.00 20.52           O  
ANISOU 1049  O   CYS A 229     3039   2029   2729    175   -178     78       O  
ATOM   1050  CB  CYS A 229      89.962  95.369 -36.660  1.00 18.76           C  
ANISOU 1050  CB  CYS A 229     3158   1514   2458     60   -439    223       C  
ATOM   1051  SG  CYS A 229      89.008  95.087 -35.118  1.00 19.08           S  
ANISOU 1051  SG  CYS A 229     3146   1667   2437    263   -343    -46       S  
ATOM   1052  N   THR A 230      89.011  92.988 -38.189  1.00 17.41           N  
ANISOU 1052  N   THR A 230     3071   1434   2109    304   -526    442       N  
ATOM   1053  CA  THR A 230      88.357  91.703 -38.036  1.00 17.21           C  
ANISOU 1053  CA  THR A 230     2889   1630   2019    257   -626    379       C  
ATOM   1054  C   THR A 230      88.888  91.026 -36.787  1.00 14.48           C  
ANISOU 1054  C   THR A 230     2273   1338   1892    169   -585    436       C  
ATOM   1055  O   THR A 230      89.919  91.412 -36.233  1.00 15.11           O  
ANISOU 1055  O   THR A 230     2173   1592   1977   -214   -571    622       O  
ATOM   1056  CB  THR A 230      88.565  90.821 -39.261  1.00 20.83           C  
ANISOU 1056  CB  THR A 230     3497   2253   2166    555   -774    349       C  
ATOM   1057  OG1 THR A 230      89.960  90.566 -39.446  1.00 23.75           O  
ANISOU 1057  OG1 THR A 230     3579   3107   2337    467   -733    530       O  
ATOM   1058  CG2 THR A 230      88.022  91.510 -40.469  1.00 21.98           C  
ANISOU 1058  CG2 THR A 230     4070   2134   2148    631   -885    322       C  
ATOM   1059  N   THR A 231      88.153  90.033 -36.323  1.00 13.85           N  
ANISOU 1059  N   THR A 231     2073   1279   1909     67   -444    300       N  
ATOM   1060  CA  THR A 231      88.474  89.376 -35.070  1.00 13.50           C  
ANISOU 1060  CA  THR A 231     1962   1272   1894     62   -493    103       C  
ATOM   1061  C   THR A 231      88.424  87.877 -35.276  1.00 12.99           C  
ANISOU 1061  C   THR A 231     2006   1114   1817    -63   -604    137       C  
ATOM   1062  O   THR A 231      87.514  87.360 -35.932  1.00 15.40           O  
ANISOU 1062  O   THR A 231     2214   1392   2247   -219   -987    106       O  
ATOM   1063  CB  THR A 231      87.487  89.800 -33.988  1.00 15.30           C  
ANISOU 1063  CB  THR A 231     2176   1540   2096     46   -391    141       C  
ATOM   1064  OG1 THR A 231      87.559  91.217 -33.848  1.00 17.23           O  
ANISOU 1064  OG1 THR A 231     2453   1666   2426     24   -171    -82       O  
ATOM   1065  CG2 THR A 231      87.839  89.172 -32.654  1.00 16.84           C  
ANISOU 1065  CG2 THR A 231     2426   1811   2161    255   -351    531       C  
ATOM   1066  N   ILE A 232      89.426  87.191 -34.749  1.00 10.85           N  
ANISOU 1066  N   ILE A 232     1817    811   1493     21   -242    127       N  
ATOM   1067  CA  ILE A 232      89.429  85.738 -34.682  1.00 10.97           C  
ANISOU 1067  CA  ILE A 232     1845    736   1586     35   -108    104       C  
ATOM   1068  C   ILE A 232      89.217  85.352 -33.229  1.00 10.28           C  
ANISOU 1068  C   ILE A 232     1694    830   1383   -284   -202    -56       C  
ATOM   1069  O   ILE A 232      89.781  85.977 -32.323  1.00 12.11           O  
ANISOU 1069  O   ILE A 232     1954   1340   1306   -533   -310    -77       O  
ATOM   1070  CB  ILE A 232      90.740  85.128 -35.219  1.00 12.83           C  
ANISOU 1070  CB  ILE A 232     1941   1240   1692    164     68    120       C  
ATOM   1071  CG1 ILE A 232      90.940  85.474 -36.690  1.00 14.38           C  
ANISOU 1071  CG1 ILE A 232     2144   1638   1683    166    245     87       C  
ATOM   1072  CG2 ILE A 232      90.737  83.606 -35.051  1.00 13.20           C  
ANISOU 1072  CG2 ILE A 232     1913   1194   1908     64   -154     49       C  
ATOM   1073  CD1 ILE A 232      92.231  84.953 -37.266  1.00 16.25           C  
ANISOU 1073  CD1 ILE A 232     2346   2019   1810     63    160    -38       C  
ATOM   1074  N   HIS A 233      88.406  84.330 -32.997  1.00 10.28           N  
ANISOU 1074  N   HIS A 233     1604    809   1493   -103   -186     78       N  
ATOM   1075  CA  HIS A 233      88.162  83.850 -31.644  1.00 10.60           C  
ANISOU 1075  CA  HIS A 233     1563    879   1587    -22   -127     96       C  
ATOM   1076  C   HIS A 233      88.938  82.558 -31.450  1.00 10.39           C  
ANISOU 1076  C   HIS A 233     1491    863   1592    113   -287    -77       C  
ATOM   1077  O   HIS A 233      88.616  81.538 -32.061  1.00 13.21           O  
ANISOU 1077  O   HIS A 233     1939   1159   1922   -118   -558   -424       O  
ATOM   1078  CB  HIS A 233      86.669  83.653 -31.415  1.00 11.71           C  
ANISOU 1078  CB  HIS A 233     1404   1213   1832     -3   -192     76       C  
ATOM   1079  CG  HIS A 233      85.887  84.908 -31.595  1.00 15.31           C  
ANISOU 1079  CG  HIS A 233     2006   1727   2083    283   -347    242       C  
ATOM   1080  ND1 HIS A 233      85.024  85.103 -32.650  1.00 20.11           N  
ANISOU 1080  ND1 HIS A 233     2826   2359   2458    733   -576    273       N  
ATOM   1081  CD2 HIS A 233      85.890  86.063 -30.891  1.00 18.35           C  
ANISOU 1081  CD2 HIS A 233     2399   2183   2392    419   -326    143       C  
ATOM   1082  CE1 HIS A 233      84.505  86.314 -32.569  1.00 19.96           C  
ANISOU 1082  CE1 HIS A 233     2661   2339   2584    915   -314    180       C  
ATOM   1083  NE2 HIS A 233      85.016  86.918 -31.512  1.00 18.76           N  
ANISOU 1083  NE2 HIS A 233     2259   2305   2562    763   -311    178       N  
ATOM   1084  N   TYR A 234      89.971  82.610 -30.622  1.00 10.01           N  
ANISOU 1084  N   TYR A 234     1536    832   1435    105   -172    168       N  
ATOM   1085  CA  TYR A 234      90.792  81.447 -30.343  1.00 10.27           C  
ANISOU 1085  CA  TYR A 234     1609    908   1383    202    -84    183       C  
ATOM   1086  C   TYR A 234      90.383  80.822 -29.022  1.00 10.39           C  
ANISOU 1086  C   TYR A 234     1738    819   1393     59    -10    234       C  
ATOM   1087  O   TYR A 234      89.854  81.492 -28.133  1.00 11.21           O  
ANISOU 1087  O   TYR A 234     2128    777   1354    132    111    -39       O  
ATOM   1088  CB  TYR A 234      92.264  81.829 -30.265  1.00 10.29           C  
ANISOU 1088  CB  TYR A 234     1474   1080   1357    -61    -28    190       C  
ATOM   1089  CG  TYR A 234      92.853  82.213 -31.600  1.00  9.94           C  
ANISOU 1089  CG  TYR A 234     1595    978   1202     61   -110     18       C  
ATOM   1090  CD1 TYR A 234      93.073  81.255 -32.581  1.00  9.86           C  
ANISOU 1090  CD1 TYR A 234     1550   1065   1131    297    -94   -195       C  
ATOM   1091  CD2 TYR A 234      93.191  83.531 -31.883  1.00 10.95           C  
ANISOU 1091  CD2 TYR A 234     1844   1049   1269    100     -9    -99       C  
ATOM   1092  CE1 TYR A 234      93.616  81.595 -33.797  1.00 10.40           C  
ANISOU 1092  CE1 TYR A 234     1587   1145   1218    241    -97   -173       C  
ATOM   1093  CE2 TYR A 234      93.743  83.875 -33.096  1.00 11.10           C  
ANISOU 1093  CE2 TYR A 234     1765   1176   1279    217    -31   -250       C  
ATOM   1094  CZ  TYR A 234      93.954  82.902 -34.049  1.00  9.36           C  
ANISOU 1094  CZ  TYR A 234     1399    970   1188    117    -81    -47       C  
ATOM   1095  OH  TYR A 234      94.501  83.255 -35.256  1.00 11.03           O  
ANISOU 1095  OH  TYR A 234     1637   1219   1334    170    139     20       O  
ATOM   1096  N   ASN A 235      90.635  79.525 -28.906  1.00 10.13           N  
ANISOU 1096  N   ASN A 235     1658    805   1386    139   -246    236       N  
ATOM   1097  CA  ASN A 235      90.520  78.815 -27.643  1.00 10.64           C  
ANISOU 1097  CA  ASN A 235     1625    910   1510     46   -234    305       C  
ATOM   1098  C   ASN A 235      91.836  78.104 -27.397  1.00  9.50           C  
ANISOU 1098  C   ASN A 235     1552    715   1343    171   -106     50       C  
ATOM   1099  O   ASN A 235      92.409  77.515 -28.319  1.00 11.51           O  
ANISOU 1099  O   ASN A 235     1755   1270   1350    461   -125   -137       O  
ATOM   1100  CB  ASN A 235      89.443  77.721 -27.665  1.00 12.65           C  
ANISOU 1100  CB  ASN A 235     1522   1205   2080    -93   -138     83       C  
ATOM   1101  CG  ASN A 235      88.051  78.241 -27.925  1.00 16.38           C  
ANISOU 1101  CG  ASN A 235     1942   1568   2715   -290   -270   -204       C  
ATOM   1102  OD1 ASN A 235      87.206  77.498 -28.416  1.00 20.25           O  
ANISOU 1102  OD1 ASN A 235     2427   1978   3288    -95   -455   -563       O  
ATOM   1103  ND2 ASN A 235      87.786  79.490 -27.571  1.00 16.76           N  
ANISOU 1103  ND2 ASN A 235     2056   1525   2785    -50    -82    -83       N  
ATOM   1104  N   TYR A 236      92.285  78.110 -26.147  1.00  9.21           N  
ANISOU 1104  N   TYR A 236     1346    735   1417   -115   -111    167       N  
ATOM   1105  CA  TYR A 236      93.464  77.364 -25.729  1.00  8.95           C  
ANISOU 1105  CA  TYR A 236     1392    542   1465   -104   -187    161       C  
ATOM   1106  C   TYR A 236      93.005  76.187 -24.882  1.00  9.15           C  
ANISOU 1106  C   TYR A 236     1562    550   1364   -241   -137     17       C  
ATOM   1107  O   TYR A 236      92.263  76.367 -23.910  1.00 10.36           O  
ANISOU 1107  O   TYR A 236     1612    998   1327    116     43     24       O  
ATOM   1108  CB  TYR A 236      94.420  78.262 -24.941  1.00 10.33           C  
ANISOU 1108  CB  TYR A 236     1389   1033   1501   -443      1    176       C  
ATOM   1109  CG  TYR A 236      95.028  79.327 -25.819  1.00  9.20           C  
ANISOU 1109  CG  TYR A 236     1384    719   1394    -26    -56    -22       C  
ATOM   1110  CD1 TYR A 236      94.351  80.514 -26.086  1.00  9.95           C  
ANISOU 1110  CD1 TYR A 236     1640    788   1353   -154    -79    -50       C  
ATOM   1111  CD2 TYR A 236      96.279  79.138 -26.395  1.00 11.34           C  
ANISOU 1111  CD2 TYR A 236     1531   1143   1636   -143     -8   -127       C  
ATOM   1112  CE1 TYR A 236      94.915  81.484 -26.902  1.00  9.91           C  
ANISOU 1112  CE1 TYR A 236     1494    872   1399   -353     22     98       C  
ATOM   1113  CE2 TYR A 236      96.842  80.096 -27.219  1.00 11.50           C  
ANISOU 1113  CE2 TYR A 236     1747   1035   1586     -1     28    -14       C  
ATOM   1114  CZ  TYR A 236      96.151  81.263 -27.469  1.00 11.29           C  
ANISOU 1114  CZ  TYR A 236     1763    968   1558   -287     56     49       C  
ATOM   1115  OH  TYR A 236      96.709  82.215 -28.277  1.00 12.27           O  
ANISOU 1115  OH  TYR A 236     1908   1221   1534   -386    184    121       O  
ATOM   1116  N   MET A 237      93.447  74.985 -25.248  1.00  8.85           N  
ANISOU 1116  N   MET A 237     1581    408   1371     36   -107     18       N  
ATOM   1117  CA  MET A 237      92.789  73.766 -24.794  1.00  9.83           C  
ANISOU 1117  CA  MET A 237     1848    520   1366    -51   -196    183       C  
ATOM   1118  C   MET A 237      93.567  72.988 -23.737  1.00 10.77           C  
ANISOU 1118  C   MET A 237     1891    738   1463    -48    -42    118       C  
ATOM   1119  O   MET A 237      93.213  71.841 -23.442  1.00 11.02           O  
ANISOU 1119  O   MET A 237     1803    698   1685   -108   -180     57       O  
ATOM   1120  CB  MET A 237      92.459  72.893 -25.999  1.00 10.77           C  
ANISOU 1120  CB  MET A 237     2038    657   1397    -66   -402     56       C  
ATOM   1121  CG  MET A 237      91.621  73.601 -27.040  1.00 12.68           C  
ANISOU 1121  CG  MET A 237     1964   1150   1704    -33   -539   -210       C  
ATOM   1122  SD  MET A 237      90.034  74.172 -26.395  1.00 14.32           S  
ANISOU 1122  SD  MET A 237     2109   1141   2191    -32   -486    -20       S  
ATOM   1123  CE  MET A 237      89.349  72.640 -25.749  1.00 13.90           C  
ANISOU 1123  CE  MET A 237     1971   1115   2195    -98   -344    -21       C  
ATOM   1124  N   CYS A 238      94.596  73.591 -23.146  1.00 10.61           N  
ANISOU 1124  N   CYS A 238     1930    888   1213   -108   -211     65       N  
ATOM   1125  CA  CYS A 238      95.290  73.053 -21.985  1.00 11.59           C  
ANISOU 1125  CA  CYS A 238     2130    881   1395    -31   -143    154       C  
ATOM   1126  C   CYS A 238      95.697  74.219 -21.116  1.00 11.74           C  
ANISOU 1126  C   CYS A 238     2034   1206   1220   -565   -330    277       C  
ATOM   1127  O   CYS A 238      95.892  75.329 -21.618  1.00 13.42           O  
ANISOU 1127  O   CYS A 238     2172   1423   1506   -539   -191    278       O  
ATOM   1128  CB  CYS A 238      96.601  72.395 -22.356  1.00 14.89           C  
ANISOU 1128  CB  CYS A 238     2768   1017   1872    570    307    387       C  
ATOM   1129  SG  CYS A 238      96.515  70.649 -22.527  1.00 17.95           S  
ANISOU 1129  SG  CYS A 238     3408   1323   2091    458    851    274       S  
ATOM   1130  N   TYR A 239      95.839  73.955 -19.819  1.00 12.11           N  
ANISOU 1130  N   TYR A 239     1728   1626   1247   -524   -489    167       N  
ATOM   1131  CA  TYR A 239      96.407  74.941 -18.920  1.00 12.17           C  
ANISOU 1131  CA  TYR A 239     1748   1452   1422   -609   -283    247       C  
ATOM   1132  C   TYR A 239      97.914  75.009 -19.103  1.00 12.54           C  
ANISOU 1132  C   TYR A 239     1982   1325   1458   -447   -265    182       C  
ATOM   1133  O   TYR A 239      98.564  74.015 -19.439  1.00 12.25           O  
ANISOU 1133  O   TYR A 239     2106   1141   1406   -369   -250    126       O  
ATOM   1134  CB  TYR A 239      96.143  74.529 -17.477  1.00 13.59           C  
ANISOU 1134  CB  TYR A 239     1876   1766   1524   -454   -199    386       C  
ATOM   1135  CG  TYR A 239      94.712  74.698 -17.045  1.00 13.73           C  
ANISOU 1135  CG  TYR A 239     1628   1895   1692   -390    -97    434       C  
ATOM   1136  CD1 TYR A 239      94.160  75.960 -16.897  1.00 15.49           C  
ANISOU 1136  CD1 TYR A 239     2008   2014   1864   -299    -76    608       C  
ATOM   1137  CD2 TYR A 239      93.916  73.601 -16.770  1.00 15.95           C  
ANISOU 1137  CD2 TYR A 239     2048   2168   1845   -402   -183    477       C  
ATOM   1138  CE1 TYR A 239      92.858  76.127 -16.494  1.00 16.19           C  
ANISOU 1138  CE1 TYR A 239     1901   2231   2022   -456    128    783       C  
ATOM   1139  CE2 TYR A 239      92.605  73.754 -16.366  1.00 17.06           C  
ANISOU 1139  CE2 TYR A 239     2046   2373   2061   -449   -125    617       C  
ATOM   1140  CZ  TYR A 239      92.076  75.018 -16.227  1.00 17.72           C  
ANISOU 1140  CZ  TYR A 239     2036   2477   2218   -429    104    750       C  
ATOM   1141  OH  TYR A 239      90.767  75.178 -15.820  1.00 20.74           O  
ANISOU 1141  OH  TYR A 239     2380   3001   2498   -193     42    843       O  
ATOM   1142  N   SER A 240      98.479  76.196 -18.854  1.00 11.24           N  
ANISOU 1142  N   SER A 240     1795   1163   1312   -481   -237    311       N  
ATOM   1143  CA  SER A 240      99.934  76.308 -18.847  1.00 10.82           C  
ANISOU 1143  CA  SER A 240     1904    787   1419   -323   -437     89       C  
ATOM   1144  C   SER A 240     100.572  75.311 -17.894  1.00 11.73           C  
ANISOU 1144  C   SER A 240     2160    774   1521   -328   -192    228       C  
ATOM   1145  O   SER A 240     101.688  74.844 -18.144  1.00 14.01           O  
ANISOU 1145  O   SER A 240     2358   1195   1771     59   -395     66       O  
ATOM   1146  CB  SER A 240     100.354  77.722 -18.470  1.00 11.37           C  
ANISOU 1146  CB  SER A 240     2208    622   1491   -175   -393    -13       C  
ATOM   1147  OG  SER A 240     100.007  78.607 -19.515  1.00 12.13           O  
ANISOU 1147  OG  SER A 240     2079    808   1723   -100   -452    360       O  
ATOM   1148  N   SER A 241      99.873  74.958 -16.816  1.00 13.07           N  
ANISOU 1148  N   SER A 241     2492    866   1606   -364   -451    277       N  
ATOM   1149  CA  SER A 241     100.393  74.078 -15.780  1.00 14.17           C  
ANISOU 1149  CA  SER A 241     2802   1073   1510   -244   -433    232       C  
ATOM   1150  C   SER A 241     100.248  72.593 -16.095  1.00 14.71           C  
ANISOU 1150  C   SER A 241     3011   1085   1495   -147   -473     26       C  
ATOM   1151  O   SER A 241     100.712  71.778 -15.297  1.00 17.28           O  
ANISOU 1151  O   SER A 241     3392   1346   1827     -7   -623    224       O  
ATOM   1152  CB  SER A 241      99.657  74.363 -14.473  1.00 15.83           C  
ANISOU 1152  CB  SER A 241     2816   1593   1607     21   -297    320       C  
ATOM   1153  OG  SER A 241      98.279  74.052 -14.623  1.00 17.82           O  
ANISOU 1153  OG  SER A 241     2958   2091   1722   -209   -118    237       O  
ATOM   1154  N   CYS A 242      99.626  72.211 -17.207  1.00 13.13           N  
ANISOU 1154  N   CYS A 242     2642    884   1464   -314   -258    -16       N  
ATOM   1155  CA  CYS A 242      99.302  70.800 -17.414  1.00 13.41           C  
ANISOU 1155  CA  CYS A 242     2721    729   1646   -268   -138     24       C  
ATOM   1156  C   CYS A 242     100.551  69.918 -17.406  1.00 15.06           C  
ANISOU 1156  C   CYS A 242     2936    914   1871   -396    -54    321       C  
ATOM   1157  O   CYS A 242     101.478  70.123 -18.196  1.00 16.05           O  
ANISOU 1157  O   CYS A 242     2919   1005   2174   -436     48    209       O  
ATOM   1158  CB  CYS A 242      98.531  70.612 -18.724  1.00 15.83           C  
ANISOU 1158  CB  CYS A 242     2749   1342   1924    -20     88   -299       C  
ATOM   1159  SG  CYS A 242      96.739  70.907 -18.603  1.00 15.02           S  
ANISOU 1159  SG  CYS A 242     2611   1070   2025   -304    299   -281       S  
ATOM   1160  N   MET A 243     100.552  68.907 -16.537  1.00 17.70           N  
ANISOU 1160  N   MET A 243     3648   1200   1875   -165   -106    374       N  
ATOM   1161  CA  MET A 243     101.685  67.995 -16.455  1.00 21.26           C  
ANISOU 1161  CA  MET A 243     4116   1878   2085    200   -181    315       C  
ATOM   1162  C   MET A 243     101.795  67.174 -17.727  1.00 18.60           C  
ANISOU 1162  C   MET A 243     3550   1450   2065    352    -71    432       C  
ATOM   1163  O   MET A 243     100.791  66.708 -18.277  1.00 17.24           O  
ANISOU 1163  O   MET A 243     3288   1282   1981    278   -254    348       O  
ATOM   1164  CB  MET A 243     101.495  67.010 -15.310  1.00 27.63           C  
ANISOU 1164  CB  MET A 243     5272   3088   2136    235   -144    361       C  
ATOM   1165  CG  MET A 243     101.216  67.598 -13.952  1.00 35.56           C  
ANISOU 1165  CG  MET A 243     6341   4438   2730     80     31    412       C  
ATOM   1166  SD  MET A 243     100.802  66.243 -12.828  1.00 43.19           S  
ANISOU 1166  SD  MET A 243     7307   5765   3338   -164    165    505       S  
ATOM   1167  CE  MET A 243      99.060  66.576 -12.638  1.00 41.98           C  
ANISOU 1167  CE  MET A 243     7079   5639   3232   -126    210    571       C  
ATOM   1168  N   GLY A 244     103.030  66.963 -18.175  1.00 18.09           N  
ANISOU 1168  N   GLY A 244     3175   1402   2297    178    -55    283       N  
ATOM   1169  CA  GLY A 244     103.261  66.232 -19.400  1.00 19.03           C  
ANISOU 1169  CA  GLY A 244     3331   1514   2384   -101     94    116       C  
ATOM   1170  C   GLY A 244     102.956  67.006 -20.658  1.00 19.24           C  
ANISOU 1170  C   GLY A 244     3368   1385   2559   -223    280     12       C  
ATOM   1171  O   GLY A 244     103.177  66.482 -21.754  1.00 21.39           O  
ANISOU 1171  O   GLY A 244     3678   1726   2724   -601    398   -216       O  
ATOM   1172  N   GLY A 245     102.450  68.233 -20.533  1.00 17.76           N  
ANISOU 1172  N   GLY A 245     3231    950   2566   -179    106    326       N  
ATOM   1173  CA  GLY A 245     102.233  69.116 -21.657  1.00 16.79           C  
ANISOU 1173  CA  GLY A 245     2922   1019   2438   -436    227    369       C  
ATOM   1174  C   GLY A 245     103.071  70.359 -21.468  1.00 15.82           C  
ANISOU 1174  C   GLY A 245     2759    980   2271   -277    194    196       C  
ATOM   1175  O   GLY A 245     104.293  70.263 -21.330  1.00 17.76           O  
ANISOU 1175  O   GLY A 245     2812   1433   2504   -207     70    156       O  
ATOM   1176  N   MET A 246     102.435  71.530 -21.415  1.00 14.28           N  
ANISOU 1176  N   MET A 246     2626    974   1824   -378    155     34       N  
ATOM   1177  CA  MET A 246     103.201  72.753 -21.231  1.00 14.11           C  
ANISOU 1177  CA  MET A 246     2431   1145   1785   -254   -173    305       C  
ATOM   1178  C   MET A 246     103.983  72.747 -19.923  1.00 14.77           C  
ANISOU 1178  C   MET A 246     2336   1312   1965   -128   -148    313       C  
ATOM   1179  O   MET A 246     105.070  73.329 -19.855  1.00 15.24           O  
ANISOU 1179  O   MET A 246     2226   1408   2158    -20   -238    118       O  
ATOM   1180  CB  MET A 246     102.288  73.967 -21.364  1.00 14.23           C  
ANISOU 1180  CB  MET A 246     2512   1258   1638    -66   -291    302       C  
ATOM   1181  CG  MET A 246     101.890  74.189 -22.814  1.00 14.23           C  
ANISOU 1181  CG  MET A 246     2452   1376   1576   -195   -211    206       C  
ATOM   1182  SD  MET A 246     100.856  75.630 -23.037  1.00 14.15           S  
ANISOU 1182  SD  MET A 246     2115   1615   1648   -289   -143    321       S  
ATOM   1183  CE  MET A 246      99.260  75.011 -22.501  1.00 15.46           C  
ANISOU 1183  CE  MET A 246     2171   2142   1562   -144    140    418       C  
ATOM   1184  N   ASN A 247     103.457  72.095 -18.884  1.00 14.80           N  
ANISOU 1184  N   ASN A 247     2324   1425   1875   -165   -123    400       N  
ATOM   1185  CA  ASN A 247     104.233  71.805 -17.673  1.00 18.06           C  
ANISOU 1185  CA  ASN A 247     2602   2054   2207      5   -267    493       C  
ATOM   1186  C   ASN A 247     104.822  73.071 -17.051  1.00 16.66           C  
ANISOU 1186  C   ASN A 247     2323   1942   2063   -164   -302    682       C  
ATOM   1187  O   ASN A 247     105.988  73.105 -16.649  1.00 18.51           O  
ANISOU 1187  O   ASN A 247     2592   2159   2281    138   -527    686       O  
ATOM   1188  CB  ASN A 247     105.313  70.749 -17.929  1.00 22.47           C  
ANISOU 1188  CB  ASN A 247     3361   2550   2627    372   -266    645       C  
ATOM   1189  CG  ASN A 247     105.901  70.191 -16.640  1.00 27.82           C  
ANISOU 1189  CG  ASN A 247     4150   3395   3027    643      6    755       C  
ATOM   1190  OD1 ASN A 247     105.272  70.250 -15.585  1.00 30.53           O  
ANISOU 1190  OD1 ASN A 247     4607   3875   3117    724    -91    856       O  
ATOM   1191  ND2 ASN A 247     107.114  69.656 -16.721  1.00 28.95           N  
ANISOU 1191  ND2 ASN A 247     4243   3501   3256    650      8    683       N  
ATOM   1192  N  AARG A 248     104.004  74.119 -16.979  0.50 15.57           N  
ANISOU 1192  N  AARG A 248     2149   1843   1923   -109   -318    542       N  
ATOM   1193  N  BARG A 248     104.008  74.121 -16.967  0.50 15.72           N  
ANISOU 1193  N  BARG A 248     2223   1857   1891   -104   -321    506       N  
ATOM   1194  CA AARG A 248     104.299  75.432 -16.402  0.50 16.03           C  
ANISOU 1194  CA AARG A 248     2256   1930   1905   -228   -560    290       C  
ATOM   1195  CA BARG A 248     104.364  75.407 -16.370  0.50 16.27           C  
ANISOU 1195  CA BARG A 248     2395   1949   1837   -216   -558    211       C  
ATOM   1196  C  AARG A 248     105.162  76.312 -17.305  0.50 15.77           C  
ANISOU 1196  C  AARG A 248     2263   1753   1975   -107   -536    145       C  
ATOM   1197  C  BARG A 248     105.371  76.203 -17.191  0.50 16.37           C  
ANISOU 1197  C  BARG A 248     2377   1859   1984   -193   -499    110       C  
ATOM   1198  O  AARG A 248     105.393  77.481 -16.963  0.50 16.22           O  
ANISOU 1198  O  AARG A 248     2393   1699   2070      4   -673     -4       O  
ATOM   1199  O  BARG A 248     105.932  77.186 -16.686  0.50 18.10           O  
ANISOU 1199  O  BARG A 248     2637   2065   2176   -138   -478     29       O  
ATOM   1200  CB AARG A 248     104.878  75.375 -14.978  0.50 18.64           C  
ANISOU 1200  CB AARG A 248     2513   2514   2057   -261   -588    319       C  
ATOM   1201  CB BARG A 248     104.817  75.287 -14.909  0.50 18.62           C  
ANISOU 1201  CB BARG A 248     2719   2471   1885   -244   -636    145       C  
ATOM   1202  CG AARG A 248     103.959  74.681 -13.983  0.50 20.46           C  
ANISOU 1202  CG AARG A 248     2675   2865   2234   -367   -543    479       C  
ATOM   1203  CG BARG A 248     103.832  74.535 -14.039  0.50 20.27           C  
ANISOU 1203  CG BARG A 248     2923   2806   1971   -350   -622    242       C  
ATOM   1204  CD AARG A 248     104.642  74.474 -12.639  0.50 22.44           C  
ANISOU 1204  CD AARG A 248     2818   3254   2454   -300   -495    525       C  
ATOM   1205  CD BARG A 248     104.183  74.636 -12.562  0.50 22.56           C  
ANISOU 1205  CD BARG A 248     3226   3195   2150   -272   -527    267       C  
ATOM   1206  NE AARG A 248     105.767  73.550 -12.745  0.50 24.64           N  
ANISOU 1206  NE AARG A 248     3129   3559   2674   -218   -383    550       N  
ATOM   1207  NE BARG A 248     103.171  73.975 -11.746  0.50 25.09           N  
ANISOU 1207  NE BARG A 248     3628   3565   2340   -155   -480    177       N  
ATOM   1208  CZ AARG A 248     105.675  72.238 -12.555  0.50 26.88           C  
ANISOU 1208  CZ AARG A 248     3340   3916   2956   -210   -327    385       C  
ATOM   1209  CZ BARG A 248     102.039  74.549 -11.355  0.50 26.33           C  
ANISOU 1209  CZ BARG A 248     3784   3743   2477    -83   -352    121       C  
ATOM   1210  NH1AARG A 248     104.510  71.694 -12.239  0.50 27.92           N1+
ANISOU 1210  NH1AARG A 248     3428   4079   3100   -316   -372    415       N1+
ATOM   1211  NH1BARG A 248     101.776  75.804 -11.693  0.50 26.82           N1+
ANISOU 1211  NH1BARG A 248     3855   3832   2503   -100   -328    -37       N1+
ATOM   1212  NH2AARG A 248     106.748  71.470 -12.673  0.50 27.76           N  
ANISOU 1212  NH2AARG A 248     3469   4013   3064     -8   -214    235       N  
ATOM   1213  NH2BARG A 248     101.170  73.869 -10.621  0.50 27.43           N  
ANISOU 1213  NH2BARG A 248     3883   3831   2709   -196   -332    100       N  
ATOM   1214  N   ARG A 249     105.618  75.814 -18.449  1.00 15.15           N  
ANISOU 1214  N   ARG A 249     2252   1616   1888   -202   -472    244       N  
ATOM   1215  CA  ARG A 249     106.494  76.594 -19.317  1.00 13.98           C  
ANISOU 1215  CA  ARG A 249     2125   1279   1909    -98   -425    116       C  
ATOM   1216  C   ARG A 249     105.682  77.620 -20.088  1.00 14.48           C  
ANISOU 1216  C   ARG A 249     2228   1363   1911   -291   -464     73       C  
ATOM   1217  O   ARG A 249     104.657  77.269 -20.681  1.00 14.69           O  
ANISOU 1217  O   ARG A 249     2216   1426   1940   -191   -422    231       O  
ATOM   1218  CB  ARG A 249     107.195  75.679 -20.310  1.00 14.01           C  
ANISOU 1218  CB  ARG A 249     2155   1333   1835     70   -319    108       C  
ATOM   1219  CG  ARG A 249     108.131  74.689 -19.650  1.00 15.26           C  
ANISOU 1219  CG  ARG A 249     2268   1418   2113     61   -364     88       C  
ATOM   1220  CD  ARG A 249     108.677  73.710 -20.659  1.00 16.12           C  
ANISOU 1220  CD  ARG A 249     2316   1473   2336   -163   -261     85       C  
ATOM   1221  NE  ARG A 249     107.667  72.753 -21.095  1.00 16.41           N  
ANISOU 1221  NE  ARG A 249     2322   1450   2463   -107   -145    259       N  
ATOM   1222  CZ  ARG A 249     107.907  71.781 -21.966  1.00 15.28           C  
ANISOU 1222  CZ  ARG A 249     2038   1375   2392    -72    -41    434       C  
ATOM   1223  NH1 ARG A 249     109.118  71.647 -22.487  1.00 16.41           N1+
ANISOU 1223  NH1 ARG A 249     2057   1569   2607    -10     75    464       N1+
ATOM   1224  NH2 ARG A 249     106.943  70.946 -22.314  1.00 15.25           N  
ANISOU 1224  NH2 ARG A 249     2069   1362   2362   -144   -380    643       N  
ATOM   1225  N   PRO A 250     106.110  78.878 -20.118  1.00 13.75           N  
ANISOU 1225  N   PRO A 250     2314   1162   1746   -266   -526    -42       N  
ATOM   1226  CA APRO A 250     105.378  79.873 -20.904  0.52 12.82           C  
ANISOU 1226  CA APRO A 250     2305    951   1613    -99   -480     27       C  
ATOM   1227  CA BPRO A 250     105.387  79.882 -20.903  0.48 12.75           C  
ANISOU 1227  CA BPRO A 250     2260    948   1636   -136   -439     27       C  
ATOM   1228  C   PRO A 250     105.467  79.599 -22.393  1.00 12.17           C  
ANISOU 1228  C   PRO A 250     2102    949   1573     22   -376     -5       C  
ATOM   1229  O   PRO A 250     106.461  79.070 -22.903  1.00 12.56           O  
ANISOU 1229  O   PRO A 250     2142   1053   1577    175   -352     49       O  
ATOM   1230  CB APRO A 250     106.082  81.187 -20.554  0.52 13.74           C  
ANISOU 1230  CB APRO A 250     2456   1051   1716   -188   -655    -88       C  
ATOM   1231  CB BPRO A 250     106.123  81.183 -20.568  0.48 13.41           C  
ANISOU 1231  CB BPRO A 250     2314   1012   1769   -294   -532    -86       C  
ATOM   1232  CG APRO A 250     106.598  80.958 -19.182  0.52 13.95           C  
ANISOU 1232  CG APRO A 250     2464   1156   1682   -191   -714    -50       C  
ATOM   1233  CG BPRO A 250     107.510  80.737 -20.213  0.48 13.42           C  
ANISOU 1233  CG BPRO A 250     2236   1087   1776   -441   -516    -41       C  
ATOM   1234  CD APRO A 250     107.032  79.512 -19.160  0.52 14.17           C  
ANISOU 1234  CD APRO A 250     2423   1185   1775   -202   -649    -47       C  
ATOM   1235  CD BPRO A 250     107.327  79.429 -19.497  0.48 14.19           C  
ANISOU 1235  CD BPRO A 250     2360   1227   1806   -375   -569    -17       C  
ATOM   1236  N   ILE A 251     104.405  79.982 -23.089  1.00 10.80           N  
ANISOU 1236  N   ILE A 251     1803    967   1333     -5   -272    190       N  
ATOM   1237  CA  ILE A 251     104.350  79.865 -24.533  1.00  9.76           C  
ANISOU 1237  CA  ILE A 251     1635    783   1292    -82   -172     35       C  
ATOM   1238  C   ILE A 251     104.080  81.229 -25.126  1.00  9.50           C  
ANISOU 1238  C   ILE A 251     1475    812   1321    -24     15    -20       C  
ATOM   1239  O   ILE A 251     103.614  82.157 -24.460  1.00 10.17           O  
ANISOU 1239  O   ILE A 251     1526    961   1378    113    -29    -17       O  
ATOM   1240  CB  ILE A 251     103.280  78.873 -25.028  1.00  9.86           C  
ANISOU 1240  CB  ILE A 251     1533    692   1522     70    -56    -98       C  
ATOM   1241  CG1 ILE A 251     101.887  79.323 -24.573  1.00 11.20           C  
ANISOU 1241  CG1 ILE A 251     1664   1019   1572   -117     24   -122       C  
ATOM   1242  CG2 ILE A 251     103.615  77.448 -24.599  1.00 10.32           C  
ANISOU 1242  CG2 ILE A 251     1734    609   1577    -38      2    158       C  
ATOM   1243  CD1 ILE A 251     100.775  78.703 -25.385  1.00 11.87           C  
ANISOU 1243  CD1 ILE A 251     1716   1244   1549   -201    -11     56       C  
ATOM   1244  N  ALEU A 252     104.405  81.338 -26.405  0.52  9.25           N  
ANISOU 1244  N  ALEU A 252     1396    808   1313    -15    -54    155       N  
ATOM   1245  N  BLEU A 252     104.372  81.356 -26.405  0.48  9.43           N  
ANISOU 1245  N  BLEU A 252     1512    738   1331    -20   -134    185       N  
ATOM   1246  CA ALEU A 252     103.975  82.428 -27.256  0.52  9.79           C  
ANISOU 1246  CA ALEU A 252     1479    916   1324    -10    -93     84       C  
ATOM   1247  CA BLEU A 252     103.881  82.501 -27.148  0.48  9.96           C  
ANISOU 1247  CA BLEU A 252     1688    736   1361     41   -221    186       C  
ATOM   1248  C  ALEU A 252     103.002  81.875 -28.283  0.52  8.72           C  
ANISOU 1248  C  ALEU A 252     1429    714   1170     63    -68     56       C  
ATOM   1249  C  BLEU A 252     103.139  82.008 -28.375  0.48  8.62           C  
ANISOU 1249  C  BLEU A 252     1513    541   1220    193    -77      2       C  
ATOM   1250  O  ALEU A 252     103.094  80.709 -28.682  0.52  9.34           O  
ANISOU 1250  O  ALEU A 252     1379    926   1243    122    -19    123       O  
ATOM   1251  O  BLEU A 252     103.514  80.999 -28.983  0.48  8.45           O  
ANISOU 1251  O  BLEU A 252     1458    441   1311    245     71     32       O  
ATOM   1252  CB ALEU A 252     105.161  83.013 -28.023  0.52 11.81           C  
ANISOU 1252  CB ALEU A 252     1686   1298   1503   -266      6   -146       C  
ATOM   1253  CB BLEU A 252     104.986  83.484 -27.548  0.48 12.27           C  
ANISOU 1253  CB BLEU A 252     2108    951   1602   -183   -143    183       C  
ATOM   1254  CG ALEU A 252     106.375  83.448 -27.220  0.52 12.87           C  
ANISOU 1254  CG ALEU A 252     1726   1451   1712   -282    240   -283       C  
ATOM   1255  CG BLEU A 252     106.079  82.992 -28.487  0.48 12.51           C  
ANISOU 1255  CG BLEU A 252     2038   1018   1698     -1    -78    346       C  
ATOM   1256  CD1ALEU A 252     107.434  83.973 -28.168  0.52 14.44           C  
ANISOU 1256  CD1ALEU A 252     1803   1765   1919   -354    436   -281       C  
ATOM   1257  CD1BLEU A 252     106.514  84.120 -29.410  0.48 11.85           C  
ANISOU 1257  CD1BLEU A 252     2091    698   1713      3      9    457       C  
ATOM   1258  CD2ALEU A 252     105.981  84.505 -26.216  0.52 13.02           C  
ANISOU 1258  CD2ALEU A 252     1881   1358   1709    -35    378   -416       C  
ATOM   1259  CD2BLEU A 252     107.250  82.517 -27.673  0.48 13.13           C  
ANISOU 1259  CD2BLEU A 252     2016   1184   1790    100   -124    284       C  
ATOM   1260  N   THR A 253     102.071  82.718 -28.712  1.00  9.07           N  
ANISOU 1260  N   THR A 253     1389    876   1183    127   -112     82       N  
ATOM   1261  CA  THR A 253     101.325  82.476 -29.929  1.00  9.49           C  
ANISOU 1261  CA  THR A 253     1325   1024   1257     23    -90    267       C  
ATOM   1262  C   THR A 253     101.873  83.401 -30.999  1.00  9.05           C  
ANISOU 1262  C   THR A 253     1511    683   1243   -167    -48     67       C  
ATOM   1263  O   THR A 253     102.050  84.602 -30.765  1.00  9.99           O  
ANISOU 1263  O   THR A 253     1773    749   1275    109     90     31       O  
ATOM   1264  CB  THR A 253      99.843  82.750 -29.710  1.00  9.75           C  
ANISOU 1264  CB  THR A 253     1336   1081   1289     57     18     99       C  
ATOM   1265  OG1 THR A 253      99.358  81.833 -28.726  1.00 10.86           O  
ANISOU 1265  OG1 THR A 253     1603   1214   1309   -140     -8    198       O  
ATOM   1266  CG2 THR A 253      99.078  82.541 -31.014  1.00 11.20           C  
ANISOU 1266  CG2 THR A 253     1649   1342   1266   -186   -255     89       C  
ATOM   1267  N   ILE A 254     102.175  82.830 -32.156  1.00  9.41           N  
ANISOU 1267  N   ILE A 254     1531    902   1140    110    -61     36       N  
ATOM   1268  CA  ILE A 254     102.640  83.583 -33.312  1.00  9.33           C  
ANISOU 1268  CA  ILE A 254     1491    882   1170    140     12    176       C  
ATOM   1269  C   ILE A 254     101.499  83.614 -34.308  1.00  8.44           C  
ANISOU 1269  C   ILE A 254     1436    596   1175     -5    -67     98       C  
ATOM   1270  O   ILE A 254     100.992  82.559 -34.708  1.00  9.07           O  
ANISOU 1270  O   ILE A 254     1590    493   1364   -234   -105     74       O  
ATOM   1271  CB  ILE A 254     103.879  82.935 -33.942  1.00 10.21           C  
ANISOU 1271  CB  ILE A 254     1416   1043   1420    -86     70     94       C  
ATOM   1272  CG1 ILE A 254     105.002  82.851 -32.909  1.00 12.03           C  
ANISOU 1272  CG1 ILE A 254     1447   1321   1805    227    130    170       C  
ATOM   1273  CG2 ILE A 254     104.312  83.719 -35.190  1.00 11.52           C  
ANISOU 1273  CG2 ILE A 254     1878    982   1519     14    214    391       C  
ATOM   1274  CD1 ILE A 254     106.141  81.953 -33.331  1.00 12.43           C  
ANISOU 1274  CD1 ILE A 254     1531   1230   1963    498    193    153       C  
ATOM   1275  N   ILE A 255     101.077  84.812 -34.695  1.00  8.91           N  
ANISOU 1275  N   ILE A 255     1488    773   1125    210     23    100       N  
ATOM   1276  CA  ILE A 255     100.031  84.982 -35.696  1.00  9.20           C  
ANISOU 1276  CA  ILE A 255     1436    910   1150    176   -116    213       C  
ATOM   1277  C   ILE A 255     100.701  85.460 -36.970  1.00  9.66           C  
ANISOU 1277  C   ILE A 255     1670    850   1150    -16    -53    -67       C  
ATOM   1278  O   ILE A 255     101.361  86.506 -36.978  1.00 10.26           O  
ANISOU 1278  O   ILE A 255     1834    790   1276   -240     21   -125       O  
ATOM   1279  CB  ILE A 255      98.965  85.993 -35.255  1.00  9.19           C  
ANISOU 1279  CB  ILE A 255     1393    823   1277    242   -167     -7       C  
ATOM   1280  CG1 ILE A 255      98.389  85.635 -33.883  1.00 10.72           C  
ANISOU 1280  CG1 ILE A 255     1854    767   1451     59    -49      6       C  
ATOM   1281  CG2 ILE A 255      97.891  86.090 -36.322  1.00 10.81           C  
ANISOU 1281  CG2 ILE A 255     1483   1284   1338    109   -272     -4       C  
ATOM   1282  CD1 ILE A 255      97.718  84.320 -33.835  1.00 12.12           C  
ANISOU 1282  CD1 ILE A 255     2071    929   1604     42    -25   -168       C  
ATOM   1283  N   THR A 256     100.536  84.713 -38.051  1.00  9.89           N  
ANISOU 1283  N   THR A 256     1746    911   1100     97     -2     72       N  
ATOM   1284  CA ATHR A 256     101.140  85.098 -39.315  0.52 10.09           C  
ANISOU 1284  CA ATHR A 256     1731    971   1133     48     26    162       C  
ATOM   1285  CA BTHR A 256     101.147  85.045 -39.330  0.48 10.28           C  
ANISOU 1285  CA BTHR A 256     1771   1005   1129     98     97    263       C  
ATOM   1286  C   THR A 256     100.057  85.350 -40.345  1.00  9.95           C  
ANISOU 1286  C   THR A 256     1761    843   1178   -100     28    162       C  
ATOM   1287  O   THR A 256      99.113  84.566 -40.486  1.00 11.30           O  
ANISOU 1287  O   THR A 256     1946    966   1383   -376   -106    332       O  
ATOM   1288  CB ATHR A 256     102.136  84.067 -39.840  0.52 10.51           C  
ANISOU 1288  CB ATHR A 256     1625   1180   1187     18    -15    -38       C  
ATOM   1289  CB BTHR A 256     101.977  83.864 -39.838  0.48 11.02           C  
ANISOU 1289  CB BTHR A 256     1738   1288   1160    179    238    317       C  
ATOM   1290  OG1ATHR A 256     101.560  82.767 -39.749  0.52 10.84           O  
ANISOU 1290  OG1ATHR A 256     1808    903   1407   -217    -48   -126       O  
ATOM   1291  OG1BTHR A 256     102.893  83.442 -38.820  0.48 12.26           O  
ANISOU 1291  OG1BTHR A 256     1907   1360   1392    135    171    443       O  
ATOM   1292  CG2ATHR A 256     103.440  84.118 -39.055  0.52 10.62           C  
ANISOU 1292  CG2ATHR A 256     1554   1360   1120     17   -182     18       C  
ATOM   1293  CG2BTHR A 256     102.751  84.264 -41.080  0.48 10.57           C  
ANISOU 1293  CG2BTHR A 256     1734   1236   1045    117    295    382       C  
ATOM   1294  N   LEU A 257     100.204  86.460 -41.046  1.00  9.88           N  
ANISOU 1294  N   LEU A 257     1795    835   1124    198    -57    199       N  
ATOM   1295  CA  LEU A 257      99.403  86.746 -42.218  1.00  9.45           C  
ANISOU 1295  CA  LEU A 257     1956    683    952    116     -3    207       C  
ATOM   1296  C   LEU A 257     100.168  86.152 -43.389  1.00 10.60           C  
ANISOU 1296  C   LEU A 257     1976   1024   1027      4    122     90       C  
ATOM   1297  O   LEU A 257     101.363  86.414 -43.547  1.00 12.15           O  
ANISOU 1297  O   LEU A 257     2016   1398   1202   -220    160   -134       O  
ATOM   1298  CB  LEU A 257      99.280  88.258 -42.371  1.00 10.67           C  
ANISOU 1298  CB  LEU A 257     2063    678   1313    -69   -137    230       C  
ATOM   1299  CG  LEU A 257      98.278  88.753 -43.401  1.00 11.10           C  
ANISOU 1299  CG  LEU A 257     1978    869   1370     91   -148    250       C  
ATOM   1300  CD1 LEU A 257      96.857  88.468 -42.927  1.00 12.33           C  
ANISOU 1300  CD1 LEU A 257     1840   1261   1583    162     41    -40       C  
ATOM   1301  CD2 LEU A 257      98.484  90.242 -43.675  1.00 11.92           C  
ANISOU 1301  CD2 LEU A 257     2266    905   1357   -153   -194    266       C  
ATOM   1302  N   GLU A 258      99.498  85.311 -44.172  1.00 10.79           N  
ANISOU 1302  N   GLU A 258     2122    962   1014    178    100   -149       N  
ATOM   1303  CA  GLU A 258     100.150  84.544 -45.224  1.00 12.19           C  
ANISOU 1303  CA  GLU A 258     2496   1061   1075    398    -53   -117       C  
ATOM   1304  C   GLU A 258      99.424  84.747 -46.540  1.00 11.62           C  
ANISOU 1304  C   GLU A 258     2237   1144   1035     88     59    -76       C  
ATOM   1305  O   GLU A 258      98.210  84.951 -46.565  1.00 12.19           O  
ANISOU 1305  O   GLU A 258     2230   1238   1164    124    108     73       O  
ATOM   1306  CB  GLU A 258     100.066  83.039 -44.949  1.00 15.19           C  
ANISOU 1306  CB  GLU A 258     3054   1194   1523    731   -133     69       C  
ATOM   1307  CG  GLU A 258     100.792  82.540 -43.734  1.00 17.73           C  
ANISOU 1307  CG  GLU A 258     3343   1476   1919    475    -59    408       C  
ATOM   1308  CD  GLU A 258     100.611  81.040 -43.543  1.00 19.37           C  
ANISOU 1308  CD  GLU A 258     3551   1671   2139    220    219    437       C  
ATOM   1309  OE1 GLU A 258      99.708  80.436 -44.175  1.00 19.57           O  
ANISOU 1309  OE1 GLU A 258     3517   1837   2084    655    579    706       O  
ATOM   1310  OE2 GLU A 258     101.385  80.467 -42.763  1.00 21.88           O1-
ANISOU 1310  OE2 GLU A 258     3981   1976   2355   -384    276    586       O1-
ATOM   1311  N   ASP A 259     100.168  84.641 -47.641  1.00 11.26           N  
ANISOU 1311  N   ASP A 259     2187   1172    920    -10     77    -25       N  
ATOM   1312  CA  ASP A 259      99.505  84.616 -48.933  1.00 12.04           C  
ANISOU 1312  CA  ASP A 259     2307   1197   1070   -155     48    -36       C  
ATOM   1313  C   ASP A 259      98.956  83.218 -49.204  1.00 12.25           C  
ANISOU 1313  C   ASP A 259     2331   1160   1163    140    -22   -112       C  
ATOM   1314  O   ASP A 259      99.065  82.308 -48.376  1.00 13.68           O  
ANISOU 1314  O   ASP A 259     2492   1409   1295    301     -7   -137       O  
ATOM   1315  CB  ASP A 259     100.405  85.169 -50.039  1.00 12.73           C  
ANISOU 1315  CB  ASP A 259     2225   1307   1306     80    434    237       C  
ATOM   1316  CG  ASP A 259     101.591  84.276 -50.363  1.00 14.45           C  
ANISOU 1316  CG  ASP A 259     2489   1489   1514     71    457    278       C  
ATOM   1317  OD1 ASP A 259     101.591  83.073 -50.026  1.00 14.32           O  
ANISOU 1317  OD1 ASP A 259     2476   1514   1449    280    390    198       O  
ATOM   1318  OD2 ASP A 259     102.533  84.793 -51.007  1.00 16.99           O1-
ANISOU 1318  OD2 ASP A 259     2842   1719   1894     38    542    290       O1-
ATOM   1319  N   SER A 260      98.384  83.033 -50.394  1.00 11.99           N  
ANISOU 1319  N   SER A 260     2471    972   1113    -73    -58   -119       N  
ATOM   1320  CA  SER A 260      97.721  81.770 -50.695  1.00 13.55           C  
ANISOU 1320  CA  SER A 260     2738   1182   1229      5   -120    -95       C  
ATOM   1321  C   SER A 260      98.686  80.592 -50.774  1.00 14.00           C  
ANISOU 1321  C   SER A 260     2948   1148   1224    -16     32     -7       C  
ATOM   1322  O   SER A 260      98.241  79.446 -50.643  1.00 14.39           O  
ANISOU 1322  O   SER A 260     3108    849   1509   -192     64    -68       O  
ATOM   1323  CB  SER A 260      96.916  81.898 -51.986  1.00 13.39           C  
ANISOU 1323  CB  SER A 260     2643   1317   1129   -135    -29     11       C  
ATOM   1324  OG  SER A 260      97.763  82.195 -53.074  1.00 13.21           O  
ANISOU 1324  OG  SER A 260     2583   1276   1159   -348    209    129       O  
ATOM   1325  N   SER A 261      99.982  80.837 -50.982  1.00 13.58           N  
ANISOU 1325  N   SER A 261     2799   1228   1130    288    144     29       N  
ATOM   1326  CA  SER A 261     101.005  79.793 -50.953  1.00 13.95           C  
ANISOU 1326  CA  SER A 261     2777   1112   1410    378    341     28       C  
ATOM   1327  C   SER A 261     101.569  79.542 -49.570  1.00 14.18           C  
ANISOU 1327  C   SER A 261     2691   1147   1549    317    190    -41       C  
ATOM   1328  O   SER A 261     102.412  78.650 -49.420  1.00 16.23           O  
ANISOU 1328  O   SER A 261     2875   1497   1795    398    111    -84       O  
ATOM   1329  CB  SER A 261     102.207  80.191 -51.811  1.00 17.38           C  
ANISOU 1329  CB  SER A 261     3305   1661   1639    575    497    330       C  
ATOM   1330  OG  SER A 261     101.897  80.184 -53.173  1.00 20.16           O  
ANISOU 1330  OG  SER A 261     3762   2220   1678   1145    326    449       O  
ATOM   1331  N   GLY A 262     101.181  80.333 -48.578  1.00 13.61           N  
ANISOU 1331  N   GLY A 262     2642   1179   1350      8    116   -128       N  
ATOM   1332  CA  GLY A 262     101.757  80.215 -47.257  1.00 13.98           C  
ANISOU 1332  CA  GLY A 262     2695   1168   1450    -75   -139     29       C  
ATOM   1333  C   GLY A 262     102.949  81.107 -47.017  1.00 14.79           C  
ANISOU 1333  C   GLY A 262     2586   1401   1631    148     85    -38       C  
ATOM   1334  O   GLY A 262     103.579  80.997 -45.961  1.00 17.62           O  
ANISOU 1334  O   GLY A 262     2908   1879   1907    232    -30    107       O  
ATOM   1335  N   ASN A 263     103.281  81.983 -47.962  1.00 14.60           N  
ANISOU 1335  N   ASN A 263     2588   1184   1776     67    452    -83       N  
ATOM   1336  CA  ASN A 263     104.411  82.881 -47.796  1.00 15.82           C  
ANISOU 1336  CA  ASN A 263     2712   1511   1788    102    496   -201       C  
ATOM   1337  C   ASN A 263     104.058  84.004 -46.832  1.00 14.60           C  
ANISOU 1337  C   ASN A 263     2513   1341   1694     86    342    -71       C  
ATOM   1338  O   ASN A 263     102.909  84.440 -46.741  1.00 14.15           O  
ANISOU 1338  O   ASN A 263     2274   1537   1565     60    116     61       O  
ATOM   1339  CB  ASN A 263     104.811  83.506 -49.132  1.00 18.84           C  
ANISOU 1339  CB  ASN A 263     3180   1875   2103    141    766   -253       C  
ATOM   1340  CG  ASN A 263     105.203  82.485 -50.164  1.00 23.26           C  
ANISOU 1340  CG  ASN A 263     3708   2406   2724    136    471   -369       C  
ATOM   1341  OD1 ASN A 263     106.015  81.603 -49.904  1.00 24.53           O  
ANISOU 1341  OD1 ASN A 263     3693   2445   3184    749    482   -612       O  
ATOM   1342  ND2 ASN A 263     104.619  82.596 -51.347  1.00 24.57           N  
ANISOU 1342  ND2 ASN A 263     3951   2786   2599     10    427   -324       N  
ATOM   1343  N   LEU A 264     105.079  84.494 -46.143  1.00 14.65           N  
ANISOU 1343  N   LEU A 264     2476   1440   1650    121    280   -181       N  
ATOM   1344  CA  LEU A 264     104.890  85.487 -45.098  1.00 14.40           C  
ANISOU 1344  CA  LEU A 264     2293   1448   1730    105    212   -322       C  
ATOM   1345  C   LEU A 264     104.467  86.839 -45.663  1.00 14.19           C  
ANISOU 1345  C   LEU A 264     2378   1361   1652     69    308   -127       C  
ATOM   1346  O   LEU A 264     105.136  87.398 -46.534  1.00 16.20           O  
ANISOU 1346  O   LEU A 264     2563   1657   1933    114    420    -44       O  
ATOM   1347  CB  LEU A 264     106.209  85.657 -44.357  1.00 16.12           C  
ANISOU 1347  CB  LEU A 264     2192   2049   1884     62    -80   -584       C  
ATOM   1348  CG  LEU A 264     106.229  86.742 -43.300  1.00 18.78           C  
ANISOU 1348  CG  LEU A 264     2456   2539   2139     34   -191   -727       C  
ATOM   1349  CD1 LEU A 264     105.408  86.278 -42.134  1.00 20.09           C  
ANISOU 1349  CD1 LEU A 264     2611   2941   2083    244   -178   -678       C  
ATOM   1350  CD2 LEU A 264     107.660  87.007 -42.887  1.00 20.47           C  
ANISOU 1350  CD2 LEU A 264     2550   2837   2390     92   -211   -687       C  
ATOM   1351  N   LEU A 265     103.381  87.389 -45.122  1.00 12.02           N  
ANISOU 1351  N   LEU A 265     2255    891   1423   -125    352   -206       N  
ATOM   1352  CA  LEU A 265     102.999  88.774 -45.375  1.00 12.02           C  
ANISOU 1352  CA  LEU A 265     2294    869   1404   -420    143   -138       C  
ATOM   1353  C   LEU A 265     103.103  89.651 -44.143  1.00 11.36           C  
ANISOU 1353  C   LEU A 265     2297    717   1302   -365    276     58       C  
ATOM   1354  O   LEU A 265     103.296  90.860 -44.271  1.00 13.50           O  
ANISOU 1354  O   LEU A 265     2711    821   1600   -234     90    157       O  
ATOM   1355  CB  LEU A 265     101.558  88.857 -45.881  1.00 12.93           C  
ANISOU 1355  CB  LEU A 265     2246   1279   1390   -281    137   -174       C  
ATOM   1356  CG  LEU A 265     101.274  88.095 -47.170  1.00 13.70           C  
ANISOU 1356  CG  LEU A 265     2304   1534   1369   -263    240     22       C  
ATOM   1357  CD1 LEU A 265      99.804  88.211 -47.510  1.00 14.89           C  
ANISOU 1357  CD1 LEU A 265     2407   1700   1552   -350      8     -7       C  
ATOM   1358  CD2 LEU A 265     102.157  88.606 -48.315  1.00 14.86           C  
ANISOU 1358  CD2 LEU A 265     2524   1742   1382   -266    497    346       C  
ATOM   1359  N   GLY A 266     102.975  89.072 -42.962  1.00 11.33           N  
ANISOU 1359  N   GLY A 266     2100    965   1241     44    224     59       N  
ATOM   1360  CA  GLY A 266     103.025  89.834 -41.734  1.00 10.92           C  
ANISOU 1360  CA  GLY A 266     1954   1049   1147    120     59    -85       C  
ATOM   1361  C   GLY A 266     103.077  88.875 -40.572  1.00  9.86           C  
ANISOU 1361  C   GLY A 266     1628    873   1243    -28    111     37       C  
ATOM   1362  O   GLY A 266     102.686  87.711 -40.693  1.00 11.31           O  
ANISOU 1362  O   GLY A 266     2020    836   1441   -172    171    -47       O  
ATOM   1363  N   ARG A 267     103.569  89.371 -39.445  1.00  9.81           N  
ANISOU 1363  N   ARG A 267     1571   1008   1148    183    -37    187       N  
ATOM   1364  CA  ARG A 267     103.701  88.524 -38.268  1.00  9.21           C  
ANISOU 1364  CA  ARG A 267     1510    714   1276    223    194    134       C  
ATOM   1365  C   ARG A 267     103.589  89.370 -37.011  1.00  9.41           C  
ANISOU 1365  C   ARG A 267     1410    846   1318   -170    244    -55       C  
ATOM   1366  O   ARG A 267     104.096  90.494 -36.963  1.00 10.89           O  
ANISOU 1366  O   ARG A 267     1769    942   1425   -203    202     40       O  
ATOM   1367  CB  ARG A 267     105.044  87.780 -38.254  1.00 11.74           C  
ANISOU 1367  CB  ARG A 267     1715   1013   1734    409    281    435       C  
ATOM   1368  CG  ARG A 267     105.138  86.724 -37.155  1.00 13.83           C  
ANISOU 1368  CG  ARG A 267     1934   1186   2135    570    113    664       C  
ATOM   1369  CD  ARG A 267     106.549  86.149 -37.010  1.00 16.36           C  
ANISOU 1369  CD  ARG A 267     2224   1630   2363    688    196    322       C  
ATOM   1370  NE  ARG A 267     107.038  85.494 -38.220  1.00 18.31           N  
ANISOU 1370  NE  ARG A 267     2448   2006   2503    648     10     52       N  
ATOM   1371  CZ  ARG A 267     107.932  86.005 -39.063  1.00 19.91           C  
ANISOU 1371  CZ  ARG A 267     2604   2523   2437    522   -169   -276       C  
ATOM   1372  NH1 ARG A 267     108.450  87.212 -38.860  1.00 19.49           N1+
ANISOU 1372  NH1 ARG A 267     2570   2609   2228    -34   -249   -234       N1+
ATOM   1373  NH2 ARG A 267     108.307  85.301 -40.123  1.00 22.51           N  
ANISOU 1373  NH2 ARG A 267     2817   3024   2711    931   -252   -521       N  
ATOM   1374  N   ASP A 268     102.944  88.803 -35.992  1.00  9.15           N  
ANISOU 1374  N   ASP A 268     1314    995   1167    -27     45    -29       N  
ATOM   1375  CA  ASP A 268     102.863  89.406 -34.669  1.00  9.05           C  
ANISOU 1375  CA  ASP A 268     1502    800   1136      3    155     36       C  
ATOM   1376  C   ASP A 268     102.796  88.253 -33.679  1.00  9.43           C  
ANISOU 1376  C   ASP A 268     1605    788   1191   -117     53    -15       C  
ATOM   1377  O   ASP A 268     102.629  87.098 -34.068  1.00 10.56           O  
ANISOU 1377  O   ASP A 268     1836    836   1341   -158      4     15       O  
ATOM   1378  CB  ASP A 268     101.645  90.337 -34.588  1.00  9.58           C  
ANISOU 1378  CB  ASP A 268     1684    712   1242    142     91   -169       C  
ATOM   1379  CG  ASP A 268     101.765  91.406 -33.512  1.00 10.18           C  
ANISOU 1379  CG  ASP A 268     1714    841   1311   -131     17     97       C  
ATOM   1380  OD1 ASP A 268     102.633  91.309 -32.617  1.00 11.38           O  
ANISOU 1380  OD1 ASP A 268     1739   1114   1471    109   -156    174       O  
ATOM   1381  OD2 ASP A 268     100.939  92.345 -33.548  1.00 11.66           O1-
ANISOU 1381  OD2 ASP A 268     1936   1254   1240    161      6    -45       O1-
ATOM   1382  N   SER A 269     102.946  88.557 -32.396  1.00 10.31           N  
ANISOU 1382  N   SER A 269     1896    877   1146    -59     39    110       N  
ATOM   1383  CA  SER A 269     102.981  87.478 -31.417  1.00  9.47           C  
ANISOU 1383  CA  SER A 269     1534    884   1179    159     71    130       C  
ATOM   1384  C   SER A 269     102.676  88.034 -30.044  1.00  9.57           C  
ANISOU 1384  C   SER A 269     1696    678   1261     34    112     11       C  
ATOM   1385  O   SER A 269     102.759  89.237 -29.805  1.00 10.39           O  
ANISOU 1385  O   SER A 269     2043    575   1328    123      2    -68       O  
ATOM   1386  CB  SER A 269     104.341  86.772 -31.389  1.00 10.61           C  
ANISOU 1386  CB  SER A 269     1522    975   1535     15   -198    125       C  
ATOM   1387  OG  SER A 269     105.363  87.680 -31.030  1.00 12.01           O  
ANISOU 1387  OG  SER A 269     1616   1271   1675    -24   -126      1       O  
ATOM   1388  N   PHE A 270     102.312  87.126 -29.146  1.00  8.82           N  
ANISOU 1388  N   PHE A 270     1512    682   1157     66    123    183       N  
ATOM   1389  CA  PHE A 270     102.020  87.490 -27.772  1.00  9.02           C  
ANISOU 1389  CA  PHE A 270     1503    732   1192     77     44     23       C  
ATOM   1390  C   PHE A 270     102.232  86.267 -26.904  1.00  9.67           C  
ANISOU 1390  C   PHE A 270     1711    754   1207    -14    -33     47       C  
ATOM   1391  O   PHE A 270     102.022  85.136 -27.347  1.00  9.56           O  
ANISOU 1391  O   PHE A 270     1885    563   1186     50    -76    -38       O  
ATOM   1392  CB  PHE A 270     100.587  88.015 -27.613  1.00  9.87           C  
ANISOU 1392  CB  PHE A 270     1439    919   1392    -37     59    -51       C  
ATOM   1393  CG  PHE A 270      99.533  87.105 -28.186  1.00  8.33           C  
ANISOU 1393  CG  PHE A 270     1446    485   1233    -85     76     39       C  
ATOM   1394  CD1 PHE A 270      99.223  87.152 -29.538  1.00  9.71           C  
ANISOU 1394  CD1 PHE A 270     1795    657   1237    242    -40   -157       C  
ATOM   1395  CD2 PHE A 270      98.819  86.235 -27.372  1.00  9.81           C  
ANISOU 1395  CD2 PHE A 270     1527    813   1386   -222    -21    171       C  
ATOM   1396  CE1 PHE A 270      98.237  86.329 -30.068  1.00  9.70           C  
ANISOU 1396  CE1 PHE A 270     1721    625   1338    243     38    -61       C  
ATOM   1397  CE2 PHE A 270      97.839  85.414 -27.903  1.00  9.93           C  
ANISOU 1397  CE2 PHE A 270     1523    834   1415   -108   -137    266       C  
ATOM   1398  CZ  PHE A 270      97.548  85.464 -29.253  1.00 10.41           C  
ANISOU 1398  CZ  PHE A 270     1689    811   1455    102     10     97       C  
ATOM   1399  N   GLU A 271     102.666  86.503 -25.671  1.00  8.98           N  
ANISOU 1399  N   GLU A 271     1474    798   1138   -128    -18    164       N  
ATOM   1400  CA  GLU A 271     102.742  85.418 -24.705  1.00 10.44           C  
ANISOU 1400  CA  GLU A 271     1785   1066   1116   -170    -79    202       C  
ATOM   1401  C   GLU A 271     101.337  85.040 -24.252  1.00 10.12           C  
ANISOU 1401  C   GLU A 271     1755    887   1204   -261     91     32       C  
ATOM   1402  O   GLU A 271     100.416  85.857 -24.280  1.00  9.93           O  
ANISOU 1402  O   GLU A 271     1425   1060   1288    -47     69     28       O  
ATOM   1403  CB  GLU A 271     103.587  85.856 -23.506  1.00 11.20           C  
ANISOU 1403  CB  GLU A 271     2093   1127   1034     -9   -438    220       C  
ATOM   1404  CG  GLU A 271     103.834  84.741 -22.497  1.00 13.89           C  
ANISOU 1404  CG  GLU A 271     2507   1421   1351     33   -591    322       C  
ATOM   1405  CD  GLU A 271     104.795  85.139 -21.397  1.00 15.76           C  
ANISOU 1405  CD  GLU A 271     2690   1543   1755    317   -538    153       C  
ATOM   1406  OE1 GLU A 271     105.482  86.176 -21.546  1.00 17.82           O  
ANISOU 1406  OE1 GLU A 271     2823   1929   2017     -3   -421     94       O  
ATOM   1407  OE2 GLU A 271     104.870  84.402 -20.389  1.00 18.19           O1-
ANISOU 1407  OE2 GLU A 271     3115   1829   1966    560   -522     92       O1-
ATOM   1408  N   VAL A 272     101.162  83.774 -23.875  1.00 10.04           N  
ANISOU 1408  N   VAL A 272     1710    867   1236   -140    119    -64       N  
ATOM   1409  CA  VAL A 272      99.887  83.283 -23.365  1.00 10.26           C  
ANISOU 1409  CA  VAL A 272     1541   1160   1196   -167    -68     49       C  
ATOM   1410  C   VAL A 272     100.128  82.521 -22.074  1.00 10.30           C  
ANISOU 1410  C   VAL A 272     1558    982   1374   -123    -30    161       C  
ATOM   1411  O   VAL A 272     101.076  81.736 -21.969  1.00 11.72           O  
ANISOU 1411  O   VAL A 272     1854   1014   1587    153    232    197       O  
ATOM   1412  CB  VAL A 272      99.171  82.368 -24.379  1.00 13.01           C  
ANISOU 1412  CB  VAL A 272     1992   1585   1367   -510   -182     87       C  
ATOM   1413  CG1 VAL A 272      97.833  81.881 -23.815  1.00 13.83           C  
ANISOU 1413  CG1 VAL A 272     1963   1832   1461   -558    -16    243       C  
ATOM   1414  CG2 VAL A 272      98.956  83.096 -25.666  1.00 13.50           C  
ANISOU 1414  CG2 VAL A 272     2266   1568   1297   -483   -253     53       C  
ATOM   1415  N   ARG A 273      99.286  82.784 -21.082  1.00 10.75           N  
ANISOU 1415  N   ARG A 273     1637   1292   1154   -280   -188    178       N  
ATOM   1416  CA  ARG A 273      99.160  81.933 -19.909  1.00 10.61           C  
ANISOU 1416  CA  ARG A 273     1701   1099   1231   -248     20     82       C  
ATOM   1417  C   ARG A 273      97.719  81.467 -19.841  1.00 10.39           C  
ANISOU 1417  C   ARG A 273     1658    862   1428   -118    135    177       C  
ATOM   1418  O   ARG A 273      96.800  82.292 -19.813  1.00 11.12           O  
ANISOU 1418  O   ARG A 273     1509    978   1738    -68     69    162       O  
ATOM   1419  CB  ARG A 273      99.512  82.691 -18.631  1.00 11.99           C  
ANISOU 1419  CB  ARG A 273     2028   1338   1188   -270    -70    -46       C  
ATOM   1420  CG  ARG A 273      99.271  81.872 -17.373  1.00 13.36           C  
ANISOU 1420  CG  ARG A 273     2382   1400   1293   -346   -257     59       C  
ATOM   1421  CD  ARG A 273      99.727  82.645 -16.157  1.00 16.40           C  
ANISOU 1421  CD  ARG A 273     3085   1749   1398   -261   -235     59       C  
ATOM   1422  NE  ARG A 273      99.349  81.972 -14.919  1.00 20.18           N  
ANISOU 1422  NE  ARG A 273     3606   2354   1707   -105   -214    250       N  
ATOM   1423  CZ  ARG A 273      99.958  80.889 -14.453  1.00 25.17           C  
ANISOU 1423  CZ  ARG A 273     4096   3332   2138    173   -200    572       C  
ATOM   1424  NH1 ARG A 273     100.962  80.350 -15.135  1.00 27.71           N1+
ANISOU 1424  NH1 ARG A 273     4235   3789   2506    288   -365    620       N1+
ATOM   1425  NH2 ARG A 273      99.553  80.336 -13.318  1.00 26.94           N  
ANISOU 1425  NH2 ARG A 273     4277   3651   2309     82   -228    954       N  
ATOM   1426  N   VAL A 274      97.519  80.156 -19.834  1.00 11.13           N  
ANISOU 1426  N   VAL A 274     1938    860   1431   -472    -33    384       N  
ATOM   1427  CA  VAL A 274      96.194  79.578 -19.684  1.00 11.29           C  
ANISOU 1427  CA  VAL A 274     1846    901   1543   -447     -7    244       C  
ATOM   1428  C   VAL A 274      96.079  79.152 -18.233  1.00 12.76           C  
ANISOU 1428  C   VAL A 274     2113   1108   1626   -163     -3    289       C  
ATOM   1429  O   VAL A 274      96.867  78.324 -17.763  1.00 13.37           O  
ANISOU 1429  O   VAL A 274     2306   1000   1773   -206    -30    368       O  
ATOM   1430  CB  VAL A 274      95.986  78.386 -20.628  1.00 11.12           C  
ANISOU 1430  CB  VAL A 274     1718    816   1690   -492    117     61       C  
ATOM   1431  CG1 VAL A 274      94.520  77.953 -20.597  1.00 11.89           C  
ANISOU 1431  CG1 VAL A 274     1729    941   1849   -293    -95    -28       C  
ATOM   1432  CG2 VAL A 274      96.425  78.749 -22.045  1.00 12.84           C  
ANISOU 1432  CG2 VAL A 274     2102   1058   1717   -479    158    107       C  
ATOM   1433  N   CYS A 275      95.131  79.744 -17.511  1.00 13.33           N  
ANISOU 1433  N   CYS A 275     2061   1303   1699   -348    102    284       N  
ATOM   1434  CA  CYS A 275      95.116  79.602 -16.067  1.00 14.18           C  
ANISOU 1434  CA  CYS A 275     2356   1373   1657   -284    119    112       C  
ATOM   1435  C   CYS A 275      93.698  79.750 -15.545  1.00 16.02           C  
ANISOU 1435  C   CYS A 275     2700   1663   1723   -379    272    175       C  
ATOM   1436  O   CYS A 275      92.795  80.198 -16.251  1.00 17.33           O  
ANISOU 1436  O   CYS A 275     2817   2059   1708   -400    336     81       O  
ATOM   1437  CB  CYS A 275      96.032  80.636 -15.410  1.00 14.94           C  
ANISOU 1437  CB  CYS A 275     2436   1498   1742   -436   -125    -12       C  
ATOM   1438  SG  CYS A 275      95.683  82.347 -15.872  1.00 16.94           S  
ANISOU 1438  SG  CYS A 275     2748   1694   1993   -328     38    -64       S  
ATOM   1439  N   ALA A 276      93.520  79.390 -14.272  1.00 16.82           N  
ANISOU 1439  N   ALA A 276     3010   1621   1762   -513    422    209       N  
ATOM   1440  CA  ALA A 276      92.185  79.402 -13.687  1.00 18.08           C  
ANISOU 1440  CA  ALA A 276     3199   1778   1891   -641    663    320       C  
ATOM   1441  C   ALA A 276      91.682  80.815 -13.420  1.00 18.91           C  
ANISOU 1441  C   ALA A 276     3211   2065   1908   -607    512    195       C  
ATOM   1442  O   ALA A 276      90.476  81.065 -13.515  1.00 20.33           O  
ANISOU 1442  O   ALA A 276     3367   2322   2034   -587    644    263       O  
ATOM   1443  CB  ALA A 276      92.161  78.574 -12.399  1.00 20.33           C  
ANISOU 1443  CB  ALA A 276     3555   2035   2135   -671    671    559       C  
ATOM   1444  N   CYS A 277      92.569  81.752 -13.086  1.00 17.86           N  
ANISOU 1444  N   CYS A 277     2988   2133   1664   -699    454    156       N  
ATOM   1445  CA ACYS A 277      92.172  83.105 -12.698  0.71 18.37           C  
ANISOU 1445  CA ACYS A 277     3086   2297   1598   -584    308    114       C  
ATOM   1446  CA BCYS A 277      92.181  83.105 -12.685  0.29 18.24           C  
ANISOU 1446  CA BCYS A 277     3071   2201   1657   -668    375    109       C  
ATOM   1447  C   CYS A 277      93.016  84.125 -13.446  1.00 16.75           C  
ANISOU 1447  C   CYS A 277     2744   2123   1498   -646    209     63       C  
ATOM   1448  O   CYS A 277      93.949  84.719 -12.886  1.00 17.24           O  
ANISOU 1448  O   CYS A 277     2794   2225   1530   -490     69      7       O  
ATOM   1449  CB ACYS A 277      92.258  83.309 -11.188  0.71 20.03           C  
ANISOU 1449  CB ACYS A 277     3403   2707   1502   -427    300     47       C  
ATOM   1450  CB BCYS A 277      92.349  83.301 -11.177  0.29 19.86           C  
ANISOU 1450  CB BCYS A 277     3426   2363   1759   -673    472     69       C  
ATOM   1451  SG ACYS A 277      91.415  84.804 -10.640  0.71 21.63           S  
ANISOU 1451  SG ACYS A 277     3552   3187   1480   -428    341   -206       S  
ATOM   1452  SG BCYS A 277      91.473  82.100 -10.155  0.29 21.48           S  
ANISOU 1452  SG BCYS A 277     3721   2564   1878   -770    578    -33       S  
ATOM   1453  N   PRO A 278      92.694  84.369 -14.716  1.00 15.61           N  
ANISOU 1453  N   PRO A 278     2577   1920   1434   -532    152     33       N  
ATOM   1454  CA  PRO A 278      93.489  85.317 -15.513  1.00 15.03           C  
ANISOU 1454  CA  PRO A 278     2527   1758   1426   -673    132    -92       C  
ATOM   1455  C   PRO A 278      93.566  86.709 -14.926  1.00 14.83           C  
ANISOU 1455  C   PRO A 278     2412   1774   1448   -341     89    -16       C  
ATOM   1456  O   PRO A 278      94.598  87.371 -15.066  1.00 14.55           O  
ANISOU 1456  O   PRO A 278     2220   1725   1585   -322    216    -18       O  
ATOM   1457  CB  PRO A 278      92.749  85.340 -16.855  1.00 16.15           C  
ANISOU 1457  CB  PRO A 278     2873   1892   1371   -615    -83    -84       C  
ATOM   1458  CG  PRO A 278      91.992  84.082 -16.911  1.00 17.61           C  
ANISOU 1458  CG  PRO A 278     3136   2048   1506   -657      0    143       C  
ATOM   1459  CD  PRO A 278      91.671  83.677 -15.514  1.00 16.51           C  
ANISOU 1459  CD  PRO A 278     2835   1960   1478   -527   -102     49       C  
ATOM   1460  N   GLY A 279      92.487  87.192 -14.312  1.00 14.82           N  
ANISOU 1460  N   GLY A 279     2478   1714   1441   -179    124     -6       N  
ATOM   1461  CA  GLY A 279      92.510  88.535 -13.757  1.00 15.43           C  
ANISOU 1461  CA  GLY A 279     2664   1644   1557   -272    112    -49       C  
ATOM   1462  C   GLY A 279      93.522  88.681 -12.640  1.00 15.94           C  
ANISOU 1462  C   GLY A 279     2688   1727   1640   -390    188   -147       C  
ATOM   1463  O   GLY A 279      94.307  89.634 -12.614  1.00 16.00           O  
ANISOU 1463  O   GLY A 279     2648   1757   1674   -382    170   -430       O  
ATOM   1464  N   ARG A 280      93.519  87.733 -11.701  1.00 17.17           N  
ANISOU 1464  N   ARG A 280     2923   2033   1567   -311      3     -6       N  
ATOM   1465  CA  ARG A 280      94.494  87.770 -10.620  1.00 17.78           C  
ANISOU 1465  CA  ARG A 280     3146   2090   1520   -246    -44     37       C  
ATOM   1466  C   ARG A 280      95.904  87.566 -11.151  1.00 17.36           C  
ANISOU 1466  C   ARG A 280     2998   2168   1429   -374   -143    -75       C  
ATOM   1467  O   ARG A 280      96.839  88.253 -10.725  1.00 17.44           O  
ANISOU 1467  O   ARG A 280     2817   2272   1539   -466    -89    -33       O  
ATOM   1468  CB  ARG A 280      94.165  86.712  -9.571  1.00 20.09           C  
ANISOU 1468  CB  ARG A 280     3449   2457   1730   -526   -117    163       C  
ATOM   1469  CG  ARG A 280      95.185  86.657  -8.453  1.00 21.86           C  
ANISOU 1469  CG  ARG A 280     3667   2818   1819   -697    -90    362       C  
ATOM   1470  N   ASP A 281      96.084  86.630 -12.084  1.00 16.11           N  
ANISOU 1470  N   ASP A 281     2953   1805   1363   -310   -200    -20       N  
ATOM   1471  CA  ASP A 281      97.433  86.383 -12.579  1.00 16.30           C  
ANISOU 1471  CA  ASP A 281     2972   1816   1405   -188   -227     96       C  
ATOM   1472  C   ASP A 281      97.970  87.577 -13.354  1.00 15.50           C  
ANISOU 1472  C   ASP A 281     2717   1670   1502   -191   -283     71       C  
ATOM   1473  O   ASP A 281      99.152  87.914 -13.232  1.00 16.08           O  
ANISOU 1473  O   ASP A 281     2670   1814   1626   -323   -293    303       O  
ATOM   1474  CB  ASP A 281      97.485  85.104 -13.404  1.00 18.77           C  
ANISOU 1474  CB  ASP A 281     3595   1995   1542   -280    -96    276       C  
ATOM   1475  CG  ASP A 281      97.361  83.866 -12.547  1.00 21.89           C  
ANISOU 1475  CG  ASP A 281     4430   2358   1527   -334   -138    365       C  
ATOM   1476  OD1 ASP A 281      97.364  83.986 -11.294  1.00 23.95           O  
ANISOU 1476  OD1 ASP A 281     4767   2732   1602   -407    114    424       O  
ATOM   1477  OD2 ASP A 281      97.266  82.770 -13.125  1.00 23.99           O1-
ANISOU 1477  OD2 ASP A 281     4907   2452   1755   -206    -94    315       O1-
ATOM   1478  N   ARG A 282      97.122  88.239 -14.147  1.00 15.07           N  
ANISOU 1478  N   ARG A 282     2703   1540   1483    -76   -143     21       N  
ATOM   1479  CA  ARG A 282      97.578  89.448 -14.822  1.00 14.75           C  
ANISOU 1479  CA  ARG A 282     2684   1432   1488   -339   -214   -138       C  
ATOM   1480  C   ARG A 282      97.969  90.518 -13.813  1.00 15.66           C  
ANISOU 1480  C   ARG A 282     2762   1677   1512   -684   -118   -110       C  
ATOM   1481  O   ARG A 282      99.017  91.155 -13.950  1.00 16.45           O  
ANISOU 1481  O   ARG A 282     2689   1859   1701   -868   -190     65       O  
ATOM   1482  CB  ARG A 282      96.516  89.987 -15.773  1.00 13.99           C  
ANISOU 1482  CB  ARG A 282     2490   1351   1474   -325   -191     40       C  
ATOM   1483  CG  ARG A 282      96.929  91.326 -16.366  1.00 13.27           C  
ANISOU 1483  CG  ARG A 282     2378   1159   1506   -307    -83    119       C  
ATOM   1484  CD  ARG A 282      95.960  91.846 -17.423  1.00 11.98           C  
ANISOU 1484  CD  ARG A 282     2190    931   1433    -65   -125     -5       C  
ATOM   1485  NE  ARG A 282      96.242  93.242 -17.725  1.00 12.21           N  
ANISOU 1485  NE  ARG A 282     2002   1138   1499   -149     52   -123       N  
ATOM   1486  CZ  ARG A 282      95.382  94.088 -18.278  1.00 13.10           C  
ANISOU 1486  CZ  ARG A 282     2061   1347   1571   -284   -113   -221       C  
ATOM   1487  NH1 ARG A 282      94.170  93.686 -18.636  1.00 13.61           N1+
ANISOU 1487  NH1 ARG A 282     2025   1650   1498   -273    -75   -407       N1+
ATOM   1488  NH2 ARG A 282      95.745  95.353 -18.463  1.00 14.80           N  
ANISOU 1488  NH2 ARG A 282     2445   1347   1832   -174   -225    -85       N  
ATOM   1489  N   ARG A 283      97.152  90.713 -12.773  1.00 16.94           N  
ANISOU 1489  N   ARG A 283     2877   2015   1546   -586    -15   -397       N  
ATOM   1490  CA  ARG A 283      97.501  91.702 -11.757  1.00 19.19           C  
ANISOU 1490  CA  ARG A 283     3089   2383   1820   -741    -30   -548       C  
ATOM   1491  C   ARG A 283      98.814  91.350 -11.067  1.00 19.42           C  
ANISOU 1491  C   ARG A 283     3020   2638   1719   -918   -275   -357       C  
ATOM   1492  O   ARG A 283      99.664  92.222 -10.855  1.00 20.06           O  
ANISOU 1492  O   ARG A 283     3136   2767   1717  -1106   -441   -485       O  
ATOM   1493  CB  ARG A 283      96.366  91.847 -10.744  1.00 20.88           C  
ANISOU 1493  CB  ARG A 283     3481   2459   1993   -446    145   -759       C  
ATOM   1494  CG  ARG A 283      95.280  92.803 -11.196  1.00 23.89           C  
ANISOU 1494  CG  ARG A 283     3773   2968   2334   -474    208   -770       C  
ATOM   1495  CD  ARG A 283      94.188  92.969 -10.155  1.00 25.37           C  
ANISOU 1495  CD  ARG A 283     3920   3155   2563   -521    269   -802       C  
ATOM   1496  NE  ARG A 283      93.147  91.956 -10.289  1.00 27.14           N  
ANISOU 1496  NE  ARG A 283     4119   3537   2659   -386    193   -825       N  
ATOM   1497  CZ  ARG A 283      92.911  90.999  -9.398  1.00 27.86           C  
ANISOU 1497  CZ  ARG A 283     4172   3781   2632   -255    182   -785       C  
ATOM   1498  NH1 ARG A 283      93.643  90.918  -8.293  1.00 28.53           N1+
ANISOU 1498  NH1 ARG A 283     4257   4058   2525   -121    201   -936       N1+
ATOM   1499  NH2 ARG A 283      91.936  90.125  -9.609  1.00 28.08           N  
ANISOU 1499  NH2 ARG A 283     4189   3784   2696   -250    202   -782       N  
ATOM   1500  N   THR A 284      99.004  90.073 -10.728  1.00 19.47           N  
ANISOU 1500  N   THR A 284     2832   2804   1760   -727   -281   -176       N  
ATOM   1501  CA  THR A 284     100.226  89.654 -10.048  1.00 20.60           C  
ANISOU 1501  CA  THR A 284     2896   3126   1805   -684   -373    172       C  
ATOM   1502  C   THR A 284     101.447  89.869 -10.929  1.00 20.13           C  
ANISOU 1502  C   THR A 284     2805   3006   1839   -577   -510    221       C  
ATOM   1503  O   THR A 284     102.474  90.381 -10.473  1.00 21.55           O  
ANISOU 1503  O   THR A 284     3024   3184   1981   -755   -506    144       O  
ATOM   1504  CB  THR A 284     100.106  88.185  -9.643  1.00 22.94           C  
ANISOU 1504  CB  THR A 284     3227   3569   1918   -371   -548    537       C  
ATOM   1505  OG1 THR A 284      99.024  88.042  -8.719  1.00 25.18           O  
ANISOU 1505  OG1 THR A 284     3629   4026   1911   -440   -222    461       O  
ATOM   1506  CG2 THR A 284     101.401  87.678  -8.991  1.00 24.72           C  
ANISOU 1506  CG2 THR A 284     3434   3813   2147   -343   -665    684       C  
ATOM   1507  N   GLU A 285     101.354  89.488 -12.202  1.00 18.56           N  
ANISOU 1507  N   GLU A 285     2817   2538   1697   -261   -512    326       N  
ATOM   1508  CA  GLU A 285     102.523  89.597 -13.067  1.00 18.96           C  
ANISOU 1508  CA  GLU A 285     2922   2454   1829   -267   -487    223       C  
ATOM   1509  C   GLU A 285     102.830  91.048 -13.409  1.00 19.60           C  
ANISOU 1509  C   GLU A 285     2931   2549   1968   -426   -495    136       C  
ATOM   1510  O   GLU A 285     104.002  91.428 -13.510  1.00 20.20           O  
ANISOU 1510  O   GLU A 285     2773   2786   2117   -416   -521    300       O  
ATOM   1511  CB  GLU A 285     102.353  88.734 -14.318  1.00 19.47           C  
ANISOU 1511  CB  GLU A 285     3173   2415   1808   -297   -747    352       C  
ATOM   1512  CG  GLU A 285     102.259  87.252 -13.982  1.00 20.60           C  
ANISOU 1512  CG  GLU A 285     3388   2412   2029   -181   -783    402       C  
ATOM   1513  CD  GLU A 285     102.395  86.351 -15.184  1.00 22.10           C  
ANISOU 1513  CD  GLU A 285     3549   2595   2254   -258   -721    437       C  
ATOM   1514  OE1 GLU A 285     102.944  86.797 -16.212  1.00 23.06           O  
ANISOU 1514  OE1 GLU A 285     3678   2868   2216     57   -816    424       O  
ATOM   1515  OE2 GLU A 285     101.958  85.183 -15.092  1.00 22.74           O1-
ANISOU 1515  OE2 GLU A 285     3581   2595   2464   -609   -740    390       O1-
ATOM   1516  N   GLU A 286     101.797  91.878 -13.579  1.00 19.12           N  
ANISOU 1516  N   GLU A 286     2984   2349   1932   -511   -482   -207       N  
ATOM   1517  CA  GLU A 286     102.043  93.304 -13.780  1.00 18.67           C  
ANISOU 1517  CA  GLU A 286     2995   2177   1922   -891   -658   -322       C  
ATOM   1518  C   GLU A 286     102.656  93.941 -12.541  1.00 21.78           C  
ANISOU 1518  C   GLU A 286     3464   2755   2058  -1319   -767   -251       C  
ATOM   1519  O   GLU A 286     103.513  94.824 -12.653  1.00 22.58           O  
ANISOU 1519  O   GLU A 286     3591   2840   2150  -1469   -721   -295       O  
ATOM   1520  CB  GLU A 286     100.756  94.023 -14.187  1.00 17.69           C  
ANISOU 1520  CB  GLU A 286     2749   2071   1902   -372   -384   -419       C  
ATOM   1521  CG  GLU A 286     100.293  93.637 -15.580  1.00 17.24           C  
ANISOU 1521  CG  GLU A 286     2572   2142   1835    -56   -322   -512       C  
ATOM   1522  CD  GLU A 286      99.183  94.519 -16.122  1.00 17.63           C  
ANISOU 1522  CD  GLU A 286     2571   2120   2006    -14    -82   -747       C  
ATOM   1523  OE1 GLU A 286      98.668  95.384 -15.384  1.00 21.92           O  
ANISOU 1523  OE1 GLU A 286     2998   3091   2240    364   -124   -958       O  
ATOM   1524  OE2 GLU A 286      98.826  94.341 -17.299  1.00 15.52           O1-
ANISOU 1524  OE2 GLU A 286     2452   1516   1928   -195   -100   -724       O1-
ATOM   1525  N   GLU A 287     102.229  93.507 -11.352  1.00 25.12           N  
ANISOU 1525  N   GLU A 287     3855   3458   2232  -1442   -872   -101       N  
ATOM   1526  CA  GLU A 287     102.843  93.991 -10.121  1.00 27.26           C  
ANISOU 1526  CA  GLU A 287     3981   4014   2363  -1628   -969    -24       C  
ATOM   1527  C   GLU A 287     104.297  93.551 -10.030  1.00 29.11           C  
ANISOU 1527  C   GLU A 287     3976   4478   2608  -1794  -1175    115       C  
ATOM   1528  O   GLU A 287     105.171  94.339  -9.647  1.00 31.01           O  
ANISOU 1528  O   GLU A 287     4257   4720   2806  -1784  -1150    106       O  
ATOM   1529  CB  GLU A 287     102.051  93.484  -8.916  1.00 26.85           C  
ANISOU 1529  CB  GLU A 287     4034   3999   2168  -1594  -1072     42       C  
ATOM   1530  N   ASN A 288     104.578  92.295 -10.387  1.00 30.22           N  
ANISOU 1530  N   ASN A 288     3903   4814   2765  -1789  -1237    373       N  
ATOM   1531  CA  ASN A 288     105.958  91.817 -10.382  1.00 32.43           C  
ANISOU 1531  CA  ASN A 288     4025   5207   3090  -1668  -1143    467       C  
ATOM   1532  C   ASN A 288     106.817  92.612 -11.357  1.00 32.15           C  
ANISOU 1532  C   ASN A 288     3799   5202   3214  -1870  -1096    395       C  
ATOM   1533  O   ASN A 288     107.990  92.887 -11.082  1.00 32.71           O  
ANISOU 1533  O   ASN A 288     3783   5354   3289  -2088  -1152    404       O  
ATOM   1534  CB  ASN A 288     106.007  90.326 -10.721  1.00 35.18           C  
ANISOU 1534  CB  ASN A 288     4411   5609   3345  -1232  -1105    599       C  
ATOM   1535  CG  ASN A 288     105.359  89.457  -9.655  1.00 37.41           C  
ANISOU 1535  CG  ASN A 288     4599   6049   3567   -890  -1090    549       C  
ATOM   1536  OD1 ASN A 288     105.165  89.885  -8.518  1.00 38.57           O  
ANISOU 1536  OD1 ASN A 288     4790   6274   3592   -653  -1083    632       O  
ATOM   1537  ND2 ASN A 288     105.033  88.222 -10.019  1.00 38.28           N  
ANISOU 1537  ND2 ASN A 288     4659   6158   3726   -741  -1042    569       N  
ATOM   1538  N   LEU A 289     106.248  92.992 -12.502  1.00 31.46           N  
ANISOU 1538  N   LEU A 289     3715   5002   3236  -1808   -907    377       N  
ATOM   1539  CA  LEU A 289     106.991  93.795 -13.468  1.00 30.73           C  
ANISOU 1539  CA  LEU A 289     3541   4839   3297  -1970   -921    170       C  
ATOM   1540  C   LEU A 289     107.258  95.196 -12.930  1.00 32.95           C  
ANISOU 1540  C   LEU A 289     3822   5150   3549  -2133   -852    -88       C  
ATOM   1541  O   LEU A 289     108.356  95.737 -13.109  1.00 33.65           O  
ANISOU 1541  O   LEU A 289     3931   5269   3587  -2207   -880   -125       O  
ATOM   1542  CB  LEU A 289     106.224  93.850 -14.794  1.00 28.90           C  
ANISOU 1542  CB  LEU A 289     3314   4489   3176  -1947   -765    297       C  
ATOM   1543  CG  LEU A 289     106.836  94.705 -15.903  1.00 29.12           C  
ANISOU 1543  CG  LEU A 289     3404   4419   3241  -1669   -476    306       C  
ATOM   1544  CD1 LEU A 289     108.185  94.145 -16.339  1.00 30.21           C  
ANISOU 1544  CD1 LEU A 289     3584   4513   3381  -1526   -295    318       C  
ATOM   1545  CD2 LEU A 289     105.876  94.815 -17.077  1.00 28.38           C  
ANISOU 1545  CD2 LEU A 289     3276   4299   3208  -1637   -462    407       C  
ATOM   1546  N   ARG A 290     106.271  95.793 -12.258  1.00 34.88           N  
ANISOU 1546  N   ARG A 290     4126   5364   3764  -2156   -782   -442       N  
ATOM   1547  CA  ARG A 290     106.466  97.120 -11.680  1.00 37.28           C  
ANISOU 1547  CA  ARG A 290     4486   5700   3979  -2118   -739   -743       C  
ATOM   1548  C   ARG A 290     107.504  97.091 -10.565  1.00 39.68           C  
ANISOU 1548  C   ARG A 290     4860   6017   4201  -2136   -792   -962       C  
ATOM   1549  O   ARG A 290     108.351  97.989 -10.474  1.00 41.33           O  
ANISOU 1549  O   ARG A 290     5223   6125   4355  -2043   -656  -1032       O  
ATOM   1550  CB  ARG A 290     105.136  97.670 -11.165  1.00 37.68           C  
ANISOU 1550  CB  ARG A 290     4580   5757   3982  -1924   -587   -730       C  
ATOM   1551  N   LYS A 291     107.458  96.067  -9.709  1.00 40.80           N  
ANISOU 1551  N   LYS A 291     4929   6308   4267  -2070  -1014  -1099       N  
ATOM   1552  CA  LYS A 291     108.442  95.960  -8.637  1.00 42.20           C  
ANISOU 1552  CA  LYS A 291     5040   6635   4360  -1927  -1278  -1168       C  
ATOM   1553  C   LYS A 291     109.843  95.706  -9.182  1.00 44.05           C  
ANISOU 1553  C   LYS A 291     5223   6985   4527  -1746  -1239  -1176       C  
ATOM   1554  O   LYS A 291     110.834  96.059  -8.531  1.00 45.09           O  
ANISOU 1554  O   LYS A 291     5436   7082   4616  -1569  -1258  -1099       O  
ATOM   1555  CB  LYS A 291     108.029  94.868  -7.648  1.00 41.84           C  
ANISOU 1555  CB  LYS A 291     4980   6595   4321  -1984  -1408  -1202       C  
ATOM   1556  N   LYS A 292     109.948  95.107 -10.364  1.00 45.21           N  
ANISOU 1556  N   LYS A 292     5251   7278   4648  -1718  -1082  -1145       N  
ATOM   1557  CA  LYS A 292     111.239  94.901 -11.011  1.00 46.33           C  
ANISOU 1557  CA  LYS A 292     5384   7517   4704  -1675   -903  -1157       C  
ATOM   1558  C   LYS A 292     111.571  96.081 -11.922  1.00 46.94           C  
ANISOU 1558  C   LYS A 292     5445   7639   4750  -1691   -740  -1145       C  
ATOM   1559  O   LYS A 292     112.452  96.885 -11.619  1.00 48.20           O  
ANISOU 1559  O   LYS A 292     5716   7789   4808  -1518   -543  -1080       O  
ATOM   1560  CB  LYS A 292     111.235  93.600 -11.818  1.00 46.66           C  
ANISOU 1560  CB  LYS A 292     5419   7572   4737  -1658   -880  -1140       C  
TER    1561      LYS A 292                                                      
ATOM   1562  N   SER B  94     145.246  76.066 -31.210  1.00 40.21           N  
ANISOU 1562  N   SER B  94     5155   5510   4611    179    -98    451       N  
ATOM   1563  CA  SER B  94     145.115  77.517 -31.163  1.00 39.31           C  
ANISOU 1563  CA  SER B  94     4948   5452   4535    200     28    544       C  
ATOM   1564  C   SER B  94     145.051  78.101 -32.573  1.00 36.32           C  
ANISOU 1564  C   SER B  94     4492   5105   4203    264    258    593       C  
ATOM   1565  O   SER B  94     145.409  77.439 -33.548  1.00 35.32           O  
ANISOU 1565  O   SER B  94     4301   5036   4082    381    496    525       O  
ATOM   1566  CB  SER B  94     146.272  78.131 -30.378  1.00 41.14           C  
ANISOU 1566  CB  SER B  94     5117   5771   4745    230    -40    428       C  
ATOM   1567  OG  SER B  94     147.506  77.802 -30.986  1.00 43.05           O  
ANISOU 1567  OG  SER B  94     5323   6089   4943    323   -141    375       O  
ATOM   1568  N   SER B  95     144.595  79.347 -32.675  1.00 33.18           N  
ANISOU 1568  N   SER B  95     3983   4686   3936     81    289    642       N  
ATOM   1569  CA  SER B  95     144.291  79.955 -33.959  1.00 30.81           C  
ANISOU 1569  CA  SER B  95     3636   4344   3725    146    210    673       C  
ATOM   1570  C   SER B  95     144.923  81.336 -34.043  1.00 30.36           C  
ANISOU 1570  C   SER B  95     3890   3988   3658    417    414    497       C  
ATOM   1571  O   SER B  95     145.238  81.958 -33.026  1.00 31.47           O  
ANISOU 1571  O   SER B  95     4285   4064   3611    501    262    368       O  
ATOM   1572  CB  SER B  95     142.778  80.078 -34.147  1.00 29.89           C  
ANISOU 1572  CB  SER B  95     3288   4507   3564    102    -10    715       C  
ATOM   1573  OG  SER B  95     142.155  78.829 -33.925  1.00 28.31           O  
ANISOU 1573  OG  SER B  95     2991   4381   3383     77   -127    632       O  
ATOM   1574  N   SER B  96     145.103  81.811 -35.275  1.00 28.45           N  
ANISOU 1574  N   SER B  96     3727   3533   3552    689    742    296       N  
ATOM   1575  CA  SER B  96     145.616  83.158 -35.481  1.00 27.32           C  
ANISOU 1575  CA  SER B  96     3665   3247   3467    896    888    366       C  
ATOM   1576  C   SER B  96     144.644  84.175 -34.895  1.00 24.86           C  
ANISOU 1576  C   SER B  96     3280   2776   3388    783    929    349       C  
ATOM   1577  O   SER B  96     143.468  83.880 -34.651  1.00 26.46           O  
ANISOU 1577  O   SER B  96     3752   2760   3541    627    956    458       O  
ATOM   1578  CB  SER B  96     145.819  83.429 -36.969  1.00 27.84           C  
ANISOU 1578  CB  SER B  96     3538   3537   3501   1017    981    286       C  
ATOM   1579  OG  SER B  96     144.637  83.135 -37.688  1.00 30.46           O  
ANISOU 1579  OG  SER B  96     4028   3888   3658    752    820     13       O  
ATOM   1580  N   VAL B  97     145.139  85.387 -34.672  1.00 21.29           N  
ANISOU 1580  N   VAL B  97     2743   2205   3143    650    595    325       N  
ATOM   1581  CA  VAL B  97     144.416  86.396 -33.902  1.00 19.69           C  
ANISOU 1581  CA  VAL B  97     2454   1949   3078    552    451    256       C  
ATOM   1582  C   VAL B  97     143.860  87.442 -34.861  1.00 17.27           C  
ANISOU 1582  C   VAL B  97     1869   1632   3062    286    307    126       C  
ATOM   1583  O   VAL B  97     144.633  88.155 -35.516  1.00 18.16           O  
ANISOU 1583  O   VAL B  97     1895   1946   3059    116    185    435       O  
ATOM   1584  CB  VAL B  97     145.290  87.044 -32.818  1.00 21.40           C  
ANISOU 1584  CB  VAL B  97     2803   2103   3224    842    436    311       C  
ATOM   1585  CG1 VAL B  97     144.459  88.034 -32.002  1.00 22.25           C  
ANISOU 1585  CG1 VAL B  97     3015   2083   3357    943    465    366       C  
ATOM   1586  CG2 VAL B  97     145.879  85.981 -31.910  1.00 22.01           C  
ANISOU 1586  CG2 VAL B  97     2933   2243   3186    892    247    533       C  
ATOM   1587  N   PRO B  98     142.545  87.571 -34.968  1.00 17.26           N  
ANISOU 1587  N   PRO B  98     1762   1588   3206    208    -47    171       N  
ATOM   1588  CA  PRO B  98     141.967  88.621 -35.806  1.00 17.83           C  
ANISOU 1588  CA  PRO B  98     1731   1671   3373     32   -165    245       C  
ATOM   1589  C   PRO B  98     142.358  89.995 -35.290  1.00 18.07           C  
ANISOU 1589  C   PRO B  98     1903   1711   3251    173   -148    268       C  
ATOM   1590  O   PRO B  98     142.490  90.220 -34.085  1.00 18.95           O  
ANISOU 1590  O   PRO B  98     2286   1712   3203    -36    -86    160       O  
ATOM   1591  CB  PRO B  98     140.459  88.390 -35.660  1.00 19.39           C  
ANISOU 1591  CB  PRO B  98     1799   1875   3692    154   -301    125       C  
ATOM   1592  CG  PRO B  98     140.337  86.974 -35.191  1.00 21.25           C  
ANISOU 1592  CG  PRO B  98     2070   2305   3698    -26   -227    214       C  
ATOM   1593  CD  PRO B  98     141.520  86.730 -34.338  1.00 18.87           C  
ANISOU 1593  CD  PRO B  98     1952   1781   3437     47    -66    208       C  
ATOM   1594  N   SER B  99     142.545  90.921 -36.222  1.00 17.53           N  
ANISOU 1594  N   SER B  99     2052   1459   3150     81     79    355       N  
ATOM   1595  CA  SER B  99     142.889  92.282 -35.850  1.00 17.21           C  
ANISOU 1595  CA  SER B  99     2310   1316   2914     65    152    355       C  
ATOM   1596  C   SER B  99     141.725  92.933 -35.122  1.00 16.22           C  
ANISOU 1596  C   SER B  99     2147   1270   2746    -66    190    170       C  
ATOM   1597  O   SER B  99     140.556  92.707 -35.448  1.00 15.90           O  
ANISOU 1597  O   SER B  99     1963   1322   2755   -232    415    132       O  
ATOM   1598  CB  SER B  99     143.221  93.103 -37.094  1.00 18.41           C  
ANISOU 1598  CB  SER B  99     2645   1386   2962   -214    355    307       C  
ATOM   1599  OG  SER B  99     143.364  94.471 -36.749  1.00 20.70           O  
ANISOU 1599  OG  SER B  99     2928   1731   3208    -52    272    110       O  
ATOM   1600  N   GLN B 100     142.051  93.740 -34.119  1.00 17.20           N  
ANISOU 1600  N   GLN B 100     2325   1488   2720   -278    113     49       N  
ATOM   1601  CA  GLN B 100     141.065  94.553 -33.428  1.00 17.26           C  
ANISOU 1601  CA  GLN B 100     2365   1716   2479   -342    129     57       C  
ATOM   1602  C   GLN B 100     141.309  96.036 -33.643  1.00 17.41           C  
ANISOU 1602  C   GLN B 100     2421   1782   2411   -409    253    141       C  
ATOM   1603  O   GLN B 100     140.720  96.859 -32.936  1.00 19.94           O  
ANISOU 1603  O   GLN B 100     2921   2197   2459   -250    521    138       O  
ATOM   1604  CB  GLN B 100     141.085  94.253 -31.932  1.00 17.22           C  
ANISOU 1604  CB  GLN B 100     2427   1753   2361   -570   -168    180       C  
ATOM   1605  CG  GLN B 100     142.415  94.586 -31.272  1.00 20.41           C  
ANISOU 1605  CG  GLN B 100     2856   2322   2575   -507   -165    353       C  
ATOM   1606  CD  GLN B 100     142.393  94.284 -29.796  1.00 23.62           C  
ANISOU 1606  CD  GLN B 100     3113   2966   2896   -341   -119    454       C  
ATOM   1607  OE1 GLN B 100     142.699  93.169 -29.376  1.00 25.73           O  
ANISOU 1607  OE1 GLN B 100     3223   3335   3217   -279    -72    609       O  
ATOM   1608  NE2 GLN B 100     142.021  95.275 -28.997  1.00 24.20           N  
ANISOU 1608  NE2 GLN B 100     3136   3203   2858    -34   -203    259       N  
ATOM   1609  N  ALYS B 101     142.158  96.399 -34.601  0.59 16.51           N  
ANISOU 1609  N  ALYS B 101     2266   1628   2380   -485    221    148       N  
ATOM   1610  N  BLYS B 101     142.165  96.401 -34.593  0.41 16.66           N  
ANISOU 1610  N  BLYS B 101     2253   1735   2341   -378    220    206       N  
ATOM   1611  CA ALYS B 101     142.529  97.797 -34.777  0.59 16.65           C  
ANISOU 1611  CA ALYS B 101     2359   1572   2395   -466    132    115       C  
ATOM   1612  CA BLYS B 101     142.534  97.800 -34.760  0.41 16.55           C  
ANISOU 1612  CA BLYS B 101     2261   1727   2299   -284    145    251       C  
ATOM   1613  C  ALYS B 101     141.368  98.585 -35.368  0.59 16.20           C  
ANISOU 1613  C  ALYS B 101     2335   1605   2217   -484    105     48       C  
ATOM   1614  C  BLYS B 101     141.382  98.588 -35.369  0.41 16.06           C  
ANISOU 1614  C  BLYS B 101     2271   1668   2163   -391    128    143       C  
ATOM   1615  O  ALYS B 101     140.782  98.190 -36.382  0.59 16.00           O  
ANISOU 1615  O  ALYS B 101     2372   1553   2152   -547    -64     -8       O  
ATOM   1616  O  BLYS B 101     140.816  98.196 -36.394  0.41 16.07           O  
ANISOU 1616  O  BLYS B 101     2315   1670   2120   -424      2    115       O  
ATOM   1617  CB ALYS B 101     143.749  97.906 -35.688  0.59 17.38           C  
ANISOU 1617  CB ALYS B 101     2432   1571   2599   -643    171     87       C  
ATOM   1618  CB BLYS B 101     143.777  97.913 -35.641  0.41 17.00           C  
ANISOU 1618  CB BLYS B 101     2235   1822   2401   -211    152    360       C  
ATOM   1619  CG ALYS B 101     144.323  99.310 -35.782  0.59 18.28           C  
ANISOU 1619  CG ALYS B 101     2666   1581   2697   -582    229     29       C  
ATOM   1620  CG BLYS B 101     145.026  97.301 -35.024  0.41 17.41           C  
ANISOU 1620  CG BLYS B 101     2293   1885   2437     16    151    477       C  
ATOM   1621  N   THR B 102     141.035  99.702 -34.731  1.00 14.72           N  
ANISOU 1621  N   THR B 102     2177   1416   1999   -467    183    144       N  
ATOM   1622  CA  THR B 102     139.960 100.542 -35.232  1.00 13.46           C  
ANISOU 1622  CA  THR B 102     2063   1272   1779   -595    201    156       C  
ATOM   1623  C   THR B 102     140.322 101.073 -36.611  1.00 13.94           C  
ANISOU 1623  C   THR B 102     2224   1351   1724   -725    315     20       C  
ATOM   1624  O   THR B 102     141.452 101.506 -36.855  1.00 15.56           O  
ANISOU 1624  O   THR B 102     2322   1570   2022   -802    357    140       O  
ATOM   1625  CB  THR B 102     139.744 101.704 -34.272  1.00 15.06           C  
ANISOU 1625  CB  THR B 102     2337   1549   1834   -332     62     45       C  
ATOM   1626  OG1 THR B 102     139.350 101.174 -33.004  1.00 16.54           O  
ANISOU 1626  OG1 THR B 102     2545   1872   1866   -309    114     72       O  
ATOM   1627  CG2 THR B 102     138.666 102.623 -34.787  1.00 15.90           C  
ANISOU 1627  CG2 THR B 102     2537   1669   1837     81     88     59       C  
ATOM   1628  N   TYR B 103     139.351 101.034 -37.517  1.00 13.95           N  
ANISOU 1628  N   TYR B 103     2247   1414   1638   -673    369    -94       N  
ATOM   1629  CA  TYR B 103     139.592 101.422 -38.903  1.00 14.03           C  
ANISOU 1629  CA  TYR B 103     2440   1340   1552   -443    474    -53       C  
ATOM   1630  C   TYR B 103     138.272 101.962 -39.439  1.00 13.17           C  
ANISOU 1630  C   TYR B 103     2438   1049   1518   -357    508     52       C  
ATOM   1631  O   TYR B 103     137.354 101.186 -39.703  1.00 13.35           O  
ANISOU 1631  O   TYR B 103     2573    936   1562   -631    336    -76       O  
ATOM   1632  CB  TYR B 103     140.059 100.217 -39.702  1.00 16.49           C  
ANISOU 1632  CB  TYR B 103     2742   1859   1665   -365    689   -117       C  
ATOM   1633  CG  TYR B 103     140.261 100.496 -41.174  1.00 19.80           C  
ANISOU 1633  CG  TYR B 103     3344   2361   1819   -102    880    -11       C  
ATOM   1634  CD1 TYR B 103     141.178 101.440 -41.600  1.00 22.21           C  
ANISOU 1634  CD1 TYR B 103     3758   2806   1874   -187   1234    105       C  
ATOM   1635  CD2 TYR B 103     139.536  99.804 -42.136  1.00 21.74           C  
ANISOU 1635  CD2 TYR B 103     3517   2851   1893    288    767    -79       C  
ATOM   1636  CE1 TYR B 103     141.369 101.691 -42.950  1.00 24.33           C  
ANISOU 1636  CE1 TYR B 103     4120   3219   1904    -95   1203    227       C  
ATOM   1637  CE2 TYR B 103     139.719 100.045 -43.482  1.00 23.09           C  
ANISOU 1637  CE2 TYR B 103     3696   3151   1928    411    822    -42       C  
ATOM   1638  CZ  TYR B 103     140.634 100.990 -43.884  1.00 24.99           C  
ANISOU 1638  CZ  TYR B 103     4179   3360   1955    287   1101    201       C  
ATOM   1639  OH  TYR B 103     140.824 101.237 -45.226  1.00 27.89           O  
ANISOU 1639  OH  TYR B 103     4730   3693   2171    423   1172    412       O  
ATOM   1640  N   GLN B 104     138.171 103.283 -39.579  1.00 14.02           N  
ANISOU 1640  N   GLN B 104     2609   1034   1685    -95    604     47       N  
ATOM   1641  CA  GLN B 104     136.923 103.842 -40.087  1.00 13.88           C  
ANISOU 1641  CA  GLN B 104     2814    922   1538   -290    385      8       C  
ATOM   1642  C   GLN B 104     136.723 103.547 -41.564  1.00 14.22           C  
ANISOU 1642  C   GLN B 104     2734   1118   1550   -506    512    -59       C  
ATOM   1643  O   GLN B 104     135.582 103.374 -42.003  1.00 14.65           O  
ANISOU 1643  O   GLN B 104     2649   1344   1574   -295    415   -202       O  
ATOM   1644  CB  GLN B 104     136.865 105.345 -39.850  1.00 14.29           C  
ANISOU 1644  CB  GLN B 104     3029    867   1533   -371    409   -130       C  
ATOM   1645  CG  GLN B 104     136.674 105.700 -38.398  1.00 15.46           C  
ANISOU 1645  CG  GLN B 104     3243   1119   1513   -233    578   -262       C  
ATOM   1646  CD  GLN B 104     135.917 106.995 -38.227  1.00 17.96           C  
ANISOU 1646  CD  GLN B 104     3723   1428   1675    -10    317    -31       C  
ATOM   1647  OE1 GLN B 104     135.662 107.714 -39.195  1.00 21.90           O  
ANISOU 1647  OE1 GLN B 104     4293   2102   1928    159    -41   -168       O  
ATOM   1648  NE2 GLN B 104     135.528 107.290 -36.997  1.00 19.53           N  
ANISOU 1648  NE2 GLN B 104     3669   1963   1789   -165    341   -117       N  
ATOM   1649  N   GLY B 105     137.803 103.501 -42.343  1.00 14.79           N  
ANISOU 1649  N   GLY B 105     2859   1188   1571   -438    433   -123       N  
ATOM   1650  CA  GLY B 105     137.682 103.186 -43.746  1.00 15.60           C  
ANISOU 1650  CA  GLY B 105     3038   1240   1651   -407    319   -192       C  
ATOM   1651  C   GLY B 105     137.010 104.302 -44.530  1.00 16.23           C  
ANISOU 1651  C   GLY B 105     3175   1350   1642   -561    635     -9       C  
ATOM   1652  O   GLY B 105     136.755 105.398 -44.031  1.00 17.97           O  
ANISOU 1652  O   GLY B 105     3429   1558   1840   -223    619    -97       O  
ATOM   1653  N   SER B 106     136.694 103.976 -45.785  1.00 16.78           N  
ANISOU 1653  N   SER B 106     3069   1675   1631   -449    750    -66       N  
ATOM   1654  CA  SER B 106     136.204 104.981 -46.722  1.00 17.94           C  
ANISOU 1654  CA  SER B 106     3363   1916   1539   -159    886     10       C  
ATOM   1655  C   SER B 106     134.831 105.506 -46.346  1.00 17.69           C  
ANISOU 1655  C   SER B 106     3526   1645   1549   -195    728    -24       C  
ATOM   1656  O   SER B 106     134.475 106.625 -46.738  1.00 19.43           O  
ANISOU 1656  O   SER B 106     3823   1857   1701   -220    588     62       O  
ATOM   1657  CB  SER B 106     136.126 104.388 -48.127  1.00 21.34           C  
ANISOU 1657  CB  SER B 106     3859   2573   1678    229    997    115       C  
ATOM   1658  OG  SER B 106     137.407 104.013 -48.584  1.00 26.15           O  
ANISOU 1658  OG  SER B 106     4342   3344   2251    160    794    227       O  
ATOM   1659  N   TYR B 107     134.037 104.716 -45.622  1.00 16.27           N  
ANISOU 1659  N   TYR B 107     3316   1598   1268   -233    664   -245       N  
ATOM   1660  CA  TYR B 107     132.676 105.102 -45.293  1.00 15.66           C  
ANISOU 1660  CA  TYR B 107     3281   1249   1418   -307    540   -267       C  
ATOM   1661  C   TYR B 107     132.552 105.757 -43.928  1.00 15.19           C  
ANISOU 1661  C   TYR B 107     3229    997   1546   -213    416    -29       C  
ATOM   1662  O   TYR B 107     131.438 106.091 -43.524  1.00 16.41           O  
ANISOU 1662  O   TYR B 107     3235   1183   1818     30    478    117       O  
ATOM   1663  CB  TYR B 107     131.731 103.897 -45.419  1.00 15.80           C  
ANISOU 1663  CB  TYR B 107     3424   1183   1397   -402    425   -197       C  
ATOM   1664  CG  TYR B 107     131.825 103.336 -46.806  1.00 16.21           C  
ANISOU 1664  CG  TYR B 107     3394   1258   1509   -470    393   -289       C  
ATOM   1665  CD1 TYR B 107     131.242 103.998 -47.871  1.00 17.34           C  
ANISOU 1665  CD1 TYR B 107     3486   1523   1578   -381    267    -63       C  
ATOM   1666  CD2 TYR B 107     132.551 102.181 -47.067  1.00 17.60           C  
ANISOU 1666  CD2 TYR B 107     3552   1472   1662   -361    333   -631       C  
ATOM   1667  CE1 TYR B 107     131.354 103.523 -49.158  1.00 18.37           C  
ANISOU 1667  CE1 TYR B 107     3543   1946   1489   -462    310   -346       C  
ATOM   1668  CE2 TYR B 107     132.672 101.695 -48.353  1.00 18.88           C  
ANISOU 1668  CE2 TYR B 107     3478   2050   1644   -213    430   -678       C  
ATOM   1669  CZ  TYR B 107     132.069 102.370 -49.397  1.00 19.66           C  
ANISOU 1669  CZ  TYR B 107     3593   2350   1527   -280    510   -645       C  
ATOM   1670  OH  TYR B 107     132.185 101.895 -50.684  1.00 22.59           O  
ANISOU 1670  OH  TYR B 107     3876   3041   1668   -474    362   -959       O  
ATOM   1671  N   GLY B 108     133.660 105.959 -43.217  1.00 14.38           N  
ANISOU 1671  N   GLY B 108     3082    809   1572   -131    436    -29       N  
ATOM   1672  CA  GLY B 108     133.594 106.565 -41.897  1.00 14.90           C  
ANISOU 1672  CA  GLY B 108     3179    932   1550   -141    574     -5       C  
ATOM   1673  C   GLY B 108     132.850 105.707 -40.902  1.00 13.02           C  
ANISOU 1673  C   GLY B 108     2732    743   1474   -251    305    -84       C  
ATOM   1674  O   GLY B 108     132.011 106.215 -40.148  1.00 14.19           O  
ANISOU 1674  O   GLY B 108     2828    993   1570   -127    366   -144       O  
ATOM   1675  N   PHE B 109     133.137 104.406 -40.890  1.00 12.11           N  
ANISOU 1675  N   PHE B 109     2474    664   1464   -212    232     24       N  
ATOM   1676  CA  PHE B 109     132.397 103.451 -40.077  1.00 10.96           C  
ANISOU 1676  CA  PHE B 109     2334    632   1199   -103    220     51       C  
ATOM   1677  C   PHE B 109     132.831 103.509 -38.618  1.00 11.92           C  
ANISOU 1677  C   PHE B 109     2308    920   1300      1    226     70       C  
ATOM   1678  O   PHE B 109     134.028 103.476 -38.312  1.00 13.01           O  
ANISOU 1678  O   PHE B 109     2395   1154   1393    -84    224    140       O  
ATOM   1679  CB  PHE B 109     132.649 102.046 -40.624  1.00 11.98           C  
ANISOU 1679  CB  PHE B 109     2404    735   1413    -17    256    156       C  
ATOM   1680  CG  PHE B 109     132.056 100.950 -39.785  1.00 11.65           C  
ANISOU 1680  CG  PHE B 109     2341    827   1260      4    365    164       C  
ATOM   1681  CD1 PHE B 109     130.695 100.714 -39.800  1.00 13.10           C  
ANISOU 1681  CD1 PHE B 109     2519   1108   1349   -169    373     78       C  
ATOM   1682  CD2 PHE B 109     132.870 100.144 -39.000  1.00 11.71           C  
ANISOU 1682  CD2 PHE B 109     2410    901   1137     85    266    129       C  
ATOM   1683  CE1 PHE B 109     130.142  99.697 -39.034  1.00 13.99           C  
ANISOU 1683  CE1 PHE B 109     2592   1287   1435     91    391    268       C  
ATOM   1684  CE2 PHE B 109     132.325  99.122 -38.239  1.00 12.26           C  
ANISOU 1684  CE2 PHE B 109     2394    831   1432     63    304    138       C  
ATOM   1685  CZ  PHE B 109     130.960  98.901 -38.251  1.00 13.37           C  
ANISOU 1685  CZ  PHE B 109     2593   1067   1419    149    324    205       C  
ATOM   1686  N   ARG B 110     131.853 103.558 -37.719  1.00 11.03           N  
ANISOU 1686  N   ARG B 110     2242    814   1135     70    175    -63       N  
ATOM   1687  CA  ARG B 110     132.142 103.453 -36.298  1.00 11.94           C  
ANISOU 1687  CA  ARG B 110     2360    969   1209   -166    124     62       C  
ATOM   1688  C   ARG B 110     130.873 103.038 -35.577  1.00 11.58           C  
ANISOU 1688  C   ARG B 110     2262    977   1159   -138     87     67       C  
ATOM   1689  O   ARG B 110     129.762 103.199 -36.088  1.00 12.57           O  
ANISOU 1689  O   ARG B 110     2343   1143   1291    -66     24    106       O  
ATOM   1690  CB  ARG B 110     132.703 104.759 -35.712  1.00 12.63           C  
ANISOU 1690  CB  ARG B 110     2499    872   1429     17    182    -94       C  
ATOM   1691  CG  ARG B 110     131.705 105.900 -35.591  1.00 13.15           C  
ANISOU 1691  CG  ARG B 110     2665    898   1435    275     48    167       C  
ATOM   1692  CD  ARG B 110     131.506 106.636 -36.918  1.00 12.98           C  
ANISOU 1692  CD  ARG B 110     2768    797   1365    350    118    153       C  
ATOM   1693  NE  ARG B 110     130.723 107.854 -36.732  1.00 13.41           N  
ANISOU 1693  NE  ARG B 110     2956    819   1322    300     94    136       N  
ATOM   1694  CZ  ARG B 110     130.357 108.649 -37.725  1.00 15.74           C  
ANISOU 1694  CZ  ARG B 110     3559   1076   1348    570    525     97       C  
ATOM   1695  NH1 ARG B 110     130.714 108.358 -38.966  1.00 18.21           N1+
ANISOU 1695  NH1 ARG B 110     4073   1557   1290    768    530     91       N1+
ATOM   1696  NH2 ARG B 110     129.636 109.731 -37.477  1.00 18.30           N  
ANISOU 1696  NH2 ARG B 110     3905   1390   1659    848    541     78       N  
ATOM   1697  N   LEU B 111     131.053 102.500 -34.380  1.00 10.51           N  
ANISOU 1697  N   LEU B 111     2017    893   1081     -7     45    170       N  
ATOM   1698  CA  LEU B 111     129.924 102.026 -33.604  1.00 10.70           C  
ANISOU 1698  CA  LEU B 111     1894    958   1214     54    -18    168       C  
ATOM   1699  C   LEU B 111     129.356 103.130 -32.725  1.00 11.12           C  
ANISOU 1699  C   LEU B 111     1922    967   1337     21     69     57       C  
ATOM   1700  O   LEU B 111     129.991 104.155 -32.465  1.00 12.76           O  
ANISOU 1700  O   LEU B 111     2086   1076   1686    -92    322   -104       O  
ATOM   1701  CB  LEU B 111     130.369 100.873 -32.714  1.00  9.36           C  
ANISOU 1701  CB  LEU B 111     1609    737   1210    158    -88    159       C  
ATOM   1702  CG  LEU B 111     130.971  99.690 -33.449  1.00 10.21           C  
ANISOU 1702  CG  LEU B 111     1648    954   1277    304    -58   -153       C  
ATOM   1703  CD1 LEU B 111     131.497  98.695 -32.436  1.00 10.86           C  
ANISOU 1703  CD1 LEU B 111     1876    933   1318     25    -42    -25       C  
ATOM   1704  CD2 LEU B 111     129.949  99.054 -34.383  1.00 10.13           C  
ANISOU 1704  CD2 LEU B 111     1521    960   1370    323   -169   -229       C  
ATOM   1705  N   GLY B 112     128.136 102.897 -32.252  1.00 10.76           N  
ANISOU 1705  N   GLY B 112     1943    954   1191    208    292     31       N  
ATOM   1706  CA  GLY B 112     127.556 103.737 -31.229  1.00 10.96           C  
ANISOU 1706  CA  GLY B 112     2036    881   1247      9    238    -15       C  
ATOM   1707  C   GLY B 112     126.711 102.881 -30.313  1.00 10.33           C  
ANISOU 1707  C   GLY B 112     1859    818   1246    -89   -105     11       C  
ATOM   1708  O   GLY B 112     126.294 101.779 -30.668  1.00 11.20           O  
ANISOU 1708  O   GLY B 112     2032    832   1390   -112    -47     -5       O  
ATOM   1709  N   PHE B 113     126.463 103.407 -29.122  1.00 10.32           N  
ANISOU 1709  N   PHE B 113     1766    958   1198    115     73      5       N  
ATOM   1710  CA  PHE B 113     125.699 102.682 -28.126  1.00 11.70           C  
ANISOU 1710  CA  PHE B 113     2066   1083   1298     54     25   -113       C  
ATOM   1711  C   PHE B 113     124.693 103.620 -27.492  1.00 12.07           C  
ANISOU 1711  C   PHE B 113     1976   1099   1511     84    237   -266       C  
ATOM   1712  O   PHE B 113     124.940 104.822 -27.367  1.00 14.04           O  
ANISOU 1712  O   PHE B 113     2474   1240   1621    134    268   -287       O  
ATOM   1713  CB  PHE B 113     126.616 102.090 -27.055  1.00 11.98           C  
ANISOU 1713  CB  PHE B 113     2173   1161   1218    275   -143    -57       C  
ATOM   1714  CG  PHE B 113     127.637 101.158 -27.616  1.00 10.94           C  
ANISOU 1714  CG  PHE B 113     2215    822   1119    176    -40    -29       C  
ATOM   1715  CD1 PHE B 113     128.834 101.651 -28.115  1.00 10.65           C  
ANISOU 1715  CD1 PHE B 113     1909    921   1215    220   -102   -149       C  
ATOM   1716  CD2 PHE B 113     127.393  99.798 -27.684  1.00 12.29           C  
ANISOU 1716  CD2 PHE B 113     2478    944   1249    220   -123    101       C  
ATOM   1717  CE1 PHE B 113     129.776 100.821 -28.665  1.00 12.19           C  
ANISOU 1717  CE1 PHE B 113     2222   1131   1279    556   -176   -219       C  
ATOM   1718  CE2 PHE B 113     128.340  98.951 -28.222  1.00 13.06           C  
ANISOU 1718  CE2 PHE B 113     2585   1031   1346    300   -193    -72       C  
ATOM   1719  CZ  PHE B 113     129.535  99.463 -28.722  1.00 13.28           C  
ANISOU 1719  CZ  PHE B 113     2583   1114   1351    281   -272   -110       C  
ATOM   1720  N   LEU B 114     123.553 103.053 -27.107  1.00 13.24           N  
ANISOU 1720  N   LEU B 114     1843   1450   1738    122    522   -179       N  
ATOM   1721  CA  LEU B 114     122.556 103.803 -26.363  1.00 13.49           C  
ANISOU 1721  CA  LEU B 114     1857   1323   1944    236    449   -245       C  
ATOM   1722  C   LEU B 114     123.118 104.223 -25.010  1.00 14.38           C  
ANISOU 1722  C   LEU B 114     2158   1370   1936    204    298   -223       C  
ATOM   1723  O   LEU B 114     124.119 103.695 -24.527  1.00 16.43           O  
ANISOU 1723  O   LEU B 114     2443   1690   2109    549    286   -457       O  
ATOM   1724  CB  LEU B 114     121.303 102.954 -26.145  1.00 14.63           C  
ANISOU 1724  CB  LEU B 114     1899   1535   2123    457    177   -211       C  
ATOM   1725  CG  LEU B 114     120.606 102.492 -27.424  1.00 17.72           C  
ANISOU 1725  CG  LEU B 114     2389   2037   2309    162    -64   -175       C  
ATOM   1726  CD1 LEU B 114     119.471 101.545 -27.089  1.00 18.66           C  
ANISOU 1726  CD1 LEU B 114     2330   2300   2460    -83     -9   -133       C  
ATOM   1727  CD2 LEU B 114     120.094 103.681 -28.225  1.00 19.46           C  
ANISOU 1727  CD2 LEU B 114     2785   2270   2339     56    -94   -162       C  
ATOM   1728  N   HIS B 115     122.461 105.192 -24.398  1.00 14.41           N  
ANISOU 1728  N   HIS B 115     2273   1360   1842     96    215   -421       N  
ATOM   1729  CA  HIS B 115     122.821 105.664 -23.067  1.00 14.62           C  
ANISOU 1729  CA  HIS B 115     2385   1153   2016     79    262   -411       C  
ATOM   1730  C   HIS B 115     121.752 105.137 -22.125  1.00 16.04           C  
ANISOU 1730  C   HIS B 115     2427   1354   2313     10    560   -333       C  
ATOM   1731  O   HIS B 115     120.756 105.803 -21.848  1.00 18.52           O  
ANISOU 1731  O   HIS B 115     2622   1648   2765    216    581   -224       O  
ATOM   1732  CB  HIS B 115     122.932 107.166 -23.064  1.00 15.41           C  
ANISOU 1732  CB  HIS B 115     2664   1022   2167    -55    107   -336       C  
ATOM   1733  CG  HIS B 115     124.055 107.659 -23.908  1.00 16.79           C  
ANISOU 1733  CG  HIS B 115     3116   1077   2186    -58    225   -241       C  
ATOM   1734  ND1 HIS B 115     123.929 107.861 -25.265  1.00 18.61           N  
ANISOU 1734  ND1 HIS B 115     3503   1201   2367   -218    100     71       N  
ATOM   1735  CD2 HIS B 115     125.349 107.914 -23.606  1.00 16.37           C  
ANISOU 1735  CD2 HIS B 115     3084    910   2227    -55    209   -115       C  
ATOM   1736  CE1 HIS B 115     125.092 108.247 -25.758  1.00 18.55           C  
ANISOU 1736  CE1 HIS B 115     3449   1267   2333   -294    153    -14       C  
ATOM   1737  NE2 HIS B 115     125.969 108.293 -24.771  1.00 17.42           N  
ANISOU 1737  NE2 HIS B 115     3202   1191   2225     38    168     65       N  
ATOM   1738  N   SER B 116     121.971 103.918 -21.642  1.00 15.30           N  
ANISOU 1738  N   SER B 116     2494   1123   2196   -225    595   -313       N  
ATOM   1739  CA  SER B 116     120.949 103.165 -20.932  1.00 16.04           C  
ANISOU 1739  CA  SER B 116     2691   1282   2124   -162    802   -301       C  
ATOM   1740  C   SER B 116     121.032 103.305 -19.424  1.00 16.50           C  
ANISOU 1740  C   SER B 116     2765   1263   2240     31    670   -256       C  
ATOM   1741  O   SER B 116     120.134 102.822 -18.728  1.00 18.58           O  
ANISOU 1741  O   SER B 116     3004   1540   2515     36    520   -134       O  
ATOM   1742  CB  SER B 116     121.042 101.680 -21.300  1.00 18.42           C  
ANISOU 1742  CB  SER B 116     3373   1582   2045   -387    676   -435       C  
ATOM   1743  OG  SER B 116     120.881 101.508 -22.696  1.00 21.69           O  
ANISOU 1743  OG  SER B 116     3972   2189   2082   -460    422   -562       O  
ATOM   1744  N   GLY B 117     122.075 103.927 -18.908  1.00 16.85           N  
ANISOU 1744  N   GLY B 117     2779   1406   2218     18    646   -225       N  
ATOM   1745  CA  GLY B 117     122.178 104.148 -17.484  1.00 16.93           C  
ANISOU 1745  CA  GLY B 117     2808   1541   2085    -56    760   -229       C  
ATOM   1746  C   GLY B 117     122.626 102.902 -16.745  1.00 16.22           C  
ANISOU 1746  C   GLY B 117     2777   1300   2086   -137    718   -130       C  
ATOM   1747  O   GLY B 117     122.949 101.867 -17.335  1.00 17.35           O  
ANISOU 1747  O   GLY B 117     2899   1575   2119    -52    833    -34       O  
ATOM   1748  N   THR B 118     122.648 103.013 -15.419  1.00 17.37           N  
ANISOU 1748  N   THR B 118     2974   1533   2095    -83    744     -9       N  
ATOM   1749  CA  THR B 118     123.227 101.962 -14.587  1.00 19.92           C  
ANISOU 1749  CA  THR B 118     3535   1853   2180     54    929   -178       C  
ATOM   1750  C   THR B 118     122.277 101.485 -13.496  1.00 22.00           C  
ANISOU 1750  C   THR B 118     3894   2253   2211     97   1144   -171       C  
ATOM   1751  O   THR B 118     122.724 100.962 -12.469  1.00 22.50           O  
ANISOU 1751  O   THR B 118     4104   2274   2170    207   1053   -162       O  
ATOM   1752  CB  THR B 118     124.557 102.403 -13.982  1.00 22.89           C  
ANISOU 1752  CB  THR B 118     3944   2329   2423    134    770   -385       C  
ATOM   1753  OG1 THR B 118     124.347 103.577 -13.185  1.00 24.20           O  
ANISOU 1753  OG1 THR B 118     4270   2374   2551     46    754   -506       O  
ATOM   1754  CG2 THR B 118     125.576 102.702 -15.066  1.00 23.99           C  
ANISOU 1754  CG2 THR B 118     3922   2675   2519    243    820   -430       C  
ATOM   1755  N   ALA B 119     120.970 101.640 -13.699  1.00 21.48           N  
ANISOU 1755  N   ALA B 119     3742   2199   2220     -6   1457    -39       N  
ATOM   1756  CA  ALA B 119     120.018 101.116 -12.728  1.00 23.40           C  
ANISOU 1756  CA  ALA B 119     4025   2497   2370   -186   1431    -18       C  
ATOM   1757  C   ALA B 119     120.200  99.609 -12.589  1.00 25.57           C  
ANISOU 1757  C   ALA B 119     4611   2662   2442   -348   1365    -50       C  
ATOM   1758  O   ALA B 119     120.613  98.925 -13.529  1.00 26.69           O  
ANISOU 1758  O   ALA B 119     4841   2814   2486   -153   1037   -257       O  
ATOM   1759  CB  ALA B 119     118.588 101.429 -13.163  1.00 23.71           C  
ANISOU 1759  CB  ALA B 119     3863   2635   2512   -160   1377     23       C  
ATOM   1760  N   LYS B 120     119.902  99.092 -11.393  1.00 27.90           N  
ANISOU 1760  N   LYS B 120     5093   2945   2562   -462   1269     18       N  
ATOM   1761  CA  LYS B 120     120.095  97.667 -11.140  1.00 29.55           C  
ANISOU 1761  CA  LYS B 120     5282   3179   2767   -420   1227     49       C  
ATOM   1762  C   LYS B 120     119.315  96.806 -12.127  1.00 29.89           C  
ANISOU 1762  C   LYS B 120     5107   3289   2961   -165   1275    162       C  
ATOM   1763  O   LYS B 120     119.737  95.689 -12.442  1.00 30.39           O  
ANISOU 1763  O   LYS B 120     5340   3104   3103     72   1200    240       O  
ATOM   1764  CB  LYS B 120     119.707  97.324  -9.699  1.00 31.30           C  
ANISOU 1764  CB  LYS B 120     5512   3473   2909   -501   1012    118       C  
ATOM   1765  N   SER B 121     118.200  97.316 -12.649  1.00 29.33           N  
ANISOU 1765  N   SER B 121     4612   3452   3081   -104   1447     61       N  
ATOM   1766  CA  SER B 121     117.352  96.561 -13.562  1.00 28.79           C  
ANISOU 1766  CA  SER B 121     4129   3609   3203   -103   1339    -34       C  
ATOM   1767  C   SER B 121     117.840  96.570 -15.007  1.00 26.88           C  
ANISOU 1767  C   SER B 121     3738   3345   3131   -227   1218   -224       C  
ATOM   1768  O   SER B 121     117.289  95.828 -15.828  1.00 28.46           O  
ANISOU 1768  O   SER B 121     3828   3743   3240   -274   1155   -171       O  
ATOM   1769  CB  SER B 121     115.932  97.127 -13.526  1.00 30.76           C  
ANISOU 1769  CB  SER B 121     4302   3970   3414    180   1243     58       C  
ATOM   1770  OG  SER B 121     115.922  98.467 -13.995  1.00 31.95           O  
ANISOU 1770  OG  SER B 121     4339   4274   3527    331   1352     41       O  
ATOM   1771  N   VAL B 122     118.844  97.379 -15.348  1.00 23.61           N  
ANISOU 1771  N   VAL B 122     3337   2756   2879   -222   1239   -282       N  
ATOM   1772  CA  VAL B 122     119.209  97.553 -16.751  1.00 20.00           C  
ANISOU 1772  CA  VAL B 122     2841   2214   2544   -217    848   -429       C  
ATOM   1773  C   VAL B 122     119.752  96.248 -17.328  1.00 19.28           C  
ANISOU 1773  C   VAL B 122     2730   2071   2524   -226    591   -306       C  
ATOM   1774  O   VAL B 122     120.492  95.506 -16.670  1.00 21.45           O  
ANISOU 1774  O   VAL B 122     3255   2340   2554    -71    456   -219       O  
ATOM   1775  CB  VAL B 122     120.173  98.743 -16.922  1.00 19.04           C  
ANISOU 1775  CB  VAL B 122     2585   2168   2480   -340    644   -295       C  
ATOM   1776  CG1 VAL B 122     121.606  98.381 -16.542  1.00 19.07           C  
ANISOU 1776  CG1 VAL B 122     2641   2073   2531   -457    388   -276       C  
ATOM   1777  CG2 VAL B 122     120.109  99.288 -18.335  1.00 19.65           C  
ANISOU 1777  CG2 VAL B 122     2724   2299   2444   -191    694   -369       C  
ATOM   1778  N   THR B 123     119.360  95.944 -18.561  1.00 17.41           N  
ANISOU 1778  N   THR B 123     2329   1778   2507   -214    711   -318       N  
ATOM   1779  CA  THR B 123     119.746  94.675 -19.161  1.00 17.74           C  
ANISOU 1779  CA  THR B 123     2338   1874   2529     77    581   -408       C  
ATOM   1780  C   THR B 123     120.986  94.787 -20.031  1.00 15.88           C  
ANISOU 1780  C   THR B 123     2083   1636   2316   -100    475   -281       C  
ATOM   1781  O   THR B 123     121.634  93.772 -20.303  1.00 16.29           O  
ANISOU 1781  O   THR B 123     2159   1663   2369    137    178   -227       O  
ATOM   1782  CB  THR B 123     118.612  94.128 -20.026  1.00 20.48           C  
ANISOU 1782  CB  THR B 123     2635   2378   2767    -88    499   -366       C  
ATOM   1783  OG1 THR B 123     118.284  95.094 -21.030  1.00 22.13           O  
ANISOU 1783  OG1 THR B 123     2920   2644   2844     11    352   -569       O  
ATOM   1784  CG2 THR B 123     117.379  93.816 -19.177  1.00 22.05           C  
ANISOU 1784  CG2 THR B 123     2694   2658   3026   -213    561   -122       C  
ATOM   1785  N   CYS B 124     121.319  95.990 -20.478  1.00 15.25           N  
ANISOU 1785  N   CYS B 124     2089   1559   2147   -148    413   -113       N  
ATOM   1786  CA  CYS B 124     122.479  96.209 -21.323  1.00 12.99           C  
ANISOU 1786  CA  CYS B 124     1753   1203   1981   -276    140   -253       C  
ATOM   1787  C   CYS B 124     122.879  97.657 -21.123  1.00 13.50           C  
ANISOU 1787  C   CYS B 124     1771   1356   2003    -73    209   -105       C  
ATOM   1788  O   CYS B 124     122.022  98.539 -21.174  1.00 16.02           O  
ANISOU 1788  O   CYS B 124     1832   1817   2437    115    224   -108       O  
ATOM   1789  CB  CYS B 124     122.102  95.980 -22.789  1.00 15.00           C  
ANISOU 1789  CB  CYS B 124     2281   1439   1981   -319    270   -487       C  
ATOM   1790  SG  CYS B 124     123.458  96.207 -23.941  1.00 16.81           S  
ANISOU 1790  SG  CYS B 124     2668   1699   2020    -56    187   -299       S  
ATOM   1791  N   THR B 125     124.157  97.900 -20.875  1.00 12.65           N  
ANISOU 1791  N   THR B 125     1868   1294   1645   -126    264   -103       N  
ATOM   1792  CA  THR B 125     124.611  99.270 -20.701  1.00 10.62           C  
ANISOU 1792  CA  THR B 125     1692    840   1502     56    343    -26       C  
ATOM   1793  C   THR B 125     126.066  99.377 -21.137  1.00 10.44           C  
ANISOU 1793  C   THR B 125     1789    715   1464     43    306    243       C  
ATOM   1794  O   THR B 125     126.859  98.464 -20.910  1.00 13.01           O  
ANISOU 1794  O   THR B 125     2018   1005   1922    152    175    307       O  
ATOM   1795  CB  THR B 125     124.402  99.747 -19.257  1.00 12.12           C  
ANISOU 1795  CB  THR B 125     2099    954   1552    -20    243   -147       C  
ATOM   1796  OG1 THR B 125     124.772 101.126 -19.137  1.00 13.68           O  
ANISOU 1796  OG1 THR B 125     2336   1116   1747    -83    179   -141       O  
ATOM   1797  CG2 THR B 125     125.205  98.898 -18.263  1.00 12.91           C  
ANISOU 1797  CG2 THR B 125     2148   1315   1442      4    105   -404       C  
ATOM   1798  N   TYR B 126     126.402 100.486 -21.783  1.00 10.72           N  
ANISOU 1798  N   TYR B 126     2081    665   1326   -250    357     30       N  
ATOM   1799  CA  TYR B 126     127.716 100.674 -22.374  1.00 10.76           C  
ANISOU 1799  CA  TYR B 126     1897    935   1256   -129    252     37       C  
ATOM   1800  C   TYR B 126     128.478 101.756 -21.617  1.00 10.79           C  
ANISOU 1800  C   TYR B 126     1873    932   1293     17    102   -143       C  
ATOM   1801  O   TYR B 126     127.935 102.833 -21.351  1.00 12.30           O  
ANISOU 1801  O   TYR B 126     2187    940   1545     94    154   -334       O  
ATOM   1802  CB  TYR B 126     127.587 101.061 -23.846  1.00 10.95           C  
ANISOU 1802  CB  TYR B 126     1879   1120   1161    -56    259     13       C  
ATOM   1803  CG  TYR B 126     128.911 101.408 -24.445  1.00 10.61           C  
ANISOU 1803  CG  TYR B 126     1820   1024   1187    -61      9   -187       C  
ATOM   1804  CD1 TYR B 126     129.837 100.416 -24.746  1.00 11.20           C  
ANISOU 1804  CD1 TYR B 126     2024   1093   1138    260    164   -229       C  
ATOM   1805  CD2 TYR B 126     129.259 102.731 -24.684  1.00 10.58           C  
ANISOU 1805  CD2 TYR B 126     1851    897   1271   -174    -11   -203       C  
ATOM   1806  CE1 TYR B 126     131.070 100.735 -25.267  1.00 10.99           C  
ANISOU 1806  CE1 TYR B 126     2048   1003   1124    212    286    -10       C  
ATOM   1807  CE2 TYR B 126     130.472 103.056 -25.221  1.00 10.38           C  
ANISOU 1807  CE2 TYR B 126     1621   1211   1111    191      5   -245       C  
ATOM   1808  CZ  TYR B 126     131.376 102.058 -25.510  1.00 10.70           C  
ANISOU 1808  CZ  TYR B 126     1814   1152   1100    187    102     50       C  
ATOM   1809  OH  TYR B 126     132.599 102.390 -26.018  1.00 12.42           O  
ANISOU 1809  OH  TYR B 126     1988   1587   1143    156    125     81       O  
ATOM   1810  N   SER B 127     129.740 101.469 -21.282  1.00 10.33           N  
ANISOU 1810  N   SER B 127     1807    865   1254   -188     38    -88       N  
ATOM   1811  CA  SER B 127     130.603 102.430 -20.617  1.00 11.83           C  
ANISOU 1811  CA  SER B 127     2080    978   1437   -103    -73    -29       C  
ATOM   1812  C   SER B 127     131.565 103.017 -21.630  1.00 11.50           C  
ANISOU 1812  C   SER B 127     2354    658   1356     16     -3   -145       C  
ATOM   1813  O   SER B 127     132.496 102.316 -22.052  1.00 11.92           O  
ANISOU 1813  O   SER B 127     2268    795   1468   -202     27   -115       O  
ATOM   1814  CB  SER B 127     131.398 101.723 -19.527  1.00 13.38           C  
ANISOU 1814  CB  SER B 127     2401   1141   1544   -154   -393    198       C  
ATOM   1815  OG  SER B 127     132.427 102.565 -19.044  1.00 13.43           O  
ANISOU 1815  OG  SER B 127     2498    968   1638   -258   -127    -15       O  
ATOM   1816  N   PRO B 128     131.430 104.296 -22.003  1.00 12.36           N  
ANISOU 1816  N   PRO B 128     2323    713   1658   -165     71    119       N  
ATOM   1817  CA  PRO B 128     132.443 104.902 -22.882  1.00 13.51           C  
ANISOU 1817  CA  PRO B 128     2552    771   1811    -57   -191    219       C  
ATOM   1818  C   PRO B 128     133.806 104.965 -22.236  1.00 13.16           C  
ANISOU 1818  C   PRO B 128     2376    849   1776   -252   -166      8       C  
ATOM   1819  O   PRO B 128     134.822 104.781 -22.917  1.00 15.74           O  
ANISOU 1819  O   PRO B 128     2660   1249   2072   -222   -226    -90       O  
ATOM   1820  CB  PRO B 128     131.881 106.306 -23.150  1.00 14.58           C  
ANISOU 1820  CB  PRO B 128     2657    853   2028   -129   -294    241       C  
ATOM   1821  CG  PRO B 128     130.426 106.181 -22.937  1.00 15.69           C  
ANISOU 1821  CG  PRO B 128     2875   1206   1880    135    128    241       C  
ATOM   1822  CD  PRO B 128     130.231 105.141 -21.871  1.00 13.09           C  
ANISOU 1822  CD  PRO B 128     2443    796   1736    136     29     66       C  
ATOM   1823  N   ALA B 129     133.862 105.212 -20.926  1.00 13.64           N  
ANISOU 1823  N   ALA B 129     2462   1036   1684   -266   -260    -79       N  
ATOM   1824  CA  ALA B 129     135.163 105.347 -20.282  1.00 14.37           C  
ANISOU 1824  CA  ALA B 129     2406   1242   1812   -190   -255   -298       C  
ATOM   1825  C   ALA B 129     135.948 104.047 -20.334  1.00 14.64           C  
ANISOU 1825  C   ALA B 129     2412   1179   1970   -177   -132   -272       C  
ATOM   1826  O   ALA B 129     137.182 104.072 -20.401  1.00 17.67           O  
ANISOU 1826  O   ALA B 129     2716   1667   2332      4    -33    -33       O  
ATOM   1827  CB  ALA B 129     134.998 105.815 -18.840  1.00 15.49           C  
ANISOU 1827  CB  ALA B 129     2693   1373   1818    -41   -329   -635       C  
ATOM   1828  N   LEU B 130     135.256 102.910 -20.315  1.00 13.26           N  
ANISOU 1828  N   LEU B 130     2336   1039   1661     29   -152    -84       N  
ATOM   1829  CA  LEU B 130     135.883 101.602 -20.360  1.00 14.16           C  
ANISOU 1829  CA  LEU B 130     2539   1206   1635     22   -144   -153       C  
ATOM   1830  C   LEU B 130     135.853 100.981 -21.745  1.00 14.69           C  
ANISOU 1830  C   LEU B 130     2624   1247   1711    127    -53   -232       C  
ATOM   1831  O   LEU B 130     136.437  99.907 -21.935  1.00 16.19           O  
ANISOU 1831  O   LEU B 130     2697   1425   2029    176   -118   -181       O  
ATOM   1832  CB  LEU B 130     135.161 100.658 -19.402  1.00 14.78           C  
ANISOU 1832  CB  LEU B 130     2795   1255   1563   -115   -136    -73       C  
ATOM   1833  CG  LEU B 130     135.253 101.033 -17.928  1.00 16.61           C  
ANISOU 1833  CG  LEU B 130     2889   1816   1605    -90   -188     36       C  
ATOM   1834  CD1 LEU B 130     134.234 100.246 -17.129  1.00 16.16           C  
ANISOU 1834  CD1 LEU B 130     2972   1618   1550   -234    -35    419       C  
ATOM   1835  CD2 LEU B 130     136.658 100.767 -17.416  1.00 17.90           C  
ANISOU 1835  CD2 LEU B 130     2876   2015   1911     38   -378    -63       C  
ATOM   1836  N   ASN B 131     135.180 101.620 -22.700  1.00 14.08           N  
ANISOU 1836  N   ASN B 131     2464   1234   1651   -142   -195   -173       N  
ATOM   1837  CA  ASN B 131     134.810 101.012 -23.982  1.00 11.43           C  
ANISOU 1837  CA  ASN B 131     2099    788   1454   -356    -30   -256       C  
ATOM   1838  C   ASN B 131     134.317  99.588 -23.777  1.00 10.98           C  
ANISOU 1838  C   ASN B 131     1939    815   1419   -201     -9   -189       C  
ATOM   1839  O   ASN B 131     134.845  98.627 -24.335  1.00 11.69           O  
ANISOU 1839  O   ASN B 131     2128    714   1601    -55     92   -115       O  
ATOM   1840  CB  ASN B 131     135.945 101.053 -25.000  1.00 11.83           C  
ANISOU 1840  CB  ASN B 131     2190    818   1487   -351    184   -271       C  
ATOM   1841  CG  ASN B 131     135.516 100.532 -26.360  1.00 12.68           C  
ANISOU 1841  CG  ASN B 131     2299    867   1653   -463    258   -180       C  
ATOM   1842  OD1 ASN B 131     134.360 100.679 -26.759  1.00 13.00           O  
ANISOU 1842  OD1 ASN B 131     2347    988   1603   -286    242    -67       O  
ATOM   1843  ND2 ASN B 131     136.441  99.909 -27.069  1.00 13.43           N  
ANISOU 1843  ND2 ASN B 131     2427    897   1777   -240    476   -150       N  
ATOM   1844  N   LYS B 132     133.306  99.461 -22.926  1.00 10.68           N  
ANISOU 1844  N   LYS B 132     1811    900   1346   -109   -113    -19       N  
ATOM   1845  CA  LYS B 132     132.915  98.148 -22.447  1.00 10.45           C  
ANISOU 1845  CA  LYS B 132     1882    714   1375     57   -178    222       C  
ATOM   1846  C   LYS B 132     131.408  98.069 -22.335  1.00 10.79           C  
ANISOU 1846  C   LYS B 132     1857    827   1415    -33    110    226       C  
ATOM   1847  O   LYS B 132     130.781  98.915 -21.691  1.00 10.53           O  
ANISOU 1847  O   LYS B 132     1821    666   1514     92     41     55       O  
ATOM   1848  CB  LYS B 132     133.552  97.859 -21.088  1.00 11.05           C  
ANISOU 1848  CB  LYS B 132     2137    741   1321    127   -409    280       C  
ATOM   1849  CG  LYS B 132     133.290  96.452 -20.568  1.00 11.69           C  
ANISOU 1849  CG  LYS B 132     2173    875   1394    225   -339    398       C  
ATOM   1850  CD  LYS B 132     134.229  96.140 -19.419  1.00 13.23           C  
ANISOU 1850  CD  LYS B 132     2234   1229   1563    -37   -293    563       C  
ATOM   1851  CE  LYS B 132     134.015  94.743 -18.880  1.00 15.04           C  
ANISOU 1851  CE  LYS B 132     2513   1422   1780    -81   -275    603       C  
ATOM   1852  NZ  LYS B 132     135.084  94.419 -17.902  1.00 17.54           N1+
ANISOU 1852  NZ  LYS B 132     2715   1936   2013    100   -437    500       N1+
ATOM   1853  N   LEU B 133     130.841  97.051 -22.968  1.00 10.15           N  
ANISOU 1853  N   LEU B 133     1615    893   1350   -310    -56    180       N  
ATOM   1854  CA  LEU B 133     129.417  96.771 -22.892  1.00  9.86           C  
ANISOU 1854  CA  LEU B 133     1662    706   1378   -290   -140      3       C  
ATOM   1855  C   LEU B 133     129.188  95.762 -21.779  1.00 11.22           C  
ANISOU 1855  C   LEU B 133     1852    861   1552     19    229     45       C  
ATOM   1856  O   LEU B 133     129.917  94.777 -21.678  1.00 12.22           O  
ANISOU 1856  O   LEU B 133     2028    942   1674    439    309    182       O  
ATOM   1857  CB  LEU B 133     128.953  96.180 -24.220  1.00 12.40           C  
ANISOU 1857  CB  LEU B 133     1697   1454   1562    162   -117   -329       C  
ATOM   1858  CG  LEU B 133     127.454  95.984 -24.359  1.00 14.57           C  
ANISOU 1858  CG  LEU B 133     1718   1994   1825     37   -322   -508       C  
ATOM   1859  CD1 LEU B 133     126.764  97.346 -24.359  1.00 17.63           C  
ANISOU 1859  CD1 LEU B 133     2137   2427   2133    187   -325   -481       C  
ATOM   1860  CD2 LEU B 133     127.193  95.244 -25.644  1.00 17.73           C  
ANISOU 1860  CD2 LEU B 133     2070   2770   1898   -293   -224   -570       C  
ATOM   1861  N   PHE B 134     128.196  96.025 -20.939  1.00 11.14           N  
ANISOU 1861  N   PHE B 134     1870    938   1425   -267    146     70       N  
ATOM   1862  CA  PHE B 134     127.800  95.125 -19.871  1.00 12.04           C  
ANISOU 1862  CA  PHE B 134     1982   1138   1457     -8    123     35       C  
ATOM   1863  C   PHE B 134     126.387  94.660 -20.175  1.00 10.99           C  
ANISOU 1863  C   PHE B 134     1930    702   1543   -193    146     39       C  
ATOM   1864  O   PHE B 134     125.505  95.482 -20.414  1.00 12.37           O  
ANISOU 1864  O   PHE B 134     2139    957   1603     36    208    177       O  
ATOM   1865  CB  PHE B 134     127.784  95.872 -18.539  1.00 12.71           C  
ANISOU 1865  CB  PHE B 134     2314   1000   1514     -8     44   -160       C  
ATOM   1866  CG  PHE B 134     129.129  96.367 -18.094  1.00 12.85           C  
ANISOU 1866  CG  PHE B 134     2388    996   1497   -147    108   -167       C  
ATOM   1867  CD1 PHE B 134     129.663  97.535 -18.612  1.00 11.97           C  
ANISOU 1867  CD1 PHE B 134     2493    791   1265   -286     74   -164       C  
ATOM   1868  CD2 PHE B 134     129.850  95.680 -17.135  1.00 12.59           C  
ANISOU 1868  CD2 PHE B 134     2402    870   1511   -191   -102    -75       C  
ATOM   1869  CE1 PHE B 134     130.903  97.996 -18.198  1.00 11.61           C  
ANISOU 1869  CE1 PHE B 134     2516    682   1214   -152   -198   -114       C  
ATOM   1870  CE2 PHE B 134     131.086  96.138 -16.710  1.00 13.57           C  
ANISOU 1870  CE2 PHE B 134     2699    903   1552   -419   -134     56       C  
ATOM   1871  CZ  PHE B 134     131.617  97.301 -17.240  1.00 13.64           C  
ANISOU 1871  CZ  PHE B 134     2702   1027   1454   -300    -73     84       C  
ATOM   1872  N   CYS B 135     126.161  93.353 -20.177  1.00 11.40           N  
ANISOU 1872  N   CYS B 135     1967    806   1557   -294    151    115       N  
ATOM   1873  CA  CYS B 135     124.832  92.893 -20.541  1.00 11.86           C  
ANISOU 1873  CA  CYS B 135     2016    987   1503   -278     68    138       C  
ATOM   1874  C   CYS B 135     124.485  91.622 -19.797  1.00 12.63           C  
ANISOU 1874  C   CYS B 135     1998   1010   1792   -296     80     69       C  
ATOM   1875  O   CYS B 135     125.358  90.883 -19.346  1.00 13.98           O  
ANISOU 1875  O   CYS B 135     2143   1096   2073      8     20    178       O  
ATOM   1876  CB  CYS B 135     124.726  92.646 -22.039  1.00 13.09           C  
ANISOU 1876  CB  CYS B 135     2506   1151   1316    113    186   -122       C  
ATOM   1877  SG  CYS B 135     125.860  91.394 -22.640  1.00 16.63           S  
ANISOU 1877  SG  CYS B 135     3172   1592   1553    371    -80   -122       S  
ATOM   1878  N   GLN B 136     123.186  91.387 -19.670  1.00 13.19           N  
ANISOU 1878  N   GLN B 136     2000   1124   1886   -263    319     78       N  
ATOM   1879  CA  GLN B 136     122.689  90.146 -19.109  1.00 13.95           C  
ANISOU 1879  CA  GLN B 136     2112   1153   2036   -343    544    -38       C  
ATOM   1880  C   GLN B 136     122.710  89.043 -20.160  1.00 13.88           C  
ANISOU 1880  C   GLN B 136     2111   1224   1941   -252    376     53       C  
ATOM   1881  O   GLN B 136     122.786  89.291 -21.366  1.00 15.01           O  
ANISOU 1881  O   GLN B 136     2472   1307   1924   -147    243    249       O  
ATOM   1882  CB  GLN B 136     121.272  90.346 -18.583  1.00 15.70           C  
ANISOU 1882  CB  GLN B 136     2194   1583   2189   -476    645   -218       C  
ATOM   1883  CG  GLN B 136     121.227  91.210 -17.343  1.00 18.11           C  
ANISOU 1883  CG  GLN B 136     2409   2102   2368   -414    669   -608       C  
ATOM   1884  CD  GLN B 136     119.822  91.462 -16.857  1.00 21.84           C  
ANISOU 1884  CD  GLN B 136     2684   2953   2662   -429    695   -586       C  
ATOM   1885  OE1 GLN B 136     118.853  91.110 -17.522  1.00 25.29           O  
ANISOU 1885  OE1 GLN B 136     2989   3712   2910    -85    784   -519       O  
ATOM   1886  NE2 GLN B 136     119.704  92.063 -15.681  1.00 24.77           N  
ANISOU 1886  NE2 GLN B 136     3208   3294   2910   -345    674   -607       N  
ATOM   1887  N   LEU B 137     122.641  87.809 -19.677  1.00 13.37           N  
ANISOU 1887  N   LEU B 137     2088   1035   1958   -320    224    -58       N  
ATOM   1888  CA  LEU B 137     122.718  86.639 -20.540  1.00 12.95           C  
ANISOU 1888  CA  LEU B 137     2038   1026   1857   -256    212     84       C  
ATOM   1889  C   LEU B 137     121.563  86.609 -21.530  1.00 13.10           C  
ANISOU 1889  C   LEU B 137     2086   1108   1783   -351    454    101       C  
ATOM   1890  O   LEU B 137     120.394  86.683 -21.144  1.00 14.08           O  
ANISOU 1890  O   LEU B 137     2061   1384   1904   -345    360     87       O  
ATOM   1891  CB  LEU B 137     122.665  85.392 -19.661  1.00 12.63           C  
ANISOU 1891  CB  LEU B 137     2115    917   1768   -119    104     88       C  
ATOM   1892  CG  LEU B 137     122.646  84.063 -20.392  1.00 13.33           C  
ANISOU 1892  CG  LEU B 137     2178    980   1908    -46    350    -37       C  
ATOM   1893  CD1 LEU B 137     123.961  83.870 -21.103  1.00 14.30           C  
ANISOU 1893  CD1 LEU B 137     2061   1380   1992    -56    114   -225       C  
ATOM   1894  CD2 LEU B 137     122.381  82.941 -19.409  1.00 14.93           C  
ANISOU 1894  CD2 LEU B 137     2502   1131   2039    -14    666    134       C  
ATOM   1895  N   ALA B 138     121.898  86.514 -22.815  1.00 12.43           N  
ANISOU 1895  N   ALA B 138     2115    948   1658   -184    411    103       N  
ATOM   1896  CA  ALA B 138     120.946  86.305 -23.903  1.00 14.48           C  
ANISOU 1896  CA  ALA B 138     2207   1274   2019   -253    125    -47       C  
ATOM   1897  C   ALA B 138     119.983  87.468 -24.131  1.00 16.89           C  
ANISOU 1897  C   ALA B 138     2356   1787   2275   -104   -106   -126       C  
ATOM   1898  O   ALA B 138     119.045  87.331 -24.918  1.00 21.05           O  
ANISOU 1898  O   ALA B 138     2892   2425   2682    313   -612   -184       O  
ATOM   1899  CB  ALA B 138     120.182  84.978 -23.775  1.00 16.12           C  
ANISOU 1899  CB  ALA B 138     2268   1602   2255   -347    111   -194       C  
ATOM   1900  N   LYS B 139     120.201  88.615 -23.504  1.00 14.44           N  
ANISOU 1900  N   LYS B 139     2137   1296   2054     -8    332    120       N  
ATOM   1901  CA  LYS B 139     119.311  89.752 -23.664  1.00 14.26           C  
ANISOU 1901  CA  LYS B 139     2111   1408   1898     75    345    173       C  
ATOM   1902  C   LYS B 139     119.762  90.627 -24.830  1.00 13.90           C  
ANISOU 1902  C   LYS B 139     2144   1339   1797    147    367     27       C  
ATOM   1903  O   LYS B 139     120.904  90.568 -25.282  1.00 14.35           O  
ANISOU 1903  O   LYS B 139     2199   1489   1766    124    489     25       O  
ATOM   1904  CB  LYS B 139     119.300  90.588 -22.387  1.00 17.75           C  
ANISOU 1904  CB  LYS B 139     2542   2051   2152    177    423    312       C  
ATOM   1905  CG  LYS B 139     118.816  89.846 -21.156  1.00 22.21           C  
ANISOU 1905  CG  LYS B 139     3011   2817   2612    109    656    589       C  
ATOM   1906  CD  LYS B 139     117.323  89.626 -21.218  1.00 26.08           C  
ANISOU 1906  CD  LYS B 139     3453   3460   2998   -236    633    744       C  
ATOM   1907  CE  LYS B 139     116.836  88.813 -20.029  1.00 29.33           C  
ANISOU 1907  CE  LYS B 139     3942   3926   3278   -335    583    712       C  
ATOM   1908  NZ  LYS B 139     117.048  89.515 -18.734  1.00 32.07           N1+
ANISOU 1908  NZ  LYS B 139     4262   4320   3602   -440    525    744       N1+
ATOM   1909  N   THR B 140     118.841  91.463 -25.299  1.00 14.22           N  
ANISOU 1909  N   THR B 140     2113   1473   1816    361    269    206       N  
ATOM   1910  CA  THR B 140     119.095  92.321 -26.451  1.00 12.22           C  
ANISOU 1910  CA  THR B 140     1742   1211   1690    146    196     67       C  
ATOM   1911  C   THR B 140     120.189  93.333 -26.147  1.00 12.51           C  
ANISOU 1911  C   THR B 140     1782   1312   1660    -69    281   -123       C  
ATOM   1912  O   THR B 140     120.095  94.096 -25.180  1.00 14.78           O  
ANISOU 1912  O   THR B 140     2379   1587   1651   -264    332   -208       O  
ATOM   1913  CB  THR B 140     117.814  93.077 -26.790  1.00 14.38           C  
ANISOU 1913  CB  THR B 140     2188   1450   1825    132     61    152       C  
ATOM   1914  OG1 THR B 140     116.758  92.136 -26.999  1.00 15.95           O  
ANISOU 1914  OG1 THR B 140     2283   1685   2094    -67    -57    -90       O  
ATOM   1915  CG2 THR B 140     118.004  93.932 -28.047  1.00 15.94           C  
ANISOU 1915  CG2 THR B 140     2670   1578   1807     72     33    295       C  
ATOM   1916  N   CYS B 141     121.204  93.371 -27.006  1.00 11.50           N  
ANISOU 1916  N   CYS B 141     1666   1120   1586    -72    234    -96       N  
ATOM   1917  CA  CYS B 141     122.264  94.376 -26.940  1.00 12.23           C  
ANISOU 1917  CA  CYS B 141     2013    973   1660    -21    115     97       C  
ATOM   1918  C   CYS B 141     122.227  95.190 -28.219  1.00 12.27           C  
ANISOU 1918  C   CYS B 141     2082   1022   1560    -46    245     11       C  
ATOM   1919  O   CYS B 141     122.705  94.722 -29.267  1.00 13.01           O  
ANISOU 1919  O   CYS B 141     2354    997   1591     56    320    -84       O  
ATOM   1920  CB  CYS B 141     123.627  93.706 -26.814  1.00 13.52           C  
ANISOU 1920  CB  CYS B 141     2134   1333   1668     11     67    280       C  
ATOM   1921  SG  CYS B 141     123.793  92.705 -25.355  1.00 15.33           S  
ANISOU 1921  SG  CYS B 141     2459   1665   1700    111    -40    184       S  
ATOM   1922  N   PRO B 142     121.682  96.405 -28.197  1.00 11.93           N  
ANISOU 1922  N   PRO B 142     2100    978   1455     57    350     15       N  
ATOM   1923  CA  PRO B 142     121.658  97.217 -29.418  1.00 12.25           C  
ANISOU 1923  CA  PRO B 142     2103   1106   1445    -26    332     29       C  
ATOM   1924  C   PRO B 142     123.037  97.804 -29.670  1.00 12.55           C  
ANISOU 1924  C   PRO B 142     2226   1133   1411   -387     39   -182       C  
ATOM   1925  O   PRO B 142     123.647  98.411 -28.783  1.00 14.91           O  
ANISOU 1925  O   PRO B 142     2781   1330   1555   -518    -73   -387       O  
ATOM   1926  CB  PRO B 142     120.649  98.327 -29.095  1.00 13.44           C  
ANISOU 1926  CB  PRO B 142     2137   1331   1639    397    417     -7       C  
ATOM   1927  CG  PRO B 142     119.938  97.872 -27.842  1.00 15.49           C  
ANISOU 1927  CG  PRO B 142     2413   1762   1711    554    499     48       C  
ATOM   1928  CD  PRO B 142     120.931  97.036 -27.100  1.00 14.07           C  
ANISOU 1928  CD  PRO B 142     2414   1290   1642    415    426   -131       C  
ATOM   1929  N   VAL B 143     123.529  97.613 -30.884  1.00 11.14           N  
ANISOU 1929  N   VAL B 143     1868   1009   1354    -37     34      3       N  
ATOM   1930  CA  VAL B 143     124.783  98.198 -31.319  1.00 11.78           C  
ANISOU 1930  CA  VAL B 143     1983   1047   1445    -41   -169    128       C  
ATOM   1931  C   VAL B 143     124.472  99.014 -32.559  1.00 11.24           C  
ANISOU 1931  C   VAL B 143     1935    971   1364   -218   -172    132       C  
ATOM   1932  O   VAL B 143     123.908  98.493 -33.528  1.00 12.75           O  
ANISOU 1932  O   VAL B 143     2167   1208   1469   -184   -403    -55       O  
ATOM   1933  CB  VAL B 143     125.842  97.122 -31.600  1.00 11.67           C  
ANISOU 1933  CB  VAL B 143     1914    989   1532     57   -126    237       C  
ATOM   1934  CG1 VAL B 143     127.109  97.771 -32.120  1.00 12.72           C  
ANISOU 1934  CG1 VAL B 143     1927   1094   1813     18     68    251       C  
ATOM   1935  CG2 VAL B 143     126.121  96.323 -30.329  1.00 11.70           C  
ANISOU 1935  CG2 VAL B 143     1947   1006   1493    304   -228    130       C  
ATOM   1936  N   GLN B 144     124.806 100.296 -32.517  1.00 11.20           N  
ANISOU 1936  N   GLN B 144     1998    896   1362   -152   -232    184       N  
ATOM   1937  CA  GLN B 144     124.553 101.175 -33.643  1.00 10.47           C  
ANISOU 1937  CA  GLN B 144     1856    700   1421    211     68    189       C  
ATOM   1938  C   GLN B 144     125.727 101.156 -34.599  1.00 10.56           C  
ANISOU 1938  C   GLN B 144     1963    653   1397    163    -30    -74       C  
ATOM   1939  O   GLN B 144     126.884 101.080 -34.180  1.00 11.40           O  
ANISOU 1939  O   GLN B 144     1905    839   1588    -24     71     89       O  
ATOM   1940  CB  GLN B 144     124.374 102.606 -33.149  1.00 12.12           C  
ANISOU 1940  CB  GLN B 144     2158    773   1674    429    203   -121       C  
ATOM   1941  CG  GLN B 144     123.227 102.762 -32.191  1.00 14.23           C  
ANISOU 1941  CG  GLN B 144     2444   1194   1769    319    310   -292       C  
ATOM   1942  CD  GLN B 144     123.145 104.152 -31.644  1.00 16.21           C  
ANISOU 1942  CD  GLN B 144     2659   1740   1761    213    258   -345       C  
ATOM   1943  OE1 GLN B 144     124.143 104.875 -31.603  1.00 15.83           O  
ANISOU 1943  OE1 GLN B 144     2556   1711   1750    258    431     -5       O  
ATOM   1944  NE2 GLN B 144     121.957 104.545 -31.221  1.00 19.88           N  
ANISOU 1944  NE2 GLN B 144     2903   2534   2114    256    209   -663       N  
ATOM   1945  N   LEU B 145     125.422 101.263 -35.885  1.00 11.70           N  
ANISOU 1945  N   LEU B 145     2333    827   1286     97     64    -49       N  
ATOM   1946  CA  LEU B 145     126.433 101.411 -36.920  1.00 11.74           C  
ANISOU 1946  CA  LEU B 145     2438    702   1323    150    132   -127       C  
ATOM   1947  C   LEU B 145     126.277 102.806 -37.501  1.00 12.65           C  
ANISOU 1947  C   LEU B 145     2521    791   1497    299     43    180       C  
ATOM   1948  O   LEU B 145     125.209 103.144 -38.021  1.00 14.54           O  
ANISOU 1948  O   LEU B 145     2467   1110   1947    320   -155    239       O  
ATOM   1949  CB  LEU B 145     126.217 100.379 -38.025  1.00 13.65           C  
ANISOU 1949  CB  LEU B 145     2742    915   1528    231   -162   -339       C  
ATOM   1950  CG  LEU B 145     125.962  98.951 -37.548  1.00 14.54           C  
ANISOU 1950  CG  LEU B 145     2701   1216   1608    383   -311   -233       C  
ATOM   1951  CD1 LEU B 145     125.667  98.049 -38.756  1.00 16.75           C  
ANISOU 1951  CD1 LEU B 145     3060   1438   1864    476   -306   -476       C  
ATOM   1952  CD2 LEU B 145     127.136  98.419 -36.719  1.00 14.51           C  
ANISOU 1952  CD2 LEU B 145     2507   1415   1591    726   -311    -47       C  
ATOM   1953  N   TRP B 146     127.333 103.604 -37.414  1.00 11.64           N  
ANISOU 1953  N   TRP B 146     2463    656   1305    118    315     97       N  
ATOM   1954  CA  TRP B 146     127.353 104.952 -37.961  1.00 11.35           C  
ANISOU 1954  CA  TRP B 146     2374    691   1246    145    227     43       C  
ATOM   1955  C   TRP B 146     128.314 105.001 -39.137  1.00 12.81           C  
ANISOU 1955  C   TRP B 146     2532    978   1355    219    176    204       C  
ATOM   1956  O   TRP B 146     129.410 104.444 -39.068  1.00 13.53           O  
ANISOU 1956  O   TRP B 146     2457   1198   1488    389    203     77       O  
ATOM   1957  CB  TRP B 146     127.822 105.939 -36.889  1.00 11.88           C  
ANISOU 1957  CB  TRP B 146     2461    655   1400    -32    150    -89       C  
ATOM   1958  CG  TRP B 146     126.832 106.077 -35.796  1.00 12.06           C  
ANISOU 1958  CG  TRP B 146     2431    694   1459    170    301     -6       C  
ATOM   1959  CD1 TRP B 146     126.747 105.324 -34.656  1.00 12.62           C  
ANISOU 1959  CD1 TRP B 146     2496    817   1483     97    361    -51       C  
ATOM   1960  CD2 TRP B 146     125.758 107.015 -35.741  1.00 11.97           C  
ANISOU 1960  CD2 TRP B 146     2216    735   1598    208    145    -45       C  
ATOM   1961  NE1 TRP B 146     125.685 105.752 -33.891  1.00 12.56           N  
ANISOU 1961  NE1 TRP B 146     2196    916   1658    232    233    -59       N  
ATOM   1962  CE2 TRP B 146     125.060 106.784 -34.540  1.00 12.24           C  
ANISOU 1962  CE2 TRP B 146     2218    811   1623    253    108   -109       C  
ATOM   1963  CE3 TRP B 146     125.308 108.022 -36.600  1.00 13.36           C  
ANISOU 1963  CE3 TRP B 146     2428    932   1716    464     39     23       C  
ATOM   1964  CZ2 TRP B 146     123.945 107.534 -34.171  1.00 12.73           C  
ANISOU 1964  CZ2 TRP B 146     2389    671   1778    185     26     23       C  
ATOM   1965  CZ3 TRP B 146     124.207 108.763 -36.228  1.00 15.34           C  
ANISOU 1965  CZ3 TRP B 146     2825   1098   1907    411     80    -90       C  
ATOM   1966  CH2 TRP B 146     123.530 108.506 -35.035  1.00 13.98           C  
ANISOU 1966  CH2 TRP B 146     2548    949   1814    267    -58    -13       C  
ATOM   1967  N   VAL B 147     127.894 105.665 -40.217  1.00 14.14           N  
ANISOU 1967  N   VAL B 147     2755   1297   1320    327    150    371       N  
ATOM   1968  CA  VAL B 147     128.743 105.876 -41.382  1.00 14.72           C  
ANISOU 1968  CA  VAL B 147     3174   1109   1312    427    140    190       C  
ATOM   1969  C   VAL B 147     128.580 107.312 -41.848  1.00 16.26           C  
ANISOU 1969  C   VAL B 147     3628   1147   1403    453    154    269       C  
ATOM   1970  O   VAL B 147     127.527 107.926 -41.663  1.00 18.70           O  
ANISOU 1970  O   VAL B 147     3873   1643   1589    636    104    348       O  
ATOM   1971  CB  VAL B 147     128.427 104.908 -42.547  1.00 14.61           C  
ANISOU 1971  CB  VAL B 147     3064   1171   1315    559    -69    -18       C  
ATOM   1972  CG1 VAL B 147     128.835 103.481 -42.180  1.00 15.91           C  
ANISOU 1972  CG1 VAL B 147     3174   1283   1586    645    161    207       C  
ATOM   1973  CG2 VAL B 147     126.954 104.966 -42.894  1.00 16.46           C  
ANISOU 1973  CG2 VAL B 147     3321   1595   1339    589   -275   -115       C  
ATOM   1974  N   ASP B 148     129.640 107.845 -42.454  1.00 17.10           N  
ANISOU 1974  N   ASP B 148     3886   1164   1446    307    394    271       N  
ATOM   1975  CA  ASP B 148     129.550 109.155 -43.092  1.00 18.67           C  
ANISOU 1975  CA  ASP B 148     4141   1200   1753    226     97    325       C  
ATOM   1976  C   ASP B 148     128.931 109.074 -44.480  1.00 19.64           C  
ANISOU 1976  C   ASP B 148     4401   1231   1830    294      9    267       C  
ATOM   1977  O   ASP B 148     128.358 110.058 -44.963  1.00 20.96           O  
ANISOU 1977  O   ASP B 148     4536   1553   1875    550    -93    291       O  
ATOM   1978  CB  ASP B 148     130.937 109.780 -43.197  1.00 19.84           C  
ANISOU 1978  CB  ASP B 148     4417   1316   1803    -98     45    309       C  
ATOM   1979  CG  ASP B 148     131.528 110.107 -41.848  1.00 22.08           C  
ANISOU 1979  CG  ASP B 148     4689   1729   1970     -8    -11    189       C  
ATOM   1980  OD1 ASP B 148     130.761 110.478 -40.933  1.00 22.37           O  
ANISOU 1980  OD1 ASP B 148     4754   1709   2038    159    107     36       O  
ATOM   1981  OD2 ASP B 148     132.762 109.992 -41.708  1.00 23.93           O1-
ANISOU 1981  OD2 ASP B 148     4945   2018   2128    -14   -161    172       O1-
ATOM   1982  N   SER B 149     129.060 107.936 -45.151  1.00 19.74           N  
ANISOU 1982  N   SER B 149     4541   1172   1787    164    -12    131       N  
ATOM   1983  CA  SER B 149     128.418 107.748 -46.440  1.00 20.89           C  
ANISOU 1983  CA  SER B 149     4713   1368   1857    133    120     30       C  
ATOM   1984  C   SER B 149     127.948 106.306 -46.534  1.00 19.21           C  
ANISOU 1984  C   SER B 149     4421   1159   1718    345    121     56       C  
ATOM   1985  O   SER B 149     128.484 105.414 -45.873  1.00 18.80           O  
ANISOU 1985  O   SER B 149     4379   1331   1432    374     -3    224       O  
ATOM   1986  CB  SER B 149     129.337 108.107 -47.615  1.00 24.59           C  
ANISOU 1986  CB  SER B 149     5036   2019   2287    141    316    194       C  
ATOM   1987  OG  SER B 149     130.535 107.361 -47.572  1.00 25.86           O  
ANISOU 1987  OG  SER B 149     5255   2036   2534    -11    415    182       O  
ATOM   1988  N   THR B 150     126.936 106.094 -47.360  1.00 19.92           N  
ANISOU 1988  N   THR B 150     4134   1369   2064    329     28   -102       N  
ATOM   1989  CA  THR B 150     126.273 104.801 -47.422  1.00 19.30           C  
ANISOU 1989  CA  THR B 150     3830   1352   2151    616    -64   -128       C  
ATOM   1990  C   THR B 150     127.139 103.804 -48.181  1.00 17.44           C  
ANISOU 1990  C   THR B 150     3560   1261   1806    530    -43     24       C  
ATOM   1991  O   THR B 150     127.491 104.057 -49.339  1.00 18.89           O  
ANISOU 1991  O   THR B 150     3618   1719   1840    335    -66    -70       O  
ATOM   1992  CB  THR B 150     124.937 104.950 -48.127  1.00 21.84           C  
ANISOU 1992  CB  THR B 150     3883   1795   2619   1030    -88   -371       C  
ATOM   1993  OG1 THR B 150     124.168 105.965 -47.468  1.00 25.01           O  
ANISOU 1993  OG1 THR B 150     4161   2246   3094   1263    -29   -416       O  
ATOM   1994  CG2 THR B 150     124.177 103.631 -48.100  1.00 22.08           C  
ANISOU 1994  CG2 THR B 150     3774   1995   2620    865   -193   -413       C  
ATOM   1995  N   PRO B 151     127.494 102.670 -47.587  1.00 16.09           N  
ANISOU 1995  N   PRO B 151     3478   1078   1558    443    -37     -7       N  
ATOM   1996  CA  PRO B 151     128.262 101.664 -48.318  1.00 16.11           C  
ANISOU 1996  CA  PRO B 151     3238   1363   1518    361      6    -83       C  
ATOM   1997  C   PRO B 151     127.390 100.960 -49.342  1.00 15.21           C  
ANISOU 1997  C   PRO B 151     3025   1283   1471    250    -91     83       C  
ATOM   1998  O   PRO B 151     126.152 101.021 -49.275  1.00 16.34           O  
ANISOU 1998  O   PRO B 151     3095   1506   1606    305   -163   -210       O  
ATOM   1999  CB  PRO B 151     128.722 100.700 -47.214  1.00 16.56           C  
ANISOU 1999  CB  PRO B 151     3365   1423   1505    571     98   -127       C  
ATOM   2000  CG  PRO B 151     127.754 100.886 -46.113  1.00 17.04           C  
ANISOU 2000  CG  PRO B 151     3504   1407   1563    774    393    -49       C  
ATOM   2001  CD  PRO B 151     127.270 102.299 -46.177  1.00 16.40           C  
ANISOU 2001  CD  PRO B 151     3513   1171   1548    367    195    109       C  
ATOM   2002  N   PRO B 152     128.004 100.288 -50.307  1.00 14.14           N  
ANISOU 2002  N   PRO B 152     2943   1059   1371    219    -73     42       N  
ATOM   2003  CA  PRO B 152     127.259  99.741 -51.449  1.00 14.41           C  
ANISOU 2003  CA  PRO B 152     3007   1080   1388     75    -58    -99       C  
ATOM   2004  C   PRO B 152     126.318  98.620 -51.047  1.00 14.08           C  
ANISOU 2004  C   PRO B 152     2765   1226   1357    338   -206    114       C  
ATOM   2005  O   PRO B 152     126.532  97.936 -50.034  1.00 15.00           O  
ANISOU 2005  O   PRO B 152     2877   1368   1453    141   -153    125       O  
ATOM   2006  CB  PRO B 152     128.373  99.197 -52.356  1.00 15.83           C  
ANISOU 2006  CB  PRO B 152     3102   1559   1356     25    386   -182       C  
ATOM   2007  CG  PRO B 152     129.585  99.933 -51.972  1.00 16.44           C  
ANISOU 2007  CG  PRO B 152     3229   1611   1407    121    193   -213       C  
ATOM   2008  CD  PRO B 152     129.461 100.233 -50.515  1.00 14.61           C  
ANISOU 2008  CD  PRO B 152     2914   1258   1381    142    170    -57       C  
ATOM   2009  N   PRO B 153     125.289  98.364 -51.853  1.00 14.75           N  
ANISOU 2009  N   PRO B 153     2752   1350   1501    437   -434    267       N  
ATOM   2010  CA  PRO B 153     124.457  97.173 -51.633  1.00 14.66           C  
ANISOU 2010  CA  PRO B 153     2693   1415   1462    334   -391    175       C  
ATOM   2011  C   PRO B 153     125.324  95.926 -51.634  1.00 14.32           C  
ANISOU 2011  C   PRO B 153     2762   1255   1424    214   -306    111       C  
ATOM   2012  O   PRO B 153     126.201  95.758 -52.483  1.00 15.08           O  
ANISOU 2012  O   PRO B 153     2896   1421   1412    314    -25     53       O  
ATOM   2013  CB  PRO B 153     123.503  97.175 -52.833  1.00 16.80           C  
ANISOU 2013  CB  PRO B 153     2768   1925   1688    437   -696    202       C  
ATOM   2014  CG  PRO B 153     123.536  98.553 -53.362  1.00 17.61           C  
ANISOU 2014  CG  PRO B 153     2948   1901   1844    391   -737    231       C  
ATOM   2015  CD  PRO B 153     124.872  99.133 -53.040  1.00 16.34           C  
ANISOU 2015  CD  PRO B 153     2702   1839   1666    644   -705    343       C  
ATOM   2016  N   GLY B 154     125.076  95.047 -50.674  1.00 13.00           N  
ANISOU 2016  N   GLY B 154     2595    975   1368    143   -303    170       N  
ATOM   2017  CA  GLY B 154     125.878  93.854 -50.523  1.00 11.90           C  
ANISOU 2017  CA  GLY B 154     2415    850   1257    186   -265     13       C  
ATOM   2018  C   GLY B 154     126.917  93.959 -49.435  1.00 11.28           C  
ANISOU 2018  C   GLY B 154     2251    808   1225    146   -255     26       C  
ATOM   2019  O   GLY B 154     127.549  92.950 -49.101  1.00 12.50           O  
ANISOU 2019  O   GLY B 154     2319   1070   1362     55   -131     24       O  
ATOM   2020  N   THR B 155     127.116  95.151 -48.886  1.00 11.71           N  
ANISOU 2020  N   THR B 155     2312   1037   1101      9   -217   -148       N  
ATOM   2021  CA  THR B 155     127.956  95.295 -47.709  1.00 10.83           C  
ANISOU 2021  CA  THR B 155     2339    821    955    -82   -265     64       C  
ATOM   2022  C   THR B 155     127.357  94.481 -46.574  1.00 11.37           C  
ANISOU 2022  C   THR B 155     2271   1043   1007     39    -93     75       C  
ATOM   2023  O   THR B 155     126.135  94.346 -46.470  1.00 11.76           O  
ANISOU 2023  O   THR B 155     2169   1060   1240    139    -68     51       O  
ATOM   2024  CB  THR B 155     128.026  96.780 -47.334  1.00 10.92           C  
ANISOU 2024  CB  THR B 155     2402    763    986    -22    -48   -101       C  
ATOM   2025  OG1 THR B 155     128.593  97.507 -48.431  1.00 11.91           O  
ANISOU 2025  OG1 THR B 155     2455    824   1246    -74    224     81       O  
ATOM   2026  CG2 THR B 155     128.883  97.010 -46.100  1.00 11.49           C  
ANISOU 2026  CG2 THR B 155     2399    936   1030   -166   -149     13       C  
ATOM   2027  N   ARG B 156     128.222  93.900 -45.743  1.00 10.27           N  
ANISOU 2027  N   ARG B 156     2020    977    906    -32     20    223       N  
ATOM   2028  CA  ARG B 156     127.777  93.104 -44.614  1.00 10.43           C  
ANISOU 2028  CA  ARG B 156     2012    875   1077   -136    -46    110       C  
ATOM   2029  C   ARG B 156     128.473  93.576 -43.350  1.00  9.04           C  
ANISOU 2029  C   ARG B 156     1936    496   1004     64     43     65       C  
ATOM   2030  O   ARG B 156     129.449  94.329 -43.388  1.00 10.38           O  
ANISOU 2030  O   ARG B 156     1892    909   1143   -237      6    -39       O  
ATOM   2031  CB  ARG B 156     128.020  91.613 -44.854  1.00 11.37           C  
ANISOU 2031  CB  ARG B 156     2252    884   1186    -88   -422     28       C  
ATOM   2032  CG  ARG B 156     127.308  91.094 -46.077  1.00 12.45           C  
ANISOU 2032  CG  ARG B 156     2583    933   1214   -222   -390     39       C  
ATOM   2033  CD  ARG B 156     126.912  89.647 -45.910  1.00 13.04           C  
ANISOU 2033  CD  ARG B 156     2693    817   1446   -167   -198   -135       C  
ATOM   2034  NE  ARG B 156     128.068  88.771 -45.941  1.00 12.69           N  
ANISOU 2034  NE  ARG B 156     2705    704   1411    -98      0   -127       N  
ATOM   2035  CZ  ARG B 156     127.991  87.458 -45.783  1.00 13.35           C  
ANISOU 2035  CZ  ARG B 156     2775    846   1449   -229   -143    -75       C  
ATOM   2036  NH1 ARG B 156     126.815  86.899 -45.526  1.00 14.07           N1+
ANISOU 2036  NH1 ARG B 156     2885   1042   1417   -597    117    -20       N1+
ATOM   2037  NH2 ARG B 156     129.089  86.714 -45.867  1.00 15.22           N  
ANISOU 2037  NH2 ARG B 156     3027   1101   1656     74   -142    -36       N  
ATOM   2038  N   VAL B 157     127.943  93.128 -42.216  1.00  9.44           N  
ANISOU 2038  N   VAL B 157     1949    696    940     13     35    122       N  
ATOM   2039  CA  VAL B 157     128.432  93.518 -40.902  1.00  9.63           C  
ANISOU 2039  CA  VAL B 157     2072    738    847    155   -226     25       C  
ATOM   2040  C   VAL B 157     128.653  92.242 -40.106  1.00  9.35           C  
ANISOU 2040  C   VAL B 157     1891    770    892    -62   -242    214       C  
ATOM   2041  O   VAL B 157     127.705  91.475 -39.887  1.00  9.39           O  
ANISOU 2041  O   VAL B 157     1584    854   1131   -141    -49     47       O  
ATOM   2042  CB  VAL B 157     127.424  94.416 -40.167  1.00 11.22           C  
ANISOU 2042  CB  VAL B 157     2392    785   1085    213    -86    -19       C  
ATOM   2043  CG1 VAL B 157     128.025  94.899 -38.850  1.00 12.68           C  
ANISOU 2043  CG1 VAL B 157     2594   1000   1225    134   -250   -245       C  
ATOM   2044  CG2 VAL B 157     126.978  95.573 -41.056  1.00 13.37           C  
ANISOU 2044  CG2 VAL B 157     2581   1106   1392    274      0    110       C  
ATOM   2045  N   ARG B 158     129.890  92.009 -39.680  1.00  9.41           N  
ANISOU 2045  N   ARG B 158     1821    893    860    111   -229    142       N  
ATOM   2046  CA  ARG B 158     130.258  90.774 -39.000  1.00  9.11           C  
ANISOU 2046  CA  ARG B 158     1686    876    900    178   -144    -35       C  
ATOM   2047  C   ARG B 158     130.637  91.066 -37.557  1.00  8.93           C  
ANISOU 2047  C   ARG B 158     1637    745   1011    -61   -155    -14       C  
ATOM   2048  O   ARG B 158     131.262  92.085 -37.266  1.00  9.79           O  
ANISOU 2048  O   ARG B 158     1671    854   1197   -308   -150     55       O  
ATOM   2049  CB  ARG B 158     131.441  90.095 -39.702  1.00  9.49           C  
ANISOU 2049  CB  ARG B 158     1794    697   1116    358    100   -110       C  
ATOM   2050  CG  ARG B 158     131.820  88.753 -39.089  1.00 10.55           C  
ANISOU 2050  CG  ARG B 158     2042    777   1189    496     84   -108       C  
ATOM   2051  CD  ARG B 158     132.947  88.086 -39.873  1.00 12.11           C  
ANISOU 2051  CD  ARG B 158     2200   1016   1383    702    260    -89       C  
ATOM   2052  NE  ARG B 158     132.613  87.983 -41.293  1.00 13.11           N  
ANISOU 2052  NE  ARG B 158     2480   1171   1330    446    199   -138       N  
ATOM   2053  CZ  ARG B 158     131.924  86.992 -41.851  1.00 12.64           C  
ANISOU 2053  CZ  ARG B 158     2603    943   1255    582    304     19       C  
ATOM   2054  NH1 ARG B 158     131.508  85.961 -41.125  1.00 13.45           N1+
ANISOU 2054  NH1 ARG B 158     2694    879   1537     10    190    185       N1+
ATOM   2055  NH2 ARG B 158     131.656  87.030 -43.155  1.00 14.18           N  
ANISOU 2055  NH2 ARG B 158     2810   1485   1092    471    258   -109       N  
ATOM   2056  N   ALA B 159     130.264  90.162 -36.655  1.00  9.04           N  
ANISOU 2056  N   ALA B 159     1606    842    987     12   -188    240       N  
ATOM   2057  CA  ALA B 159     130.658  90.245 -35.258  1.00  8.06           C  
ANISOU 2057  CA  ALA B 159     1302    713   1047     74   -141     78       C  
ATOM   2058  C   ALA B 159     131.413  88.982 -34.876  1.00  8.53           C  
ANISOU 2058  C   ALA B 159     1377    778   1086      4     -3    139       C  
ATOM   2059  O   ALA B 159     131.002  87.867 -35.219  1.00  9.18           O  
ANISOU 2059  O   ALA B 159     1454    844   1191    -40   -136     72       O  
ATOM   2060  CB  ALA B 159     129.444  90.391 -34.340  1.00  9.52           C  
ANISOU 2060  CB  ALA B 159     1438   1115   1065     84    142     59       C  
ATOM   2061  N   MET B 160     132.496  89.166 -34.139  1.00  8.74           N  
ANISOU 2061  N   MET B 160     1408    830   1081     72    -66     83       N  
ATOM   2062  CA  MET B 160     133.317  88.058 -33.677  1.00  8.62           C  
ANISOU 2062  CA  MET B 160     1316    801   1160     86   -137      8       C  
ATOM   2063  C   MET B 160     133.857  88.426 -32.305  1.00  9.22           C  
ANISOU 2063  C   MET B 160     1602    763   1140    -56    -87     73       C  
ATOM   2064  O   MET B 160     134.186  89.587 -32.061  1.00 11.15           O  
ANISOU 2064  O   MET B 160     2146    637   1454   -219   -331    190       O  
ATOM   2065  CB  MET B 160     134.487  87.840 -34.641  1.00 10.80           C  
ANISOU 2065  CB  MET B 160     1708   1019   1375    561     11     68       C  
ATOM   2066  CG  MET B 160     135.444  86.740 -34.236  1.00 12.51           C  
ANISOU 2066  CG  MET B 160     1697   1460   1595    267     93    217       C  
ATOM   2067  SD  MET B 160     136.849  86.627 -35.343  1.00 14.16           S  
ANISOU 2067  SD  MET B 160     1777   1802   1800    159    131   -199       S  
ATOM   2068  CE  MET B 160     136.091  85.986 -36.828  1.00 15.17           C  
ANISOU 2068  CE  MET B 160     2133   1969   1663    335     25   -483       C  
ATOM   2069  N   ALA B 161     133.947  87.446 -31.412  1.00  8.53           N  
ANISOU 2069  N   ALA B 161     1368    839   1032    -30   -146    134       N  
ATOM   2070  CA  ALA B 161     134.549  87.659 -30.106  1.00  8.63           C  
ANISOU 2070  CA  ALA B 161     1378    822   1081    251   -135    100       C  
ATOM   2071  C   ALA B 161     135.960  87.094 -30.090  1.00  9.30           C  
ANISOU 2071  C   ALA B 161     1307    875   1352    150    -81      3       C  
ATOM   2072  O   ALA B 161     136.227  86.054 -30.698  1.00 11.08           O  
ANISOU 2072  O   ALA B 161     1679    951   1582    249   -129    -97       O  
ATOM   2073  CB  ALA B 161     133.734  86.976 -29.010  1.00  9.65           C  
ANISOU 2073  CB  ALA B 161     1710    990    968     51    -94    329       C  
ATOM   2074  N   ILE B 162     136.862  87.791 -29.399  1.00  9.88           N  
ANISOU 2074  N   ILE B 162     1390    904   1459    255   -193    -33       N  
ATOM   2075  CA  ILE B 162     138.191  87.286 -29.085  1.00 10.16           C  
ANISOU 2075  CA  ILE B 162     1338   1028   1496    204   -185     27       C  
ATOM   2076  C   ILE B 162     138.484  87.580 -27.619  1.00  9.42           C  
ANISOU 2076  C   ILE B 162     1123    965   1491     65    -84     42       C  
ATOM   2077  O   ILE B 162     137.915  88.495 -27.022  1.00 10.39           O  
ANISOU 2077  O   ILE B 162     1371    915   1660    216    -31     66       O  
ATOM   2078  CB  ILE B 162     139.306  87.869 -29.980  1.00 11.92           C  
ANISOU 2078  CB  ILE B 162     1737   1193   1599     90     35     53       C  
ATOM   2079  CG1 ILE B 162     139.497  89.364 -29.732  1.00 13.88           C  
ANISOU 2079  CG1 ILE B 162     1971   1499   1802   -330    111    344       C  
ATOM   2080  CG2 ILE B 162     139.044  87.559 -31.457  1.00 13.48           C  
ANISOU 2080  CG2 ILE B 162     1979   1511   1634    166      7    -13       C  
ATOM   2081  CD1 ILE B 162     140.805  89.901 -30.325  1.00 15.72           C  
ANISOU 2081  CD1 ILE B 162     2372   1542   2060   -534    238    421       C  
ATOM   2082  N   TYR B 163     139.391  86.801 -27.037  1.00 10.38           N  
ANISOU 2082  N   TYR B 163     1221   1232   1492     62   -159    266       N  
ATOM   2083  CA  TYR B 163     139.824  87.103 -25.679  1.00 10.83           C  
ANISOU 2083  CA  TYR B 163     1288   1095   1731   -128   -408     65       C  
ATOM   2084  C   TYR B 163     140.708  88.337 -25.681  1.00 11.84           C  
ANISOU 2084  C   TYR B 163     1599   1102   1798   -243   -294    -67       C  
ATOM   2085  O   TYR B 163     141.526  88.533 -26.584  1.00 13.11           O  
ANISOU 2085  O   TYR B 163     1716   1436   1830   -126   -113    -68       O  
ATOM   2086  CB  TYR B 163     140.546  85.909 -25.040  1.00 11.06           C  
ANISOU 2086  CB  TYR B 163     1235   1140   1829    166   -409    256       C  
ATOM   2087  CG  TYR B 163     139.564  84.832 -24.690  1.00 11.11           C  
ANISOU 2087  CG  TYR B 163     1471   1026   1724    -54   -337    168       C  
ATOM   2088  CD1 TYR B 163     138.593  85.061 -23.723  1.00 11.54           C  
ANISOU 2088  CD1 TYR B 163     1655   1126   1602    -10   -229     85       C  
ATOM   2089  CD2 TYR B 163     139.565  83.601 -25.348  1.00 11.51           C  
ANISOU 2089  CD2 TYR B 163     1680   1050   1645     88   -413    216       C  
ATOM   2090  CE1 TYR B 163     137.653  84.108 -23.414  1.00 11.76           C  
ANISOU 2090  CE1 TYR B 163     1810    950   1708    209   -301     55       C  
ATOM   2091  CE2 TYR B 163     138.619  82.634 -25.040  1.00 11.47           C  
ANISOU 2091  CE2 TYR B 163     1713   1117   1526    209   -367    215       C  
ATOM   2092  CZ  TYR B 163     137.670  82.898 -24.071  1.00 11.80           C  
ANISOU 2092  CZ  TYR B 163     1852   1004   1627    158   -198    108       C  
ATOM   2093  OH  TYR B 163     136.713  81.968 -23.762  1.00 13.33           O  
ANISOU 2093  OH  TYR B 163     2054   1271   1739     12    151     44       O  
ATOM   2094  N   LYS B 164     140.526  89.176 -24.662  1.00 12.59           N  
ANISOU 2094  N   LYS B 164     1892   1051   1841   -440   -321   -282       N  
ATOM   2095  CA  LYS B 164     141.247  90.437 -24.584  1.00 14.53           C  
ANISOU 2095  CA  LYS B 164     2028   1351   2142   -496   -225   -384       C  
ATOM   2096  C   LYS B 164     142.699  90.236 -24.173  1.00 16.24           C  
ANISOU 2096  C   LYS B 164     1855   1984   2333   -573   -344   -357       C  
ATOM   2097  O   LYS B 164     143.591  90.929 -24.678  1.00 18.72           O  
ANISOU 2097  O   LYS B 164     2110   2440   2563   -710   -225   -351       O  
ATOM   2098  CB  LYS B 164     140.534  91.369 -23.604  1.00 16.01           C  
ANISOU 2098  CB  LYS B 164     2593   1253   2238   -512    -13   -760       C  
ATOM   2099  CG  LYS B 164     141.217  92.712 -23.418  1.00 20.04           C  
ANISOU 2099  CG  LYS B 164     3047   1840   2727   -623    191   -787       C  
ATOM   2100  CD  LYS B 164     140.503  93.538 -22.380  1.00 23.18           C  
ANISOU 2100  CD  LYS B 164     3491   2129   3188   -788    233   -849       C  
ATOM   2101  CE  LYS B 164     141.248  94.840 -22.115  1.00 25.47           C  
ANISOU 2101  CE  LYS B 164     3788   2413   3475   -698    234   -999       C  
ATOM   2102  NZ  LYS B 164     140.629  95.594 -20.995  1.00 27.78           N1+
ANISOU 2102  NZ  LYS B 164     4066   2841   3650   -394     65   -974       N1+
ATOM   2103  N   GLN B 165     142.955  89.312 -23.252  1.00 16.86           N  
ANISOU 2103  N   GLN B 165     1630   2467   2308   -372   -532   -354       N  
ATOM   2104  CA  GLN B 165     144.292  89.168 -22.693  1.00 18.57           C  
ANISOU 2104  CA  GLN B 165     1623   3021   2411   -299   -478   -536       C  
ATOM   2105  C   GLN B 165     145.206  88.455 -23.678  1.00 19.68           C  
ANISOU 2105  C   GLN B 165     1561   3315   2601   -547   -331   -714       C  
ATOM   2106  O   GLN B 165     144.793  87.513 -24.358  1.00 19.25           O  
ANISOU 2106  O   GLN B 165     1751   2988   2575   -536   -323   -799       O  
ATOM   2107  CB  GLN B 165     144.238  88.376 -21.390  1.00 20.88           C  
ANISOU 2107  CB  GLN B 165     2126   3426   2380    -97   -396   -640       C  
ATOM   2108  CG  GLN B 165     143.483  89.073 -20.273  1.00 22.24           C  
ANISOU 2108  CG  GLN B 165     2326   3692   2430      9   -600   -602       C  
ATOM   2109  CD  GLN B 165     143.121  88.117 -19.162  1.00 24.34           C  
ANISOU 2109  CD  GLN B 165     2818   3975   2455    -66   -773   -439       C  
ATOM   2110  OE1 GLN B 165     142.179  87.336 -19.287  1.00 22.89           O  
ANISOU 2110  OE1 GLN B 165     2644   3694   2361    249   -798   -507       O  
ATOM   2111  NE2 GLN B 165     143.874  88.166 -18.067  1.00 27.47           N  
ANISOU 2111  NE2 GLN B 165     3380   4391   2666   -265   -862   -183       N  
ATOM   2112  N   SER B 166     146.468  88.885 -23.725  1.00 22.34           N  
ANISOU 2112  N   SER B 166     1856   3755   2875   -699    -19   -740       N  
ATOM   2113  CA  SER B 166     147.390  88.321 -24.705  1.00 22.98           C  
ANISOU 2113  CA  SER B 166     1732   4055   2944   -733   -107   -620       C  
ATOM   2114  C   SER B 166     147.588  86.820 -24.514  1.00 21.65           C  
ANISOU 2114  C   SER B 166     1611   4041   2575   -215   -218   -325       C  
ATOM   2115  O   SER B 166     147.803  86.100 -25.493  1.00 21.77           O  
ANISOU 2115  O   SER B 166     1901   3790   2583   -323   -112   -478       O  
ATOM   2116  CB  SER B 166     148.720  89.077 -24.693  1.00 26.95           C  
ANISOU 2116  CB  SER B 166     2285   4616   3339   -730   -358   -627       C  
ATOM   2117  OG  SER B 166     149.265  89.078 -23.395  1.00 30.64           O  
ANISOU 2117  OG  SER B 166     2802   5227   3613   -541   -358   -483       O  
ATOM   2118  N  AGLN B 167     147.494  86.329 -23.274  0.50 20.99           N  
ANISOU 2118  N  AGLN B 167     1431   4164   2380   -118   -490   -255       N  
ATOM   2119  N  BGLN B 167     147.512  86.319 -23.279  0.50 21.37           N  
ANISOU 2119  N  BGLN B 167     1523   4223   2373    -30   -555   -372       N  
ATOM   2120  CA AGLN B 167     147.704  84.907 -23.017  0.50 21.03           C  
ANISOU 2120  CA AGLN B 167     1536   4179   2274    196   -496    -26       C  
ATOM   2121  CA BGLN B 167     147.730  84.888 -23.087  0.50 21.67           C  
ANISOU 2121  CA BGLN B 167     1686   4295   2254    371   -629   -249       C  
ATOM   2122  C  AGLN B 167     146.545  84.046 -23.499  0.50 19.58           C  
ANISOU 2122  C  AGLN B 167     1580   3665   2195    362   -396    -68       C  
ATOM   2123  C  BGLN B 167     146.561  84.046 -23.579  0.50 19.90           C  
ANISOU 2123  C  BGLN B 167     1668   3701   2190    440   -525   -161       C  
ATOM   2124  O  AGLN B 167     146.705  82.828 -23.631  0.50 20.75           O  
ANISOU 2124  O  AGLN B 167     1665   3847   2372    552   -381      3       O  
ATOM   2125  O  BGLN B 167     146.731  82.842 -23.806  0.50 21.05           O  
ANISOU 2125  O  BGLN B 167     1806   3837   2356    630   -618    -71       O  
ATOM   2126  CB AGLN B 167     147.958  84.657 -21.527  0.50 22.69           C  
ANISOU 2126  CB AGLN B 167     1623   4706   2292    175   -457     67       C  
ATOM   2127  CB BGLN B 167     148.053  84.558 -21.627  0.50 23.83           C  
ANISOU 2127  CB BGLN B 167     1879   4943   2232    556   -655   -390       C  
ATOM   2128  CG AGLN B 167     146.826  85.088 -20.607  0.50 24.38           C  
ANISOU 2128  CG AGLN B 167     1808   5036   2418     82   -440    202       C  
ATOM   2129  CG BGLN B 167     146.908  84.775 -20.666  0.50 25.86           C  
ANISOU 2129  CG BGLN B 167     2101   5428   2297    714   -619   -472       C  
ATOM   2130  CD AGLN B 167     147.014  84.592 -19.186  0.50 25.19           C  
ANISOU 2130  CD AGLN B 167     1864   5233   2473    -28   -420    384       C  
ATOM   2131  CD BGLN B 167     147.059  86.057 -19.879  0.50 27.61           C  
ANISOU 2131  CD BGLN B 167     2336   5867   2286    768   -523   -606       C  
ATOM   2132  OE1AGLN B 167     147.208  83.399 -18.955  0.50 25.85           O  
ANISOU 2132  OE1AGLN B 167     1945   5419   2457   -246   -492    621       O  
ATOM   2133  OE1BGLN B 167     147.433  87.099 -20.424  0.50 27.70           O  
ANISOU 2133  OE1BGLN B 167     2182   6108   2235    904   -452   -720       O  
ATOM   2134  NE2AGLN B 167     146.973  85.508 -18.227  0.50 25.96           N  
ANISOU 2134  NE2AGLN B 167     1963   5366   2536    108   -409    392       N  
ATOM   2135  NE2BGLN B 167     146.776  85.988 -18.584  0.50 29.07           N  
ANISOU 2135  NE2BGLN B 167     2662   6066   2317    675   -500   -563       N  
ATOM   2136  N   HIS B 168     145.388  84.646 -23.761  1.00 17.17           N  
ANISOU 2136  N   HIS B 168     1322   3176   2028    297   -474    -39       N  
ATOM   2137  CA  HIS B 168     144.213  83.913 -24.201  1.00 14.83           C  
ANISOU 2137  CA  HIS B 168     1263   2408   1964    178   -447     64       C  
ATOM   2138  C   HIS B 168     143.767  84.247 -25.615  1.00 14.24           C  
ANISOU 2138  C   HIS B 168     1564   1948   1899    152   -370      1       C  
ATOM   2139  O   HIS B 168     142.867  83.578 -26.135  1.00 13.45           O  
ANISOU 2139  O   HIS B 168     1663   1692   1758    378   -377   -125       O  
ATOM   2140  CB  HIS B 168     143.052  84.188 -23.240  1.00 14.86           C  
ANISOU 2140  CB  HIS B 168     1221   2422   2001    302   -433    105       C  
ATOM   2141  CG  HIS B 168     143.348  83.791 -21.834  1.00 16.71           C  
ANISOU 2141  CG  HIS B 168     1590   2711   2051    390   -676    104       C  
ATOM   2142  ND1 HIS B 168     143.675  82.499 -21.488  1.00 18.60           N  
ANISOU 2142  ND1 HIS B 168     1975   2974   2120    542   -768    459       N  
ATOM   2143  CD2 HIS B 168     143.374  84.510 -20.688  1.00 18.47           C  
ANISOU 2143  CD2 HIS B 168     1843   3078   2094    279   -815     55       C  
ATOM   2144  CE1 HIS B 168     143.892  82.438 -20.186  1.00 19.99           C  
ANISOU 2144  CE1 HIS B 168     2278   3167   2150    583   -967    295       C  
ATOM   2145  NE2 HIS B 168     143.712  83.644 -19.676  1.00 19.93           N  
ANISOU 2145  NE2 HIS B 168     2155   3184   2235    540   -899    137       N  
ATOM   2146  N  AMET B 169     144.376  85.248 -26.258  0.05 14.04           N  
ANISOU 2146  N  AMET B 169     1515   1843   1977    209   -230     33       N  
ATOM   2147  N  BMET B 169     144.382  85.239 -26.257  0.95 14.41           N  
ANISOU 2147  N  BMET B 169     1733   1803   1940     85   -311    199       N  
ATOM   2148  CA AMET B 169     143.860  85.742 -27.531  0.05 13.77           C  
ANISOU 2148  CA AMET B 169     1469   1723   2041    246   -112     48       C  
ATOM   2149  CA BMET B 169     143.848  85.732 -27.521  0.95 13.97           C  
ANISOU 2149  CA BMET B 169     1507   1747   2053     65   -303    141       C  
ATOM   2150  C  AMET B 169     143.884  84.693 -28.638  0.05 13.47           C  
ANISOU 2150  C  AMET B 169     1393   1667   2059    249      1     54       C  
ATOM   2151  C  BMET B 169     143.860  84.677 -28.619  0.95 13.32           C  
ANISOU 2151  C  BMET B 169     1438   1515   2107    471    -65     52       C  
ATOM   2152  O  AMET B 169     143.098  84.799 -29.585  0.05 13.57           O  
ANISOU 2152  O  AMET B 169     1399   1687   2072    250     -4     66       O  
ATOM   2153  O  BMET B 169     143.046  84.754 -29.541  0.95 14.21           O  
ANISOU 2153  O  BMET B 169     1627   1649   2123    404   -266     31       O  
ATOM   2154  CB AMET B 169     144.603  87.007 -27.972  0.05 13.90           C  
ANISOU 2154  CB AMET B 169     1526   1664   2091    289    -93     41       C  
ATOM   2155  CB BMET B 169     144.595  86.985 -27.965  0.95 16.99           C  
ANISOU 2155  CB BMET B 169     1737   2234   2483   -121   -238    132       C  
ATOM   2156  CG AMET B 169     146.107  86.844 -28.107  0.05 14.08           C  
ANISOU 2156  CG AMET B 169     1621   1595   2133    340    -77     31       C  
ATOM   2157  CG BMET B 169     146.067  86.781 -28.139  0.95 20.51           C  
ANISOU 2157  CG BMET B 169     2416   2512   2865   -190    -53    166       C  
ATOM   2158  SD AMET B 169     146.887  88.273 -28.885  0.05 14.13           S  
ANISOU 2158  SD AMET B 169     1688   1509   2171    428    -70      6       S  
ATOM   2159  SD BMET B 169     146.841  88.364 -28.455  0.95 23.06           S  
ANISOU 2159  SD BMET B 169     2712   2813   3238    -51     52    116       S  
ATOM   2160  CE AMET B 169     146.267  89.608 -27.866  0.05 14.06           C  
ANISOU 2160  CE AMET B 169     1716   1452   2172    470    -53      6       C  
ATOM   2161  CE BMET B 169     148.557  87.856 -28.429  0.95 22.35           C  
ANISOU 2161  CE BMET B 169     2230   2957   3305     73    159    103       C  
ATOM   2162  N   THR B 170     144.755  83.687 -28.550  1.00 13.11           N  
ANISOU 2162  N   THR B 170     1333   1602   2047    223     99     55       N  
ATOM   2163  CA  THR B 170     144.786  82.666 -29.594  1.00 13.19           C  
ANISOU 2163  CA  THR B 170     1434   1596   1984    311    160    -24       C  
ATOM   2164  C   THR B 170     143.732  81.585 -29.415  1.00 12.45           C  
ANISOU 2164  C   THR B 170     1492   1314   1923    361    276    -15       C  
ATOM   2165  O   THR B 170     143.613  80.716 -30.287  1.00 15.04           O  
ANISOU 2165  O   THR B 170     2045   1787   1881     92    233   -153       O  
ATOM   2166  CB  THR B 170     146.158  81.997 -29.690  1.00 13.79           C  
ANISOU 2166  CB  THR B 170     1441   1800   1999    369    108    176       C  
ATOM   2167  OG1 THR B 170     146.453  81.326 -28.456  1.00 16.11           O  
ANISOU 2167  OG1 THR B 170     1984   1897   2240    383   -149    414       O  
ATOM   2168  CG2 THR B 170     147.225  83.034 -29.995  1.00 13.24           C  
ANISOU 2168  CG2 THR B 170     1189   1815   2026    238    153    158       C  
ATOM   2169  N   GLU B 171     142.976  81.606 -28.321  1.00 12.86           N  
ANISOU 2169  N   GLU B 171     1445   1424   2017    306    178    170       N  
ATOM   2170  CA  GLU B 171     141.959  80.592 -28.075  1.00 12.63           C  
ANISOU 2170  CA  GLU B 171     1539   1308   1950    335     84    270       C  
ATOM   2171  C   GLU B 171     140.618  81.051 -28.640  1.00 12.63           C  
ANISOU 2171  C   GLU B 171     1632   1195   1971    377    -62    135       C  
ATOM   2172  O   GLU B 171     140.209  82.198 -28.432  1.00 13.37           O  
ANISOU 2172  O   GLU B 171     1747   1177   2156    372   -115    -92       O  
ATOM   2173  CB  GLU B 171     141.833  80.343 -26.572  1.00 15.41           C  
ANISOU 2173  CB  GLU B 171     1937   1831   2087    423    -99    343       C  
ATOM   2174  CG  GLU B 171     140.790  79.307 -26.204  1.00 17.49           C  
ANISOU 2174  CG  GLU B 171     2252   2103   2289    236   -188    302       C  
ATOM   2175  CD  GLU B 171     140.733  79.041 -24.709  1.00 20.99           C  
ANISOU 2175  CD  GLU B 171     2700   2703   2574     45   -189    193       C  
ATOM   2176  OE1 GLU B 171     141.754  79.268 -24.026  1.00 23.08           O  
ANISOU 2176  OE1 GLU B 171     3086   2974   2710    -57   -267    126       O  
ATOM   2177  OE2 GLU B 171     139.673  78.600 -24.218  1.00 22.26           O1-
ANISOU 2177  OE2 GLU B 171     2658   3084   2717   -258   -129    106       O1-
ATOM   2178  N   VAL B 172     139.930  80.152 -29.350  1.00 12.37           N  
ANISOU 2178  N   VAL B 172     1656   1271   1774    144    -88    107       N  
ATOM   2179  CA  VAL B 172     138.604  80.470 -29.871  1.00 11.40           C  
ANISOU 2179  CA  VAL B 172     1538   1126   1667    297    -30   -107       C  
ATOM   2180  C   VAL B 172     137.653  80.743 -28.714  1.00 11.09           C  
ANISOU 2180  C   VAL B 172     1554   1135   1526    475   -146   -177       C  
ATOM   2181  O   VAL B 172     137.564  79.951 -27.765  1.00 13.02           O  
ANISOU 2181  O   VAL B 172     1728   1573   1645    249   -263    -51       O  
ATOM   2182  CB  VAL B 172     138.090  79.318 -30.749  1.00 12.29           C  
ANISOU 2182  CB  VAL B 172     1630   1354   1687    397    -47    -92       C  
ATOM   2183  CG1 VAL B 172     136.643  79.555 -31.143  1.00 12.78           C  
ANISOU 2183  CG1 VAL B 172     1603   1427   1826     79    -26   -184       C  
ATOM   2184  CG2 VAL B 172     138.976  79.131 -31.975  1.00 13.82           C  
ANISOU 2184  CG2 VAL B 172     2057   1456   1738    526    114     22       C  
ATOM   2185  N   VAL B 173     136.943  81.870 -28.776  1.00  9.98           N  
ANISOU 2185  N   VAL B 173     1411    912   1470    391    -55   -116       N  
ATOM   2186  CA  VAL B 173     135.892  82.150 -27.804  1.00  9.54           C  
ANISOU 2186  CA  VAL B 173     1208    971   1447    184     76   -186       C  
ATOM   2187  C   VAL B 173     134.683  81.326 -28.207  1.00  9.27           C  
ANISOU 2187  C   VAL B 173     1111    931   1479     77    -26    151       C  
ATOM   2188  O   VAL B 173     134.172  81.467 -29.319  1.00 10.23           O  
ANISOU 2188  O   VAL B 173     1329   1132   1425     -1   -125    182       O  
ATOM   2189  CB  VAL B 173     135.518  83.637 -27.787  1.00  9.24           C  
ANISOU 2189  CB  VAL B 173      948    999   1564    121    239    -44       C  
ATOM   2190  CG1 VAL B 173     134.351  83.862 -26.832  1.00 10.33           C  
ANISOU 2190  CG1 VAL B 173     1223   1110   1593    189    230    -34       C  
ATOM   2191  CG2 VAL B 173     136.701  84.502 -27.388  1.00  9.65           C  
ANISOU 2191  CG2 VAL B 173      889   1094   1682   -233    105    206       C  
ATOM   2192  N   ARG B 174     134.190  80.497 -27.295  1.00 10.19           N  
ANISOU 2192  N   ARG B 174     1341    904   1626   -243     82     91       N  
ATOM   2193  CA  ARG B 174     133.042  79.667 -27.596  1.00 10.01           C  
ANISOU 2193  CA  ARG B 174     1331    915   1559     14    154    157       C  
ATOM   2194  C   ARG B 174     132.182  79.551 -26.355  1.00  9.61           C  
ANISOU 2194  C   ARG B 174     1271    907   1473     62    -71    212       C  
ATOM   2195  O   ARG B 174     132.595  79.909 -25.249  1.00 10.80           O  
ANISOU 2195  O   ARG B 174     1624   1028   1452   -175   -117    110       O  
ATOM   2196  CB  ARG B 174     133.488  78.282 -28.060  1.00 11.76           C  
ANISOU 2196  CB  ARG B 174     1947    857   1666    167    -74   -120       C  
ATOM   2197  CG  ARG B 174     134.330  77.564 -27.034  1.00 12.65           C  
ANISOU 2197  CG  ARG B 174     2196   1058   1553    460   -145     38       C  
ATOM   2198  CD  ARG B 174     134.626  76.113 -27.412  1.00 13.40           C  
ANISOU 2198  CD  ARG B 174     2569    982   1541    305   -156     88       C  
ATOM   2199  NE  ARG B 174     135.362  75.995 -28.669  1.00 14.60           N  
ANISOU 2199  NE  ARG B 174     2843   1042   1661    408   -132    100       N  
ATOM   2200  CZ  ARG B 174     134.790  75.736 -29.844  1.00 16.58           C  
ANISOU 2200  CZ  ARG B 174     3185   1227   1887    378    -12     93       C  
ATOM   2201  NH1 ARG B 174     133.473  75.579 -29.915  1.00 16.96           N1+
ANISOU 2201  NH1 ARG B 174     3288   1245   1913    259   -252    378       N1+
ATOM   2202  NH2 ARG B 174     135.528  75.628 -30.943  1.00 17.37           N  
ANISOU 2202  NH2 ARG B 174     3409   1065   2126    598    413     14       N  
ATOM   2203  N   ARG B 175     130.981  79.022 -26.544  1.00  9.27           N  
ANISOU 2203  N   ARG B 175     1236    878   1406    -28    127     35       N  
ATOM   2204  CA  ARG B 175     130.145  78.769 -25.386  1.00 10.20           C  
ANISOU 2204  CA  ARG B 175     1525   1005   1347     -4    -98    104       C  
ATOM   2205  C   ARG B 175     130.698  77.618 -24.563  1.00 10.64           C  
ANISOU 2205  C   ARG B 175     1817    873   1351    -49   -194     42       C  
ATOM   2206  O   ARG B 175     131.386  76.722 -25.066  1.00 11.75           O  
ANISOU 2206  O   ARG B 175     2103   1031   1331    -44     80     85       O  
ATOM   2207  CB  ARG B 175     128.716  78.472 -25.812  1.00 10.16           C  
ANISOU 2207  CB  ARG B 175     1769    728   1365   -160    -40    132       C  
ATOM   2208  CG  ARG B 175     128.060  79.712 -26.381  1.00 10.14           C  
ANISOU 2208  CG  ARG B 175     1667    727   1458     98    -32    -25       C  
ATOM   2209  CD  ARG B 175     126.658  79.388 -26.763  1.00 10.32           C  
ANISOU 2209  CD  ARG B 175     1402   1051   1468    178    221   -126       C  
ATOM   2210  NE  ARG B 175     125.723  79.486 -25.656  1.00 10.95           N  
ANISOU 2210  NE  ARG B 175     1765   1052   1344    -73    277    169       N  
ATOM   2211  CZ  ARG B 175     124.490  78.997 -25.699  1.00 10.34           C  
ANISOU 2211  CZ  ARG B 175     1914    869   1146   -426    128    332       C  
ATOM   2212  NH1 ARG B 175     124.104  78.262 -26.741  1.00 10.86           N1+
ANISOU 2212  NH1 ARG B 175     1746   1268   1111   -168   -157    236       N1+
ATOM   2213  NH2 ARG B 175     123.653  79.217 -24.698  1.00 12.07           N  
ANISOU 2213  NH2 ARG B 175     2214   1184   1186   -109    125    255       N  
ATOM   2214  N   CYS B 176     130.338  77.638 -23.285  1.00 10.90           N  
ANISOU 2214  N   CYS B 176     2207    637   1295     88   -269    150       N  
ATOM   2215  CA  CYS B 176     130.839  76.707 -22.300  1.00 11.71           C  
ANISOU 2215  CA  CYS B 176     2350    798   1300    236   -293     60       C  
ATOM   2216  C   CYS B 176     130.208  75.329 -22.504  1.00 13.14           C  
ANISOU 2216  C   CYS B 176     2545    932   1515     99   -242     94       C  
ATOM   2217  O   CYS B 176     129.246  75.179 -23.263  1.00 13.05           O  
ANISOU 2217  O   CYS B 176     2616    845   1498    -81    -52     55       O  
ATOM   2218  CB  CYS B 176     130.537  77.255 -20.904  1.00 11.79           C  
ANISOU 2218  CB  CYS B 176     2305    895   1281    244    -75    -50       C  
ATOM   2219  SG  CYS B 176     128.812  77.137 -20.401  1.00 12.24           S  
ANISOU 2219  SG  CYS B 176     2417    738   1497    -44     38     95       S  
ATOM   2220  N   PRO B 177     130.748  74.295 -21.842  1.00 14.04           N  
ANISOU 2220  N   PRO B 177     2791    852   1690    241   -100     48       N  
ATOM   2221  CA  PRO B 177     130.218  72.936 -22.042  1.00 15.51           C  
ANISOU 2221  CA  PRO B 177     3240    848   1805   -106     50    122       C  
ATOM   2222  C   PRO B 177     128.772  72.775 -21.637  1.00 15.86           C  
ANISOU 2222  C   PRO B 177     3457    925   1643   -312    124     80       C  
ATOM   2223  O   PRO B 177     128.087  71.894 -22.174  1.00 19.28           O  
ANISOU 2223  O   PRO B 177     4059   1483   1786   -551    365    -27       O  
ATOM   2224  CB  PRO B 177     131.135  72.068 -21.177  1.00 15.41           C  
ANISOU 2224  CB  PRO B 177     3114    841   1899      5    -31    264       C  
ATOM   2225  CG  PRO B 177     132.374  72.852 -21.031  1.00 16.52           C  
ANISOU 2225  CG  PRO B 177     3213   1057   2007      9    -45    347       C  
ATOM   2226  CD  PRO B 177     131.991  74.284 -21.051  1.00 14.71           C  
ANISOU 2226  CD  PRO B 177     2785   1079   1725    342   -172    218       C  
ATOM   2227  N   HIS B 178     128.289  73.576 -20.689  1.00 14.59           N  
ANISOU 2227  N   HIS B 178     3146    815   1582   -185    -36     93       N  
ATOM   2228  CA  HIS B 178     126.881  73.512 -20.329  1.00 14.11           C  
ANISOU 2228  CA  HIS B 178     3010    821   1528   -165   -113    205       C  
ATOM   2229  C   HIS B 178     126.012  74.137 -21.410  1.00 13.71           C  
ANISOU 2229  C   HIS B 178     2960    785   1463    -22   -180    168       C  
ATOM   2230  O   HIS B 178     125.071  73.514 -21.906  1.00 14.79           O  
ANISOU 2230  O   HIS B 178     3166    873   1581    -21   -164    160       O  
ATOM   2231  CB  HIS B 178     126.632  74.233 -19.012  1.00 15.88           C  
ANISOU 2231  CB  HIS B 178     3311   1158   1565   -196    -24    295       C  
ATOM   2232  CG  HIS B 178     125.184  74.469 -18.750  1.00 16.07           C  
ANISOU 2232  CG  HIS B 178     3298   1247   1560     -9    238    450       C  
ATOM   2233  ND1 HIS B 178     124.289  73.439 -18.551  1.00 17.34           N  
ANISOU 2233  ND1 HIS B 178     3393   1507   1687    216    403    449       N  
ATOM   2234  CD2 HIS B 178     124.462  75.612 -18.711  1.00 17.34           C  
ANISOU 2234  CD2 HIS B 178     3460   1540   1589    193    277    519       C  
ATOM   2235  CE1 HIS B 178     123.082  73.943 -18.365  1.00 18.46           C  
ANISOU 2235  CE1 HIS B 178     3348   1787   1878    122    404    460       C  
ATOM   2236  NE2 HIS B 178     123.159  75.259 -18.461  1.00 19.14           N  
ANISOU 2236  NE2 HIS B 178     3466   1873   1934     17    269    484       N  
ATOM   2237  N   HIS B 179     126.302  75.391 -21.765  1.00 13.29           N  
ANISOU 2237  N   HIS B 179     2848    799   1403    179   -105    192       N  
ATOM   2238  CA  HIS B 179     125.413  76.121 -22.659  1.00 11.29           C  
ANISOU 2238  CA  HIS B 179     2337    605   1347    -89    101     91       C  
ATOM   2239  C   HIS B 179     125.430  75.577 -24.080  1.00 11.58           C  
ANISOU 2239  C   HIS B 179     2369    785   1247     -9    162     86       C  
ATOM   2240  O   HIS B 179     124.400  75.629 -24.763  1.00 12.82           O  
ANISOU 2240  O   HIS B 179     2514   1007   1350     86    -60     11       O  
ATOM   2241  CB  HIS B 179     125.718  77.612 -22.609  1.00 10.91           C  
ANISOU 2241  CB  HIS B 179     2167    572   1407     80    297     14       C  
ATOM   2242  CG  HIS B 179     125.117  78.288 -21.421  1.00 12.47           C  
ANISOU 2242  CG  HIS B 179     2262    910   1565    159    218    -88       C  
ATOM   2243  ND1 HIS B 179     125.874  78.894 -20.444  1.00 14.13           N  
ANISOU 2243  ND1 HIS B 179     2390   1267   1714   -163    135     42       N  
ATOM   2244  CD2 HIS B 179     123.827  78.425 -21.039  1.00 14.49           C  
ANISOU 2244  CD2 HIS B 179     2466   1294   1745    -55    205    -66       C  
ATOM   2245  CE1 HIS B 179     125.073  79.400 -19.523  1.00 14.49           C  
ANISOU 2245  CE1 HIS B 179     2429   1337   1739    -33    196     72       C  
ATOM   2246  NE2 HIS B 179     123.826  79.126 -19.860  1.00 15.10           N  
ANISOU 2246  NE2 HIS B 179     2599   1387   1752    -13     60    -89       N  
ATOM   2247  N   GLU B 180     126.555  75.031 -24.547  1.00 12.19           N  
ANISOU 2247  N   GLU B 180     2521    808   1304    -29     21    122       N  
ATOM   2248  CA  GLU B 180     126.512  74.460 -25.889  1.00 12.88           C  
ANISOU 2248  CA  GLU B 180     2488    869   1538     21     12    -17       C  
ATOM   2249  C   GLU B 180     125.623  73.230 -25.954  1.00 13.10           C  
ANISOU 2249  C   GLU B 180     2662    775   1543     19     -1    -17       C  
ATOM   2250  O   GLU B 180     125.255  72.813 -27.059  1.00 13.85           O  
ANISOU 2250  O   GLU B 180     2820    936   1504     90     29   -104       O  
ATOM   2251  CB  GLU B 180     127.913  74.147 -26.430  1.00 14.35           C  
ANISOU 2251  CB  GLU B 180     2667   1031   1756    -50     68    156       C  
ATOM   2252  CG  GLU B 180     128.567  72.933 -25.789  1.00 14.69           C  
ANISOU 2252  CG  GLU B 180     2707   1124   1750    237    188    278       C  
ATOM   2253  CD  GLU B 180     129.843  72.487 -26.492  1.00 15.55           C  
ANISOU 2253  CD  GLU B 180     3183   1112   1615    325    274    339       C  
ATOM   2254  OE1 GLU B 180     130.342  73.196 -27.392  1.00 15.78           O  
ANISOU 2254  OE1 GLU B 180     3253   1192   1552     77    243     86       O  
ATOM   2255  OE2 GLU B 180     130.346  71.399 -26.149  1.00 18.98           O1-
ANISOU 2255  OE2 GLU B 180     3735   1548   1931    696    392    608       O1-
ATOM   2256  N   ARG B 181     125.246  72.667 -24.801  1.00 12.65           N  
ANISOU 2256  N   ARG B 181     2407    611   1790     12      3    104       N  
ATOM   2257  CA  ARG B 181     124.428  71.467 -24.722  1.00 12.66           C  
ANISOU 2257  CA  ARG B 181     2334    593   1883     59     70     79       C  
ATOM   2258  C   ARG B 181     123.018  71.719 -24.198  1.00 14.24           C  
ANISOU 2258  C   ARG B 181     2439    807   2163    111    254    167       C  
ATOM   2259  O   ARG B 181     122.335  70.764 -23.823  1.00 16.71           O  
ANISOU 2259  O   ARG B 181     2675   1182   2491   -258    229    273       O  
ATOM   2260  CB  ARG B 181     125.120  70.416 -23.849  1.00 12.19           C  
ANISOU 2260  CB  ARG B 181     2193    739   1701     86    175     34       C  
ATOM   2261  CG  ARG B 181     126.431  69.944 -24.425  1.00 12.30           C  
ANISOU 2261  CG  ARG B 181     2258    698   1716     62    264    294       C  
ATOM   2262  CD  ARG B 181     127.062  68.837 -23.616  1.00 12.72           C  
ANISOU 2262  CD  ARG B 181     2385    794   1654     25      8    174       C  
ATOM   2263  NE  ARG B 181     126.287  67.601 -23.632  1.00 12.14           N  
ANISOU 2263  NE  ARG B 181     2445    708   1460     55    153     44       N  
ATOM   2264  CZ  ARG B 181     125.680  67.073 -22.574  1.00 12.05           C  
ANISOU 2264  CZ  ARG B 181     2244    757   1577      5    -73     46       C  
ATOM   2265  NH1 ARG B 181     125.730  67.682 -21.401  1.00 11.90           N1+
ANISOU 2265  NH1 ARG B 181     2123    951   1446    156   -213    112       N1+
ATOM   2266  NH2 ARG B 181     125.038  65.918 -22.684  1.00 12.44           N  
ANISOU 2266  NH2 ARG B 181     2193    806   1727    -15   -301     59       N  
ATOM   2267  N  ACYS B 182     122.553  72.966 -24.147  0.51 15.05           N  
ANISOU 2267  N  ACYS B 182     2532    921   2264    186    357     15       N  
ATOM   2268  N  BCYS B 182     122.566  72.977 -24.191  0.49 14.60           N  
ANISOU 2268  N  BCYS B 182     2396    931   2218    135    299     82       N  
ATOM   2269  CA ACYS B 182     121.251  73.223 -23.543  0.51 16.94           C  
ANISOU 2269  CA ACYS B 182     2796   1231   2408    201    390   -233       C  
ATOM   2270  CA BCYS B 182     121.287  73.351 -23.595  0.49 16.05           C  
ANISOU 2270  CA BCYS B 182     2529   1251   2318    111    286   -136       C  
ATOM   2271  C  ACYS B 182     120.123  73.397 -24.563  0.51 18.09           C  
ANISOU 2271  C  ACYS B 182     2905   1326   2643     50    377    -59       C  
ATOM   2272  C  BCYS B 182     120.105  73.267 -24.544  0.49 17.75           C  
ANISOU 2272  C  BCYS B 182     2721   1409   2615     28    370    -25       C  
ATOM   2273  O  ACYS B 182     119.042  73.873 -24.195  0.51 18.61           O  
ANISOU 2273  O  ACYS B 182     2947   1363   2762   -214    352    -30       O  
ATOM   2274  O  BCYS B 182     118.967  73.463 -24.101  0.49 18.13           O  
ANISOU 2274  O  BCYS B 182     2619   1504   2767   -276    430    -26       O  
ATOM   2275  CB ACYS B 182     121.307  74.383 -22.546  0.51 17.79           C  
ANISOU 2275  CB ACYS B 182     2974   1487   2300    168    430   -256       C  
ATOM   2276  CB BCYS B 182     121.349  74.777 -23.059  0.49 15.89           C  
ANISOU 2276  CB BCYS B 182     2442   1469   2128    -64    203    -86       C  
ATOM   2277  SG ACYS B 182     121.511  75.991 -23.291  0.51 18.56           S  
ANISOU 2277  SG ACYS B 182     3129   1739   2182    270    321   -159       S  
ATOM   2278  SG BCYS B 182     121.991  74.827 -21.418  0.49 16.05           S  
ANISOU 2278  SG BCYS B 182     2340   1840   1919    -39    171    -35       S  
ATOM   2279  N   SER B 183     120.341  73.003 -25.825  1.00 18.45           N  
ANISOU 2279  N   SER B 183     2866   1427   2718    -85    385    176       N  
ATOM   2280  CA  SER B 183     119.276  72.974 -26.836  1.00 18.60           C  
ANISOU 2280  CA  SER B 183     2643   1255   3170   -418    -57    134       C  
ATOM   2281  C   SER B 183     118.565  74.318 -26.976  1.00 17.89           C  
ANISOU 2281  C   SER B 183     2194   1424   3179   -244    -92    -93       C  
ATOM   2282  O   SER B 183     117.352  74.382 -27.170  1.00 19.33           O  
ANISOU 2282  O   SER B 183     2371   1466   3509   -445   -232    -44       O  
ATOM   2283  CB  SER B 183     118.263  71.851 -26.591  1.00 22.33           C  
ANISOU 2283  CB  SER B 183     3167   1650   3667   -407   -102    126       C  
ATOM   2284  OG  SER B 183     118.888  70.589 -26.544  1.00 24.73           O  
ANISOU 2284  OG  SER B 183     3473   1924   4000    -84   -356     82       O  
ATOM   2285  N   ASP B 184     119.320  75.408 -26.878  1.00 15.11           N  
ANISOU 2285  N   ASP B 184     1858   1114   2770   -147    137   -132       N  
ATOM   2286  CA  ASP B 184     118.708  76.730 -26.879  1.00 14.60           C  
ANISOU 2286  CA  ASP B 184     1546   1431   2571   -261    144    363       C  
ATOM   2287  C   ASP B 184     118.928  77.501 -28.174  1.00 17.94           C  
ANISOU 2287  C   ASP B 184     1659   2441   2718   -527     52    766       C  
ATOM   2288  O   ASP B 184     118.738  78.717 -28.195  1.00 19.76           O  
ANISOU 2288  O   ASP B 184     2014   2562   2931   -403    221    888       O  
ATOM   2289  CB  ASP B 184     119.145  77.545 -25.664  1.00 14.65           C  
ANISOU 2289  CB  ASP B 184     1461   1621   2483   -348     32    -20       C  
ATOM   2290  CG  ASP B 184     120.615  77.913 -25.696  1.00 14.83           C  
ANISOU 2290  CG  ASP B 184     1533   1641   2460   -105   -133   -183       C  
ATOM   2291  OD1 ASP B 184     121.300  77.615 -26.697  1.00 14.09           O  
ANISOU 2291  OD1 ASP B 184     1640   1469   2245   -311   -121    204       O  
ATOM   2292  OD2 ASP B 184     121.087  78.518 -24.706  1.00 18.25           O1-
ANISOU 2292  OD2 ASP B 184     2011   2318   2605   -383   -172   -478       O1-
ATOM   2293  N   SER B 185     119.326  76.827 -29.245  1.00 22.79           N  
ANISOU 2293  N   SER B 185     2269   3584   2804   -793   -165   1042       N  
ATOM   2294  CA  SER B 185     119.493  77.514 -30.512  1.00 28.00           C  
ANISOU 2294  CA  SER B 185     2692   4890   3055  -1108   -381   1309       C  
ATOM   2295  C   SER B 185     118.150  78.028 -31.020  1.00 30.68           C  
ANISOU 2295  C   SER B 185     2784   5602   3270  -1303   -599   1593       C  
ATOM   2296  O   SER B 185     117.079  77.540 -30.648  1.00 31.70           O  
ANISOU 2296  O   SER B 185     2849   5941   3254  -1565   -814   1532       O  
ATOM   2297  CB  SER B 185     120.115  76.582 -31.553  1.00 31.06           C  
ANISOU 2297  CB  SER B 185     3292   5405   3106  -1293   -175   1191       C  
ATOM   2298  OG  SER B 185     120.233  77.229 -32.813  1.00 34.01           O  
ANISOU 2298  OG  SER B 185     3815   5922   3185  -1362   -169    925       O  
ATOM   2299  N   ASP B 186     118.223  79.044 -31.872  1.00 32.40           N  
ANISOU 2299  N   ASP B 186     2881   5967   3462   -996   -713   1824       N  
ATOM   2300  CA  ASP B 186     117.056  79.597 -32.538  1.00 34.09           C  
ANISOU 2300  CA  ASP B 186     3029   6265   3657   -937   -468   1981       C  
ATOM   2301  C   ASP B 186     116.826  78.975 -33.908  1.00 35.54           C  
ANISOU 2301  C   ASP B 186     3464   6382   3657  -1287   -804   1787       C  
ATOM   2302  O   ASP B 186     116.074  79.532 -34.715  1.00 37.61           O  
ANISOU 2302  O   ASP B 186     3751   6687   3851  -1173  -1098   1799       O  
ATOM   2303  CB  ASP B 186     117.190  81.116 -32.649  1.00 35.21           C  
ANISOU 2303  CB  ASP B 186     3109   6496   3774   -520      6   2225       C  
ATOM   2304  CG  ASP B 186     118.428  81.540 -33.425  1.00 36.04           C  
ANISOU 2304  CG  ASP B 186     3214   6642   3838   -234    260   2361       C  
ATOM   2305  OD1 ASP B 186     119.274  80.672 -33.732  1.00 35.25           O  
ANISOU 2305  OD1 ASP B 186     3015   6634   3745    218     74   2465       O  
ATOM   2306  OD2 ASP B 186     118.555  82.748 -33.722  1.00 37.30           O1-
ANISOU 2306  OD2 ASP B 186     3421   6765   3986   -237    535   2278       O1-
ATOM   2307  N   GLY B 187     117.447  77.827 -34.185  1.00 35.26           N  
ANISOU 2307  N   GLY B 187     3668   6285   3443  -1627   -830   1414       N  
ATOM   2308  CA  GLY B 187     117.378  77.216 -35.493  1.00 34.68           C  
ANISOU 2308  CA  GLY B 187     3999   5979   3197  -1855   -924   1136       C  
ATOM   2309  C   GLY B 187     118.401  77.723 -36.481  1.00 33.48           C  
ANISOU 2309  C   GLY B 187     4194   5613   2913  -1916   -936    827       C  
ATOM   2310  O   GLY B 187     118.592  77.092 -37.530  1.00 35.65           O  
ANISOU 2310  O   GLY B 187     4712   5848   2985  -2095   -913    649       O  
ATOM   2311  N   LEU B 188     119.067  78.838 -36.184  1.00 28.94           N  
ANISOU 2311  N   LEU B 188     3525   4893   2578  -1642  -1060    909       N  
ATOM   2312  CA  LEU B 188     120.072  79.424 -37.058  1.00 25.48           C  
ANISOU 2312  CA  LEU B 188     3070   4088   2523  -1235   -860    722       C  
ATOM   2313  C   LEU B 188     121.456  79.400 -36.433  1.00 19.66           C  
ANISOU 2313  C   LEU B 188     2544   2835   2090  -1079   -653    402       C  
ATOM   2314  O   LEU B 188     122.418  78.964 -37.068  1.00 20.13           O  
ANISOU 2314  O   LEU B 188     2951   2673   2023  -1041   -450     16       O  
ATOM   2315  CB  LEU B 188     119.707  80.877 -37.400  1.00 29.13           C  
ANISOU 2315  CB  LEU B 188     3405   4708   2953   -720   -730    760       C  
ATOM   2316  CG  LEU B 188     118.542  81.207 -38.332  1.00 32.51           C  
ANISOU 2316  CG  LEU B 188     3865   5104   3384   -622   -473    816       C  
ATOM   2317  CD1 LEU B 188     117.212  81.045 -37.619  1.00 33.49           C  
ANISOU 2317  CD1 LEU B 188     3945   5240   3538   -731   -448    834       C  
ATOM   2318  CD2 LEU B 188     118.709  82.624 -38.855  1.00 33.61           C  
ANISOU 2318  CD2 LEU B 188     4073   5181   3516   -541   -410    841       C  
ATOM   2319  N   ALA B 189     121.576  79.855 -35.197  1.00 15.97           N  
ANISOU 2319  N   ALA B 189     2267   2021   1778   -398   -447    362       N  
ATOM   2320  CA  ALA B 189     122.881  79.920 -34.563  1.00 13.23           C  
ANISOU 2320  CA  ALA B 189     1957   1426   1642     -6   -216     94       C  
ATOM   2321  C   ALA B 189     123.313  78.526 -34.133  1.00 13.05           C  
ANISOU 2321  C   ALA B 189     2149   1265   1543   -251   -134    146       C  
ATOM   2322  O   ALA B 189     122.538  77.823 -33.480  1.00 14.57           O  
ANISOU 2322  O   ALA B 189     2422   1512   1604   -310     -7    295       O  
ATOM   2323  CB  ALA B 189     122.799  80.799 -33.326  1.00 13.21           C  
ANISOU 2323  CB  ALA B 189     2045   1235   1738    -90   -202    -21       C  
ATOM   2324  N   PRO B 190     124.526  78.097 -34.475  1.00 12.34           N  
ANISOU 2324  N   PRO B 190     2265    935   1487   -369    -55    229       N  
ATOM   2325  CA  PRO B 190     125.045  76.866 -33.895  1.00 11.83           C  
ANISOU 2325  CA  PRO B 190     2167    886   1443   -101    -50    146       C  
ATOM   2326  C   PRO B 190     125.121  77.009 -32.388  1.00 11.09           C  
ANISOU 2326  C   PRO B 190     2001    783   1430   -320    -14    145       C  
ATOM   2327  O   PRO B 190     125.391  78.106 -31.867  1.00 11.03           O  
ANISOU 2327  O   PRO B 190     1911    727   1552    -84    -44    149       O  
ATOM   2328  CB  PRO B 190     126.447  76.751 -34.511  1.00 12.59           C  
ANISOU 2328  CB  PRO B 190     2130   1070   1585    157     53    116       C  
ATOM   2329  CG  PRO B 190     126.400  77.605 -35.750  1.00 12.92           C  
ANISOU 2329  CG  PRO B 190     2287   1005   1616     18    -24    117       C  
ATOM   2330  CD  PRO B 190     125.489  78.734 -35.386  1.00 12.55           C  
ANISOU 2330  CD  PRO B 190     2384    802   1580   -290     99    251       C  
ATOM   2331  N   PRO B 191     124.876  75.932 -31.651  1.00 11.36           N  
ANISOU 2331  N   PRO B 191     2182    802   1333   -486   -186     20       N  
ATOM   2332  CA  PRO B 191     124.851  76.045 -30.183  1.00 12.22           C  
ANISOU 2332  CA  PRO B 191     2289   1022   1334   -503   -229    127       C  
ATOM   2333  C   PRO B 191     126.185  76.420 -29.571  1.00 11.54           C  
ANISOU 2333  C   PRO B 191     2078    893   1415   -221   -171     92       C  
ATOM   2334  O   PRO B 191     126.208  76.853 -28.417  1.00 11.25           O  
ANISOU 2334  O   PRO B 191     1964    870   1441   -230    -55    -39       O  
ATOM   2335  CB  PRO B 191     124.392  74.657 -29.734  1.00 13.68           C  
ANISOU 2335  CB  PRO B 191     2578   1114   1505   -768    -15    234       C  
ATOM   2336  CG  PRO B 191     124.755  73.757 -30.873  1.00 14.45           C  
ANISOU 2336  CG  PRO B 191     2840   1025   1624   -552    -63    251       C  
ATOM   2337  CD  PRO B 191     124.539  74.577 -32.110  1.00 13.63           C  
ANISOU 2337  CD  PRO B 191     2630    989   1560   -696   -247     73       C  
ATOM   2338  N   GLN B 192     127.290  76.298 -30.313  1.00 10.44           N  
ANISOU 2338  N   GLN B 192     1711    803   1452    -78   -196    173       N  
ATOM   2339  CA  GLN B 192     128.591  76.695 -29.793  1.00  9.77           C  
ANISOU 2339  CA  GLN B 192     1755    471   1486    154    -97    -19       C  
ATOM   2340  C   GLN B 192     128.839  78.196 -29.862  1.00  9.40           C  
ANISOU 2340  C   GLN B 192     1704    448   1419     42    144     74       C  
ATOM   2341  O   GLN B 192     129.777  78.677 -29.210  1.00 10.10           O  
ANISOU 2341  O   GLN B 192     1796    636   1404   -233    -15     15       O  
ATOM   2342  CB  GLN B 192     129.713  76.022 -30.586  1.00 10.24           C  
ANISOU 2342  CB  GLN B 192     1816    615   1459    250    141   -281       C  
ATOM   2343  CG  GLN B 192     129.663  74.477 -30.623  1.00 10.80           C  
ANISOU 2343  CG  GLN B 192     1993    559   1552     53    -57   -244       C  
ATOM   2344  CD  GLN B 192     128.942  73.923 -31.830  1.00 12.47           C  
ANISOU 2344  CD  GLN B 192     2371    707   1662    104    168      1       C  
ATOM   2345  OE1 GLN B 192     127.921  74.453 -32.260  1.00 13.83           O  
ANISOU 2345  OE1 GLN B 192     2444   1095   1715    183    191   -106       O  
ATOM   2346  NE2 GLN B 192     129.476  72.834 -32.389  1.00 12.62           N  
ANISOU 2346  NE2 GLN B 192     2464    660   1673    -53    398    -18       N  
ATOM   2347  N   HIS B 193     128.060  78.944 -30.648  1.00  8.96           N  
ANISOU 2347  N   HIS B 193     1553    550   1302    -64     40    145       N  
ATOM   2348  CA  HIS B 193     128.395  80.344 -30.904  1.00  8.17           C  
ANISOU 2348  CA  HIS B 193     1532    441   1130    -52     21     -1       C  
ATOM   2349  C   HIS B 193     127.979  81.250 -29.756  1.00  8.79           C  
ANISOU 2349  C   HIS B 193     1440    650   1250    -15     57    -43       C  
ATOM   2350  O   HIS B 193     126.807  81.289 -29.371  1.00 10.42           O  
ANISOU 2350  O   HIS B 193     1455   1058   1447   -150    -31    116       O  
ATOM   2351  CB  HIS B 193     127.732  80.851 -32.178  1.00  8.35           C  
ANISOU 2351  CB  HIS B 193     1452    599   1122    112    -72     33       C  
ATOM   2352  CG  HIS B 193     128.447  80.448 -33.424  1.00  8.76           C  
ANISOU 2352  CG  HIS B 193     1548    637   1144    -20    -58   -104       C  
ATOM   2353  ND1 HIS B 193     128.555  81.281 -34.517  1.00  9.09           N  
ANISOU 2353  ND1 HIS B 193     1477    772   1205    -42     37     55       N  
ATOM   2354  CD2 HIS B 193     129.084  79.302 -33.758  1.00 10.42           C  
ANISOU 2354  CD2 HIS B 193     1893    799   1266    222     17   -109       C  
ATOM   2355  CE1 HIS B 193     129.236  80.669 -35.466  1.00  9.47           C  
ANISOU 2355  CE1 HIS B 193     1605    725   1266    188     35   -169       C  
ATOM   2356  NE2 HIS B 193     129.566  79.466 -35.035  1.00 10.67           N  
ANISOU 2356  NE2 HIS B 193     1814    897   1342    132    -11    140       N  
ATOM   2357  N   LEU B 194     128.935  82.029 -29.260  1.00  8.70           N  
ANISOU 2357  N   LEU B 194     1380    600   1327    -24   -173   -129       N  
ATOM   2358  CA  LEU B 194     128.630  82.974 -28.191  1.00  8.31           C  
ANISOU 2358  CA  LEU B 194     1384    482   1290    113   -121   -208       C  
ATOM   2359  C   LEU B 194     127.708  84.093 -28.664  1.00  8.48           C  
ANISOU 2359  C   LEU B 194     1269    694   1259    -40    -17     51       C  
ATOM   2360  O   LEU B 194     126.780  84.483 -27.948  1.00  9.66           O  
ANISOU 2360  O   LEU B 194     1425    994   1253     59     85    129       O  
ATOM   2361  CB  LEU B 194     129.923  83.572 -27.653  1.00  9.09           C  
ANISOU 2361  CB  LEU B 194     1594    738   1123   -183   -166    -84       C  
ATOM   2362  CG  LEU B 194     129.733  84.675 -26.611  1.00 10.19           C  
ANISOU 2362  CG  LEU B 194     1734    907   1232   -337    145    -36       C  
ATOM   2363  CD1 LEU B 194     129.165  84.089 -25.322  1.00 12.11           C  
ANISOU 2363  CD1 LEU B 194     1808   1467   1328   -201     98    -22       C  
ATOM   2364  CD2 LEU B 194     131.037  85.379 -26.346  1.00 10.77           C  
ANISOU 2364  CD2 LEU B 194     1460   1393   1238   -267    122    -97       C  
ATOM   2365  N   ILE B 195     127.984  84.676 -29.829  1.00  8.76           N  
ANISOU 2365  N   ILE B 195     1432    683   1215   -154   -151    252       N  
ATOM   2366  CA  ILE B 195     127.263  85.857 -30.290  1.00  8.15           C  
ANISOU 2366  CA  ILE B 195     1432    503   1162    -77   -270    147       C  
ATOM   2367  C   ILE B 195     126.191  85.436 -31.279  1.00  8.65           C  
ANISOU 2367  C   ILE B 195     1356    741   1189    -52    -56    -10       C  
ATOM   2368  O   ILE B 195     126.489  84.804 -32.303  1.00  9.56           O  
ANISOU 2368  O   ILE B 195     1306   1002   1323     19      0   -125       O  
ATOM   2369  CB  ILE B 195     128.208  86.883 -30.942  1.00  8.92           C  
ANISOU 2369  CB  ILE B 195     1605    531   1252     19   -242     48       C  
ATOM   2370  CG1 ILE B 195     129.341  87.272 -29.993  1.00  9.37           C  
ANISOU 2370  CG1 ILE B 195     1466    689   1406    -42   -334    334       C  
ATOM   2371  CG2 ILE B 195     127.432  88.128 -31.352  1.00  9.74           C  
ANISOU 2371  CG2 ILE B 195     1622    708   1373    250   -209     78       C  
ATOM   2372  CD1 ILE B 195     130.316  88.251 -30.625  1.00 10.25           C  
ANISOU 2372  CD1 ILE B 195     1605    620   1670   -196    -94    315       C  
ATOM   2373  N   ARG B 196     124.955  85.838 -31.004  1.00  8.69           N  
ANISOU 2373  N   ARG B 196     1278    815   1207      1    -29     75       N  
ATOM   2374  CA  ARG B 196     123.867  85.703 -31.949  1.00  9.37           C  
ANISOU 2374  CA  ARG B 196     1349    817   1395    -43    -95     56       C  
ATOM   2375  C   ARG B 196     123.371  87.077 -32.356  1.00  9.47           C  
ANISOU 2375  C   ARG B 196     1453    775   1369   -108   -174   -159       C  
ATOM   2376  O   ARG B 196     123.533  88.064 -31.630  1.00 10.19           O  
ANISOU 2376  O   ARG B 196     1580    935   1356     96   -129   -369       O  
ATOM   2377  CB  ARG B 196     122.691  84.944 -31.349  1.00  9.81           C  
ANISOU 2377  CB  ARG B 196     1473    609   1646   -164    -45    105       C  
ATOM   2378  CG  ARG B 196     123.045  83.544 -30.950  1.00 11.60           C  
ANISOU 2378  CG  ARG B 196     1818    695   1894    -59    -85    345       C  
ATOM   2379  CD  ARG B 196     121.829  82.798 -30.444  1.00 11.73           C  
ANISOU 2379  CD  ARG B 196     1808    830   1817   -336    -55    314       C  
ATOM   2380  NE  ARG B 196     122.222  81.496 -29.928  1.00 11.67           N  
ANISOU 2380  NE  ARG B 196     1649   1006   1779   -250     58    349       N  
ATOM   2381  CZ  ARG B 196     121.408  80.652 -29.308  1.00 13.39           C  
ANISOU 2381  CZ  ARG B 196     1654   1396   2035   -232     24    478       C  
ATOM   2382  NH1 ARG B 196     120.132  80.965 -29.114  1.00 15.46           N1+
ANISOU 2382  NH1 ARG B 196     1723   1929   2222     33    261    538       N1+
ATOM   2383  NH2 ARG B 196     121.883  79.492 -28.879  1.00 13.85           N  
ANISOU 2383  NH2 ARG B 196     1939   1267   2058   -159   -280    498       N  
ATOM   2384  N   VAL B 197     122.751  87.128 -33.530  1.00 10.12           N  
ANISOU 2384  N   VAL B 197     1341   1068   1434     46   -214     34       N  
ATOM   2385  CA  VAL B 197     121.970  88.289 -33.935  1.00 10.46           C  
ANISOU 2385  CA  VAL B 197     1508    937   1529    252   -103    231       C  
ATOM   2386  C   VAL B 197     120.511  87.964 -33.688  1.00 11.18           C  
ANISOU 2386  C   VAL B 197     1458    964   1826     26   -134    105       C  
ATOM   2387  O   VAL B 197     120.029  86.886 -34.068  1.00 13.48           O  
ANISOU 2387  O   VAL B 197     1711   1050   2361   -241   -149   -316       O  
ATOM   2388  CB  VAL B 197     122.214  88.669 -35.405  1.00 11.77           C  
ANISOU 2388  CB  VAL B 197     1657   1303   1514    253   -130    292       C  
ATOM   2389  CG1 VAL B 197     121.167  89.674 -35.874  1.00 12.25           C  
ANISOU 2389  CG1 VAL B 197     1931   1107   1618    292    -40    334       C  
ATOM   2390  CG2 VAL B 197     123.591  89.275 -35.563  1.00 12.13           C  
ANISOU 2390  CG2 VAL B 197     1498   1449   1660     10    -57     54       C  
ATOM   2391  N   GLU B 198     119.818  88.880 -33.029  1.00 12.15           N  
ANISOU 2391  N   GLU B 198     1390   1451   1775    142    -17    272       N  
ATOM   2392  CA  GLU B 198     118.411  88.716 -32.723  1.00 14.15           C  
ANISOU 2392  CA  GLU B 198     1575   1857   1943    163    143    299       C  
ATOM   2393  C   GLU B 198     117.579  89.383 -33.806  1.00 16.23           C  
ANISOU 2393  C   GLU B 198     1729   2411   2027     17    132    460       C  
ATOM   2394  O   GLU B 198     117.892  90.491 -34.248  1.00 18.25           O  
ANISOU 2394  O   GLU B 198     2079   2510   2346    415    133    734       O  
ATOM   2395  CB  GLU B 198     118.128  89.382 -31.377  1.00 16.11           C  
ANISOU 2395  CB  GLU B 198     1863   2186   2070    227    310    -12       C  
ATOM   2396  CG  GLU B 198     116.686  89.405 -30.984  1.00 18.95           C  
ANISOU 2396  CG  GLU B 198     2223   2669   2306    155    272   -141       C  
ATOM   2397  CD  GLU B 198     116.468  90.022 -29.626  1.00 20.41           C  
ANISOU 2397  CD  GLU B 198     2245   3108   2401    228     78   -257       C  
ATOM   2398  OE1 GLU B 198     117.460  90.432 -28.979  1.00 18.03           O  
ANISOU 2398  OE1 GLU B 198     1973   2613   2266    267    -87   -229       O  
ATOM   2399  OE2 GLU B 198     115.292  90.095 -29.209  1.00 23.98           O1-
ANISOU 2399  OE2 GLU B 198     2635   3840   2637    250     83   -202       O1-
ATOM   2400  N   GLY B 199     116.536  88.688 -34.250  1.00 18.82           N  
ANISOU 2400  N   GLY B 199     2015   3078   2057     80    -92    407       N  
ATOM   2401  CA  GLY B 199     115.546  89.283 -35.132  1.00 20.91           C  
ANISOU 2401  CA  GLY B 199     2169   3670   2106    323   -197    498       C  
ATOM   2402  C   GLY B 199     116.034  89.658 -36.515  1.00 22.33           C  
ANISOU 2402  C   GLY B 199     2471   3822   2194    529   -307    542       C  
ATOM   2403  O   GLY B 199     115.602  90.682 -37.065  1.00 25.07           O  
ANISOU 2403  O   GLY B 199     2752   4385   2388    668   -205    556       O  
ATOM   2404  N   ASN B 200     116.922  88.859 -37.099  1.00 20.30           N  
ANISOU 2404  N   ASN B 200     2056   3549   2109    117   -313    334       N  
ATOM   2405  CA  ASN B 200     117.339  89.071 -38.485  1.00 19.03           C  
ANISOU 2405  CA  ASN B 200     2070   3040   2120    -89   -355    313       C  
ATOM   2406  C   ASN B 200     117.454  87.708 -39.159  1.00 20.03           C  
ANISOU 2406  C   ASN B 200     2138   3086   2386   -386   -343    365       C  
ATOM   2407  O   ASN B 200     118.437  86.988 -38.956  1.00 19.03           O  
ANISOU 2407  O   ASN B 200     2067   2742   2420   -262   -300    505       O  
ATOM   2408  CB  ASN B 200     118.644  89.849 -38.568  1.00 17.80           C  
ANISOU 2408  CB  ASN B 200     2120   2643   2002     61   -391    209       C  
ATOM   2409  CG  ASN B 200     118.944  90.319 -39.978  1.00 17.57           C  
ANISOU 2409  CG  ASN B 200     2322   2270   2085    145   -608     37       C  
ATOM   2410  OD1 ASN B 200     118.567  89.666 -40.957  1.00 19.20           O  
ANISOU 2410  OD1 ASN B 200     2682   2312   2299    -54   -634   -378       O  
ATOM   2411  ND2 ASN B 200     119.614  91.456 -40.091  1.00 18.26           N  
ANISOU 2411  ND2 ASN B 200     2476   2165   2295    399   -508     87       N  
ATOM   2412  N   LEU B 201     116.455  87.373 -39.979  1.00 21.78           N  
ANISOU 2412  N   LEU B 201     2363   3294   2621   -710   -406     55       N  
ATOM   2413  CA  LEU B 201     116.440  86.089 -40.669  1.00 23.73           C  
ANISOU 2413  CA  LEU B 201     2709   3328   2980   -833   -475    101       C  
ATOM   2414  C   LEU B 201     117.578  85.942 -41.669  1.00 21.28           C  
ANISOU 2414  C   LEU B 201     2574   2747   2766   -831   -565    266       C  
ATOM   2415  O   LEU B 201     117.858  84.822 -42.112  1.00 22.66           O  
ANISOU 2415  O   LEU B 201     2946   2863   2800   -824   -619    251       O  
ATOM   2416  CB  LEU B 201     115.097  85.879 -41.374  1.00 27.24           C  
ANISOU 2416  CB  LEU B 201     3111   3977   3263  -1005   -545    -12       C  
ATOM   2417  CG  LEU B 201     114.938  86.431 -42.798  1.00 30.55           C  
ANISOU 2417  CG  LEU B 201     3731   4296   3580  -1006   -315    -21       C  
ATOM   2418  CD1 LEU B 201     113.662  85.894 -43.435  1.00 31.95           C  
ANISOU 2418  CD1 LEU B 201     3968   4455   3718  -1046   -386    -77       C  
ATOM   2419  CD2 LEU B 201     114.963  87.963 -42.855  1.00 31.39           C  
ANISOU 2419  CD2 LEU B 201     3858   4451   3616   -982   -199    -57       C  
ATOM   2420  N   ARG B 202     118.246  87.035 -42.033  1.00 18.69           N  
ANISOU 2420  N   ARG B 202     2085   2487   2528   -552   -602    518       N  
ATOM   2421  CA  ARG B 202     119.367  86.968 -42.958  1.00 17.63           C  
ANISOU 2421  CA  ARG B 202     2104   2303   2293   -188   -697    439       C  
ATOM   2422  C   ARG B 202     120.705  86.801 -42.255  1.00 16.19           C  
ANISOU 2422  C   ARG B 202     1962   2129   2061   -115   -569    252       C  
ATOM   2423  O   ARG B 202     121.745  86.815 -42.921  1.00 16.51           O  
ANISOU 2423  O   ARG B 202     2126   2126   2021    -10   -337    245       O  
ATOM   2424  CB  ARG B 202     119.385  88.185 -43.885  1.00 20.12           C  
ANISOU 2424  CB  ARG B 202     2474   2699   2473   -181   -787    742       C  
ATOM   2425  CG  ARG B 202     118.176  88.245 -44.810  1.00 22.28           C  
ANISOU 2425  CG  ARG B 202     2813   3026   2628   -450   -899    712       C  
ATOM   2426  CD  ARG B 202     118.339  89.302 -45.890  1.00 25.06           C  
ANISOU 2426  CD  ARG B 202     3209   3497   2816   -490   -841    708       C  
ATOM   2427  N   ALA B 203     120.706  86.639 -40.932  1.00 15.29           N  
ANISOU 2427  N   ALA B 203     2059   1784   1965    -73   -638    229       N  
ATOM   2428  CA  ALA B 203     121.951  86.375 -40.229  1.00 14.64           C  
ANISOU 2428  CA  ALA B 203     2109   1544   1908     32   -409     82       C  
ATOM   2429  C   ALA B 203     122.532  85.045 -40.688  1.00 14.07           C  
ANISOU 2429  C   ALA B 203     1959   1286   2102   -277   -373     38       C  
ATOM   2430  O   ALA B 203     121.815  84.052 -40.842  1.00 15.51           O  
ANISOU 2430  O   ALA B 203     1888   1483   2522   -514   -353     62       O  
ATOM   2431  CB  ALA B 203     121.699  86.320 -38.720  1.00 14.54           C  
ANISOU 2431  CB  ALA B 203     2081   1754   1690   -209   -404    161       C  
ATOM   2432  N   GLU B 204     123.839  85.030 -40.910  1.00 12.53           N  
ANISOU 2432  N   GLU B 204     2019    922   1821    -97   -327     76       N  
ATOM   2433  CA  GLU B 204     124.562  83.812 -41.220  1.00 12.19           C  
ANISOU 2433  CA  GLU B 204     2053    999   1582   -298   -320    166       C  
ATOM   2434  C   GLU B 204     125.644  83.608 -40.177  1.00 11.10           C  
ANISOU 2434  C   GLU B 204     1757    874   1588   -202   -320    -57       C  
ATOM   2435  O   GLU B 204     126.261  84.569 -39.702  1.00 11.09           O  
ANISOU 2435  O   GLU B 204     1934    754   1528   -293   -351     27       O  
ATOM   2436  CB  GLU B 204     125.184  83.878 -42.607  1.00 14.30           C  
ANISOU 2436  CB  GLU B 204     2472   1506   1456   -368   -449    235       C  
ATOM   2437  CG  GLU B 204     124.143  84.027 -43.703  1.00 17.20           C  
ANISOU 2437  CG  GLU B 204     3196   1841   1500   -401   -429    281       C  
ATOM   2438  CD  GLU B 204     124.758  84.173 -45.075  1.00 21.29           C  
ANISOU 2438  CD  GLU B 204     4084   2269   1735   -307   -389    241       C  
ATOM   2439  OE1 GLU B 204     126.007  84.095 -45.179  1.00 22.59           O  
ANISOU 2439  OE1 GLU B 204     4730   2065   1788   -489   -107    106       O  
ATOM   2440  OE2 GLU B 204     123.994  84.381 -46.041  1.00 23.30           O1-
ANISOU 2440  OE2 GLU B 204     4150   2660   2041   -187   -651    185       O1-
ATOM   2441  N   TYR B 205     125.878  82.349 -39.842  1.00 11.03           N  
ANISOU 2441  N   TYR B 205     1802    926   1462    341   -122     25       N  
ATOM   2442  CA  TYR B 205     126.839  81.965 -38.824  1.00 10.54           C  
ANISOU 2442  CA  TYR B 205     1669    865   1470    178   -186    105       C  
ATOM   2443  C   TYR B 205     127.974  81.207 -39.482  1.00 10.97           C  
ANISOU 2443  C   TYR B 205     1706    845   1618     18   -108   -116       C  
ATOM   2444  O   TYR B 205     127.739  80.239 -40.219  1.00 13.95           O  
ANISOU 2444  O   TYR B 205     2119   1131   2051   -123   -169   -520       O  
ATOM   2445  CB  TYR B 205     126.159  81.107 -37.761  1.00  9.51           C  
ANISOU 2445  CB  TYR B 205     1557    457   1598      2    -21    130       C  
ATOM   2446  CG  TYR B 205     125.207  81.929 -36.952  1.00  9.44           C  
ANISOU 2446  CG  TYR B 205     1547    487   1553    255   -115     72       C  
ATOM   2447  CD1 TYR B 205     123.913  82.176 -37.402  1.00 10.29           C  
ANISOU 2447  CD1 TYR B 205     1548    744   1617    123     13     -5       C  
ATOM   2448  CD2 TYR B 205     125.613  82.502 -35.758  1.00  9.24           C  
ANISOU 2448  CD2 TYR B 205     1559    492   1460     24   -120   -129       C  
ATOM   2449  CE1 TYR B 205     123.044  82.954 -36.670  1.00  9.91           C  
ANISOU 2449  CE1 TYR B 205     1623    644   1498    117    -20   -211       C  
ATOM   2450  CE2 TYR B 205     124.756  83.277 -35.014  1.00  9.97           C  
ANISOU 2450  CE2 TYR B 205     1632    545   1611     49     85     69       C  
ATOM   2451  CZ  TYR B 205     123.476  83.510 -35.472  1.00 10.22           C  
ANISOU 2451  CZ  TYR B 205     1542    746   1596    163    -94   -256       C  
ATOM   2452  OH  TYR B 205     122.628  84.298 -34.731  1.00 12.30           O  
ANISOU 2452  OH  TYR B 205     1834   1109   1729    191    -35   -185       O  
ATOM   2453  N   LEU B 206     129.199  81.647 -39.222  1.00 10.84           N  
ANISOU 2453  N   LEU B 206     1686    935   1498    -17     32   -108       N  
ATOM   2454  CA  LEU B 206     130.382  81.055 -39.829  1.00 11.88           C  
ANISOU 2454  CA  LEU B 206     1898   1137   1479    201      0   -210       C  
ATOM   2455  C   LEU B 206     131.221  80.357 -38.769  1.00 11.41           C  
ANISOU 2455  C   LEU B 206     2075    842   1420     25    -54    -48       C  
ATOM   2456  O   LEU B 206     131.536  80.954 -37.732  1.00 10.89           O  
ANISOU 2456  O   LEU B 206     2067    874   1198    -76   -106    -91       O  
ATOM   2457  CB  LEU B 206     131.236  82.138 -40.491  1.00 12.68           C  
ANISOU 2457  CB  LEU B 206     2033   1190   1592    145    278   -152       C  
ATOM   2458  CG  LEU B 206     132.532  81.656 -41.152  1.00 13.69           C  
ANISOU 2458  CG  LEU B 206     2287   1353   1560     56    370   -242       C  
ATOM   2459  CD1 LEU B 206     132.241  80.694 -42.290  1.00 15.00           C  
ANISOU 2459  CD1 LEU B 206     2581   1464   1654    238    374   -664       C  
ATOM   2460  CD2 LEU B 206     133.347  82.851 -41.641  1.00 14.47           C  
ANISOU 2460  CD2 LEU B 206     2273   1648   1578   -225    503    260       C  
ATOM   2461  N   ASP B 207     131.587  79.104 -39.042  1.00 12.76           N  
ANISOU 2461  N   ASP B 207     2097   1049   1701    313    305    115       N  
ATOM   2462  CA  ASP B 207     132.701  78.428 -38.390  1.00 13.67           C  
ANISOU 2462  CA  ASP B 207     2269   1110   1816     60    458      3       C  
ATOM   2463  C   ASP B 207     133.851  78.526 -39.383  1.00 13.75           C  
ANISOU 2463  C   ASP B 207     2318   1092   1813     76    506    -75       C  
ATOM   2464  O   ASP B 207     133.820  77.878 -40.434  1.00 15.74           O  
ANISOU 2464  O   ASP B 207     2610   1389   1981    122    387   -306       O  
ATOM   2465  CB  ASP B 207     132.388  76.948 -38.159  1.00 14.73           C  
ANISOU 2465  CB  ASP B 207     2565   1071   1961      7    763     27       C  
ATOM   2466  CG  ASP B 207     131.283  76.710 -37.156  1.00 18.56           C  
ANISOU 2466  CG  ASP B 207     3242   1511   2298   -381    565   -179       C  
ATOM   2467  OD1 ASP B 207     131.115  77.516 -36.235  1.00 18.99           O  
ANISOU 2467  OD1 ASP B 207     3311   1683   2221   -220    688   -181       O  
ATOM   2468  OD2 ASP B 207     130.600  75.664 -37.277  1.00 21.35           O1-
ANISOU 2468  OD2 ASP B 207     3676   1937   2501   -831    340   -346       O1-
ATOM   2469  N   ASP B 208     134.855  79.336 -39.073  1.00 13.15           N  
ANISOU 2469  N   ASP B 208     2227   1005   1765    110    515      9       N  
ATOM   2470  CA  ASP B 208     135.931  79.530 -40.033  1.00 13.95           C  
ANISOU 2470  CA  ASP B 208     2132   1190   1981    174    433   -144       C  
ATOM   2471  C   ASP B 208     136.679  78.219 -40.239  1.00 15.63           C  
ANISOU 2471  C   ASP B 208     2337   1581   2019    298    412   -288       C  
ATOM   2472  O   ASP B 208     137.101  77.573 -39.277  1.00 15.98           O  
ANISOU 2472  O   ASP B 208     2328   1813   1930    386    257   -179       O  
ATOM   2473  CB  ASP B 208     136.891  80.600 -39.532  1.00 14.76           C  
ANISOU 2473  CB  ASP B 208     2222   1237   2150    155    444    -84       C  
ATOM   2474  CG  ASP B 208     137.850  81.053 -40.612  1.00 17.24           C  
ANISOU 2474  CG  ASP B 208     2661   1640   2250    242    502   -110       C  
ATOM   2475  OD1 ASP B 208     138.793  80.294 -40.928  1.00 19.05           O  
ANISOU 2475  OD1 ASP B 208     3057   1866   2314    280    618   -250       O  
ATOM   2476  OD2 ASP B 208     137.651  82.159 -41.158  1.00 18.83           O1-
ANISOU 2476  OD2 ASP B 208     2841   1967   2345    224    387   -110       O1-
ATOM   2477  N   ARG B 209     136.839  77.820 -41.503  1.00 18.11           N  
ANISOU 2477  N   ARG B 209     2615   2002   2265    494    507   -595       N  
ATOM   2478  CA  ARG B 209     137.412  76.509 -41.782  1.00 20.76           C  
ANISOU 2478  CA  ARG B 209     3037   2338   2514    648    443   -860       C  
ATOM   2479  C   ARG B 209     138.891  76.434 -41.434  1.00 22.40           C  
ANISOU 2479  C   ARG B 209     3328   2461   2723    762    388   -834       C  
ATOM   2480  O   ARG B 209     139.416  75.331 -41.232  1.00 24.06           O  
ANISOU 2480  O   ARG B 209     3640   2533   2968    942    497   -793       O  
ATOM   2481  CB  ARG B 209     137.186  76.129 -43.249  1.00 23.04           C  
ANISOU 2481  CB  ARG B 209     3542   2611   2602    714    499  -1021       C  
ATOM   2482  N   ASN B 210     139.576  77.573 -41.362  1.00 22.15           N  
ANISOU 2482  N   ASN B 210     3205   2581   2628    544    430   -850       N  
ATOM   2483  CA  ASN B 210     141.001  77.598 -41.053  1.00 23.94           C  
ANISOU 2483  CA  ASN B 210     3162   3027   2909    338    418   -755       C  
ATOM   2484  C   ASN B 210     141.281  77.932 -39.594  1.00 22.76           C  
ANISOU 2484  C   ASN B 210     2902   2747   2998    650    220   -818       C  
ATOM   2485  O   ASN B 210     142.098  77.266 -38.954  1.00 24.03           O  
ANISOU 2485  O   ASN B 210     3207   2681   3241    896     13   -847       O  
ATOM   2486  CB  ASN B 210     141.725  78.589 -41.974  1.00 27.22           C  
ANISOU 2486  CB  ASN B 210     3590   3674   3079    208    629   -668       C  
ATOM   2487  CG  ASN B 210     141.557  78.248 -43.440  1.00 30.74           C  
ANISOU 2487  CG  ASN B 210     4090   4251   3338    130    670   -557       C  
ATOM   2488  OD1 ASN B 210     141.681  77.092 -43.838  1.00 32.34           O  
ANISOU 2488  OD1 ASN B 210     4176   4627   3486    250    878   -744       O  
ATOM   2489  ND2 ASN B 210     141.266  79.257 -44.251  1.00 32.61           N  
ANISOU 2489  ND2 ASN B 210     4433   4589   3370     60    590   -388       N  
ATOM   2490  N   THR B 211     140.614  78.950 -39.049  1.00 19.56           N  
ANISOU 2490  N   THR B 211     2339   2308   2785    614    365   -891       N  
ATOM   2491  CA  THR B 211     140.868  79.402 -37.686  1.00 18.09           C  
ANISOU 2491  CA  THR B 211     2057   2090   2727    377     88   -781       C  
ATOM   2492  C   THR B 211     139.907  78.810 -36.671  1.00 17.16           C  
ANISOU 2492  C   THR B 211     1969   1940   2610    635    118   -802       C  
ATOM   2493  O   THR B 211     140.165  78.908 -35.465  1.00 18.60           O  
ANISOU 2493  O   THR B 211     2025   2289   2755    577     26   -769       O  
ATOM   2494  CB  THR B 211     140.753  80.925 -37.606  1.00 18.73           C  
ANISOU 2494  CB  THR B 211     2041   2246   2828    285    184   -572       C  
ATOM   2495  OG1 THR B 211     139.376  81.293 -37.747  1.00 18.07           O  
ANISOU 2495  OG1 THR B 211     1932   2184   2749    -98     63   -454       O  
ATOM   2496  CG2 THR B 211     141.575  81.580 -38.710  1.00 18.75           C  
ANISOU 2496  CG2 THR B 211     1874   2385   2866    307    267   -264       C  
ATOM   2497  N   PHE B 212     138.795  78.236 -37.120  1.00 16.00           N  
ANISOU 2497  N   PHE B 212     1861   1705   2513    584    240   -587       N  
ATOM   2498  CA  PHE B 212     137.765  77.661 -36.261  1.00 16.11           C  
ANISOU 2498  CA  PHE B 212     2159   1556   2406    977    263   -353       C  
ATOM   2499  C   PHE B 212     137.023  78.705 -35.452  1.00 15.87           C  
ANISOU 2499  C   PHE B 212     2377   1492   2163    713     44   -282       C  
ATOM   2500  O   PHE B 212     136.204  78.348 -34.606  1.00 15.91           O  
ANISOU 2500  O   PHE B 212     2701   1469   1875    616    234      4       O  
ATOM   2501  CB  PHE B 212     138.291  76.554 -35.340  1.00 18.68           C  
ANISOU 2501  CB  PHE B 212     2562   1767   2768   1197    158   -255       C  
ATOM   2502  CG  PHE B 212     139.097  75.524 -36.049  1.00 21.74           C  
ANISOU 2502  CG  PHE B 212     3030   2083   3146   1320    282   -328       C  
ATOM   2503  CD1 PHE B 212     138.493  74.639 -36.921  1.00 22.73           C  
ANISOU 2503  CD1 PHE B 212     3219   2089   3329   1229    308   -541       C  
ATOM   2504  CD2 PHE B 212     140.464  75.449 -35.857  1.00 24.40           C  
ANISOU 2504  CD2 PHE B 212     3341   2494   3435   1485    181   -430       C  
ATOM   2505  CE1 PHE B 212     139.241  73.683 -37.583  1.00 24.80           C  
ANISOU 2505  CE1 PHE B 212     3556   2391   3476   1310    345   -781       C  
ATOM   2506  CE2 PHE B 212     141.215  74.495 -36.509  1.00 25.45           C  
ANISOU 2506  CE2 PHE B 212     3587   2538   3547   1421    276   -774       C  
ATOM   2507  CZ  PHE B 212     140.603  73.615 -37.376  1.00 25.62           C  
ANISOU 2507  CZ  PHE B 212     3628   2535   3573   1366    278   -874       C  
ATOM   2508  N   ARG B 213     137.277  79.984 -35.691  1.00 13.50           N  
ANISOU 2508  N   ARG B 213     1966   1153   2010    530    -18   -541       N  
ATOM   2509  CA  ARG B 213     136.577  81.010 -34.943  1.00 11.35           C  
ANISOU 2509  CA  ARG B 213     1440   1018   1856    494     38   -432       C  
ATOM   2510  C   ARG B 213     135.162  81.182 -35.460  1.00 10.71           C  
ANISOU 2510  C   ARG B 213     1441    998   1630    471      4    -55       C  
ATOM   2511  O   ARG B 213     134.859  80.915 -36.624  1.00 12.25           O  
ANISOU 2511  O   ARG B 213     1760   1329   1563    361     12   -227       O  
ATOM   2512  CB  ARG B 213     137.315  82.333 -35.022  1.00 12.90           C  
ANISOU 2512  CB  ARG B 213     1267   1530   2103      6    -85   -621       C  
ATOM   2513  CG  ARG B 213     138.658  82.233 -34.363  1.00 14.53           C  
ANISOU 2513  CG  ARG B 213     1189   1972   2361   -138   -137   -447       C  
ATOM   2514  CD  ARG B 213     139.272  83.570 -34.259  1.00 14.56           C  
ANISOU 2514  CD  ARG B 213     1545   1685   2301   -167   -206    -89       C  
ATOM   2515  NE  ARG B 213     140.616  83.518 -33.710  1.00 13.39           N  
ANISOU 2515  NE  ARG B 213     1565   1508   2016    -49   -351    -62       N  
ATOM   2516  CZ  ARG B 213     140.912  83.727 -32.434  1.00 12.87           C  
ANISOU 2516  CZ  ARG B 213     1564   1454   1874    111    -93     97       C  
ATOM   2517  NH1 ARG B 213     139.948  83.966 -31.548  1.00 12.72           N1+
ANISOU 2517  NH1 ARG B 213     1552   1318   1963    -38     17     -3       N1+
ATOM   2518  NH2 ARG B 213     142.182  83.712 -32.050  1.00 13.98           N  
ANISOU 2518  NH2 ARG B 213     1693   1673   1947    -68   -284    -59       N  
ATOM   2519  N   HIS B 214     134.296  81.632 -34.572  1.00 10.10           N  
ANISOU 2519  N   HIS B 214     1509    819   1511    402    112    262       N  
ATOM   2520  CA  HIS B 214     132.893  81.816 -34.880  1.00  9.71           C  
ANISOU 2520  CA  HIS B 214     1412    851   1428    126     12    263       C  
ATOM   2521  C   HIS B 214     132.625  83.274 -35.191  1.00  8.50           C  
ANISOU 2521  C   HIS B 214     1333    693   1204     13   -133    166       C  
ATOM   2522  O   HIS B 214     133.232  84.177 -34.609  1.00  9.33           O  
ANISOU 2522  O   HIS B 214     1478    755   1312   -135    -23   -133       O  
ATOM   2523  CB  HIS B 214     132.044  81.455 -33.671  1.00  9.43           C  
ANISOU 2523  CB  HIS B 214     1750    494   1341     33    153    193       C  
ATOM   2524  CG  HIS B 214     132.325  80.092 -33.141  1.00 10.34           C  
ANISOU 2524  CG  HIS B 214     1999    533   1397    -99   -114    135       C  
ATOM   2525  ND1 HIS B 214     131.983  79.710 -31.863  1.00 10.83           N  
ANISOU 2525  ND1 HIS B 214     2086    710   1320   -148    -84    368       N  
ATOM   2526  CD2 HIS B 214     132.904  79.012 -33.719  1.00 11.95           C  
ANISOU 2526  CD2 HIS B 214     2365    603   1573    -95    -76     64       C  
ATOM   2527  CE1 HIS B 214     132.352  78.457 -31.669  1.00 12.34           C  
ANISOU 2527  CE1 HIS B 214     2454    740   1495    -26   -189    169       C  
ATOM   2528  NE2 HIS B 214     132.913  78.010 -32.781  1.00 12.84           N  
ANISOU 2528  NE2 HIS B 214     2578    726   1573     81     24    119       N  
ATOM   2529  N   SER B 215     131.688  83.501 -36.099  1.00  8.47           N  
ANISOU 2529  N   SER B 215     1366    788   1066    265   -115    173       N  
ATOM   2530  CA  SER B 215     131.211  84.852 -36.303  1.00  8.68           C  
ANISOU 2530  CA  SER B 215     1553    627   1119    346   -129    140       C  
ATOM   2531  C   SER B 215     129.784  84.797 -36.818  1.00  9.06           C  
ANISOU 2531  C   SER B 215     1463    765   1214     70      4     30       C  
ATOM   2532  O   SER B 215     129.297  83.757 -37.279  1.00  9.04           O  
ANISOU 2532  O   SER B 215     1478    602   1356      1    -46     97       O  
ATOM   2533  CB  SER B 215     132.103  85.630 -37.274  1.00  9.71           C  
ANISOU 2533  CB  SER B 215     1778    831   1079    343    350     66       C  
ATOM   2534  OG  SER B 215     132.226  84.948 -38.515  1.00 10.43           O  
ANISOU 2534  OG  SER B 215     2045    802   1115     51     68    117       O  
ATOM   2535  N   VAL B 216     129.113  85.932 -36.714  1.00  8.49           N  
ANISOU 2535  N   VAL B 216     1349    759   1118    113    104     96       N  
ATOM   2536  CA  VAL B 216     127.759  86.087 -37.216  1.00  8.49           C  
ANISOU 2536  CA  VAL B 216     1381    699   1145    -23   -110    208       C  
ATOM   2537  C   VAL B 216     127.733  87.339 -38.069  1.00  8.48           C  
ANISOU 2537  C   VAL B 216     1392    661   1167    -54   -362    131       C  
ATOM   2538  O   VAL B 216     128.270  88.381 -37.674  1.00  9.19           O  
ANISOU 2538  O   VAL B 216     1432    850   1209   -303   -140     29       O  
ATOM   2539  CB  VAL B 216     126.708  86.126 -36.083  1.00  8.41           C  
ANISOU 2539  CB  VAL B 216     1247    778   1170    -99   -107    -51       C  
ATOM   2540  CG1 VAL B 216     127.002  87.223 -35.050  1.00  8.80           C  
ANISOU 2540  CG1 VAL B 216     1378    910   1058    167     65    105       C  
ATOM   2541  CG2 VAL B 216     125.312  86.242 -36.673  1.00  9.93           C  
ANISOU 2541  CG2 VAL B 216     1442    824   1506    -76   -221    149       C  
ATOM   2542  N   VAL B 217     127.160  87.226 -39.259  1.00  8.91           N  
ANISOU 2542  N   VAL B 217     1520    736   1128    -97   -370    149       N  
ATOM   2543  CA  VAL B 217     127.219  88.296 -40.241  1.00  9.05           C  
ANISOU 2543  CA  VAL B 217     1715    644   1078   -141   -185    179       C  
ATOM   2544  C   VAL B 217     125.815  88.549 -40.766  1.00 10.13           C  
ANISOU 2544  C   VAL B 217     1810    776   1261   -125   -348     54       C  
ATOM   2545  O   VAL B 217     125.046  87.603 -40.985  1.00 11.23           O  
ANISOU 2545  O   VAL B 217     1832    954   1479   -245   -544     66       O  
ATOM   2546  CB  VAL B 217     128.222  87.947 -41.373  1.00 10.61           C  
ANISOU 2546  CB  VAL B 217     2059    807   1168    -56    176    -26       C  
ATOM   2547  CG1 VAL B 217     127.852  86.641 -42.070  1.00 11.73           C  
ANISOU 2547  CG1 VAL B 217     2305    793   1359    -54    -23   -130       C  
ATOM   2548  CG2 VAL B 217     128.363  89.099 -42.375  1.00 11.32           C  
ANISOU 2548  CG2 VAL B 217     1967   1241   1091      2    131    179       C  
ATOM   2549  N   VAL B 218     125.472  89.824 -40.940  1.00 10.04           N  
ANISOU 2549  N   VAL B 218     1673    929   1211     51   -154     70       N  
ATOM   2550  CA  VAL B 218     124.180  90.217 -41.501  1.00 10.87           C  
ANISOU 2550  CA  VAL B 218     1859   1076   1196     83   -167    121       C  
ATOM   2551  C   VAL B 218     124.420  91.200 -42.633  1.00 10.65           C  
ANISOU 2551  C   VAL B 218     1756   1041   1250     33   -238     49       C  
ATOM   2552  O   VAL B 218     125.459  91.876 -42.688  1.00 11.33           O  
ANISOU 2552  O   VAL B 218     1826   1192   1288    -48   -389     81       O  
ATOM   2553  CB  VAL B 218     123.255  90.863 -40.441  1.00 12.21           C  
ANISOU 2553  CB  VAL B 218     2108   1173   1358    309     27   -122       C  
ATOM   2554  CG1 VAL B 218     122.831  89.843 -39.405  1.00 14.33           C  
ANISOU 2554  CG1 VAL B 218     2301   1767   1379    239      9    583       C  
ATOM   2555  CG2 VAL B 218     123.918  92.080 -39.796  1.00 13.97           C  
ANISOU 2555  CG2 VAL B 218     2262   1446   1600    374    -49   -374       C  
ATOM   2556  N   PRO B 219     123.458  91.330 -43.537  1.00 11.60           N  
ANISOU 2556  N   PRO B 219     1881   1176   1351    -77   -408    119       N  
ATOM   2557  CA  PRO B 219     123.555  92.384 -44.547  1.00 12.35           C  
ANISOU 2557  CA  PRO B 219     2122   1290   1279    162   -467    396       C  
ATOM   2558  C   PRO B 219     123.505  93.744 -43.879  1.00 12.63           C  
ANISOU 2558  C   PRO B 219     1997   1381   1420    164   -197    414       C  
ATOM   2559  O   PRO B 219     122.760  93.959 -42.922  1.00 13.78           O  
ANISOU 2559  O   PRO B 219     2138   1649   1449    170     82    495       O  
ATOM   2560  CB  PRO B 219     122.310  92.159 -45.409  1.00 13.40           C  
ANISOU 2560  CB  PRO B 219     2146   1511   1436    -24   -597    436       C  
ATOM   2561  CG  PRO B 219     121.938  90.736 -45.182  1.00 13.71           C  
ANISOU 2561  CG  PRO B 219     2349   1430   1431   -150   -559    261       C  
ATOM   2562  CD  PRO B 219     122.284  90.465 -43.753  1.00 12.63           C  
ANISOU 2562  CD  PRO B 219     1970   1407   1423   -360   -522     98       C  
ATOM   2563  N   HIS B 220     124.309  94.665 -44.388  1.00 12.69           N  
ANISOU 2563  N   HIS B 220     2070   1141   1610     34   -194    238       N  
ATOM   2564  CA  HIS B 220     124.185  96.046 -43.967  1.00 13.83           C  
ANISOU 2564  CA  HIS B 220     2159   1276   1820    251   -111    280       C  
ATOM   2565  C   HIS B 220     122.965  96.665 -44.631  1.00 15.07           C  
ANISOU 2565  C   HIS B 220     2296   1431   1998    521   -197    113       C  
ATOM   2566  O   HIS B 220     122.794  96.567 -45.850  1.00 17.76           O  
ANISOU 2566  O   HIS B 220     2772   1862   2114    541   -227    401       O  
ATOM   2567  CB  HIS B 220     125.422  96.845 -44.352  1.00 14.77           C  
ANISOU 2567  CB  HIS B 220     2425   1227   1961    104    157    155       C  
ATOM   2568  CG  HIS B 220     125.311  98.280 -43.975  1.00 17.03           C  
ANISOU 2568  CG  HIS B 220     2839   1423   2207    230    180    307       C  
ATOM   2569  ND1 HIS B 220     124.863  99.245 -44.851  1.00 19.49           N  
ANISOU 2569  ND1 HIS B 220     3284   1570   2551     69    170    432       N  
ATOM   2570  CD2 HIS B 220     125.520  98.905 -42.793  1.00 18.38           C  
ANISOU 2570  CD2 HIS B 220     3029   1582   2374   -145    224    165       C  
ATOM   2571  CE1 HIS B 220     124.833 100.411 -44.231  1.00 20.65           C  
ANISOU 2571  CE1 HIS B 220     3477   1733   2635    -34    206    221       C  
ATOM   2572  NE2 HIS B 220     125.223 100.231 -42.982  1.00 19.95           N  
ANISOU 2572  NE2 HIS B 220     3391   1613   2576    -45    203    330       N  
ATOM   2573  N   GLU B 221     122.114  97.283 -43.827  1.00 16.59           N  
ANISOU 2573  N   GLU B 221     2558   1363   2380    639   -378   -171       N  
ATOM   2574  CA  GLU B 221     120.975  98.006 -44.330  1.00 20.08           C  
ANISOU 2574  CA  GLU B 221     3139   1746   2744    716   -367   -260       C  
ATOM   2575  C   GLU B 221     121.107  99.459 -43.906  1.00 21.88           C  
ANISOU 2575  C   GLU B 221     3620   1873   2819    850   -556   -448       C  
ATOM   2576  O   GLU B 221     121.466  99.727 -42.748  1.00 22.16           O  
ANISOU 2576  O   GLU B 221     3537   2030   2855    971   -641   -494       O  
ATOM   2577  CB  GLU B 221     119.675  97.410 -43.773  1.00 22.20           C  
ANISOU 2577  CB  GLU B 221     3380   1984   3071    525   -292   -128       C  
ATOM   2578  CG  GLU B 221     119.333  96.044 -44.349  1.00 23.17           C  
ANISOU 2578  CG  GLU B 221     3490   2055   3260    582   -267   -214       C  
ATOM   2579  N   PRO B 222     120.872 100.413 -44.796  1.00 24.58           N  
ANISOU 2579  N   PRO B 222     4424   1982   2935    692   -628   -510       N  
ATOM   2580  CA  PRO B 222     120.927 101.821 -44.405  1.00 26.30           C  
ANISOU 2580  CA  PRO B 222     4701   2140   3149    745   -684   -338       C  
ATOM   2581  C   PRO B 222     119.864 102.145 -43.372  1.00 27.12           C  
ANISOU 2581  C   PRO B 222     4532   2289   3485    887   -844   -559       C  
ATOM   2582  O   PRO B 222     118.935 101.356 -43.158  1.00 27.44           O  
ANISOU 2582  O   PRO B 222     4440   2343   3642    965   -822   -711       O  
ATOM   2583  CB  PRO B 222     120.664 102.576 -45.727  1.00 27.85           C  
ANISOU 2583  CB  PRO B 222     5092   2405   3086    571   -698   -190       C  
ATOM   2584  CG  PRO B 222     120.666 101.552 -46.805  1.00 28.60           C  
ANISOU 2584  CG  PRO B 222     5214   2495   3157    395   -600   -313       C  
ATOM   2585  CD  PRO B 222     120.516 100.206 -46.208  1.00 26.52           C  
ANISOU 2585  CD  PRO B 222     4889   2192   2994    584   -716   -412       C  
ATOM   2586  N   PRO B 223     119.989 103.280 -42.687  1.00 26.96           N  
ANISOU 2586  N   PRO B 223     4363   2317   3564   1030  -1033   -792       N  
ATOM   2587  CA  PRO B 223     119.011 103.629 -41.651  1.00 29.04           C  
ANISOU 2587  CA  PRO B 223     4425   2713   3896   1185  -1073   -917       C  
ATOM   2588  C   PRO B 223     117.595 103.703 -42.202  1.00 32.81           C  
ANISOU 2588  C   PRO B 223     4713   3337   4415   1402  -1077  -1044       C  
ATOM   2589  O   PRO B 223     117.369 104.104 -43.345  1.00 33.15           O  
ANISOU 2589  O   PRO B 223     4731   3435   4430   1425  -1255   -998       O  
ATOM   2590  CB  PRO B 223     119.490 105.004 -41.170  1.00 27.81           C  
ANISOU 2590  CB  PRO B 223     4361   2462   3742   1101  -1022   -836       C  
ATOM   2591  CG  PRO B 223     120.963 104.983 -41.421  1.00 27.19           C  
ANISOU 2591  CG  PRO B 223     4455   2237   3639   1120   -930   -742       C  
ATOM   2592  CD  PRO B 223     121.136 104.207 -42.699  1.00 27.41           C  
ANISOU 2592  CD  PRO B 223     4472   2347   3596   1001   -968   -653       C  
ATOM   2593  N   GLU B 224     116.635 103.293 -41.376  1.00 35.37           N  
ANISOU 2593  N   GLU B 224     4759   3854   4825   1591  -1002  -1246       N  
ATOM   2594  CA  GLU B 224     115.241 103.500 -41.720  1.00 38.26           C  
ANISOU 2594  CA  GLU B 224     4882   4451   5205   1551  -1026  -1341       C  
ATOM   2595  C   GLU B 224     114.930 104.995 -41.715  1.00 39.72           C  
ANISOU 2595  C   GLU B 224     4778   4836   5479   1679  -1109  -1447       C  
ATOM   2596  O   GLU B 224     115.641 105.801 -41.108  1.00 39.51           O  
ANISOU 2596  O   GLU B 224     4669   4862   5482   1608  -1194  -1657       O  
ATOM   2597  CB  GLU B 224     114.337 102.774 -40.723  1.00 39.45           C  
ANISOU 2597  CB  GLU B 224     5109   4609   5271   1407  -1011  -1356       C  
ATOM   2598  N   VAL B 225     113.859 105.367 -42.421  1.00 41.18           N  
ANISOU 2598  N   VAL B 225     4809   5133   5704   1729  -1130  -1349       N  
ATOM   2599  CA  VAL B 225     113.463 106.770 -42.463  1.00 42.01           C  
ANISOU 2599  CA  VAL B 225     4743   5321   5897   1900  -1027  -1252       C  
ATOM   2600  C   VAL B 225     113.234 107.277 -41.046  1.00 42.12           C  
ANISOU 2600  C   VAL B 225     4740   5283   5980   2015   -781  -1216       C  
ATOM   2601  O   VAL B 225     112.644 106.589 -40.203  1.00 43.00           O  
ANISOU 2601  O   VAL B 225     4758   5486   6095   1813   -615  -1167       O  
ATOM   2602  CB  VAL B 225     112.221 106.956 -43.350  1.00 43.01           C  
ANISOU 2602  CB  VAL B 225     4812   5551   5977   1830  -1129  -1188       C  
ATOM   2603  CG1 VAL B 225     111.750 108.403 -43.315  1.00 43.30           C  
ANISOU 2603  CG1 VAL B 225     4841   5595   6017   1870  -1185  -1105       C  
ATOM   2604  CG2 VAL B 225     112.529 106.533 -44.774  1.00 43.76           C  
ANISOU 2604  CG2 VAL B 225     4925   5714   5987   1697  -1157  -1152       C  
ATOM   2605  N   GLY B 226     113.735 108.479 -40.768  1.00 41.15           N  
ANISOU 2605  N   GLY B 226     4790   4943   5902   2355   -693  -1206       N  
ATOM   2606  CA  GLY B 226     113.652 109.044 -39.441  1.00 40.43           C  
ANISOU 2606  CA  GLY B 226     4959   4661   5740   2205   -774  -1204       C  
ATOM   2607  C   GLY B 226     114.718 108.576 -38.478  1.00 39.12           C  
ANISOU 2607  C   GLY B 226     4991   4303   5570   2141   -693  -1199       C  
ATOM   2608  O   GLY B 226     114.685 108.966 -37.304  1.00 40.54           O  
ANISOU 2608  O   GLY B 226     5231   4481   5693   2151   -628  -1335       O  
ATOM   2609  N   SER B 227     115.653 107.748 -38.923  1.00 35.83           N  
ANISOU 2609  N   SER B 227     4676   3677   5259   1973   -790   -926       N  
ATOM   2610  CA  SER B 227     116.765 107.311 -38.099  1.00 33.97           C  
ANISOU 2610  CA  SER B 227     4777   3182   4949   1469   -797   -558       C  
ATOM   2611  C   SER B 227     118.069 107.713 -38.771  1.00 30.42           C  
ANISOU 2611  C   SER B 227     4507   2607   4445   1285   -934   -490       C  
ATOM   2612  O   SER B 227     118.156 107.784 -40.000  1.00 31.00           O  
ANISOU 2612  O   SER B 227     4532   2761   4485   1269  -1078   -571       O  
ATOM   2613  CB  SER B 227     116.737 105.795 -37.888  1.00 35.49           C  
ANISOU 2613  CB  SER B 227     5052   3342   5092   1117   -655   -260       C  
ATOM   2614  OG  SER B 227     117.832 105.378 -37.093  1.00 37.12           O  
ANISOU 2614  OG  SER B 227     5298   3601   5205    829   -495   -119       O  
ATOM   2615  N   ASP B 228     119.085 107.986 -37.953  1.00 26.09           N  
ANISOU 2615  N   ASP B 228     4088   1931   3894   1032  -1039   -416       N  
ATOM   2616  CA  ASP B 228     120.374 108.428 -38.459  1.00 24.06           C  
ANISOU 2616  CA  ASP B 228     3993   1677   3470    900   -928   -240       C  
ATOM   2617  C   ASP B 228     121.412 107.321 -38.485  1.00 21.34           C  
ANISOU 2617  C   ASP B 228     3642   1510   2956    654   -673     98       C  
ATOM   2618  O   ASP B 228     122.511 107.536 -39.001  1.00 23.31           O  
ANISOU 2618  O   ASP B 228     3916   1937   3005    649   -520    293       O  
ATOM   2619  CB  ASP B 228     120.906 109.591 -37.616  1.00 26.13           C  
ANISOU 2619  CB  ASP B 228     4444   1782   3703    717   -983   -212       C  
ATOM   2620  CG  ASP B 228     120.033 110.818 -37.706  1.00 28.92           C  
ANISOU 2620  CG  ASP B 228     4857   2242   3889    653   -985   -225       C  
ATOM   2621  OD1 ASP B 228     119.497 111.092 -38.800  1.00 30.98           O  
ANISOU 2621  OD1 ASP B 228     5133   2691   3948    571  -1108    -78       O  
ATOM   2622  OD2 ASP B 228     119.874 111.504 -36.676  1.00 28.70           O1-
ANISOU 2622  OD2 ASP B 228     4873   2019   4014    557   -875   -395       O1-
ATOM   2623  N   CYS B 229     121.101 106.153 -37.937  1.00 18.21           N  
ANISOU 2623  N   CYS B 229     3289   1116   2513    655   -409    129       N  
ATOM   2624  CA  CYS B 229     122.043 105.050 -37.928  1.00 16.64           C  
ANISOU 2624  CA  CYS B 229     2984   1158   2182    252   -477    -53       C  
ATOM   2625  C   CYS B 229     121.283 103.750 -38.110  1.00 17.52           C  
ANISOU 2625  C   CYS B 229     3134   1439   2082    164   -409    -63       C  
ATOM   2626  O   CYS B 229     120.052 103.705 -38.060  1.00 19.41           O  
ANISOU 2626  O   CYS B 229     3285   1700   2389    374   -263   -180       O  
ATOM   2627  CB  CYS B 229     122.864 105.019 -36.636  1.00 16.83           C  
ANISOU 2627  CB  CYS B 229     2975   1431   1989    259    -64     42       C  
ATOM   2628  SG  CYS B 229     121.885 104.702 -35.149  1.00 17.90           S  
ANISOU 2628  SG  CYS B 229     3057   1707   2036    194   -188    -16       S  
ATOM   2629  N   THR B 230     122.043 102.690 -38.331  1.00 16.06           N  
ANISOU 2629  N   THR B 230     3148   1222   1732    170   -295    -58       N  
ATOM   2630  CA  THR B 230     121.529 101.336 -38.369  1.00 15.77           C  
ANISOU 2630  CA  THR B 230     3148   1237   1608     94   -340    149       C  
ATOM   2631  C   THR B 230     121.829 100.694 -37.025  1.00 13.53           C  
ANISOU 2631  C   THR B 230     2468   1121   1554    101   -398    249       C  
ATOM   2632  O   THR B 230     122.842 100.993 -36.396  1.00 16.09           O  
ANISOU 2632  O   THR B 230     2579   1921   1613   -135   -408    363       O  
ATOM   2633  CB  THR B 230     122.234 100.567 -39.488  1.00 17.22           C  
ANISOU 2633  CB  THR B 230     3707   1174   1663    247   -394    135       C  
ATOM   2634  OG1 THR B 230     121.978 101.232 -40.737  1.00 20.31           O  
ANISOU 2634  OG1 THR B 230     4068   1782   1867     90   -356    199       O  
ATOM   2635  CG2 THR B 230     121.745  99.138 -39.565  1.00 19.60           C  
ANISOU 2635  CG2 THR B 230     4014   1568   1866    243   -315   -135       C  
ATOM   2636  N   THR B 231     120.928  99.834 -36.565  1.00 13.24           N  
ANISOU 2636  N   THR B 231     2248   1020   1764     84   -348    131       N  
ATOM   2637  CA  THR B 231     121.135  99.144 -35.299  1.00 13.55           C  
ANISOU 2637  CA  THR B 231     2153   1082   1913    112   -308    223       C  
ATOM   2638  C   THR B 231     121.044  97.645 -35.519  1.00 13.59           C  
ANISOU 2638  C   THR B 231     2066   1127   1971    106   -518    275       C  
ATOM   2639  O   THR B 231     120.153  97.170 -36.229  1.00 15.92           O  
ANISOU 2639  O   THR B 231     2339   1419   2292    -16   -816    264       O  
ATOM   2640  CB  THR B 231     120.114  99.617 -34.260  1.00 16.17           C  
ANISOU 2640  CB  THR B 231     2566   1435   2143    202    -88    249       C  
ATOM   2641  OG1 THR B 231     120.282 101.026 -34.062  1.00 18.64           O  
ANISOU 2641  OG1 THR B 231     2921   1751   2410    148    161    134       O  
ATOM   2642  CG2 THR B 231     120.316  98.899 -32.933  1.00 17.82           C  
ANISOU 2642  CG2 THR B 231     2798   1845   2130    385    -94    260       C  
ATOM   2643  N   ILE B 232     121.979  96.906 -34.933  1.00 11.95           N  
ANISOU 2643  N   ILE B 232     1892    899   1749     92   -235    224       N  
ATOM   2644  CA  ILE B 232     121.914  95.452 -34.876  1.00 11.61           C  
ANISOU 2644  CA  ILE B 232     1777    883   1751    101     -5    286       C  
ATOM   2645  C   ILE B 232     121.672  95.068 -33.427  1.00 11.61           C  
ANISOU 2645  C   ILE B 232     1878    934   1598      1    -95    177       C  
ATOM   2646  O   ILE B 232     122.224  95.688 -32.513  1.00 13.35           O  
ANISOU 2646  O   ILE B 232     2046   1337   1691   -213   -297     89       O  
ATOM   2647  CB  ILE B 232     123.210  94.802 -35.397  1.00 12.96           C  
ANISOU 2647  CB  ILE B 232     1943   1121   1859    118    297    342       C  
ATOM   2648  CG1 ILE B 232     123.450  95.191 -36.856  1.00 15.74           C  
ANISOU 2648  CG1 ILE B 232     2259   1804   1917    220    314    364       C  
ATOM   2649  CG2 ILE B 232     123.152  93.280 -35.250  1.00 13.04           C  
ANISOU 2649  CG2 ILE B 232     2121    792   2040   -160     29     68       C  
ATOM   2650  CD1 ILE B 232     124.763  94.702 -37.385  1.00 16.27           C  
ANISOU 2650  CD1 ILE B 232     2269   2088   1826    132    333    108       C  
ATOM   2651  N   HIS B 233     120.838  94.059 -33.214  1.00 11.46           N  
ANISOU 2651  N   HIS B 233     1827    974   1555     83     -4    217       N  
ATOM   2652  CA  HIS B 233     120.593  93.529 -31.879  1.00 10.47           C  
ANISOU 2652  CA  HIS B 233     1545    901   1532    479    -41    170       C  
ATOM   2653  C   HIS B 233     121.389  92.240 -31.729  1.00 10.09           C  
ANISOU 2653  C   HIS B 233     1509    870   1453    219    -41   -155       C  
ATOM   2654  O   HIS B 233     121.119  91.254 -32.421  1.00 11.71           O  
ANISOU 2654  O   HIS B 233     1788   1044   1618     74   -339   -171       O  
ATOM   2655  CB  HIS B 233     119.105  93.260 -31.672  1.00 12.80           C  
ANISOU 2655  CB  HIS B 233     1468   1326   2071    475   -115    227       C  
ATOM   2656  CG  HIS B 233     118.284  94.498 -31.508  1.00 15.81           C  
ANISOU 2656  CG  HIS B 233     1744   1787   2476    470    -84    121       C  
ATOM   2657  ND1 HIS B 233     116.907  94.475 -31.467  1.00 20.62           N  
ANISOU 2657  ND1 HIS B 233     2544   2374   2916    613    -82    108       N  
ATOM   2658  CD2 HIS B 233     118.644  95.794 -31.353  1.00 17.61           C  
ANISOU 2658  CD2 HIS B 233     2115   1892   2684    692   -150     15       C  
ATOM   2659  CE1 HIS B 233     116.454  95.706 -31.308  1.00 20.85           C  
ANISOU 2659  CE1 HIS B 233     2579   2287   3055    689    -12    -41       C  
ATOM   2660  NE2 HIS B 233     117.488  96.525 -31.244  1.00 20.02           N  
ANISOU 2660  NE2 HIS B 233     2353   2250   3002    580    -62    -96       N  
ATOM   2661  N   TYR B 234     122.367  92.254 -30.833  1.00  9.99           N  
ANISOU 2661  N   TYR B 234     1509    863   1424    124     -9    101       N  
ATOM   2662  CA  TYR B 234     123.158  91.078 -30.524  1.00  9.89           C  
ANISOU 2662  CA  TYR B 234     1321    959   1479    111     68    132       C  
ATOM   2663  C   TYR B 234     122.687  90.459 -29.218  1.00 10.18           C  
ANISOU 2663  C   TYR B 234     1637    839   1393     83     30    200       C  
ATOM   2664  O   TYR B 234     122.123  91.136 -28.355  1.00 11.01           O  
ANISOU 2664  O   TYR B 234     1891    833   1459    105     22    -43       O  
ATOM   2665  CB  TYR B 234     124.640  91.429 -30.408  1.00 10.09           C  
ANISOU 2665  CB  TYR B 234     1295   1027   1512   -109     74     37       C  
ATOM   2666  CG  TYR B 234     125.262  91.810 -31.727  1.00  9.61           C  
ANISOU 2666  CG  TYR B 234     1378    954   1321     90     43     26       C  
ATOM   2667  CD1 TYR B 234     125.458  90.859 -32.721  1.00  9.94           C  
ANISOU 2667  CD1 TYR B 234     1459   1032   1286    364     13    -83       C  
ATOM   2668  CD2 TYR B 234     125.649  93.120 -31.986  1.00 11.42           C  
ANISOU 2668  CD2 TYR B 234     1809   1191   1339   -100    152     24       C  
ATOM   2669  CE1 TYR B 234     126.031  91.196 -33.929  1.00  9.77           C  
ANISOU 2669  CE1 TYR B 234     1505   1029   1179    140    -95    -84       C  
ATOM   2670  CE2 TYR B 234     126.223  93.468 -33.196  1.00 11.12           C  
ANISOU 2670  CE2 TYR B 234     1724   1230   1270   -103    136    -89       C  
ATOM   2671  CZ  TYR B 234     126.409  92.500 -34.166  1.00  9.66           C  
ANISOU 2671  CZ  TYR B 234     1614    860   1195   -153      0     42       C  
ATOM   2672  OH  TYR B 234     126.985  92.853 -35.369  1.00 10.67           O  
ANISOU 2672  OH  TYR B 234     1661   1013   1379     21    161    122       O  
ATOM   2673  N   ASN B 235     122.916  89.156 -29.088  1.00 10.25           N  
ANISOU 2673  N   ASN B 235     1712    838   1343    181   -112    209       N  
ATOM   2674  CA  ASN B 235     122.719  88.448 -27.831  1.00  9.77           C  
ANISOU 2674  CA  ASN B 235     1648    744   1319    216    -58    363       C  
ATOM   2675  C   ASN B 235     124.004  87.700 -27.523  1.00  9.17           C  
ANISOU 2675  C   ASN B 235     1629    639   1216    298      0     65       C  
ATOM   2676  O   ASN B 235     124.596  87.089 -28.415  1.00 11.79           O  
ANISOU 2676  O   ASN B 235     1903   1262   1313    457    167   -185       O  
ATOM   2677  CB  ASN B 235     121.616  87.371 -27.909  1.00 11.73           C  
ANISOU 2677  CB  ASN B 235     1763    930   1762   -161    -24    106       C  
ATOM   2678  CG  ASN B 235     120.256  87.914 -28.341  1.00 15.83           C  
ANISOU 2678  CG  ASN B 235     2342   1545   2129   -228    -69    -81       C  
ATOM   2679  OD1 ASN B 235     119.473  87.195 -28.956  1.00 19.69           O  
ANISOU 2679  OD1 ASN B 235     2942   1913   2625   -206   -187   -237       O  
ATOM   2680  ND2 ASN B 235     119.967  89.163 -28.017  1.00 15.52           N  
ANISOU 2680  ND2 ASN B 235     2292   1454   2150   -154    202     99       N  
ATOM   2681  N   TYR B 236     124.428  87.736 -26.265  1.00  8.93           N  
ANISOU 2681  N   TYR B 236     1398    735   1258     47   -192     79       N  
ATOM   2682  CA  TYR B 236     125.587  86.984 -25.809  1.00  8.90           C  
ANISOU 2682  CA  TYR B 236     1462    571   1348   -149     -7     48       C  
ATOM   2683  C   TYR B 236     125.103  85.812 -24.972  1.00  8.85           C  
ANISOU 2683  C   TYR B 236     1532    478   1352   -245     60   -151       C  
ATOM   2684  O   TYR B 236     124.350  86.001 -24.012  1.00 10.43           O  
ANISOU 2684  O   TYR B 236     1783    842   1337   -107    176    -63       O  
ATOM   2685  CB  TYR B 236     126.523  87.880 -25.001  1.00  9.66           C  
ANISOU 2685  CB  TYR B 236     1550    683   1436   -281    102     -6       C  
ATOM   2686  CG  TYR B 236     127.194  88.914 -25.865  1.00  9.54           C  
ANISOU 2686  CG  TYR B 236     1403    850   1370    -16     82     -9       C  
ATOM   2687  CD1 TYR B 236     126.564  90.121 -26.144  1.00 10.39           C  
ANISOU 2687  CD1 TYR B 236     1639    816   1492    -24     14     -4       C  
ATOM   2688  CD2 TYR B 236     128.452  88.684 -26.414  1.00 10.13           C  
ANISOU 2688  CD2 TYR B 236     1298   1037   1515   -100     59   -219       C  
ATOM   2689  CE1 TYR B 236     127.168  91.070 -26.947  1.00 10.56           C  
ANISOU 2689  CE1 TYR B 236     1552    831   1628   -206    -39    295       C  
ATOM   2690  CE2 TYR B 236     129.068  89.631 -27.218  1.00 10.48           C  
ANISOU 2690  CE2 TYR B 236     1592    885   1506      8    132    -43       C  
ATOM   2691  CZ  TYR B 236     128.413  90.824 -27.490  1.00 11.46           C  
ANISOU 2691  CZ  TYR B 236     1769    951   1635   -236    131    151       C  
ATOM   2692  OH  TYR B 236     129.006  91.780 -28.287  1.00 12.05           O  
ANISOU 2692  OH  TYR B 236     1872   1222   1486   -491    150    216       O  
ATOM   2693  N   MET B 237     125.549  84.609 -25.325  1.00  9.16           N  
ANISOU 2693  N   MET B 237     1696    441   1342     -4   -127    -75       N  
ATOM   2694  CA  MET B 237     124.863  83.393 -24.906  1.00  9.87           C  
ANISOU 2694  CA  MET B 237     1825    492   1434   -103   -219     50       C  
ATOM   2695  C   MET B 237     125.563  82.629 -23.790  1.00 10.24           C  
ANISOU 2695  C   MET B 237     1853    583   1454   -247    -44    -38       C  
ATOM   2696  O   MET B 237     125.157  81.500 -23.482  1.00 11.34           O  
ANISOU 2696  O   MET B 237     2105    700   1504   -344    101     31       O  
ATOM   2697  CB  MET B 237     124.615  82.498 -26.116  1.00 10.54           C  
ANISOU 2697  CB  MET B 237     1854    568   1582   -142   -342    116       C  
ATOM   2698  CG  MET B 237     123.832  83.194 -27.218  1.00 12.11           C  
ANISOU 2698  CG  MET B 237     1892    944   1766    201   -389    189       C  
ATOM   2699  SD  MET B 237     122.224  83.806 -26.681  1.00 14.17           S  
ANISOU 2699  SD  MET B 237     2233   1119   2031      4   -441      7       S  
ATOM   2700  CE  MET B 237     121.517  82.304 -25.997  1.00 14.85           C  
ANISOU 2700  CE  MET B 237     2095   1298   2248   -258    -19    -30       C  
ATOM   2701  N   CYS B 238     126.583  83.216 -23.172  1.00 10.46           N  
ANISOU 2701  N   CYS B 238     1830    829   1315    -21    -52      7       N  
ATOM   2702  CA  CYS B 238     127.198  82.689 -21.966  1.00 10.97           C  
ANISOU 2702  CA  CYS B 238     1994    835   1340     54    -39    -32       C  
ATOM   2703  C   CYS B 238     127.552  83.867 -21.089  1.00 10.41           C  
ANISOU 2703  C   CYS B 238     2019    764   1171   -255    -32    252       C  
ATOM   2704  O   CYS B 238     127.764  84.976 -21.584  1.00 11.58           O  
ANISOU 2704  O   CYS B 238     2019    999   1382   -262     14    285       O  
ATOM   2705  CB  CYS B 238     128.514  81.968 -22.253  1.00 11.68           C  
ANISOU 2705  CB  CYS B 238     2115    799   1525    437     25    207       C  
ATOM   2706  SG  CYS B 238     128.368  80.215 -22.600  1.00 12.46           S  
ANISOU 2706  SG  CYS B 238     2299   1053   1381    177    131    123       S  
ATOM   2707  N   TYR B 239     127.601  83.619 -19.783  1.00 10.90           N  
ANISOU 2707  N   TYR B 239     1941   1118   1083   -156     -3     90       N  
ATOM   2708  CA  TYR B 239     128.154  84.601 -18.869  1.00 10.93           C  
ANISOU 2708  CA  TYR B 239     1883   1100   1169   -220    -69      6       C  
ATOM   2709  C   TYR B 239     129.665  84.640 -19.026  1.00  9.99           C  
ANISOU 2709  C   TYR B 239     1748    760   1289   -114   -243    -32       C  
ATOM   2710  O   TYR B 239     130.300  83.640 -19.373  1.00 11.02           O  
ANISOU 2710  O   TYR B 239     1925    861   1401      2   -171     88       O  
ATOM   2711  CB  TYR B 239     127.840  84.211 -17.427  1.00 13.08           C  
ANISOU 2711  CB  TYR B 239     2239   1405   1324   -266    -26    206       C  
ATOM   2712  CG  TYR B 239     126.403  84.412 -17.029  1.00 13.93           C  
ANISOU 2712  CG  TYR B 239     2327   1574   1392   -380     97    177       C  
ATOM   2713  CD1 TYR B 239     125.883  85.689 -16.893  1.00 15.04           C  
ANISOU 2713  CD1 TYR B 239     2331   1680   1704   -153    103    234       C  
ATOM   2714  CD2 TYR B 239     125.573  83.336 -16.770  1.00 14.85           C  
ANISOU 2714  CD2 TYR B 239     2490   1629   1524   -304     41    198       C  
ATOM   2715  CE1 TYR B 239     124.579  85.898 -16.517  1.00 16.02           C  
ANISOU 2715  CE1 TYR B 239     2301   1992   1793   -320    424    336       C  
ATOM   2716  CE2 TYR B 239     124.255  83.528 -16.389  1.00 15.47           C  
ANISOU 2716  CE2 TYR B 239     2434   1812   1631    -89    246    414       C  
ATOM   2717  CZ  TYR B 239     123.764  84.816 -16.269  1.00 16.16           C  
ANISOU 2717  CZ  TYR B 239     2196   2082   1864   -226    521    404       C  
ATOM   2718  OH  TYR B 239     122.457  85.023 -15.890  1.00 19.44           O  
ANISOU 2718  OH  TYR B 239     2387   2746   2255      8    511    498       O  
ATOM   2719  N   SER B 240     130.251  85.807 -18.740  1.00 10.63           N  
ANISOU 2719  N   SER B 240     1957    762   1321   -174   -226      4       N  
ATOM   2720  CA  SER B 240     131.707  85.890 -18.697  1.00 10.89           C  
ANISOU 2720  CA  SER B 240     2049    805   1286   -258   -415    -56       C  
ATOM   2721  C   SER B 240     132.296  84.869 -17.737  1.00 12.56           C  
ANISOU 2721  C   SER B 240     2386   1004   1383   -174   -367     35       C  
ATOM   2722  O   SER B 240     133.411  84.387 -17.953  1.00 14.71           O  
ANISOU 2722  O   SER B 240     2631   1383   1576    116   -314    111       O  
ATOM   2723  CB  SER B 240     132.151  87.295 -18.297  1.00 12.23           C  
ANISOU 2723  CB  SER B 240     2110    912   1623   -212   -260    -10       C  
ATOM   2724  OG  SER B 240     131.887  88.215 -19.344  1.00 12.37           O  
ANISOU 2724  OG  SER B 240     2015    987   1698    -46   -339    242       O  
ATOM   2725  N   SER B 241     131.562  84.519 -16.686  1.00 12.31           N  
ANISOU 2725  N   SER B 241     2379    990   1308   -149   -281    143       N  
ATOM   2726  CA  SER B 241     132.052  83.587 -15.678  1.00 13.28           C  
ANISOU 2726  CA  SER B 241     2633   1170   1245    231   -196    264       C  
ATOM   2727  C   SER B 241     131.862  82.115 -16.037  1.00 13.96           C  
ANISOU 2727  C   SER B 241     2833   1137   1335     68   -311    182       C  
ATOM   2728  O   SER B 241     132.276  81.264 -15.242  1.00 16.40           O  
ANISOU 2728  O   SER B 241     3432   1187   1610    264   -429    185       O  
ATOM   2729  CB  SER B 241     131.323  83.846 -14.363  1.00 15.38           C  
ANISOU 2729  CB  SER B 241     2770   1609   1464     90      3    308       C  
ATOM   2730  OG  SER B 241     129.942  83.580 -14.529  1.00 17.34           O  
ANISOU 2730  OG  SER B 241     2891   2039   1659     70    212    313       O  
ATOM   2731  N   CYS B 242     131.251  81.776 -17.178  1.00 12.83           N  
ANISOU 2731  N   CYS B 242     2633    904   1339    293     18     11       N  
ATOM   2732  CA  CYS B 242     130.901  80.376 -17.432  1.00 13.38           C  
ANISOU 2732  CA  CYS B 242     2649    967   1470    187     71    150       C  
ATOM   2733  C   CYS B 242     132.134  79.480 -17.398  1.00 14.12           C  
ANISOU 2733  C   CYS B 242     2772    895   1698     77    370    261       C  
ATOM   2734  O   CYS B 242     133.084  79.685 -18.160  1.00 15.05           O  
ANISOU 2734  O   CYS B 242     2707   1024   1989   -159    450    203       O  
ATOM   2735  CB  CYS B 242     130.185  80.225 -18.776  1.00 13.66           C  
ANISOU 2735  CB  CYS B 242     2589   1161   1440    303     69    -74       C  
ATOM   2736  SG  CYS B 242     128.409  80.534 -18.725  1.00 13.29           S  
ANISOU 2736  SG  CYS B 242     2691    924   1435     -2    203     76       S  
ATOM   2737  N   MET B 243     132.104  78.475 -16.525  1.00 15.33           N  
ANISOU 2737  N   MET B 243     3104    947   1773    158    227    369       N  
ATOM   2738  CA  MET B 243     133.235  77.571 -16.381  1.00 18.76           C  
ANISOU 2738  CA  MET B 243     3687   1469   1972    415    245    201       C  
ATOM   2739  C   MET B 243     133.391  76.733 -17.641  1.00 17.19           C  
ANISOU 2739  C   MET B 243     3191   1351   1988    251    254    437       C  
ATOM   2740  O   MET B 243     132.410  76.240 -18.203  1.00 15.97           O  
ANISOU 2740  O   MET B 243     2933   1221   1914    -18     73    406       O  
ATOM   2741  CB  MET B 243     132.998  76.621 -15.206  1.00 23.05           C  
ANISOU 2741  CB  MET B 243     4951   1941   1865    662    303    189       C  
ATOM   2742  CG  MET B 243     132.561  77.258 -13.886  1.00 29.95           C  
ANISOU 2742  CG  MET B 243     6358   2778   2244    505    526    101       C  
ATOM   2743  SD  MET B 243     131.748  76.076 -12.759  1.00 36.66           S  
ANISOU 2743  SD  MET B 243     7582   3529   2818    360    674     71       S  
ATOM   2744  CE  MET B 243     132.843  74.664 -12.900  1.00 34.25           C  
ANISOU 2744  CE  MET B 243     7486   2856   2672    612    787    273       C  
ATOM   2745  N   GLY B 244     134.635  76.548 -18.080  1.00 17.59           N  
ANISOU 2745  N   GLY B 244     3003   1453   2228    262    281    399       N  
ATOM   2746  CA  GLY B 244     134.884  75.822 -19.301  1.00 18.74           C  
ANISOU 2746  CA  GLY B 244     3059   1616   2445    143    479    340       C  
ATOM   2747  C   GLY B 244     134.601  76.597 -20.562  1.00 18.66           C  
ANISOU 2747  C   GLY B 244     3147   1396   2546    -66    625    225       C  
ATOM   2748  O   GLY B 244     134.910  76.108 -21.651  1.00 21.06           O  
ANISOU 2748  O   GLY B 244     3572   1723   2705   -155    680      2       O  
ATOM   2749  N   GLY B 245     134.016  77.786 -20.453  1.00 16.87           N  
ANISOU 2749  N   GLY B 245     2850   1090   2469     97    507    363       N  
ATOM   2750  CA  GLY B 245     133.910  78.692 -21.576  1.00 16.16           C  
ANISOU 2750  CA  GLY B 245     2806   1151   2182   -314    424    422       C  
ATOM   2751  C   GLY B 245     134.774  79.911 -21.342  1.00 15.25           C  
ANISOU 2751  C   GLY B 245     2638   1111   2045   -174    379    331       C  
ATOM   2752  O   GLY B 245     135.992  79.788 -21.169  1.00 17.19           O  
ANISOU 2752  O   GLY B 245     2846   1377   2308   -294    132    303       O  
ATOM   2753  N   MET B 246     134.159  81.092 -21.292  1.00 12.65           N  
ANISOU 2753  N   MET B 246     2240    859   1708   -122    208    293       N  
ATOM   2754  CA  MET B 246     134.949  82.296 -21.065  1.00 13.00           C  
ANISOU 2754  CA  MET B 246     2213   1078   1650     55    -84    299       C  
ATOM   2755  C   MET B 246     135.710  82.239 -19.751  1.00 13.80           C  
ANISOU 2755  C   MET B 246     2109   1318   1815    249     -1    401       C  
ATOM   2756  O   MET B 246     136.813  82.783 -19.659  1.00 14.90           O  
ANISOU 2756  O   MET B 246     1988   1554   2120    239    -48    304       O  
ATOM   2757  CB  MET B 246     134.085  83.543 -21.192  1.00 12.73           C  
ANISOU 2757  CB  MET B 246     2164   1237   1435    178    -99    313       C  
ATOM   2758  CG  MET B 246     133.698  83.785 -22.635  1.00 13.18           C  
ANISOU 2758  CG  MET B 246     2189   1327   1491     78   -274    263       C  
ATOM   2759  SD  MET B 246     132.755  85.288 -22.857  1.00 13.42           S  
ANISOU 2759  SD  MET B 246     2249   1271   1580   -281   -181    316       S  
ATOM   2760  CE  MET B 246     131.131  84.761 -22.298  1.00 12.64           C  
ANISOU 2760  CE  MET B 246     1877   1545   1379   -519    125    432       C  
ATOM   2761  N  AASN B 247     135.128  81.612 -18.726  0.44 13.75           N  
ANISOU 2761  N  AASN B 247     2046   1344   1835    191   -135    489       N  
ATOM   2762  N  BASN B 247     135.157  81.581 -18.734  0.56 13.81           N  
ANISOU 2762  N  BASN B 247     2136   1326   1786    111   -145    383       N  
ATOM   2763  CA AASN B 247     135.807  81.358 -17.452  0.44 15.49           C  
ANISOU 2763  CA AASN B 247     2202   1675   2008    247   -374    683       C  
ATOM   2764  CA BASN B 247     135.946  81.192 -17.567  0.56 15.93           C  
ANISOU 2764  CA BASN B 247     2380   1732   1941    147   -406    500       C  
ATOM   2765  C  AASN B 247     136.443  82.627 -16.886  0.44 16.50           C  
ANISOU 2765  C  AASN B 247     2396   1961   1912     60   -331    721       C  
ATOM   2766  C  BASN B 247     136.509  82.398 -16.822  0.56 16.49           C  
ANISOU 2766  C  BASN B 247     2448   2061   1757    220   -413    506       C  
ATOM   2767  O  AASN B 247     137.635  82.674 -16.572  0.44 17.08           O  
ANISOU 2767  O  AASN B 247     2543   1991   1954     -7   -277    785       O  
ATOM   2768  O  BASN B 247     137.609  82.332 -16.265  0.56 16.26           O  
ANISOU 2768  O  BASN B 247     2307   2123   1749    377   -445    605       O  
ATOM   2769  CB AASN B 247     136.821  80.220 -17.579  0.44 17.97           C  
ANISOU 2769  CB AASN B 247     2384   2111   2332    410   -526    817       C  
ATOM   2770  CB BASN B 247     137.075  80.238 -17.967  0.56 18.52           C  
ANISOU 2770  CB BASN B 247     2719   2006   2313    140   -501    628       C  
ATOM   2771  CG AASN B 247     137.374  79.772 -16.237  0.44 20.15           C  
ANISOU 2771  CG AASN B 247     2513   2622   2522    334   -530    880       C  
ATOM   2772  CG BASN B 247     137.282  79.137 -16.966  0.56 21.04           C  
ANISOU 2772  CG BASN B 247     3027   2322   2644    -67   -461    653       C  
ATOM   2773  OD1AASN B 247     136.776  80.019 -15.185  0.44 20.90           O  
ANISOU 2773  OD1AASN B 247     2491   2864   2586    314   -702   1062       O  
ATOM   2774  OD1BASN B 247     136.674  78.077 -17.076  0.56 21.17           O  
ANISOU 2774  OD1BASN B 247     3107   2085   2851   -255   -386    600       O  
ATOM   2775  ND2AASN B 247     138.524  79.104 -16.269  0.44 20.84           N  
ANISOU 2775  ND2AASN B 247     2540   2714   2664    346   -536    959       N  
ATOM   2776  ND2BASN B 247     138.136  79.381 -15.975  0.56 21.90           N  
ANISOU 2776  ND2BASN B 247     3028   2576   2716    -28   -478    623       N  
ATOM   2777  N  AARG B 248     135.627  83.675 -16.778  0.44 16.43           N  
ANISOU 2777  N  AARG B 248     2425   2039   1781     -8   -301    641       N  
ATOM   2778  N  BARG B 248     135.762  83.504 -16.830  0.56 16.04           N  
ANISOU 2778  N  BARG B 248     2562   1975   1559    137   -330    355       N  
ATOM   2779  CA AARG B 248     135.975  84.972 -16.202  0.44 16.93           C  
ANISOU 2779  CA AARG B 248     2525   2223   1684    -50   -469    409       C  
ATOM   2780  CA BARG B 248     136.113  84.763 -16.170  0.56 16.86           C  
ANISOU 2780  CA BARG B 248     2731   2206   1468    -26   -491    234       C  
ATOM   2781  C  AARG B 248     136.909  85.796 -17.080  0.44 15.94           C  
ANISOU 2781  C  AARG B 248     2384   1955   1718     70   -498    321       C  
ATOM   2782  C  BARG B 248     137.144  85.581 -16.937  0.56 16.54           C  
ANISOU 2782  C  BARG B 248     2645   2045   1597    -71   -501    249       C  
ATOM   2783  O  AARG B 248     137.201  86.952 -16.735  0.44 15.47           O  
ANISOU 2783  O  AARG B 248     2273   1842   1765    207   -509    263       O  
ATOM   2784  O  BARG B 248     137.731  86.519 -16.381  0.56 17.73           O  
ANISOU 2784  O  BARG B 248     2805   2311   1620   -385   -542    253       O  
ATOM   2785  CB AARG B 248     136.528  84.873 -14.771  0.44 18.72           C  
ANISOU 2785  CB AARG B 248     2755   2674   1686    -90   -447    496       C  
ATOM   2786  CB BARG B 248     136.516  84.598 -14.698  0.56 18.74           C  
ANISOU 2786  CB BARG B 248     2999   2725   1395    -31   -432    455       C  
ATOM   2787  CG AARG B 248     135.609  84.133 -13.816  0.44 21.05           C  
ANISOU 2787  CG AARG B 248     3127   3062   1809   -149   -415    469       C  
ATOM   2788  CG BARG B 248     135.487  83.849 -13.877  0.56 21.18           C  
ANISOU 2788  CG BARG B 248     3415   3152   1480    -36   -416    565       C  
ATOM   2789  CD AARG B 248     136.257  83.955 -12.453  0.44 23.02           C  
ANISOU 2789  CD AARG B 248     3406   3390   1951   -277   -458    407       C  
ATOM   2790  CD BARG B 248     135.793  83.923 -12.391  0.56 23.76           C  
ANISOU 2790  CD BARG B 248     3763   3617   1646    -52   -414    611       C  
ATOM   2791  NE AARG B 248     136.492  82.547 -12.146  0.44 25.61           N  
ANISOU 2791  NE AARG B 248     3768   3754   2209   -219   -365    300       N  
ATOM   2792  NE BARG B 248     134.770  83.216 -11.629  0.56 26.39           N  
ANISOU 2792  NE BARG B 248     4122   4016   1889    -18   -271    584       N  
ATOM   2793  CZ AARG B 248     137.657  81.929 -12.312  0.44 27.03           C  
ANISOU 2793  CZ AARG B 248     3976   3926   2370   -300   -200    271       C  
ATOM   2794  CZ BARG B 248     133.626  83.761 -11.231  0.56 28.04           C  
ANISOU 2794  CZ BARG B 248     4345   4258   2052     42   -103    459       C  
ATOM   2795  NH1AARG B 248     137.777  80.644 -12.005  0.44 27.20           N1+
ANISOU 2795  NH1AARG B 248     3990   3935   2411   -420   -250    251       N1+
ATOM   2796  NH1BARG B 248     132.748  83.035 -10.554  0.56 29.18           N1+
ANISOU 2796  NH1BARG B 248     4472   4406   2208     23    -31    397       N1+
ATOM   2797  NH2AARG B 248     138.705  82.595 -12.778  0.44 28.13           N  
ANISOU 2797  NH2AARG B 248     4189   4053   2444   -241    -78    291       N  
ATOM   2798  NH2BARG B 248     133.360  85.030 -11.507  0.56 28.74           N  
ANISOU 2798  NH2BARG B 248     4395   4375   2151     -2   -165    270       N  
ATOM   2799  N   ARG B 249     137.371  85.262 -18.206  1.00 15.27           N  
ANISOU 2799  N   ARG B 249     2407   1723   1671     63   -361    281       N  
ATOM   2800  CA  ARG B 249     138.325  85.994 -19.033  1.00 15.00           C  
ANISOU 2800  CA  ARG B 249     2364   1575   1760     49   -321    111       C  
ATOM   2801  C   ARG B 249     137.598  87.059 -19.839  1.00 14.36           C  
ANISOU 2801  C   ARG B 249     2194   1539   1722    -88   -443    -63       C  
ATOM   2802  O   ARG B 249     136.590  86.755 -20.485  1.00 14.92           O  
ANISOU 2802  O   ARG B 249     2363   1607   1697    -59   -403      4       O  
ATOM   2803  CB  ARG B 249     139.040  85.046 -19.977  1.00 15.32           C  
ANISOU 2803  CB  ARG B 249     2189   1817   1814    328   -291    190       C  
ATOM   2804  CG  ARG B 249     139.822  83.976 -19.258  1.00 16.43           C  
ANISOU 2804  CG  ARG B 249     2269   1986   1986    328   -115    189       C  
ATOM   2805  CD  ARG B 249     140.400  82.976 -20.226  1.00 18.10           C  
ANISOU 2805  CD  ARG B 249     2435   2186   2256    256   -129    201       C  
ATOM   2806  NE  ARG B 249     139.391  82.083 -20.780  1.00 16.94           N  
ANISOU 2806  NE  ARG B 249     2252   1873   2312    237   -192    572       N  
ATOM   2807  CZ  ARG B 249     139.673  81.120 -21.648  1.00 17.55           C  
ANISOU 2807  CZ  ARG B 249     2106   2198   2365    471   -214    603       C  
ATOM   2808  NH1 ARG B 249     140.925  80.945 -22.044  1.00 18.35           N1+
ANISOU 2808  NH1 ARG B 249     1996   2408   2569    638    -81    491       N1+
ATOM   2809  NH2 ARG B 249     138.717  80.331 -22.113  1.00 16.86           N  
ANISOU 2809  NH2 ARG B 249     1912   2193   2302    477   -317    695       N  
ATOM   2810  N   PRO B 250     138.065  88.306 -19.823  1.00 14.16           N  
ANISOU 2810  N   PRO B 250     2194   1516   1670   -175   -535   -162       N  
ATOM   2811  CA  PRO B 250     137.408  89.344 -20.623  1.00 14.14           C  
ANISOU 2811  CA  PRO B 250     2224   1568   1579     -3   -537   -112       C  
ATOM   2812  C   PRO B 250     137.532  89.063 -22.109  1.00 12.33           C  
ANISOU 2812  C   PRO B 250     1845   1334   1507    279   -276     29       C  
ATOM   2813  O   PRO B 250     138.537  88.526 -22.591  1.00 12.83           O  
ANISOU 2813  O   PRO B 250     1792   1423   1661    149   -217    205       O  
ATOM   2814  CB  PRO B 250     138.173  90.621 -20.256  1.00 16.64           C  
ANISOU 2814  CB  PRO B 250     2710   1849   1764   -295   -701    -89       C  
ATOM   2815  CG  PRO B 250     139.432  90.154 -19.610  1.00 19.72           C  
ANISOU 2815  CG  PRO B 250     3158   2138   2197   -353   -831     55       C  
ATOM   2816  CD  PRO B 250     139.101  88.860 -18.937  1.00 16.66           C  
ANISOU 2816  CD  PRO B 250     2636   1756   1939   -327   -720    -17       C  
ATOM   2817  N   ILE B 251     136.491  89.452 -22.837  1.00 10.49           N  
ANISOU 2817  N   ILE B 251     1590   1022   1375    -63   -371     75       N  
ATOM   2818  CA  ILE B 251     136.474  89.352 -24.288  1.00  9.32           C  
ANISOU 2818  CA  ILE B 251     1354    804   1385    -59   -333     13       C  
ATOM   2819  C   ILE B 251     136.260  90.727 -24.893  1.00  9.71           C  
ANISOU 2819  C   ILE B 251     1491    751   1446     36   -311   -142       C  
ATOM   2820  O   ILE B 251     135.790  91.670 -24.247  1.00 10.38           O  
ANISOU 2820  O   ILE B 251     1703    732   1508    113    -82   -118       O  
ATOM   2821  CB  ILE B 251     135.392  88.392 -24.817  1.00  9.78           C  
ANISOU 2821  CB  ILE B 251     1369    649   1700     88    -25    -63       C  
ATOM   2822  CG1 ILE B 251     134.003  88.868 -24.379  1.00 11.20           C  
ANISOU 2822  CG1 ILE B 251     1414   1161   1681     33     -1     14       C  
ATOM   2823  CG2 ILE B 251     135.663  86.958 -24.382  1.00 11.20           C  
ANISOU 2823  CG2 ILE B 251     1765    648   1844    105   -183    159       C  
ATOM   2824  CD1 ILE B 251     132.886  88.274 -25.214  1.00 13.09           C  
ANISOU 2824  CD1 ILE B 251     1814   1424   1736   -160    -45   -111       C  
ATOM   2825  N   LEU B 252     136.612  90.826 -26.164  1.00 10.67           N  
ANISOU 2825  N   LEU B 252     1802    895   1358    -59   -363    106       N  
ATOM   2826  CA  LEU B 252     136.244  91.945 -27.011  1.00 11.88           C  
ANISOU 2826  CA  LEU B 252     2075    927   1514   -275   -317    196       C  
ATOM   2827  C   LEU B 252     135.348  91.408 -28.111  1.00 10.98           C  
ANISOU 2827  C   LEU B 252     2002    827   1341    -11   -219   -173       C  
ATOM   2828  O   LEU B 252     135.543  90.284 -28.587  1.00 12.40           O  
ANISOU 2828  O   LEU B 252     2255    882   1574    365   -374   -216       O  
ATOM   2829  CB  LEU B 252     137.474  92.549 -27.703  1.00 16.51           C  
ANISOU 2829  CB  LEU B 252     2794   1465   2013   -859   -407    329       C  
ATOM   2830  CG  LEU B 252     138.678  92.876 -26.840  1.00 22.55           C  
ANISOU 2830  CG  LEU B 252     3520   2363   2685   -963     51    155       C  
ATOM   2831  CD1 LEU B 252     139.818  93.325 -27.723  1.00 24.54           C  
ANISOU 2831  CD1 LEU B 252     3536   2816   2971   -917    232    -47       C  
ATOM   2832  CD2 LEU B 252     138.297  93.956 -25.854  1.00 23.75           C  
ANISOU 2832  CD2 LEU B 252     3686   2429   2911   -663    182    -80       C  
ATOM   2833  N   THR B 253     134.374  92.215 -28.523  1.00  9.46           N  
ANISOU 2833  N   THR B 253     1574    746   1275    -76   -161   -170       N  
ATOM   2834  CA  THR B 253     133.667  91.980 -29.773  1.00  9.08           C  
ANISOU 2834  CA  THR B 253     1415    715   1319   -113     50    -30       C  
ATOM   2835  C   THR B 253     134.270  92.882 -30.834  1.00  8.95           C  
ANISOU 2835  C   THR B 253     1651    567   1183    -41     75    -75       C  
ATOM   2836  O   THR B 253     134.459  94.080 -30.597  1.00 10.40           O  
ANISOU 2836  O   THR B 253     1815    843   1294     -2    218   -207       O  
ATOM   2837  CB  THR B 253     132.178  92.268 -29.620  1.00  9.56           C  
ANISOU 2837  CB  THR B 253     1362    894   1374    -78    103     -8       C  
ATOM   2838  OG1 THR B 253     131.646  91.384 -28.634  1.00 10.80           O  
ANISOU 2838  OG1 THR B 253     1629   1016   1457   -223    195    180       O  
ATOM   2839  CG2 THR B 253     131.445  92.053 -30.941  1.00 10.41           C  
ANISOU 2839  CG2 THR B 253     1705    956   1295   -220    -44   -136       C  
ATOM   2840  N   ILE B 254     134.605  92.297 -31.979  1.00  9.00           N  
ANISOU 2840  N   ILE B 254     1485    780   1157    178      1     40       N  
ATOM   2841  CA  ILE B 254     135.112  93.032 -33.132  1.00  9.25           C  
ANISOU 2841  CA  ILE B 254     1428    898   1188    157     89     37       C  
ATOM   2842  C   ILE B 254     133.991  93.084 -34.149  1.00  9.05           C  
ANISOU 2842  C   ILE B 254     1612    716   1109     50    -54   -219       C  
ATOM   2843  O   ILE B 254     133.464  92.039 -34.549  1.00  9.42           O  
ANISOU 2843  O   ILE B 254     1743    592   1246   -150     54   -116       O  
ATOM   2844  CB  ILE B 254     136.343  92.350 -33.742  1.00  9.78           C  
ANISOU 2844  CB  ILE B 254     1375    999   1341     30    193    113       C  
ATOM   2845  CG1 ILE B 254     137.449  92.211 -32.701  1.00 11.67           C  
ANISOU 2845  CG1 ILE B 254     1471   1406   1556     88    196    117       C  
ATOM   2846  CG2 ILE B 254     136.849  93.138 -34.953  1.00 11.46           C  
ANISOU 2846  CG2 ILE B 254     1867   1023   1464     25    399    340       C  
ATOM   2847  CD1 ILE B 254     138.524  91.243 -33.117  1.00 12.98           C  
ANISOU 2847  CD1 ILE B 254     1693   1497   1743    324    500     13       C  
ATOM   2848  N   ILE B 255     133.594  94.289 -34.545  1.00  8.92           N  
ANISOU 2848  N   ILE B 255     1542    813   1036    132    -92     45       N  
ATOM   2849  CA  ILE B 255     132.574  94.468 -35.566  1.00  8.67           C  
ANISOU 2849  CA  ILE B 255     1486    692   1116     71     42    191       C  
ATOM   2850  C   ILE B 255     133.277  94.923 -36.823  1.00  8.68           C  
ANISOU 2850  C   ILE B 255     1654    493   1149    -71     -8    -52       C  
ATOM   2851  O   ILE B 255     133.966  95.951 -36.818  1.00  9.97           O  
ANISOU 2851  O   ILE B 255     1871    621   1297   -380     49    -20       O  
ATOM   2852  CB  ILE B 255     131.515  95.503 -35.160  1.00  9.06           C  
ANISOU 2852  CB  ILE B 255     1352    869   1223    136    -52    -54       C  
ATOM   2853  CG1 ILE B 255     130.900  95.174 -33.800  1.00 10.82           C  
ANISOU 2853  CG1 ILE B 255     1860    919   1332     39    -50     73       C  
ATOM   2854  CG2 ILE B 255     130.466  95.617 -36.256  1.00  9.95           C  
ANISOU 2854  CG2 ILE B 255     1433   1079   1269    -89   -186    -96       C  
ATOM   2855  CD1 ILE B 255     130.125  93.900 -33.767  1.00 12.13           C  
ANISOU 2855  CD1 ILE B 255     2014   1127   1468     31    -79    102       C  
ATOM   2856  N   THR B 256     133.096  94.181 -37.905  1.00  9.63           N  
ANISOU 2856  N   THR B 256     1883    690   1086    -59     18     74       N  
ATOM   2857  CA ATHR B 256     133.708  94.541 -39.170  0.59 10.39           C  
ANISOU 2857  CA ATHR B 256     1820    959   1168    -30    -48    138       C  
ATOM   2858  CA BTHR B 256     133.715  94.500 -39.182  0.41 10.20           C  
ANISOU 2858  CA BTHR B 256     1864    889   1123     27      3    186       C  
ATOM   2859  C   THR B 256     132.637  94.821 -40.205  1.00 10.15           C  
ANISOU 2859  C   THR B 256     1850    813   1193   -186   -105    106       C  
ATOM   2860  O   THR B 256     131.671  94.064 -40.346  1.00 11.51           O  
ANISOU 2860  O   THR B 256     1979    933   1460   -396   -222    126       O  
ATOM   2861  CB ATHR B 256     134.678  93.477 -39.678  0.59 11.14           C  
ANISOU 2861  CB ATHR B 256     1658   1319   1255   -143     -3   -155       C  
ATOM   2862  CB BTHR B 256     134.547  93.318 -39.679  0.41 10.80           C  
ANISOU 2862  CB BTHR B 256     1833   1162   1108    153    159    130       C  
ATOM   2863  OG1ATHR B 256     134.062  92.191 -39.598  0.59 11.11           O  
ANISOU 2863  OG1ATHR B 256     1531   1268   1421   -296    -48    -37       O  
ATOM   2864  OG1BTHR B 256     135.467  92.915 -38.658  0.41 12.22           O  
ANISOU 2864  OG1BTHR B 256     1970   1303   1371    162    149    226       O  
ATOM   2865  CG2ATHR B 256     135.962  93.497 -38.869  0.59 11.72           C  
ANISOU 2865  CG2ATHR B 256     1630   1510   1312   -143    -26   -222       C  
ATOM   2866  CG2BTHR B 256     135.321  93.708 -40.931  0.41  9.52           C  
ANISOU 2866  CG2BTHR B 256     1671   1006    938    209    231    166       C  
ATOM   2867  N   LEU B 257     132.818  95.920 -40.913  1.00 10.35           N  
ANISOU 2867  N   LEU B 257     1976    853   1105     30     32    327       N  
ATOM   2868  CA  LEU B 257     132.048  96.214 -42.106  1.00 11.00           C  
ANISOU 2868  CA  LEU B 257     2151    935   1094     -6    -11    232       C  
ATOM   2869  C   LEU B 257     132.822  95.595 -43.263  1.00 10.81           C  
ANISOU 2869  C   LEU B 257     2070    911   1126   -219     72    101       C  
ATOM   2870  O   LEU B 257     134.031  95.815 -43.388  1.00 12.33           O  
ANISOU 2870  O   LEU B 257     2190   1236   1260   -262     76     41       O  
ATOM   2871  CB  LEU B 257     131.971  97.730 -42.270  1.00 11.42           C  
ANISOU 2871  CB  LEU B 257     2182    876   1282   -163   -130    211       C  
ATOM   2872  CG  LEU B 257     130.977  98.237 -43.306  1.00 11.70           C  
ANISOU 2872  CG  LEU B 257     2124    952   1369   -209   -168    214       C  
ATOM   2873  CD1 LEU B 257     129.554  97.980 -42.819  1.00 12.89           C  
ANISOU 2873  CD1 LEU B 257     2160   1217   1521     12    -93    -96       C  
ATOM   2874  CD2 LEU B 257     131.206  99.712 -43.556  1.00 12.74           C  
ANISOU 2874  CD2 LEU B 257     2454    817   1570   -298   -237    221       C  
ATOM   2875  N   GLU B 258     132.141  94.788 -44.077  1.00 11.08           N  
ANISOU 2875  N   GLU B 258     2184   1024   1003      5    110   -168       N  
ATOM   2876  CA  GLU B 258     132.789  94.009 -45.122  1.00 11.64           C  
ANISOU 2876  CA  GLU B 258     2337   1009   1077    366    -57   -144       C  
ATOM   2877  C   GLU B 258     132.054  94.213 -46.431  1.00 11.44           C  
ANISOU 2877  C   GLU B 258     2172   1158   1019    100     55   -144       C  
ATOM   2878  O   GLU B 258     130.845  94.437 -46.442  1.00 12.38           O  
ANISOU 2878  O   GLU B 258     2308   1175   1220    -40     67     30       O  
ATOM   2879  CB  GLU B 258     132.670  92.510 -44.846  1.00 14.57           C  
ANISOU 2879  CB  GLU B 258     3005   1246   1285    644    -38    -12       C  
ATOM   2880  CG  GLU B 258     133.390  91.997 -43.640  1.00 17.33           C  
ANISOU 2880  CG  GLU B 258     3422   1495   1667    369     44    338       C  
ATOM   2881  CD  GLU B 258     133.188  90.500 -43.455  1.00 18.94           C  
ANISOU 2881  CD  GLU B 258     3759   1589   1848     77    277    286       C  
ATOM   2882  OE1 GLU B 258     132.294  89.903 -44.110  1.00 18.89           O  
ANISOU 2882  OE1 GLU B 258     3702   1648   1828    584    629    488       O  
ATOM   2883  OE2 GLU B 258     133.950  89.922 -42.672  1.00 21.69           O1-
ANISOU 2883  OE2 GLU B 258     4292   2078   1871   -533    338    342       O1-
ATOM   2884  N   ASP B 259     132.783  94.089 -47.540  1.00 10.96           N  
ANISOU 2884  N   ASP B 259     2117   1021   1028     51    125   -103       N  
ATOM   2885  CA  ASP B 259     132.100  94.061 -48.819  1.00 11.15           C  
ANISOU 2885  CA  ASP B 259     2165   1025   1045   -229     15     20       C  
ATOM   2886  C   ASP B 259     131.521  92.671 -49.064  1.00 11.52           C  
ANISOU 2886  C   ASP B 259     2229   1085   1063      7   -119   -110       C  
ATOM   2887  O   ASP B 259     131.622  91.773 -48.223  1.00 12.69           O  
ANISOU 2887  O   ASP B 259     2310   1315   1197    166    -43   -151       O  
ATOM   2888  CB  ASP B 259     132.986  94.588 -49.948  1.00 12.65           C  
ANISOU 2888  CB  ASP B 259     2218   1472   1116   -106    273    179       C  
ATOM   2889  CG  ASP B 259     134.179  93.695 -50.254  1.00 14.45           C  
ANISOU 2889  CG  ASP B 259     2552   1588   1350   -147    342    185       C  
ATOM   2890  OD1 ASP B 259     134.166  92.490 -49.919  1.00 14.55           O  
ANISOU 2890  OD1 ASP B 259     2629   1504   1394     59    239     89       O  
ATOM   2891  OD2 ASP B 259     135.141  94.216 -50.872  1.00 16.68           O1-
ANISOU 2891  OD2 ASP B 259     2754   1939   1644   -277    268    127       O1-
ATOM   2892  N   SER B 260     130.926  92.480 -50.242  1.00 10.80           N  
ANISOU 2892  N   SER B 260     2299    814    992   -242    -34    -64       N  
ATOM   2893  CA  SER B 260     130.222  91.230 -50.494  1.00 12.03           C  
ANISOU 2893  CA  SER B 260     2315   1084   1170    -17   -159     26       C  
ATOM   2894  C   SER B 260     131.164  90.040 -50.614  1.00 12.59           C  
ANISOU 2894  C   SER B 260     2385   1155   1244     84   -104    -12       C  
ATOM   2895  O   SER B 260     130.705  88.904 -50.491  1.00 13.22           O  
ANISOU 2895  O   SER B 260     2617    921   1484   -212    -55     19       O  
ATOM   2896  CB  SER B 260     129.345  91.357 -51.738  1.00 12.50           C  
ANISOU 2896  CB  SER B 260     2323   1396   1031     85   -206     98       C  
ATOM   2897  OG  SER B 260     130.117  91.669 -52.883  1.00 13.11           O  
ANISOU 2897  OG  SER B 260     2478   1473   1029   -161     39    217       O  
ATOM   2898  N   SER B 261     132.459  90.273 -50.843  1.00 12.75           N  
ANISOU 2898  N   SER B 261     2417   1251   1175    213    -14   -164       N  
ATOM   2899  CA  SER B 261     133.467  89.217 -50.825  1.00 13.00           C  
ANISOU 2899  CA  SER B 261     2392   1228   1319    187     84    -83       C  
ATOM   2900  C   SER B 261     134.035  88.948 -49.446  1.00 12.84           C  
ANISOU 2900  C   SER B 261     2348   1285   1246    188    124    -42       C  
ATOM   2901  O   SER B 261     134.830  88.013 -49.300  1.00 14.85           O  
ANISOU 2901  O   SER B 261     2608   1690   1345    266    119    -40       O  
ATOM   2902  CB  SER B 261     134.667  89.608 -51.687  1.00 14.40           C  
ANISOU 2902  CB  SER B 261     2499   1593   1380    272    271     32       C  
ATOM   2903  OG  SER B 261     134.334  89.680 -53.052  1.00 15.70           O  
ANISOU 2903  OG  SER B 261     2787   1875   1301    221    -37     66       O  
ATOM   2904  N   GLY B 262     133.676  89.746 -48.447  1.00 12.30           N  
ANISOU 2904  N   GLY B 262     2379   1124   1171    -47    -92   -126       N  
ATOM   2905  CA  GLY B 262     134.263  89.619 -47.130  1.00 12.71           C  
ANISOU 2905  CA  GLY B 262     2508   1132   1191   -119   -185     25       C  
ATOM   2906  C   GLY B 262     135.488  90.469 -46.898  1.00 13.04           C  
ANISOU 2906  C   GLY B 262     2475   1182   1296    160    -42     55       C  
ATOM   2907  O   GLY B 262     136.131  90.325 -45.853  1.00 15.61           O  
ANISOU 2907  O   GLY B 262     2817   1662   1453    113     16    241       O  
ATOM   2908  N   ASN B 263     135.843  91.340 -47.836  1.00 13.03           N  
ANISOU 2908  N   ASN B 263     2419   1125   1407    -65    196     52       N  
ATOM   2909  CA  ASN B 263     136.998  92.204 -47.654  1.00 14.19           C  
ANISOU 2909  CA  ASN B 263     2515   1429   1449   -229    301    -57       C  
ATOM   2910  C   ASN B 263     136.672  93.331 -46.685  1.00 12.52           C  
ANISOU 2910  C   ASN B 263     2101   1263   1395    -81    199   -122       C  
ATOM   2911  O   ASN B 263     135.543  93.826 -46.625  1.00 12.74           O  
ANISOU 2911  O   ASN B 263     2066   1417   1359     -7    157   -184       O  
ATOM   2912  CB  ASN B 263     137.414  92.837 -48.981  1.00 17.27           C  
ANISOU 2912  CB  ASN B 263     2934   1973   1656   -146    537   -139       C  
ATOM   2913  CG  ASN B 263     137.791  91.822 -50.024  1.00 22.36           C  
ANISOU 2913  CG  ASN B 263     3568   2606   2323     10    386   -242       C  
ATOM   2914  OD1 ASN B 263     138.569  90.907 -49.769  1.00 24.93           O  
ANISOU 2914  OD1 ASN B 263     3807   2841   2825    380    359   -406       O  
ATOM   2915  ND2 ASN B 263     137.237  91.979 -51.215  1.00 23.78           N  
ANISOU 2915  ND2 ASN B 263     3804   2935   2296   -144    257   -249       N  
ATOM   2916  N   LEU B 264     137.698  93.766 -45.964  1.00 13.60           N  
ANISOU 2916  N   LEU B 264     2281   1452   1435   -137    183   -213       N  
ATOM   2917  CA  LEU B 264     137.532  94.748 -44.904  1.00 13.20           C  
ANISOU 2917  CA  LEU B 264     2195   1385   1436     58    -31   -377       C  
ATOM   2918  C   LEU B 264     137.182  96.119 -45.467  1.00 12.88           C  
ANISOU 2918  C   LEU B 264     2252   1232   1411    -57    278   -180       C  
ATOM   2919  O   LEU B 264     137.897  96.654 -46.321  1.00 15.70           O  
ANISOU 2919  O   LEU B 264     2628   1654   1685    -89    424     21       O  
ATOM   2920  CB  LEU B 264     138.839  94.847 -44.122  1.00 15.39           C  
ANISOU 2920  CB  LEU B 264     2188   1985   1673    144    -72   -518       C  
ATOM   2921  CG  LEU B 264     138.919  95.988 -43.122  1.00 18.91           C  
ANISOU 2921  CG  LEU B 264     2656   2553   1975    271   -203   -635       C  
ATOM   2922  CD1 LEU B 264     138.037  95.657 -41.958  1.00 21.18           C  
ANISOU 2922  CD1 LEU B 264     2920   3082   2044    467   -101   -639       C  
ATOM   2923  CD2 LEU B 264     140.362  96.193 -42.670  1.00 19.31           C  
ANISOU 2923  CD2 LEU B 264     2682   2515   2138    155   -367   -568       C  
ATOM   2924  N   LEU B 265     136.099  96.706 -44.958  1.00 11.60           N  
ANISOU 2924  N   LEU B 265     2261    844   1301    -99    190   -157       N  
ATOM   2925  CA  LEU B 265     135.783  98.108 -45.208  1.00 12.06           C  
ANISOU 2925  CA  LEU B 265     2321    908   1354   -456    120    -79       C  
ATOM   2926  C   LEU B 265     135.921  98.982 -43.977  1.00 11.49           C  
ANISOU 2926  C   LEU B 265     2317    840   1209   -368    246    -51       C  
ATOM   2927  O   LEU B 265     136.192 100.173 -44.110  1.00 13.72           O  
ANISOU 2927  O   LEU B 265     2788    999   1425   -495    189   -109       O  
ATOM   2928  CB  LEU B 265     134.349  98.255 -45.726  1.00 13.13           C  
ANISOU 2928  CB  LEU B 265     2336   1297   1357   -311    132    -49       C  
ATOM   2929  CG  LEU B 265     134.054  97.495 -47.013  1.00 13.11           C  
ANISOU 2929  CG  LEU B 265     2228   1454   1299   -356    163    -19       C  
ATOM   2930  CD1 LEU B 265     132.578  97.625 -47.353  1.00 13.69           C  
ANISOU 2930  CD1 LEU B 265     2161   1635   1405   -215   -139     -4       C  
ATOM   2931  CD2 LEU B 265     134.945  97.995 -48.151  1.00 14.53           C  
ANISOU 2931  CD2 LEU B 265     2449   1698   1372   -279    466    135       C  
ATOM   2932  N   GLY B 266     135.704  98.427 -42.794  1.00 11.94           N  
ANISOU 2932  N   GLY B 266     2281   1244   1012   -342    215     33       N  
ATOM   2933  CA  GLY B 266     135.778  99.189 -41.563  1.00 11.59           C  
ANISOU 2933  CA  GLY B 266     2249   1147   1009   -161    117    -97       C  
ATOM   2934  C   GLY B 266     135.790  98.246 -40.386  1.00 10.13           C  
ANISOU 2934  C   GLY B 266     1806    971   1073   -282    192      0       C  
ATOM   2935  O   GLY B 266     135.353  97.098 -40.484  1.00 10.79           O  
ANISOU 2935  O   GLY B 266     2005    876   1218   -456    117    -66       O  
ATOM   2936  N   ARG B 267     136.306  98.737 -39.265  1.00  9.92           N  
ANISOU 2936  N   ARG B 267     1840    852   1079   -127    325    102       N  
ATOM   2937  CA  ARG B 267     136.418  97.885 -38.089  1.00  9.64           C  
ANISOU 2937  CA  ARG B 267     1884    534   1246     -8    215     74       C  
ATOM   2938  C   ARG B 267     136.306  98.726 -36.827  1.00 10.09           C  
ANISOU 2938  C   ARG B 267     1757    742   1333   -171    299    -33       C  
ATOM   2939  O   ARG B 267     136.833  99.838 -36.761  1.00 10.59           O  
ANISOU 2939  O   ARG B 267     1812    687   1527   -345    180     42       O  
ATOM   2940  CB  ARG B 267     137.756  97.124 -38.068  1.00 11.72           C  
ANISOU 2940  CB  ARG B 267     1890   1018   1542    292    258    203       C  
ATOM   2941  CG  ARG B 267     137.844  96.051 -36.988  1.00 13.22           C  
ANISOU 2941  CG  ARG B 267     2020   1163   1838    425    152    334       C  
ATOM   2942  CD  ARG B 267     139.253  95.455 -36.843  1.00 17.66           C  
ANISOU 2942  CD  ARG B 267     2849   1670   2192    948    -90    301       C  
ATOM   2943  NE  ARG B 267     139.758  94.791 -38.039  1.00 22.63           N  
ANISOU 2943  NE  ARG B 267     3591   2490   2518    796   -323    418       N  
ATOM   2944  CZ  ARG B 267     140.740  95.250 -38.812  1.00 23.06           C  
ANISOU 2944  CZ  ARG B 267     3551   2705   2506    764   -342     68       C  
ATOM   2945  NH1 ARG B 267     141.332  96.411 -38.551  1.00 22.88           N1+
ANISOU 2945  NH1 ARG B 267     3600   2644   2449    650   -408    253       N1+
ATOM   2946  NH2 ARG B 267     141.126  94.544 -39.863  1.00 24.54           N  
ANISOU 2946  NH2 ARG B 267     3650   2978   2698   1060   -403   -366       N  
ATOM   2947  N   ASP B 268     135.647  98.168 -35.819  1.00  9.78           N  
ANISOU 2947  N   ASP B 268     1539   1022   1156   -185     39    -97       N  
ATOM   2948  CA  ASP B 268     135.563  98.792 -34.506  1.00  9.82           C  
ANISOU 2948  CA  ASP B 268     1750    848   1133    -11     78    -24       C  
ATOM   2949  C   ASP B 268     135.430  97.655 -33.506  1.00  9.46           C  
ANISOU 2949  C   ASP B 268     1813    664   1116   -266    114     -7       C  
ATOM   2950  O   ASP B 268     135.233  96.499 -33.884  1.00 10.30           O  
ANISOU 2950  O   ASP B 268     1846    779   1287   -198    112   -116       O  
ATOM   2951  CB  ASP B 268     134.383  99.770 -34.465  1.00 10.00           C  
ANISOU 2951  CB  ASP B 268     1853    712   1234    129     45   -183       C  
ATOM   2952  CG  ASP B 268     134.511 100.843 -33.386  1.00 10.50           C  
ANISOU 2952  CG  ASP B 268     1975    815   1202   -187    -39     72       C  
ATOM   2953  OD1 ASP B 268     135.347 100.733 -32.455  1.00 12.15           O  
ANISOU 2953  OD1 ASP B 268     2118   1139   1361    -10    -27     68       O  
ATOM   2954  OD2 ASP B 268     133.713 101.799 -33.462  1.00 13.42           O1-
ANISOU 2954  OD2 ASP B 268     2474   1403   1223     63      2    -72       O1-
ATOM   2955  N   SER B 269     135.545  97.975 -32.223  1.00  9.80           N  
ANISOU 2955  N   SER B 269     1858    787   1080   -236    180    114       N  
ATOM   2956  CA  SER B 269     135.515  96.909 -31.233  1.00  9.77           C  
ANISOU 2956  CA  SER B 269     1792    712   1210   -105    199    -63       C  
ATOM   2957  C   SER B 269     135.160  97.482 -29.876  1.00  9.52           C  
ANISOU 2957  C   SER B 269     1952    559   1107   -143     56   -183       C  
ATOM   2958  O   SER B 269     135.272  98.688 -29.634  1.00 10.05           O  
ANISOU 2958  O   SER B 269     2053    563   1204   -118     40    -55       O  
ATOM   2959  CB  SER B 269     136.860  96.188 -31.143  1.00 11.46           C  
ANISOU 2959  CB  SER B 269     1883    853   1617    -42     84    -16       C  
ATOM   2960  OG  SER B 269     137.869  97.085 -30.725  1.00 13.60           O  
ANISOU 2960  OG  SER B 269     1876   1314   1980   -195     21    -85       O  
ATOM   2961  N   PHE B 270     134.739  96.588 -28.989  1.00  9.72           N  
ANISOU 2961  N   PHE B 270     1826    825   1041   -113     56   -149       N  
ATOM   2962  CA  PHE B 270     134.388  96.969 -27.631  1.00  9.39           C  
ANISOU 2962  CA  PHE B 270     1709    705   1152     27     25    -50       C  
ATOM   2963  C   PHE B 270     134.527  95.749 -26.741  1.00  9.66           C  
ANISOU 2963  C   PHE B 270     1647    771   1254    -16    -68    124       C  
ATOM   2964  O   PHE B 270     134.306  94.621 -27.182  1.00 10.17           O  
ANISOU 2964  O   PHE B 270     1790    749   1327     -1     13    -76       O  
ATOM   2965  CB  PHE B 270     132.965  97.536 -27.536  1.00 10.81           C  
ANISOU 2965  CB  PHE B 270     1809    770   1530      0   -115     12       C  
ATOM   2966  CG  PHE B 270     131.903  96.639 -28.112  1.00  9.26           C  
ANISOU 2966  CG  PHE B 270     1575    587   1355     19    -23    110       C  
ATOM   2967  CD1 PHE B 270     131.635  96.659 -29.474  1.00 10.26           C  
ANISOU 2967  CD1 PHE B 270     1817    827   1255    146    -69    -77       C  
ATOM   2968  CD2 PHE B 270     131.154  95.805 -27.298  1.00  9.89           C  
ANISOU 2968  CD2 PHE B 270     1621    652   1485      7    -57     63       C  
ATOM   2969  CE1 PHE B 270     130.657  95.861 -30.013  1.00  9.48           C  
ANISOU 2969  CE1 PHE B 270     1692    735   1176   -194      2    -82       C  
ATOM   2970  CE2 PHE B 270     130.164  94.985 -27.841  1.00 10.50           C  
ANISOU 2970  CE2 PHE B 270     1631    790   1567   -180    -38     14       C  
ATOM   2971  CZ  PHE B 270     129.918  95.009 -29.199  1.00 10.53           C  
ANISOU 2971  CZ  PHE B 270     1677    804   1521     37    -44    171       C  
ATOM   2972  N   GLU B 271     134.908  95.983 -25.488  1.00 10.21           N  
ANISOU 2972  N   GLU B 271     1611   1010   1256   -185   -112    193       N  
ATOM   2973  CA  GLU B 271     134.943  94.899 -24.519  1.00 10.43           C  
ANISOU 2973  CA  GLU B 271     1772    949   1240    -57    -74     28       C  
ATOM   2974  C   GLU B 271     133.516  94.551 -24.101  1.00 10.40           C  
ANISOU 2974  C   GLU B 271     1882    796   1272   -263    114    -95       C  
ATOM   2975  O   GLU B 271     132.613  95.381 -24.168  1.00 10.43           O  
ANISOU 2975  O   GLU B 271     1803    845   1316    -81     72     36       O  
ATOM   2976  CB  GLU B 271     135.770  95.328 -23.301  1.00 12.41           C  
ANISOU 2976  CB  GLU B 271     2415   1066   1236    144   -316     22       C  
ATOM   2977  CG  GLU B 271     136.012  94.221 -22.278  1.00 16.44           C  
ANISOU 2977  CG  GLU B 271     2920   1594   1731    124   -318    234       C  
ATOM   2978  CD  GLU B 271     136.955  94.619 -21.149  1.00 18.74           C  
ANISOU 2978  CD  GLU B 271     3230   1732   2160    150   -553    277       C  
ATOM   2979  OE1 GLU B 271     137.665  95.643 -21.290  1.00 21.08           O  
ANISOU 2979  OE1 GLU B 271     3049   2386   2575   -140   -698    108       O  
ATOM   2980  OE2 GLU B 271     136.997  93.889 -20.123  1.00 20.35           O1-
ANISOU 2980  OE2 GLU B 271     3615   1886   2231    538   -523    305       O1-
ATOM   2981  N   VAL B 272     133.300  93.299 -23.711  1.00 10.24           N  
ANISOU 2981  N   VAL B 272     1838    739   1314   -124    112   -275       N  
ATOM   2982  CA  VAL B 272     131.998  92.844 -23.248  1.00 10.49           C  
ANISOU 2982  CA  VAL B 272     1740    923   1322    -27   -147    -91       C  
ATOM   2983  C   VAL B 272     132.167  92.102 -21.935  1.00 11.28           C  
ANISOU 2983  C   VAL B 272     1747   1151   1389    -50     19    194       C  
ATOM   2984  O   VAL B 272     133.088  91.292 -21.783  1.00 13.54           O  
ANISOU 2984  O   VAL B 272     2128   1418   1598    267    248    283       O  
ATOM   2985  CB  VAL B 272     131.327  91.922 -24.286  1.00 11.81           C  
ANISOU 2985  CB  VAL B 272     1878   1279   1330   -328    -77    -30       C  
ATOM   2986  CG1 VAL B 272     129.973  91.432 -23.775  1.00 12.76           C  
ANISOU 2986  CG1 VAL B 272     1745   1754   1347   -555    158    167       C  
ATOM   2987  CG2 VAL B 272     131.159  92.651 -25.592  1.00 13.12           C  
ANISOU 2987  CG2 VAL B 272     2254   1449   1281   -237      9     84       C  
ATOM   2988  N   ARG B 273     131.284  92.379 -20.983  1.00  9.81           N  
ANISOU 2988  N   ARG B 273     1688    848   1193     59     -5    207       N  
ATOM   2989  CA  ARG B 273     131.104  91.520 -19.820  1.00 10.76           C  
ANISOU 2989  CA  ARG B 273     1983    972   1132    -48     -8    185       C  
ATOM   2990  C   ARG B 273     129.649  91.094 -19.805  1.00 10.60           C  
ANISOU 2990  C   ARG B 273     1856    842   1329    -40     95     63       C  
ATOM   2991  O   ARG B 273     128.756  91.947 -19.827  1.00 11.70           O  
ANISOU 2991  O   ARG B 273     1921    851   1673   -120    134    128       O  
ATOM   2992  CB  ARG B 273     131.435  92.254 -18.520  1.00 11.33           C  
ANISOU 2992  CB  ARG B 273     2195   1032   1076   -116    124    111       C  
ATOM   2993  CG  ARG B 273     131.013  91.490 -17.275  1.00 12.96           C  
ANISOU 2993  CG  ARG B 273     2626   1136   1163    -79     -3    -25       C  
ATOM   2994  CD  ARG B 273     131.471  92.226 -16.044  1.00 14.83           C  
ANISOU 2994  CD  ARG B 273     2920   1526   1189   -254     71    -34       C  
ATOM   2995  NE  ARG B 273     130.990  91.601 -14.816  1.00 19.05           N  
ANISOU 2995  NE  ARG B 273     3578   2182   1477   -222      8    243       N  
ATOM   2996  CZ  ARG B 273     131.512  90.501 -14.293  1.00 24.15           C  
ANISOU 2996  CZ  ARG B 273     4119   3148   1909     77     46    573       C  
ATOM   2997  NH1 ARG B 273     132.515  89.892 -14.910  1.00 26.36           N1+
ANISOU 2997  NH1 ARG B 273     4314   3482   2221    410    -25    545       N1+
ATOM   2998  NH2 ARG B 273     131.023  90.001 -13.162  1.00 26.09           N  
ANISOU 2998  NH2 ARG B 273     4399   3466   2048   -111   -105    972       N  
ATOM   2999  N   VAL B 274     129.409  89.784 -19.801  1.00 11.08           N  
ANISOU 2999  N   VAL B 274     2005    817   1390   -408    -51    170       N  
ATOM   3000  CA  VAL B 274     128.064  89.239 -19.673  1.00 11.50           C  
ANISOU 3000  CA  VAL B 274     2156    808   1405   -385    -20     93       C  
ATOM   3001  C   VAL B 274     127.888  88.843 -18.218  1.00 12.71           C  
ANISOU 3001  C   VAL B 274     2345    992   1493    -83    214    107       C  
ATOM   3002  O   VAL B 274     128.642  88.010 -17.699  1.00 13.46           O  
ANISOU 3002  O   VAL B 274     2348    951   1817     -9    186    -68       O  
ATOM   3003  CB  VAL B 274     127.854  88.032 -20.599  1.00 10.41           C  
ANISOU 3003  CB  VAL B 274     1755    732   1467   -373     81    -77       C  
ATOM   3004  CG1 VAL B 274     126.385  87.634 -20.614  1.00 12.33           C  
ANISOU 3004  CG1 VAL B 274     1931   1063   1689   -214    -10    -17       C  
ATOM   3005  CG2 VAL B 274     128.354  88.348 -22.004  1.00 12.42           C  
ANISOU 3005  CG2 VAL B 274     2000   1178   1543   -345    255    -11       C  
ATOM   3006  N   CYS B 275     126.914  89.449 -17.548  1.00 12.92           N  
ANISOU 3006  N   CYS B 275     2370   1194   1344   -232    392      4       N  
ATOM   3007  CA  CYS B 275     126.835  89.327 -16.102  1.00 14.19           C  
ANISOU 3007  CA  CYS B 275     2649   1342   1402   -228    324     45       C  
ATOM   3008  C   CYS B 275     125.395  89.507 -15.652  1.00 14.55           C  
ANISOU 3008  C   CYS B 275     2715   1423   1390   -201    482    124       C  
ATOM   3009  O   CYS B 275     124.537  89.968 -16.405  1.00 16.17           O  
ANISOU 3009  O   CYS B 275     2794   1817   1531    -94    355     19       O  
ATOM   3010  CB  CYS B 275     127.755  90.348 -15.428  1.00 15.75           C  
ANISOU 3010  CB  CYS B 275     2939   1444   1603   -409    169      8       C  
ATOM   3011  SG  CYS B 275     127.431  92.070 -15.903  1.00 17.34           S  
ANISOU 3011  SG  CYS B 275     3230   1502   1857   -146    196   -136       S  
ATOM   3012  N   ALA B 276     125.142  89.145 -14.392  1.00 16.05           N  
ANISOU 3012  N   ALA B 276     2931   1700   1468   -286    951     20       N  
ATOM   3013  CA  ALA B 276     123.777  89.186 -13.880  1.00 17.44           C  
ANISOU 3013  CA  ALA B 276     3140   1763   1721   -291    916    225       C  
ATOM   3014  C   ALA B 276     123.281  90.611 -13.657  1.00 18.09           C  
ANISOU 3014  C   ALA B 276     3287   1799   1788   -430    686     23       C  
ATOM   3015  O   ALA B 276     122.091  90.882 -13.856  1.00 20.00           O  
ANISOU 3015  O   ALA B 276     3483   2034   2084   -440    626    -20       O  
ATOM   3016  CB  ALA B 276     123.680  88.385 -12.582  1.00 19.63           C  
ANISOU 3016  CB  ALA B 276     3421   2141   1897   -265    990    417       C  
ATOM   3017  N   CYS B 277     124.159  91.534 -13.258  1.00 18.05           N  
ANISOU 3017  N   CYS B 277     3389   1879   1589   -532    598    -92       N  
ATOM   3018  CA ACYS B 277     123.779  92.903 -12.907  0.36 18.50           C  
ANISOU 3018  CA ACYS B 277     3501   1928   1598   -449    603    -28       C  
ATOM   3019  CA BCYS B 277     123.764  92.904 -12.930  0.64 18.55           C  
ANISOU 3019  CA BCYS B 277     3489   1882   1677   -288    603     15       C  
ATOM   3020  C   CYS B 277     124.676  93.889 -13.646  1.00 17.16           C  
ANISOU 3020  C   CYS B 277     3219   1714   1586   -416    505    -99       C  
ATOM   3021  O   CYS B 277     125.590  94.477 -13.048  1.00 17.49           O  
ANISOU 3021  O   CYS B 277     3361   1797   1486   -328    322    -96       O  
ATOM   3022  CB ACYS B 277     123.897  93.128 -11.398  0.36 20.32           C  
ANISOU 3022  CB ACYS B 277     3857   2220   1643   -569    658    -27       C  
ATOM   3023  CB BCYS B 277     123.738  93.154 -11.424  0.64 20.57           C  
ANISOU 3023  CB BCYS B 277     3780   2138   1900   -171    666     20       C  
ATOM   3024  SG ACYS B 277     123.080  91.895 -10.360  0.36 21.89           S  
ANISOU 3024  SG ACYS B 277     4212   2459   1645   -732    746   -110       S  
ATOM   3025  SG BCYS B 277     122.836  94.665 -11.019  0.64 21.77           S  
ANISOU 3025  SG BCYS B 277     3984   2259   2027     -4    806    -71       S  
ATOM   3026  N   PRO B 278     124.431  94.113 -14.937  1.00 15.49           N  
ANISOU 3026  N   PRO B 278     2965   1412   1508   -338    440   -153       N  
ATOM   3027  CA  PRO B 278     125.277  95.046 -15.703  1.00 15.11           C  
ANISOU 3027  CA  PRO B 278     2802   1393   1544   -640    424   -151       C  
ATOM   3028  C   PRO B 278     125.354  96.440 -15.117  1.00 15.76           C  
ANISOU 3028  C   PRO B 278     2941   1419   1627   -279    385    -77       C  
ATOM   3029  O   PRO B 278     126.412  97.072 -15.195  1.00 15.97           O  
ANISOU 3029  O   PRO B 278     2835   1524   1711     25    387    -12       O  
ATOM   3030  CB  PRO B 278     124.600  95.083 -17.077  1.00 16.56           C  
ANISOU 3030  CB  PRO B 278     3008   1765   1518   -462    220   -252       C  
ATOM   3031  CG  PRO B 278     123.806  93.868 -17.160  1.00 16.93           C  
ANISOU 3031  CG  PRO B 278     3103   1697   1632   -495    290    -10       C  
ATOM   3032  CD  PRO B 278     123.443  93.425 -15.782  1.00 15.79           C  
ANISOU 3032  CD  PRO B 278     2941   1491   1567   -370    300   -274       C  
ATOM   3033  N   GLY B 279     124.246  96.957 -14.581  1.00 15.99           N  
ANISOU 3033  N   GLY B 279     3095   1399   1580   -219    436   -116       N  
ATOM   3034  CA  GLY B 279     124.264  98.304 -14.037  1.00 16.99           C  
ANISOU 3034  CA  GLY B 279     3283   1573   1600   -231    456   -136       C  
ATOM   3035  C   GLY B 279     125.221  98.432 -12.871  1.00 16.37           C  
ANISOU 3035  C   GLY B 279     3297   1319   1603   -306    471   -159       C  
ATOM   3036  O   GLY B 279     126.040  99.356 -12.817  1.00 17.03           O  
ANISOU 3036  O   GLY B 279     3512   1277   1682   -256    412   -153       O  
ATOM   3037  N   ARG B 280     125.141  97.490 -11.932  1.00 18.13           N  
ANISOU 3037  N   ARG B 280     3548   1791   1550    -93    526    -88       N  
ATOM   3038  CA  ARG B 280     126.046  97.503 -10.793  1.00 19.19           C  
ANISOU 3038  CA  ARG B 280     3925   1698   1668   -186    390   -122       C  
ATOM   3039  C   ARG B 280     127.484  97.274 -11.232  1.00 19.09           C  
ANISOU 3039  C   ARG B 280     4084   1585   1585   -300    274   -191       C  
ATOM   3040  O   ARG B 280     128.402  97.940 -10.743  1.00 20.12           O  
ANISOU 3040  O   ARG B 280     4283   1567   1794   -666    106   -137       O  
ATOM   3041  CB  ARG B 280     125.624  96.447  -9.775  1.00 20.70           C  
ANISOU 3041  CB  ARG B 280     4033   1970   1861   -503    380     13       C  
ATOM   3042  CG  ARG B 280     126.549  96.363  -8.582  1.00 23.09           C  
ANISOU 3042  CG  ARG B 280     4312   2441   2021   -532    217    120       C  
ATOM   3043  N   ASP B 281     127.705  96.341 -12.161  1.00 18.70           N  
ANISOU 3043  N   ASP B 281     4109   1561   1436    -90    103    -38       N  
ATOM   3044  CA  ASP B 281     129.073  96.056 -12.573  1.00 18.35           C  
ANISOU 3044  CA  ASP B 281     4127   1383   1461    -35     -3     83       C  
ATOM   3045  C   ASP B 281     129.685  97.221 -13.338  1.00 17.77           C  
ANISOU 3045  C   ASP B 281     3796   1510   1447   -221   -130     95       C  
ATOM   3046  O   ASP B 281     130.872  97.519 -13.168  1.00 17.55           O  
ANISOU 3046  O   ASP B 281     3601   1628   1437   -550   -217    -11       O  
ATOM   3047  CB  ASP B 281     129.133  94.762 -13.378  1.00 19.60           C  
ANISOU 3047  CB  ASP B 281     4497   1401   1549     10     55    191       C  
ATOM   3048  CG  ASP B 281     128.922  93.538 -12.507  1.00 22.77           C  
ANISOU 3048  CG  ASP B 281     5076   1877   1700     77    197    244       C  
ATOM   3049  OD1 ASP B 281     128.809  93.689 -11.266  1.00 24.55           O  
ANISOU 3049  OD1 ASP B 281     5218   2291   1818    247    296    400       O  
ATOM   3050  OD2 ASP B 281     128.887  92.427 -13.061  1.00 23.68           O1-
ANISOU 3050  OD2 ASP B 281     5179   1979   1840    -33    247     35       O1-
ATOM   3051  N   ARG B 282     128.897  97.896 -14.179  1.00 16.69           N  
ANISOU 3051  N   ARG B 282     3604   1344   1392    -70     17    142       N  
ATOM   3052  CA  ARG B 282     129.410  99.092 -14.836  1.00 16.51           C  
ANISOU 3052  CA  ARG B 282     3423   1366   1485   -246   -104     -5       C  
ATOM   3053  C   ARG B 282     129.786 100.150 -13.807  1.00 17.07           C  
ANISOU 3053  C   ARG B 282     3519   1461   1505   -442    -96    -83       C  
ATOM   3054  O   ARG B 282     130.861 100.756 -13.886  1.00 18.07           O  
ANISOU 3054  O   ARG B 282     3501   1774   1592   -609   -189     43       O  
ATOM   3055  CB  ARG B 282     128.396  99.647 -15.833  1.00 15.70           C  
ANISOU 3055  CB  ARG B 282     3347   1029   1591   -290     29     64       C  
ATOM   3056  CG  ARG B 282     128.849 100.996 -16.380  1.00 14.03           C  
ANISOU 3056  CG  ARG B 282     2971    818   1543   -308    -22    131       C  
ATOM   3057  CD  ARG B 282     127.989 101.505 -17.512  1.00 13.09           C  
ANISOU 3057  CD  ARG B 282     2719    793   1461   -201     10    261       C  
ATOM   3058  NE  ARG B 282     128.384 102.872 -17.826  1.00 13.58           N  
ANISOU 3058  NE  ARG B 282     2745    941   1473     50     34     71       N  
ATOM   3059  CZ  ARG B 282     127.600 103.769 -18.408  1.00 13.51           C  
ANISOU 3059  CZ  ARG B 282     2717   1067   1350    -99    207     95       C  
ATOM   3060  NH1 ARG B 282     126.371 103.440 -18.791  1.00 14.01           N1+
ANISOU 3060  NH1 ARG B 282     2687   1406   1229    -86    183   -237       N1+
ATOM   3061  NH2 ARG B 282     128.057 104.995 -18.616  1.00 15.13           N  
ANISOU 3061  NH2 ARG B 282     2876   1208   1665   -493    197     -7       N  
ATOM   3062  N   ARG B 283     128.916 100.376 -12.821  1.00 18.35           N  
ANISOU 3062  N   ARG B 283     3831   1656   1486   -474   -156   -293       N  
ATOM   3063  CA  ARG B 283     129.231 101.362 -11.790  1.00 20.90           C  
ANISOU 3063  CA  ARG B 283     4268   1891   1782   -416    -25   -388       C  
ATOM   3064  C   ARG B 283     130.496 100.984 -11.033  1.00 22.03           C  
ANISOU 3064  C   ARG B 283     4308   2304   1756   -736   -224   -303       C  
ATOM   3065  O   ARG B 283     131.348 101.841 -10.764  1.00 23.23           O  
ANISOU 3065  O   ARG B 283     4370   2658   1798  -1071   -146   -165       O  
ATOM   3066  CB  ARG B 283     128.057 101.513 -10.824  1.00 23.48           C  
ANISOU 3066  CB  ARG B 283     4707   2220   1993    -13    277   -441       C  
ATOM   3067  CG  ARG B 283     126.996 102.459 -11.319  1.00 26.30           C  
ANISOU 3067  CG  ARG B 283     5054   2521   2415    137    379   -351       C  
ATOM   3068  CD  ARG B 283     125.884 102.651 -10.302  1.00 29.63           C  
ANISOU 3068  CD  ARG B 283     5460   2959   2838    208    482   -347       C  
ATOM   3069  NE  ARG B 283     124.849 101.629 -10.431  1.00 32.32           N  
ANISOU 3069  NE  ARG B 283     5928   3255   3098    273    531   -403       N  
ATOM   3070  CZ  ARG B 283     124.573 100.710  -9.509  1.00 34.07           C  
ANISOU 3070  CZ  ARG B 283     6213   3489   3242    459    562   -434       C  
ATOM   3071  NH1 ARG B 283     125.252 100.672  -8.367  1.00 35.37           N1+
ANISOU 3071  NH1 ARG B 283     6315   3771   3351    453    532   -554       N1+
ATOM   3072  NH2 ARG B 283     123.605  99.831  -9.732  1.00 34.25           N  
ANISOU 3072  NH2 ARG B 283     6250   3464   3298    601    548   -433       N  
ATOM   3073  N   THR B 284     130.644  99.704 -10.694  1.00 23.42           N  
ANISOU 3073  N   THR B 284     4362   2704   1833   -548   -469    -58       N  
ATOM   3074  CA  THR B 284     131.815  99.266  -9.941  1.00 23.58           C  
ANISOU 3074  CA  THR B 284     4206   2809   1946   -733   -722    330       C  
ATOM   3075  C   THR B 284     133.088  99.440 -10.757  1.00 22.54           C  
ANISOU 3075  C   THR B 284     4039   2578   1945   -969  -1008    414       C  
ATOM   3076  O   THR B 284     134.091  99.971 -10.262  1.00 24.25           O  
ANISOU 3076  O   THR B 284     4291   2808   2113  -1191  -1009    479       O  
ATOM   3077  CB  THR B 284     131.641  97.807  -9.521  1.00 24.74           C  
ANISOU 3077  CB  THR B 284     4240   3148   2015   -619   -513    685       C  
ATOM   3078  OG1 THR B 284     130.476  97.686  -8.697  1.00 26.28           O  
ANISOU 3078  OG1 THR B 284     4352   3510   2122   -635   -200    733       O  
ATOM   3079  CG2 THR B 284     132.862  97.322  -8.748  1.00 25.75           C  
ANISOU 3079  CG2 THR B 284     4305   3317   2162   -706   -650    755       C  
ATOM   3080  N   GLU B 285     133.062  99.019 -12.024  1.00 21.53           N  
ANISOU 3080  N   GLU B 285     3926   2328   1925   -820   -957    473       N  
ATOM   3081  CA  GLU B 285     134.267  99.120 -12.837  1.00 21.68           C  
ANISOU 3081  CA  GLU B 285     3882   2188   2168   -762  -1032    540       C  
ATOM   3082  C   GLU B 285     134.609 100.566 -13.162  1.00 22.62           C  
ANISOU 3082  C   GLU B 285     4052   2228   2316   -848  -1120    255       C  
ATOM   3083  O   GLU B 285     135.792 100.913 -13.247  1.00 23.08           O  
ANISOU 3083  O   GLU B 285     3869   2451   2448  -1069  -1208    380       O  
ATOM   3084  CB  GLU B 285     134.150  98.258 -14.093  1.00 22.08           C  
ANISOU 3084  CB  GLU B 285     3973   2163   2253   -422   -989    732       C  
ATOM   3085  CG  GLU B 285     134.051  96.779 -13.765  1.00 22.87           C  
ANISOU 3085  CG  GLU B 285     4102   2248   2337   -281   -909    687       C  
ATOM   3086  CD  GLU B 285     134.238  95.884 -14.968  1.00 23.48           C  
ANISOU 3086  CD  GLU B 285     4146   2368   2406   -213   -832    526       C  
ATOM   3087  OE1 GLU B 285     134.823  96.343 -15.971  1.00 23.49           O  
ANISOU 3087  OE1 GLU B 285     4041   2516   2369   -114   -875    494       O  
ATOM   3088  OE2 GLU B 285     133.804  94.713 -14.904  1.00 23.97           O1-
ANISOU 3088  OE2 GLU B 285     4225   2400   2482   -234   -801    271       O1-
ATOM   3089  N   GLU B 286     133.599 101.423 -13.325  1.00 21.86           N  
ANISOU 3089  N   GLU B 286     4037   2021   2248   -807  -1167    -17       N  
ATOM   3090  CA  GLU B 286     133.880 102.839 -13.547  1.00 22.44           C  
ANISOU 3090  CA  GLU B 286     4229   2020   2277  -1079  -1129    -49       C  
ATOM   3091  C   GLU B 286     134.432 103.501 -12.292  1.00 26.48           C  
ANISOU 3091  C   GLU B 286     4847   2695   2519  -1397  -1291    -51       C  
ATOM   3092  O   GLU B 286     135.320 104.356 -12.378  1.00 27.57           O  
ANISOU 3092  O   GLU B 286     5103   2781   2592  -1309  -1299   -219       O  
ATOM   3093  CB  GLU B 286     132.638 103.560 -14.060  1.00 20.35           C  
ANISOU 3093  CB  GLU B 286     3969   1665   2099   -815   -892   -167       C  
ATOM   3094  CG  GLU B 286     132.350 103.242 -15.512  1.00 19.66           C  
ANISOU 3094  CG  GLU B 286     3746   1734   1988   -344   -734   -285       C  
ATOM   3095  CD  GLU B 286     131.294 104.133 -16.108  1.00 18.99           C  
ANISOU 3095  CD  GLU B 286     3597   1613   2003   -230   -278   -464       C  
ATOM   3096  OE1 GLU B 286     130.814 105.034 -15.395  1.00 22.22           O  
ANISOU 3096  OE1 GLU B 286     3842   2318   2284    417    -87   -641       O  
ATOM   3097  OE2 GLU B 286     130.951 103.932 -17.295  1.00 17.00           O1-
ANISOU 3097  OE2 GLU B 286     3319   1399   1742   -284    -74   -476       O1-
ATOM   3098  N   GLU B 287     133.923 103.115 -11.118  1.00 30.24           N  
ANISOU 3098  N   GLU B 287     5308   3401   2783  -1648  -1440    -89       N  
ATOM   3099  CA  GLU B 287     134.489 103.623  -9.873  1.00 34.22           C  
ANISOU 3099  CA  GLU B 287     5934   4099   2969  -1878  -1611     40       C  
ATOM   3100  C   GLU B 287     135.915 103.127  -9.684  1.00 35.03           C  
ANISOU 3100  C   GLU B 287     5839   4338   3133  -2060  -1821    400       C  
ATOM   3101  O   GLU B 287     136.779 103.869  -9.202  1.00 36.41           O  
ANISOU 3101  O   GLU B 287     5813   4694   3327  -2072  -1932    417       O  
ATOM   3102  CB  GLU B 287     133.610 103.243  -8.677  1.00 37.53           C  
ANISOU 3102  CB  GLU B 287     6483   4640   3134  -1752  -1719   -139       C  
ATOM   3103  CG  GLU B 287     134.207 103.577  -7.304  1.00 40.80           C  
ANISOU 3103  CG  GLU B 287     7047   5110   3347  -1587  -1746   -218       C  
ATOM   3104  CD  GLU B 287     134.301 105.084  -7.045  1.00 44.22           C  
ANISOU 3104  CD  GLU B 287     7488   5662   3651  -1396  -1662   -235       C  
ATOM   3105  OE1 GLU B 287     133.755 105.884  -7.827  1.00 45.87           O  
ANISOU 3105  OE1 GLU B 287     7738   5897   3794  -1346  -1524   -206       O  
ATOM   3106  OE2 GLU B 287     134.929 105.463  -6.044  1.00 45.71           O1-
ANISOU 3106  OE2 GLU B 287     7671   5859   3838  -1382  -1557   -351       O1-
ATOM   3107  N   ASN B 288     136.184 101.868 -10.047  1.00 35.51           N  
ANISOU 3107  N   ASN B 288     5790   4421   3281  -2133  -1909    708       N  
ATOM   3108  CA  ASN B 288     137.554 101.366  -9.990  1.00 36.89           C  
ANISOU 3108  CA  ASN B 288     5844   4566   3607  -2100  -1816    906       C  
ATOM   3109  C   ASN B 288     138.470 102.190 -10.882  1.00 37.13           C  
ANISOU 3109  C   ASN B 288     5798   4538   3773  -2245  -1812    911       C  
ATOM   3110  O   ASN B 288     139.595 102.523 -10.492  1.00 37.45           O  
ANISOU 3110  O   ASN B 288     5907   4519   3803  -2389  -1858    983       O  
ATOM   3111  CB  ASN B 288     137.602  99.891 -10.398  1.00 38.37           C  
ANISOU 3111  CB  ASN B 288     6027   4749   3801  -1923  -1750   1112       C  
ATOM   3112  CG  ASN B 288     136.991  98.970  -9.360  1.00 39.81           C  
ANISOU 3112  CG  ASN B 288     6170   4970   3988  -1704  -1729   1245       C  
ATOM   3113  OD1 ASN B 288     136.784  99.357  -8.211  1.00 40.15           O  
ANISOU 3113  OD1 ASN B 288     6260   5074   3921  -1585  -1754   1539       O  
ATOM   3114  ND2 ASN B 288     136.716  97.732  -9.759  1.00 40.75           N  
ANISOU 3114  ND2 ASN B 288     6297   5032   4153  -1575  -1603   1316       N  
ATOM   3115  N   LEU B 289     138.003 102.531 -12.085  1.00 36.89           N  
ANISOU 3115  N   LEU B 289     5674   4470   3871  -2186  -1770    832       N  
ATOM   3116  CA  LEU B 289     138.811 103.327 -13.002  1.00 37.39           C  
ANISOU 3116  CA  LEU B 289     5648   4463   4096  -2200  -1560    682       C  
ATOM   3117  C   LEU B 289     139.124 104.696 -12.410  1.00 38.92           C  
ANISOU 3117  C   LEU B 289     5850   4671   4265  -2285  -1436    693       C  
ATOM   3118  O   LEU B 289     140.241 105.207 -12.560  1.00 39.07           O  
ANISOU 3118  O   LEU B 289     5785   4762   4298  -2293  -1272    857       O  
ATOM   3119  CB  LEU B 289     138.089 103.457 -14.344  1.00 36.53           C  
ANISOU 3119  CB  LEU B 289     5466   4270   4144  -2140  -1395    570       C  
ATOM   3120  CG  LEU B 289     138.782 104.235 -15.464  1.00 36.20           C  
ANISOU 3120  CG  LEU B 289     5475   4145   4136  -2000  -1215    535       C  
ATOM   3121  CD1 LEU B 289     140.156 103.651 -15.772  1.00 36.36           C  
ANISOU 3121  CD1 LEU B 289     5533   4128   4155  -1938  -1119    556       C  
ATOM   3122  CD2 LEU B 289     137.910 104.264 -16.709  1.00 35.33           C  
ANISOU 3122  CD2 LEU B 289     5366   3989   4070  -2066  -1166    530       C  
ATOM   3123  N   ARG B 290     138.154 105.300 -11.718  1.00 40.31           N  
ANISOU 3123  N   ARG B 290     6120   4806   4391  -2332  -1456    617       N  
ATOM   3124  CA  ARG B 290     138.403 106.583 -11.066  1.00 42.48           C  
ANISOU 3124  CA  ARG B 290     6548   5034   4557  -2150  -1400    581       C  
ATOM   3125  C   ARG B 290     139.434 106.444  -9.952  1.00 43.35           C  
ANISOU 3125  C   ARG B 290     6767   5099   4606  -2181  -1532    560       C  
ATOM   3126  O   ARG B 290     140.299 107.312  -9.784  1.00 43.96           O  
ANISOU 3126  O   ARG B 290     6930   5085   4687  -2285  -1419    524       O  
ATOM   3127  CB  ARG B 290     137.095 107.157 -10.522  1.00 43.25           C  
ANISOU 3127  CB  ARG B 290     6646   5155   4631  -1980  -1271    620       C  
ATOM   3128  N   LYS B 291     139.365 105.358  -9.189  1.00 43.38           N  
ANISOU 3128  N   LYS B 291     6734   5136   4610  -2127  -1692    604       N  
ATOM   3129  CA  LYS B 291     140.277 105.142  -8.070  1.00 43.64           C  
ANISOU 3129  CA  LYS B 291     6684   5275   4624  -1875  -1855    777       C  
ATOM   3130  C   LYS B 291     141.564 104.446  -8.511  1.00 43.85           C  
ANISOU 3130  C   LYS B 291     6634   5344   4684  -1767  -1817   1010       C  
ATOM   3131  O   LYS B 291     142.032 104.626  -9.635  1.00 43.93           O  
ANISOU 3131  O   LYS B 291     6598   5360   4734  -1808  -1758   1191       O  
ATOM   3132  CB  LYS B 291     139.588 104.324  -6.975  1.00 43.61           C  
ANISOU 3132  CB  LYS B 291     6682   5275   4613  -1818  -1945    744       C  
TER    3133      LYS B 291                                                      
HETATM 3134 ZN    ZN A 401      96.161  69.680 -20.456  1.00 13.56          ZN  
ANISOU 3134 ZN    ZN A 401     2451    937   1762   -117    201     87      ZN  
HETATM 3135  C1  EDO A 402     106.712  88.261 -27.872  1.00 26.63           C  
ANISOU 3135  C1  EDO A 402     3095   4385   2640    943   -849  -1260       C  
HETATM 3136  O1  EDO A 402     105.940  89.003 -28.823  1.00 26.05           O  
ANISOU 3136  O1  EDO A 402     3155   4225   2519    796   -854  -1148       O  
HETATM 3137  C2  EDO A 402     107.479  89.245 -26.999  1.00 27.13           C  
ANISOU 3137  C2  EDO A 402     3006   4590   2712    805   -733  -1228       C  
HETATM 3138  O2  EDO A 402     106.563  90.071 -26.271  1.00 26.09           O  
ANISOU 3138  O2  EDO A 402     2792   4529   2592    955   -450  -1065       O  
HETATM 3139  C1  GOL A 403     101.055  64.820 -33.522  1.00 24.84           C  
ANISOU 3139  C1  GOL A 403     3933   1745   3760    -26    634     25       C  
HETATM 3140  O1  GOL A 403     100.123  65.471 -32.689  1.00 20.33           O  
ANISOU 3140  O1  GOL A 403     3308   1029   3387    -23    625     -9       O  
HETATM 3141  C2  GOL A 403     101.581  65.807 -34.563  1.00 26.44           C  
ANISOU 3141  C2  GOL A 403     4039   2090   3916    202    521    -46       C  
HETATM 3142  O2  GOL A 403     102.624  66.602 -34.031  1.00 22.81           O  
ANISOU 3142  O2  GOL A 403     3461   1316   3891    536    444   -319       O  
HETATM 3143  C3  GOL A 403     102.065  65.059 -35.800  1.00 29.18           C  
ANISOU 3143  C3  GOL A 403     4300   2764   4024    -20    405     91       C  
HETATM 3144  O3  GOL A 403     102.757  65.962 -36.631  1.00 31.17           O  
ANISOU 3144  O3  GOL A 403     4515   3242   4087   -125    171    208       O  
HETATM 3145  N1  EPE A 404     111.509  89.538 -45.251  1.00 51.54           N  
ANISOU 3145  N1  EPE A 404     6420   8466   4697   1556   -797    554       N  
HETATM 3146  C2  EPE A 404     111.887  88.626 -46.338  1.00 52.34           C  
ANISOU 3146  C2  EPE A 404     6686   8464   4737   1706   -727    540       C  
HETATM 3147  C3  EPE A 404     111.910  89.356 -47.668  1.00 52.99           C  
ANISOU 3147  C3  EPE A 404     6903   8472   4759   1852   -738    511       C  
HETATM 3148  N4  EPE A 404     110.594  89.929 -47.953  1.00 53.82           N  
ANISOU 3148  N4  EPE A 404     7121   8515   4813   1882   -683    451       N  
HETATM 3149  C5  EPE A 404     110.249  90.864 -46.884  1.00 53.06           C  
ANISOU 3149  C5  EPE A 404     6911   8483   4766   1850   -676    474       C  
HETATM 3150  C6  EPE A 404     110.206  90.142 -45.554  1.00 52.30           C  
ANISOU 3150  C6  EPE A 404     6677   8480   4716   1746   -691    504       C  
HETATM 3151  C7  EPE A 404     110.545  90.570 -49.273  1.00 54.81           C  
ANISOU 3151  C7  EPE A 404     7411   8564   4852   1905   -686    408       C  
HETATM 3152  C8  EPE A 404     109.143  90.608 -49.837  1.00 55.63           C  
ANISOU 3152  C8  EPE A 404     7612   8610   4913   1879   -657    346       C  
HETATM 3153  O8  EPE A 404     109.131  91.087 -51.173  1.00 56.32           O  
ANISOU 3153  O8  EPE A 404     7777   8661   4963   1845   -607    283       O  
HETATM 3154  C9  EPE A 404     111.470  88.830 -43.966  1.00 50.15           C  
ANISOU 3154  C9  EPE A 404     5923   8443   4688   1173   -904    656       C  
HETATM 3155  C10 EPE A 404     110.767  89.641 -42.886  1.00 48.08           C  
ANISOU 3155  C10 EPE A 404     5254   8411   4605    926  -1110    770       C  
HETATM 3156  S   EPE A 404     111.009  88.850 -41.324  1.00 46.31           S  
ANISOU 3156  S   EPE A 404     4593   8443   4560    697  -1302    864       S  
HETATM 3157  O1S EPE A 404     112.432  88.809 -41.086  1.00 45.89           O  
ANISOU 3157  O1S EPE A 404     4319   8497   4619    691  -1379    808       O  
HETATM 3158  O2S EPE A 404     110.469  87.489 -41.512  1.00 47.24           O  
ANISOU 3158  O2S EPE A 404     4757   8562   4629    605  -1053    784       O  
HETATM 3159  O3S EPE A 404     110.252  89.594 -40.347  1.00 46.33           O  
ANISOU 3159  O3S EPE A 404     4575   8401   4628    805  -1461    898       O  
HETATM 3160 ZN    ZN B 401     127.886  79.250 -20.568  1.00 12.92          ZN  
ANISOU 3160 ZN    ZN B 401     2451    935   1524    -71    184     43      ZN  
HETATM 3161  C1  GOL B 402     133.188  74.314 -33.556  1.00 21.76           C  
ANISOU 3161  C1  GOL B 402     3759   1764   2743   -143    535    -53       C  
HETATM 3162  O1  GOL B 402     132.408  74.986 -32.590  1.00 17.95           O  
ANISOU 3162  O1  GOL B 402     3277   1293   2250   -143    655   -172       O  
HETATM 3163  C2  GOL B 402     133.853  75.332 -34.477  1.00 23.23           C  
ANISOU 3163  C2  GOL B 402     3960   1814   3052      1    438   -186       C  
HETATM 3164  O2  GOL B 402     134.859  76.051 -33.782  1.00 20.29           O  
ANISOU 3164  O2  GOL B 402     3572   1068   3068    564    252    -39       O  
HETATM 3165  C3  GOL B 402     134.469  74.599 -35.663  1.00 26.39           C  
ANISOU 3165  C3  GOL B 402     4310   2427   3292   -473    339   -115       C  
HETATM 3166  O3  GOL B 402     135.150  75.536 -36.464  1.00 28.80           O  
ANISOU 3166  O3  GOL B 402     4517   2958   3468   -699     28     70       O  
HETATM 3167  O   HOH A 501     114.406  89.550 -40.030  1.00 34.20           O  
HETATM 3168  O   HOH A 502     103.348  81.173 -41.650  1.00 29.58           O  
HETATM 3169  O   HOH A 503      86.524  75.186 -31.999  1.00 38.37           O  
HETATM 3170  O   HOH A 504     100.212  78.637 -53.906  1.00 22.80           O  
HETATM 3171  O   HOH A 505      80.404  95.558 -38.159  1.00 27.67           O  
HETATM 3172  O   HOH A 506      91.821  92.401 -22.488  1.00 25.63           O  
HETATM 3173  O   HOH A 507      94.663  93.554 -51.801  1.00 40.45           O  
HETATM 3174  O   HOH A 508      89.100  75.452 -45.477  1.00 40.09           O  
HETATM 3175  O   HOH A 509      81.259 101.809 -36.725  1.00 47.59           O  
HETATM 3176  O   HOH A 510     114.716  73.244 -27.466  1.00 21.11           O  
HETATM 3177  O   HOH A 511      89.328  73.096 -15.803  1.00 43.25           O  
HETATM 3178  O   HOH A 512      98.863  64.135 -38.777  1.00 37.34           O  
HETATM 3179  O   HOH A 513      88.017  73.692 -42.898  1.00 36.70           O  
HETATM 3180  O   HOH A 514     105.250  87.886 -16.337  1.00 35.69           O  
HETATM 3181  O   HOH A 515     117.830  82.874 -25.696  1.00 42.01           O  
HETATM 3182  O   HOH A 516      87.742  74.304 -34.988  1.00 21.59           O  
HETATM 3183  O   HOH A 517     101.876  71.850 -13.003  1.00 36.11           O  
HETATM 3184  O   HOH A 518      98.160  80.196 -54.652  1.00 14.73           O  
HETATM 3185  O   HOH A 519      98.432  65.874 -17.652  1.00 16.41           O  
HETATM 3186  O   HOH A 520      86.179  85.073 -23.075  1.00 21.03           O  
HETATM 3187  O   HOH A 521      99.316  96.000 -32.066  1.00 11.66           O  
HETATM 3188  O   HOH A 522     101.234  91.073 -51.378  1.00 27.50           O  
HETATM 3189  O   HOH A 523     106.137  96.950 -20.460  1.00 38.70           O  
HETATM 3190  O   HOH A 524     110.357  84.814 -41.668  1.00 46.24           O  
HETATM 3191  O   HOH A 525     102.185  94.771 -25.613  1.00 28.97           O  
HETATM 3192  O   HOH A 526      99.318  99.222 -46.186  1.00 24.62           O  
HETATM 3193  O   HOH A 527     101.178 100.592 -39.731  1.00 26.21           O  
HETATM 3194  O   HOH A 528     104.374  70.385 -25.575  1.00 16.28           O  
HETATM 3195  O   HOH A 529     101.157 100.102 -43.909  1.00 36.80           O  
HETATM 3196  O   HOH A 530      88.961  85.351 -47.521  1.00 35.84           O  
HETATM 3197  O   HOH A 531      96.587  64.710 -35.785  1.00 23.76           O  
HETATM 3198  O   HOH A 532      97.933  74.911 -43.591  1.00 16.28           O  
HETATM 3199  O   HOH A 533      95.573  70.850 -43.094  1.00 34.42           O  
HETATM 3200  O   HOH A 534     104.936  74.176 -31.458  1.00 10.94           O  
HETATM 3201  O   HOH A 535     106.244  91.427 -29.822  1.00 30.79           O  
HETATM 3202  O   HOH A 536      89.371  67.372 -18.222  1.00 34.02           O  
HETATM 3203  O   HOH A 537      91.216  90.509 -26.581  1.00 17.61           O  
HETATM 3204  O   HOH A 538     100.683  75.316 -32.181  1.00 10.33           O  
HETATM 3205  O   HOH A 539     105.426  88.556 -20.358  1.00 29.01           O  
HETATM 3206  O   HOH A 540      94.510  95.649 -13.026  1.00 33.15           O  
HETATM 3207  O   HOH A 541      99.926  60.213 -27.564  1.00 14.48           O  
HETATM 3208  O   HOH A 542      90.101  85.809 -13.854  1.00 20.14           O  
HETATM 3209  O   HOH A 543      99.158  66.129 -27.849  1.00 12.60           O  
HETATM 3210  O   HOH A 544      94.128  95.180 -22.223  1.00 14.95           O  
HETATM 3211  O   HOH A 545     104.509  92.953 -31.659  1.00 21.11           O  
HETATM 3212  O   HOH A 546     116.053  71.843 -22.821  1.00 34.92           O  
HETATM 3213  O   HOH A 547      97.993  93.995 -52.871  1.00 32.77           O  
HETATM 3214  O   HOH A 548      94.202  86.448 -55.176  1.00 12.67           O  
HETATM 3215  O   HOH A 549     106.036  89.115 -33.208  1.00 17.19           O  
HETATM 3216  O   HOH A 550     108.260  75.383 -29.198  1.00 12.86           O  
HETATM 3217  O   HOH A 551     102.043  78.046 -21.160  1.00 14.82           O  
HETATM 3218  O   HOH A 552      99.301  72.250 -30.363  1.00 10.50           O  
HETATM 3219  O   HOH A 553     100.928  84.318 -12.775  1.00 34.20           O  
HETATM 3220  O   HOH A 554      87.617  76.990 -18.216  1.00 23.49           O  
HETATM 3221  O   HOH A 555     109.419  85.990 -26.847  1.00 27.55           O  
HETATM 3222  O   HOH A 556      92.070  76.321 -48.282  1.00 21.62           O  
HETATM 3223  O   HOH A 557      90.980  79.653 -24.144  1.00 12.64           O  
HETATM 3224  O   HOH A 558     110.084  93.596 -39.008  1.00 35.25           O  
HETATM 3225  O   HOH A 559      92.295  70.383 -29.901  1.00 12.42           O  
HETATM 3226  O   HOH A 560      98.073  77.167 -15.652  1.00 17.53           O  
HETATM 3227  O   HOH A 561     106.568  81.979 -37.525  1.00 24.10           O  
HETATM 3228  O   HOH A 562      84.357  89.530 -31.542  1.00 26.91           O  
HETATM 3229  O   HOH A 563     110.336  68.126 -22.481  1.00 44.76           O  
HETATM 3230  O   HOH A 564     101.758  73.693 -38.359  1.00 14.56           O  
HETATM 3231  O  BHOH A 565     105.495  83.069 -39.421  0.58 20.98           O  
HETATM 3232  O   HOH A 566     102.960  81.979 -20.049  1.00 21.73           O  
HETATM 3233  O   HOH A 567      97.221  95.295 -13.100  1.00 32.56           O  
HETATM 3234  O   HOH A 568      98.935  94.827 -10.775  1.00 28.25           O  
HETATM 3235  O   HOH A 569      91.971  96.821 -40.120  1.00 21.79           O  
HETATM 3236  O   HOH A 570      95.268  81.241 -12.119  1.00 21.31           O  
HETATM 3237  O   HOH A 571     104.081  99.335 -41.384  1.00 34.18           O  
HETATM 3238  O   HOH A 572      82.188  83.695 -26.672  1.00 17.53           O  
HETATM 3239  O   HOH A 573      99.953  66.912 -42.481  1.00 42.04           O  
HETATM 3240  O   HOH A 574      86.758  63.384 -20.836  1.00 48.21           O  
HETATM 3241  O   HOH A 575     101.876  81.459 -37.256  1.00 12.20           O  
HETATM 3242  O   HOH A 576      98.373  85.431  -9.138  1.00 30.07           O  
HETATM 3243  O   HOH A 577     101.123  65.222 -24.539  1.00 21.65           O  
HETATM 3244  O   HOH A 578     102.908  93.109 -36.618  1.00 12.80           O  
HETATM 3245  O   HOH A 579     106.395  74.474 -38.422  1.00 24.75           O  
HETATM 3246  O   HOH A 580      85.524  87.546 -19.554  1.00 27.37           O  
HETATM 3247  O   HOH A 581     101.318  92.912 -44.331  1.00 13.02           O  
HETATM 3248  O   HOH A 582      87.195  88.740 -21.230  1.00 24.44           O  
HETATM 3249  O   HOH A 583      87.381  92.561 -15.601  1.00 22.36           O  
HETATM 3250  O   HOH A 584      96.211  74.506 -47.007  1.00 32.96           O  
HETATM 3251  O   HOH A 585      87.741  83.418 -42.086  1.00 21.78           O  
HETATM 3252  O   HOH A 586      97.956  66.458 -34.046  1.00 16.36           O  
HETATM 3253  O   HOH A 587      89.717  77.598 -16.572  1.00 17.89           O  
HETATM 3254  O   HOH A 588     108.985  78.134 -22.373  1.00 13.93           O  
HETATM 3255  O   HOH A 589      94.368  81.354 -37.231  1.00 10.49           O  
HETATM 3256  O   HOH A 590     110.118  74.064 -36.197  1.00 37.23           O  
HETATM 3257  O   HOH A 591     103.917  74.523 -39.849  1.00 17.89           O  
HETATM 3258  O   HOH A 592      98.215  97.800 -50.183  1.00 34.04           O  
HETATM 3259  O   HOH A 593      91.645  96.851 -29.292  1.00 23.49           O  
HETATM 3260  O   HOH A 594     105.858  87.584 -12.571  1.00 47.83           O  
HETATM 3261  O   HOH A 595      91.499  92.481 -40.697  1.00 26.07           O  
HETATM 3262  O   HOH A 596      98.164  60.461 -23.830  1.00 14.37           O  
HETATM 3263  O   HOH A 597     102.617  78.450 -44.197  1.00 33.12           O  
HETATM 3264  O   HOH A 598      97.277  71.506 -14.200  1.00 32.10           O  
HETATM 3265  O   HOH A 599      95.574  96.813 -50.750  1.00 37.34           O  
HETATM 3266  O   HOH A 600      85.983  92.583 -35.677  1.00 32.96           O  
HETATM 3267  O   HOH A 601     110.933  83.783 -26.970  1.00 22.30           O  
HETATM 3268  O   HOH A 602      91.419  83.856 -48.058  1.00 22.01           O  
HETATM 3269  O   HOH A 603      86.020  92.206 -23.039  1.00 44.46           O  
HETATM 3270  O   HOH A 604      86.747  83.008 -34.977  1.00 14.31           O  
HETATM 3271  O   HOH A 605     102.486  73.148 -32.022  1.00 10.76           O  
HETATM 3272  O   HOH A 606      98.186  80.402 -46.541  1.00 17.02           O  
HETATM 3273  O   HOH A 607     116.258  81.940 -29.135  1.00 45.15           O  
HETATM 3274  O   HOH A 608      90.773  96.346 -45.001  1.00 48.52           O  
HETATM 3275  O   HOH A 609     116.557  75.039 -38.170  1.00 49.07           O  
HETATM 3276  O   HOH A 610     112.297  70.962 -24.104  1.00 24.13           O  
HETATM 3277  O   HOH A 611     105.764  67.706 -28.090  1.00 21.76           O  
HETATM 3278  O   HOH A 612     111.778  71.382 -33.680  1.00 35.60           O  
HETATM 3279  O   HOH A 613     111.213  82.148 -32.205  1.00 22.85           O  
HETATM 3280  O   HOH A 614     116.563  70.360 -30.027  1.00 46.59           O  
HETATM 3281  O   HOH A 615      90.524  62.881 -27.384  1.00 25.92           O  
HETATM 3282  O   HOH A 616     103.615  98.874 -43.593  1.00 40.13           O  
HETATM 3283  O   HOH A 617      99.451  96.398 -19.094  1.00 16.43           O  
HETATM 3284  O   HOH A 618      92.537  61.247 -19.272  1.00 16.23           O  
HETATM 3285  O   HOH A 619     105.803  88.772 -23.908  1.00 30.19           O  
HETATM 3286  O   HOH A 620     113.607  81.185 -36.884  1.00 44.96           O  
HETATM 3287  O   HOH A 621      97.801  81.435 -10.214  1.00 42.28           O  
HETATM 3288  O   HOH A 622      86.965  92.903 -31.686  1.00 26.14           O  
HETATM 3289  O   HOH A 623      99.875  71.214 -22.801  1.00 16.52           O  
HETATM 3290  O   HOH A 624     106.033  89.711 -14.436  1.00 30.52           O  
HETATM 3291  O   HOH A 625      87.820  83.164 -37.534  1.00 21.01           O  
HETATM 3292  O   HOH A 626      98.797 102.853 -39.355  1.00 38.09           O  
HETATM 3293  O   HOH A 627     110.199  94.007 -35.468  1.00 38.59           O  
HETATM 3294  O   HOH A 628      85.820  76.705 -36.054  1.00 23.24           O  
HETATM 3295  O   HOH A 629      83.458  82.958 -33.623  1.00 33.82           O  
HETATM 3296  O   HOH A 630     106.043  68.189 -20.528  1.00 26.21           O  
HETATM 3297  O   HOH A 631      84.791  90.014 -41.719  1.00 34.40           O  
HETATM 3298  O   HOH A 632      85.357  92.336 -18.993  1.00 30.44           O  
HETATM 3299  O   HOH A 633     104.079  91.985 -46.752  1.00 20.27           O  
HETATM 3300  O   HOH A 634      90.220  58.770 -24.840  1.00 27.17           O  
HETATM 3301  O   HOH A 635     109.092  88.934 -23.068  1.00 38.83           O  
HETATM 3302  O   HOH A 636      96.492  74.464 -33.660  1.00 10.48           O  
HETATM 3303  O   HOH A 637      90.276  90.022 -23.869  1.00 18.27           O  
HETATM 3304  O   HOH A 638      99.058  76.926 -49.600  1.00 28.15           O  
HETATM 3305  O   HOH A 639      91.313  68.645 -39.247  1.00 36.00           O  
HETATM 3306  O   HOH A 640     109.946  91.258 -32.928  1.00 24.28           O  
HETATM 3307  O   HOH A 641     109.953  68.709 -34.031  1.00 42.28           O  
HETATM 3308  O   HOH A 642     107.606  83.223 -46.516  1.00 26.70           O  
HETATM 3309  O   HOH A 643     103.313  96.391 -15.033  1.00 38.86           O  
HETATM 3310  O   HOH A 644      96.010  98.548 -34.441  1.00 17.17           O  
HETATM 3311  O   HOH A 645      90.097  86.361 -40.735  1.00 24.53           O  
HETATM 3312  O   HOH A 646      99.544  61.871 -31.837  1.00 19.92           O  
HETATM 3313  O   HOH A 647      90.225  65.434 -26.707  1.00 46.62           O  
HETATM 3314  O   HOH A 648     106.086  90.167 -47.185  1.00 36.04           O  
HETATM 3315  O   HOH A 649      98.306  68.712 -14.774  1.00 24.84           O  
HETATM 3316  O   HOH A 650      91.684  87.118 -48.265  1.00 24.12           O  
HETATM 3317  O   HOH A 651     104.515  82.360 -43.619  1.00 27.28           O  
HETATM 3318  O   HOH A 652      96.064  91.917  -7.122  1.00 40.76           O  
HETATM 3319  O   HOH A 653      91.921  78.286 -44.285  1.00 23.06           O  
HETATM 3320  O   HOH A 654      90.362  70.209 -17.492  1.00 41.31           O  
HETATM 3321  O   HOH A 655      86.098 104.235 -38.781  1.00 39.38           O  
HETATM 3322  O   HOH A 656      97.181  97.365 -16.842  1.00 23.40           O  
HETATM 3323  O   HOH A 657      93.666  97.912 -27.875  1.00 51.91           O  
HETATM 3324  O   HOH A 658     107.322  95.802 -38.984  1.00 22.29           O  
HETATM 3325  O   HOH A 659      87.522  96.600 -25.021  1.00 28.11           O  
HETATM 3326  O   HOH A 660     109.315  81.030 -39.361  1.00 36.67           O  
HETATM 3327  O   HOH A 661      89.530  95.650 -13.986  1.00 32.62           O  
HETATM 3328  O   HOH A 662      90.649  94.352 -10.821  1.00 35.23           O  
HETATM 3329  O   HOH A 663     103.208  69.942 -43.894  1.00 27.57           O  
HETATM 3330  O   HOH A 664      91.621  70.799 -40.919  1.00 20.35           O  
HETATM 3331  O   HOH A 665      95.815  78.817 -49.175  1.00 15.78           O  
HETATM 3332  O   HOH A 666     107.584  84.495 -19.352  1.00 31.90           O  
HETATM 3333  O   HOH A 667      88.947  78.751 -14.396  1.00 29.30           O  
HETATM 3334  O   HOH A 668      81.745  79.538 -39.934  1.00 35.54           O  
HETATM 3335  O   HOH A 669     117.615  74.321 -32.906  1.00 43.90           O  
HETATM 3336  O   HOH A 670     107.269  95.734 -42.266  1.00 24.57           O  
HETATM 3337  O   HOH A 671     109.014  88.719 -30.421  1.00 49.50           O  
HETATM 3338  O   HOH A 672      94.281  63.400 -34.377  1.00 22.23           O  
HETATM 3339  O   HOH A 673      99.213  77.879 -47.141  1.00 25.25           O  
HETATM 3340  O   HOH A 674      97.794  68.192 -41.376  1.00 22.35           O  
HETATM 3341  O   HOH A 675      92.047  89.604 -47.671  1.00 26.89           O  
HETATM 3342  O   HOH A 676      90.344  60.290 -20.971  1.00 24.05           O  
HETATM 3343  O   HOH A 677      94.106  68.106 -39.549  1.00 34.49           O  
HETATM 3344  O   HOH A 678      84.276  81.607 -42.491  1.00 38.28           O  
HETATM 3345  O   HOH A 679     108.631  67.900 -29.845  1.00 19.82           O  
HETATM 3346  O   HOH A 680      92.815  98.863 -48.859  1.00 37.23           O  
HETATM 3347  O   HOH A 681     112.443  85.284 -34.402  1.00 30.47           O  
HETATM 3348  O   HOH A 682      84.880  89.559 -10.444  1.00 46.90           O  
HETATM 3349  O   HOH A 683      84.373  79.007 -25.997  1.00 33.78           O  
HETATM 3350  O   HOH A 684     106.197  65.963 -30.777  1.00 34.00           O  
HETATM 3351  O   HOH A 685     114.692  82.197 -23.172  1.00 32.36           O  
HETATM 3352  O   HOH A 686      85.594  89.689 -37.815  1.00 29.87           O  
HETATM 3353  O   HOH A 687      86.385  97.912 -35.219  1.00 38.28           O  
HETATM 3354  O   HOH A 688      84.556  92.770 -38.959  1.00 41.92           O  
HETATM 3355  O   HOH A 689      98.157  74.508 -31.519  1.00 10.14           O  
HETATM 3356  O   HOH A 690     110.807  65.301 -40.480  1.00 44.63           O  
HETATM 3357  O   HOH A 691      87.875 101.710 -33.972  1.00 48.24           O  
HETATM 3358  O   HOH A 692     104.478  95.659 -25.302  1.00 49.58           O  
HETATM 3359  O   HOH A 693      86.793  74.490 -28.972  1.00 38.20           O  
HETATM 3360  O   HOH A 694     114.714  77.746 -37.459  1.00 53.28           O  
HETATM 3361  O   HOH A 695     107.357  92.842 -20.299  1.00 40.43           O  
HETATM 3362  O   HOH A 696      88.075  85.861 -38.594  1.00 27.83           O  
HETATM 3363  O   HOH A 697     100.863 100.534 -37.240  1.00 33.24           O  
HETATM 3364  O   HOH A 698     103.266  95.527 -35.219  1.00 17.43           O  
HETATM 3365  O   HOH A 699     113.548  94.995 -38.452  1.00 43.44           O  
HETATM 3366  O   HOH A 700     101.719  77.329 -14.746  1.00 26.09           O  
HETATM 3367  O   HOH A 701     103.464  91.806 -49.589  1.00 32.32           O  
HETATM 3368  O   HOH A 702      91.651  88.050  -7.248  1.00 34.03           O  
HETATM 3369  O   HOH A 703      84.435  87.991 -35.641  1.00 30.98           O  
HETATM 3370  O   HOH A 704     102.612  81.506 -17.600  1.00 35.30           O  
HETATM 3371  O   HOH A 705     113.104  69.237 -27.928  1.00 46.59           O  
HETATM 3372  O   HOH A 706      89.446  85.907 -50.061  1.00 40.04           O  
HETATM 3373  O   HOH A 707     109.361  77.148 -16.934  1.00 40.23           O  
HETATM 3374  O   HOH A 708     112.933  83.904 -23.339  1.00 41.70           O  
HETATM 3375  O   HOH A 709     113.912  71.019 -26.088  1.00 33.19           O  
HETATM 3376  O   HOH A 710     105.528  99.187 -36.908  1.00 38.10           O  
HETATM 3377  O   HOH A 711     104.460  67.958 -24.482  1.00 27.89           O  
HETATM 3378  O   HOH A 712      87.606  58.011 -24.782  1.00 36.05           O  
HETATM 3379  O   HOH A 713      82.904  67.294 -27.058  1.00 42.07           O  
HETATM 3380  O   HOH A 714      90.374  65.788 -15.082  1.00 48.35           O  
HETATM 3381  O   HOH A 715     101.220  76.718 -45.868  1.00 26.23           O  
HETATM 3382  O   HOH A 716     103.105  76.829 -40.842  1.00 24.91           O  
HETATM 3383  O   HOH A 717      91.197  98.175 -42.992  1.00 49.18           O  
HETATM 3384  O   HOH A 718     105.384  96.974 -35.255  1.00 27.35           O  
HETATM 3385  O   HOH A 719     113.790  91.535 -33.188  1.00 51.44           O  
HETATM 3386  O   HOH A 720      85.110  91.039 -15.686  1.00 36.60           O  
HETATM 3387  O   HOH A 721     110.347  75.830 -38.090  1.00 43.20           O  
HETATM 3388  O   HOH A 722      83.747  75.540 -35.821  1.00 42.89           O  
HETATM 3389  O   HOH A 723      93.114  70.087 -16.026  1.00 27.98           O  
HETATM 3390  O   HOH A 724      91.162  93.768 -44.864  1.00 29.48           O  
HETATM 3391  O   HOH A 725      94.759  76.322 -49.111  1.00 20.14           O  
HETATM 3392  O   HOH A 726     104.366  80.365 -37.038  1.00 18.30           O  
HETATM 3393  O   HOH A 727     100.067  74.382 -45.219  1.00 26.25           O  
HETATM 3394  O   HOH A 728      85.929  78.585 -14.638  1.00 47.02           O  
HETATM 3395  O   HOH A 729      90.997  78.574 -47.322  1.00 26.37           O  
HETATM 3396  O   HOH A 730      94.784  97.473 -15.323  1.00 39.58           O  
HETATM 3397  O   HOH A 731      84.031  87.375  -9.021  1.00 45.95           O  
HETATM 3398  O   HOH A 732     100.912  96.861  -9.679  1.00 46.62           O  
HETATM 3399  O   HOH A 733     114.453  83.497 -30.431  1.00 34.71           O  
HETATM 3400  O   HOH A 734      84.616  84.863  -9.634  1.00 45.37           O  
HETATM 3401  O   HOH A 735      83.672  89.908 -34.231  1.00 42.26           O  
HETATM 3402  O   HOH A 736      87.123  99.204 -23.555  1.00 39.92           O  
HETATM 3403  O   HOH A 737      91.720  80.974 -48.384  1.00 18.30           O  
HETATM 3404  O   HOH A 738      90.495  75.058 -50.076  1.00 30.36           O  
HETATM 3405  O   HOH A 739      94.754  92.938 -53.932  1.00 33.10           O  
HETATM 3406  O   HOH A 740      96.080  68.092 -16.817  1.00 36.23           O  
HETATM 3407  O   HOH A 741      85.465  90.801 -29.966  1.00 28.82           O  
HETATM 3408  O   HOH A 742     119.187  76.660 -20.332  1.00 32.59           O  
HETATM 3409  O   HOH A 743      86.818  95.405 -14.914  1.00 33.95           O  
HETATM 3410  O   HOH A 744      98.447  92.821 -55.051  1.00 41.49           O  
HETATM 3411  O   HOH A 745      88.197  61.579 -20.013  1.00 38.88           O  
HETATM 3412  O   HOH A 746     113.654  82.610 -32.781  1.00 33.08           O  
HETATM 3413  O   HOH A 747     109.723  83.029 -20.547  1.00 38.21           O  
HETATM 3414  O   HOH A 748     109.289  95.423 -40.396  1.00 48.88           O  
HETATM 3415  O   HOH A 749     104.308  79.133 -39.732  1.00 26.21           O  
HETATM 3416  O   HOH A 750     100.317  99.627 -15.842  1.00 45.61           O  
HETATM 3417  O   HOH A 751      87.670  98.864 -32.981  1.00 39.89           O  
HETATM 3418  O   HOH A 752      94.555  71.368 -13.951  1.00 31.62           O  
HETATM 3419  O   HOH A 753     107.944  76.274 -38.947  1.00 42.98           O  
HETATM 3420  O   HOH A 754     108.336  66.536 -32.072  1.00 39.17           O  
HETATM 3421  O   HOH A 755     107.149  78.769 -39.522  1.00 41.04           O  
HETATM 3422  O   HOH B 501     135.801  90.553 -41.378  1.00 26.50           O  
HETATM 3423  O   HOH B 502     124.305 102.347 -22.541  1.00 27.97           O  
HETATM 3424  O   HOH B 503     133.835 100.298 -51.411  1.00 33.80           O  
HETATM 3425  O   HOH B 504     118.227  94.418 -23.396  1.00 31.93           O  
HETATM 3426  O   HOH B 505     124.589 104.307 -40.117  1.00 33.90           O  
HETATM 3427  O   HOH B 506     115.783  75.935 -29.202  1.00 26.97           O  
HETATM 3428  O   HOH B 507     120.173  84.107 -35.277  1.00 22.86           O  
HETATM 3429  O   HOH B 508     128.048 103.148 -51.627  1.00 33.76           O  
HETATM 3430  O   HOH B 509     134.151 109.983 -39.579  1.00 28.65           O  
HETATM 3431  O   HOH B 510     142.003  76.865 -32.305  1.00 29.01           O  
HETATM 3432  O   HOH B 511     137.186  97.353 -15.876  1.00 37.97           O  
HETATM 3433  O   HOH B 512     143.251  94.858 -41.286  1.00 35.71           O  
HETATM 3434  O   HOH B 513     120.723  83.130 -15.650  1.00 35.82           O  
HETATM 3435  O   HOH B 514     123.692 105.987 -44.934  1.00 36.21           O  
HETATM 3436  O   HOH B 515     130.240  89.700 -54.544  1.00 13.73           O  
HETATM 3437  O   HOH B 516     138.510  98.438 -28.623  1.00 26.78           O  
HETATM 3438  O   HOH B 517     132.634  93.771 -12.801  1.00 34.47           O  
HETATM 3439  O   HOH B 518     121.636  95.552 -14.353  1.00 21.46           O  
HETATM 3440  O   HOH B 519     132.148 105.519 -32.010  1.00 13.14           O  
HETATM 3441  O   HOH B 520     129.996  75.407 -17.665  1.00 18.03           O  
HETATM 3442  O   HOH B 521     136.376  79.856 -25.259  1.00 14.68           O  
HETATM 3443  O   HOH B 522     137.173  83.659 -31.140  1.00 10.96           O  
HETATM 3444  O   HOH B 523     137.668  98.018 -20.184  1.00 33.09           O  
HETATM 3445  O   HOH B 524     131.445  73.593 -38.647  1.00 32.58           O  
HETATM 3446  O   HOH B 525     114.319  93.048 -26.682  1.00 40.02           O  
HETATM 3447  O   HOH B 526     138.667  98.499 -32.905  1.00 18.26           O  
HETATM 3448  O   HOH B 527     140.460  84.796 -28.739  1.00 12.88           O  
HETATM 3449  O   HOH B 528     128.930  74.277 -35.782  1.00 21.80           O  
HETATM 3450  O   HOH B 529     134.691 104.174 -25.483  1.00 25.93           O  
HETATM 3451  O   HOH B 530     138.499 106.362 -20.380  1.00 42.45           O  
HETATM 3452  O   HOH B 531     122.195 107.256 -27.171  1.00 38.08           O  
HETATM 3453  O   HOH B 532     145.856  76.485 -35.977  1.00 44.80           O  
HETATM 3454  O   HOH B 533     130.715 104.414 -10.784  1.00 27.70           O  
HETATM 3455  O   HOH B 534     120.532  83.224 -43.010  1.00 40.46           O  
HETATM 3456  O   HOH B 535     118.829 102.532 -35.695  1.00 26.45           O  
HETATM 3457  O   HOH B 536     126.482  96.019 -55.112  1.00 13.75           O  
HETATM 3458  O   HOH B 537     115.725  86.344 -33.297  1.00 27.98           O  
HETATM 3459  O   HOH B 538     122.452  75.232 -26.935  1.00 22.70           O  
HETATM 3460  O   HOH B 539     133.030  84.803 -32.026  1.00  9.54           O  
HETATM 3461  O   HOH B 540     126.544 104.832 -22.435  1.00 15.75           O  
HETATM 3462  O   HOH B 541     115.038  92.589 -31.209  1.00 46.23           O  
HETATM 3463  O   HOH B 542     131.553  81.783 -30.229  1.00 10.11           O  
HETATM 3464  O   HOH B 543     134.241  83.212 -38.207  1.00 14.46           O  
HETATM 3465  O   HOH B 544     128.194  82.969 -44.121  1.00 27.26           O  
HETATM 3466  O   HOH B 545     131.192  75.715 -27.729  1.00 13.16           O  
HETATM 3467  O   HOH B 546     130.275  69.965 -23.884  1.00 17.74           O  
HETATM 3468  O   HOH B 547     123.488 100.204 -26.795  1.00 17.47           O  
HETATM 3469  O   HOH B 548     135.574  73.921 -23.057  1.00 47.35           O  
HETATM 3470  O   HOH B 549     136.492  83.982 -39.560  1.00 17.85           O  
HETATM 3471  O   HOH B 550     137.182 102.499 -31.595  1.00 20.82           O  
HETATM 3472  O   HOH B 551     118.553 102.591 -23.507  1.00 34.56           O  
HETATM 3473  O   HOH B 552     132.179  69.821 -27.338  1.00 15.66           O  
HETATM 3474  O   HOH B 553     119.389 102.356 -16.180  1.00 23.52           O  
HETATM 3475  O   HOH B 554     124.570  79.927 -30.011  1.00 11.06           O  
HETATM 3476  O   HOH B 555     135.741 102.508 -36.468  1.00 13.05           O  
HETATM 3477  O   HOH B 556     134.336 102.269 -44.129  1.00 13.90           O  
HETATM 3478  O   HOH B 557     118.221  86.518 -36.049  1.00 25.07           O  
HETATM 3479  O   HOH B 558     113.224  88.636 -30.171  1.00 46.29           O  
HETATM 3480  O   HOH B 559     123.125  89.349 -24.322  1.00 12.08           O  
HETATM 3481  O   HOH B 560     134.013  87.589 -20.906  1.00 15.16           O  
HETATM 3482  O   HOH B 561     139.126  91.324 -37.293  1.00 20.56           O  
HETATM 3483  O   HOH B 562     130.019  94.925  -9.174  1.00 31.22           O  
HETATM 3484  O   HOH B 563     124.592  85.866 -48.234  1.00 18.50           O  
HETATM 3485  O   HOH B 564     119.864  78.523 -22.279  1.00 34.22           O  
HETATM 3486  O   HOH B 565     132.239  88.102 -53.777  1.00 17.90           O  
HETATM 3487  O   HOH B 566     124.323 102.390 -41.490  1.00 30.87           O  
HETATM 3488  O   HOH B 567     147.618  85.895 -35.675  1.00 33.79           O  
HETATM 3489  O   HOH B 568     133.237  74.881 -24.289  1.00 27.98           O  
HETATM 3490  O   HOH B 569     139.719  93.956 -19.017  1.00 42.77           O  
HETATM 3491  O   HOH B 570     148.815  81.083 -23.782  1.00 20.65           O  
HETATM 3492  O   HOH B 571     132.428  76.620 -42.418  1.00 35.36           O  
HETATM 3493  O   HOH B 572     137.499 108.519 -41.050  1.00 33.55           O  
HETATM 3494  O   HOH B 573     145.203  88.405 -38.177  1.00 41.32           O  
HETATM 3495  O   HOH B 574     131.141 103.484 -52.648  1.00 34.86           O  
HETATM 3496  O   HOH B 575     134.900  91.403 -19.738  1.00 26.26           O  
HETATM 3497  O   HOH B 576     126.739  91.000 -12.147  1.00 22.52           O  
HETATM 3498  O   HOH B 577     126.870  90.878 -37.262  1.00 10.31           O  
HETATM 3499  O   HOH B 578     137.991  77.244 -27.796  1.00 23.49           O  
HETATM 3500  O   HOH B 579     121.512  87.440 -16.775  1.00 17.45           O  
HETATM 3501  O   HOH B 580     120.928  76.853 -18.388  1.00 27.63           O  
HETATM 3502  O   HOH B 581     143.695  91.581 -32.030  1.00 25.35           O  
HETATM 3503  O   HOH B 582     116.756  86.972 -28.636  1.00 36.17           O  
HETATM 3504  O   HOH B 583     138.931  83.984 -38.068  1.00 23.73           O  
HETATM 3505  O   HOH B 584     140.507  96.198 -47.055  1.00 44.91           O  
HETATM 3506  O   HOH B 585     120.209  93.045 -42.441  1.00 21.69           O  
HETATM 3507  O   HOH B 586     135.029  87.856 -44.136  1.00 29.41           O  
HETATM 3508  O   HOH B 587     124.360 106.561 -29.438  1.00 23.70           O  
HETATM 3509  O   HOH B 588     136.685 108.067 -43.360  1.00 38.44           O  
HETATM 3510  O   HOH B 589     119.722 102.490 -31.798  1.00 26.16           O  
HETATM 3511  O   HOH B 590     130.281  76.039 -33.994  1.00 16.05           O  
HETATM 3512  O   HOH B 591     119.320  98.463 -21.740  1.00 25.28           O  
HETATM 3513  O   HOH B 592     128.936  81.023 -14.246  1.00 29.10           O  
HETATM 3514  O   HOH B 593     123.775  78.107 -39.321  1.00 42.17           O  
HETATM 3515  O   HOH B 594     119.339  86.869 -18.592  1.00 22.10           O  
HETATM 3516  O   HOH B 595     129.769  86.726 -15.521  1.00 16.92           O  
HETATM 3517  O   HOH B 596     127.905  80.466 -42.976  1.00 31.22           O  
HETATM 3518  O   HOH B 597     134.342  90.941 -37.070  1.00 11.33           O  
HETATM 3519  O   HOH B 598     132.652 108.615 -46.096  1.00 27.50           O  
HETATM 3520  O   HOH B 599     134.489 109.551 -43.835  1.00 30.44           O  
HETATM 3521  O   HOH B 600     130.731  89.805 -46.476  1.00 15.30           O  
HETATM 3522  O   HOH B 601     129.173 104.880 -13.154  1.00 34.74           O  
HETATM 3523  O   HOH B 602     143.245  90.429 -27.676  1.00 26.36           O  
HETATM 3524  O   HOH B 603     137.004 101.249 -46.550  1.00 21.19           O  
HETATM 3525  O   HOH B 604     143.343  93.139 -26.359  1.00 37.72           O  
HETATM 3526  O   HOH B 605     136.153 108.547 -47.868  1.00 40.01           O  
HETATM 3527  O   HOH B 606     137.764  99.088 -14.004  1.00 31.60           O  
HETATM 3528  O   HOH B 607     141.196  86.333 -16.873  1.00 34.24           O  
HETATM 3529  O   HOH B 608     126.504  77.790 -39.655  1.00 34.76           O  
HETATM 3530  O   HOH B 609     141.985  95.113 -26.199  1.00 45.43           O  
HETATM 3531  O   HOH B 610     119.297 113.875 -39.078  1.00 46.95           O  
HETATM 3532  O   HOH B 611     134.791  82.601 -31.810  1.00  9.78           O  
HETATM 3533  O   HOH B 612     129.113 108.159 -34.453  1.00 19.18           O  
HETATM 3534  O   HOH B 613     141.080  87.544 -21.920  1.00 16.05           O  
HETATM 3535  O   HOH B 614     118.756  83.405 -29.313  1.00 39.19           O  
HETATM 3536  O   HOH B 615     131.773 105.955 -19.066  1.00 16.55           O  
HETATM 3537  O   HOH B 616     131.611  86.395 -49.600  1.00 29.10           O  
HETATM 3538  O   HOH B 617     131.633  80.892 -22.792  1.00 14.55           O  
HETATM 3539  O   HOH B 618     122.294  68.327 -25.244  1.00 27.91           O  
HETATM 3540  O   HOH B 619     122.454 104.164 -11.175  1.00 34.12           O  
HETATM 3541  O   HOH B 620     128.860  84.002 -33.611  1.00 10.01           O  
HETATM 3542  O   HOH B 621     146.170  90.376 -34.686  1.00 38.57           O  
HETATM 3543  O   HOH B 622     122.340  99.640 -24.235  1.00 21.34           O  
HETATM 3544  O   HOH B 623     152.000  88.799 -24.051  1.00 40.53           O  
HETATM 3545  O   HOH B 624     140.213  83.524 -15.784  1.00 43.15           O  
HETATM 3546  O   HOH B 625     147.288  90.794 -21.808  1.00 37.51           O  
HETATM 3547  O   HOH B 626     124.412  70.720 -19.318  1.00 16.30           O  
HETATM 3548  O   HOH B 627     121.012 111.002 -34.135  1.00 35.82           O  
HETATM 3549  O   HOH B 628     123.992  93.374 -48.041  1.00 23.42           O  
HETATM 3550  O   HOH B 629     120.463  92.893 -37.806  1.00 21.30           O  
HETATM 3551  O   HOH B 630     124.319  96.685 -48.232  1.00 25.02           O  
HETATM 3552  O   HOH B 631     126.508 105.401 -13.056  1.00 35.75           O  
HETATM 3553  O   HOH B 632     124.578  99.194 -47.668  1.00 24.32           O  
HETATM 3554  O   HOH B 633     137.311  96.036 -50.810  1.00 36.16           O  
HETATM 3555  O   HOH B 634     121.411  79.565 -18.445  1.00 25.91           O  
HETATM 3556  O   HOH B 635     124.433  87.791 -44.277  1.00 20.66           O  
HETATM 3557  O   HOH B 636     136.990  91.593 -43.467  1.00 27.09           O  
HETATM 3558  O   HOH B 637     144.381  80.305 -23.143  1.00 36.35           O  
HETATM 3559  O  BHOH B 638     138.226  92.550 -39.230  0.66 23.71           O  
HETATM 3560  O   HOH B 639     116.675  90.866 -42.705  1.00 41.41           O  
HETATM 3561  O   HOH B 640     123.127  98.142  -7.493  1.00 39.72           O  
HETATM 3562  O   HOH B 641     132.682 107.100 -14.812  1.00 46.66           O  
HETATM 3563  O   HOH B 642     129.299 106.954 -16.852  1.00 24.44           O  
HETATM 3564  O   HOH B 643     125.008 106.684 -40.079  1.00 20.98           O  
HETATM 3565  O   HOH B 644     120.045 106.360 -25.365  1.00 24.71           O  
HETATM 3566  O   HOH B 645     128.290  88.369 -49.070  1.00 13.95           O  
HETATM 3567  O   HOH B 646     143.604  84.259 -16.890  1.00 38.58           O  
HETATM 3568  O   HOH B 647     145.633  81.035 -25.730  1.00 21.62           O  
HETATM 3569  O   HOH B 648     117.455 102.519 -38.748  1.00 34.96           O  
HETATM 3570  O   HOH B 649     117.543 102.137 -19.727  1.00 32.39           O  
HETATM 3571  O   HOH B 650     122.506  72.272 -27.637  1.00 18.07           O  
HETATM 3572  O   HOH B 651     119.587  69.952 -23.830  1.00 37.22           O  
HETATM 3573  O   HOH B 652     119.253  92.781 -35.305  1.00 15.71           O  
HETATM 3574  O   HOH B 653     131.924  71.528 -31.659  1.00 18.56           O  
HETATM 3575  O   HOH B 654     122.476  96.064 -40.989  1.00 20.12           O  
HETATM 3576  O   HOH B 655     137.811  77.762 -20.217  1.00 28.99           O  
HETATM 3577  O   HOH B 656     140.332 104.945 -38.634  1.00 21.53           O  
HETATM 3578  O   HOH B 657     130.483  84.411 -43.490  1.00 16.28           O  
HETATM 3579  O   HOH B 658     130.265  77.708 -41.213  1.00 21.33           O  
HETATM 3580  O   HOH B 659     124.182  80.308 -41.013  1.00 18.72           O  
HETATM 3581  O   HOH B 660     121.517 105.536 -14.535  1.00 27.77           O  
HETATM 3582  O   HOH B 661     134.470  85.709 -51.029  1.00 30.69           O  
HETATM 3583  O   HOH B 662     125.953 108.348 -48.906  1.00 45.75           O  
HETATM 3584  O   HOH B 663     140.248  92.405 -46.276  1.00 26.54           O  
HETATM 3585  O   HOH B 664     120.398  88.718 -14.808  1.00 29.22           O  
HETATM 3586  O   HOH B 665     139.086  99.321 -26.000  1.00 28.70           O  
HETATM 3587  O   HOH B 666     131.231 107.114 -50.392  1.00 45.31           O  
HETATM 3588  O   HOH B 667     142.591 100.456 -32.384  1.00 24.40           O  
HETATM 3589  O   HOH B 668     124.969 108.125 -43.049  1.00 44.72           O  
HETATM 3590  O   HOH B 669     126.557  72.951 -34.355  1.00 21.93           O  
HETATM 3591  O   HOH B 670     142.196  90.204 -39.031  1.00 35.61           O  
HETATM 3592  O   HOH B 671     143.217  74.877 -32.947  1.00 42.10           O  
HETATM 3593  O   HOH B 672     135.758  79.466 -43.669  1.00 24.95           O  
HETATM 3594  O   HOH B 673     122.440  69.788 -21.065  1.00 22.12           O  
HETATM 3595  O   HOH B 674     135.383 105.949 -14.838  1.00 37.87           O  
HETATM 3596  O   HOH B 675     140.437 104.741 -41.970  1.00 25.04           O  
HETATM 3597  O   HOH B 676     131.685  87.307 -47.107  1.00 20.72           O  
HETATM 3598  O   HOH B 677     140.957  77.406 -29.547  1.00 20.00           O  
HETATM 3599  O   HOH B 678     148.542  76.101 -33.147  1.00 27.20           O  
HETATM 3600  O   HOH B 679     118.461  99.880 -38.166  1.00 24.49           O  
HETATM 3601  O   HOH B 680     118.539  72.719 -21.286  1.00 42.05           O  
HETATM 3602  O   HOH B 681     129.729  78.287 -14.791  1.00 22.89           O  
HETATM 3603  O   HOH B 682     118.294  99.502 -40.953  1.00 35.60           O  
HETATM 3604  O   HOH B 683     119.011 101.027  -9.341  1.00 37.02           O  
HETATM 3605  O   HOH B 684     120.501  95.640 -38.751  1.00 24.91           O  
HETATM 3606  O   HOH B 685     138.430  75.569 -30.299  1.00 33.20           O  
HETATM 3607  O   HOH B 686     137.695  72.967 -40.682  1.00 43.29           O  
HETATM 3608  O   HOH B 687     140.919 101.669 -30.504  1.00 52.30           O  
HETATM 3609  O   HOH B 688     117.102  97.620 -19.599  1.00 38.65           O  
HETATM 3610  O   HOH B 689     128.837 106.406 -50.638  1.00 39.08           O  
HETATM 3611  O   HOH B 690     116.069  90.643 -24.469  1.00 25.99           O  
HETATM 3612  O   HOH B 691     136.257  77.345 -24.041  1.00 28.20           O  
HETATM 3613  O   HOH B 692     130.458  84.046 -31.437  1.00 10.05           O  
HETATM 3614  O   HOH B 693     144.990  94.138 -33.556  1.00 23.99           O  
HETATM 3615  O   HOH B 694     138.174  97.887 -23.373  1.00 39.11           O  
HETATM 3616  O   HOH B 695     128.427  84.032 -47.122  1.00 26.87           O  
HETATM 3617  O   HOH B 696     144.692  79.589 -37.342  1.00 28.55           O  
HETATM 3618  O   HOH B 697     116.506  84.690 -34.940  1.00 32.13           O  
HETATM 3619  O   HOH B 698     116.582  99.319 -10.966  1.00 40.21           O  
HETATM 3620  O   HOH B 699     133.980 109.955 -37.035  1.00 34.48           O  
HETATM 3621  O   HOH B 700     118.259  74.119 -30.295  1.00 40.90           O  
HETATM 3622  O   HOH B 701     136.086 104.883 -35.053  1.00 18.70           O  
HETATM 3623  O   HOH B 702     118.892  84.990 -31.530  1.00 44.09           O  
HETATM 3624  O   HOH B 703     142.257  74.021 -40.830  1.00 43.96           O  
HETATM 3625  O   HOH B 704     119.340 107.520 -34.822  1.00 46.59           O  
HETATM 3626  O   HOH B 705     136.407 101.139 -49.512  1.00 43.55           O  
HETATM 3627  O   HOH B 706     124.415 105.995 -19.717  1.00 12.68           O  
HETATM 3628  O   HOH B 707     145.139  78.601 -27.252  1.00 48.85           O  
HETATM 3629  O   HOH B 708     133.440  86.788 -14.525  1.00 23.23           O  
HETATM 3630  O   HOH B 709     134.499  90.924 -17.312  1.00 32.54           O  
HETATM 3631  O   HOH B 710     147.014  80.213 -21.611  1.00 39.21           O  
HETATM 3632  O   HOH B 711     137.620  90.169 -54.003  1.00 40.85           O  
HETATM 3633  O   HOH B 712     138.370  76.404 -22.007  1.00 46.28           O  
HETATM 3634  O   HOH B 713     137.910  96.732 -12.776  1.00 43.19           O  
HETATM 3635  O   HOH B 714     133.666  86.168 -45.757  1.00 22.96           O  
HETATM 3636  O   HOH B 715     138.586 101.220 -29.439  1.00 31.29           O  
HETATM 3637  O   HOH B 716     115.685  92.897 -23.724  1.00 42.36           O  
HETATM 3638  O   HOH B 717     119.955  67.445 -25.242  1.00 35.61           O  
HETATM 3639  O   HOH B 718     138.289 106.352 -34.932  1.00 25.78           O  
HETATM 3640  O   HOH B 719     123.276  75.495 -36.946  1.00 44.51           O  
HETATM 3641  O   HOH B 720     120.891  73.633 -29.718  1.00 37.93           O  
HETATM 3642  O   HOH B 721     124.136 103.359 -44.396  1.00 28.89           O  
HETATM 3643  O   HOH B 722     135.735  86.314 -40.632  1.00 25.36           O  
HETATM 3644  O   HOH B 723     116.826 100.921 -16.491  1.00 40.25           O  
HETATM 3645  O   HOH B 724     133.744 106.216 -50.326  1.00 49.20           O  
HETATM 3646  O   HOH B 725     127.162  85.805 -49.091  1.00 18.67           O  
HETATM 3647  O   HOH B 726     117.433  96.785 -25.031  1.00 41.60           O  
HETATM 3648  O   HOH B 727     125.188 106.538 -16.582  1.00 35.81           O  
HETATM 3649  O   HOH B 728     119.094  98.473 -24.274  1.00 30.33           O  
HETATM 3650  O   HOH B 729     136.841  89.764 -36.863  1.00 16.07           O  
HETATM 3651  O   HOH B 730     124.867  79.779 -16.162  1.00 33.27           O  
HETATM 3652  O   HOH B 731     143.804  98.251 -30.788  1.00 40.74           O  
HETATM 3653  O   HOH B 732     123.495  88.138 -47.200  1.00 22.88           O  
HETATM 3654  O   HOH B 733     143.354  77.040 -27.885  1.00 40.06           O  
HETATM 3655  O   HOH B 734     132.579  83.700 -45.124  1.00 23.53           O  
HETATM 3656  O   HOH B 735     146.311  91.750 -37.284  1.00 40.50           O  
HETATM 3657  O   HOH B 736     131.064 112.971 -35.478  1.00 29.04           O  
HETATM 3658  O   HOH B 737     122.976  84.645 -50.016  1.00 26.84           O  
HETATM 3659  O   HOH B 738     118.884 104.982 -15.429  1.00 29.89           O  
HETATM 3660  O   HOH B 739     122.103  98.901 -49.201  1.00 46.04           O  
HETATM 3661  O   HOH B 740     118.088 104.886 -24.904  1.00 38.81           O  
HETATM 3662  O   HOH B 741     124.287  90.533 -48.196  1.00 16.45           O  
HETATM 3663  O   HOH B 742     138.953  91.504 -41.747  1.00 40.97           O  
HETATM 3664  O   HOH B 743     120.154  71.147 -20.271  1.00 31.58           O  
HETATM 3665  O   HOH B 744     125.918  77.051 -15.854  1.00 45.56           O  
HETATM 3666  O   HOH B 745     115.864  85.825 -30.688  1.00 39.60           O  
HETATM 3667  O   HOH B 746     127.011 102.527 -53.804  1.00 32.28           O  
HETATM 3668  O   HOH B 747     117.163 100.533 -24.586  1.00 43.06           O  
HETATM 3669  O   HOH B 748     114.128  83.335 -35.166  1.00 43.76           O  
HETATM 3670  O   HOH B 749     142.233 104.648 -39.931  1.00 50.37           O  
HETATM 3671  O   HOH B 750     121.757  80.731 -16.274  1.00 44.82           O  
HETATM 3672  O   HOH B 751     125.064  79.854 -43.668  1.00 38.46           O  
HETATM 3673  O   HOH B 752     140.633 105.730 -36.006  1.00 39.99           O  
HETATM 3674  O   HOH B 753     136.937  88.711 -39.543  1.00 24.20           O  
HETATM 3675  O   HOH B 754     132.680 109.179 -15.807  1.00 40.75           O  
HETATM 3676  O   HOH B 755     142.192  94.648 -45.962  1.00 46.92           O  
HETATM 3677  O   HOH B 756     118.701  74.600 -19.492  1.00 40.69           O  
HETATM 3678  O   HOH B 757     126.266  80.764 -14.212  1.00 36.86           O  
HETATM 3679  O   HOH B 758     120.274 108.621 -32.979  1.00 38.82           O  
HETATM 3680  O   HOH B 759     144.993 101.848 -33.196  1.00 40.73           O  
HETATM 3681  O   HOH B 760     114.619  88.410 -22.878  1.00 42.54           O  
HETATM 3682  O   HOH B 761     139.597  88.045 -39.719  1.00 45.57           O  
CONECT  629 3134                                                                
CONECT  653 3134                                                                
CONECT 1129 3134                                                                
CONECT 1159 3134                                                                
CONECT 2219 3160                                                                
CONECT 2243 3160                                                                
CONECT 2706 3160                                                                
CONECT 2736 3160                                                                
CONECT 3134  629  653 1129 1159                                                 
CONECT 3135 3136 3137                                                           
CONECT 3136 3135                                                                
CONECT 3137 3135 3138                                                           
CONECT 3138 3137                                                                
CONECT 3139 3140 3141                                                           
CONECT 3140 3139                                                                
CONECT 3141 3139 3142 3143                                                      
CONECT 3142 3141                                                                
CONECT 3143 3141 3144                                                           
CONECT 3144 3143                                                                
CONECT 3145 3146 3150 3154                                                      
CONECT 3146 3145 3147                                                           
CONECT 3147 3146 3148                                                           
CONECT 3148 3147 3149 3151                                                      
CONECT 3149 3148 3150                                                           
CONECT 3150 3145 3149                                                           
CONECT 3151 3148 3152                                                           
CONECT 3152 3151 3153                                                           
CONECT 3153 3152                                                                
CONECT 3154 3145 3155                                                           
CONECT 3155 3154 3156                                                           
CONECT 3156 3155 3157 3158 3159                                                 
CONECT 3157 3156                                                                
CONECT 3158 3156                                                                
CONECT 3159 3156                                                                
CONECT 3160 2219 2243 2706 2736                                                 
CONECT 3161 3162 3163                                                           
CONECT 3162 3161                                                                
CONECT 3163 3161 3164 3165                                                      
CONECT 3164 3163                                                                
CONECT 3165 3163 3166                                                           
CONECT 3166 3165                                                                
MASTER      365    0    6    5   22    0    9    6 3580    2   41   34          
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.