CNRS Nantes University UFIP UFIP
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***  didier  ***

elNémo ID: 19112911384897198

Job options:

ID        	=	 19112911384897198
JOBID     	=	 didier
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER didier

HEADER    VIRAL PROTEIN                           24-MAY-16   5K6K              
TITLE     ZIKA VIRUS NON-STRUCTURAL PROTEIN 1 (NS1)                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ZIKA VIRUS PROTEIN;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ZIKA VIRUS;                                     
SOURCE   3 ORGANISM_COMMON: ZIKV;                                               
SOURCE   4 ORGANISM_TAXID: 64320;                                               
SOURCE   5 STRAIN: MR 766;                                                      
SOURCE   6 EXPRESSION_SYSTEM: UNIDENTIFIED BACULOVIRUS;                         
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10469                                       
KEYWDS    VIRAL PROTEIN                                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.L.AKEY,W.C.BROWN,J.L.SMITH                                          
REVDAT   5   22-NOV-17 5K6K    1       REMARK                                   
REVDAT   4   21-SEP-16 5K6K    1       JRNL                                     
REVDAT   3   10-AUG-16 5K6K    1       JRNL                                     
REVDAT   2   13-JUL-16 5K6K    1       AUTHOR JRNL                              
REVDAT   1   06-JUL-16 5K6K    0                                                
JRNL        AUTH   W.C.BROWN,D.L.AKEY,J.R.KONWERSKI,J.T.TARRASCH,G.SKINIOTIS,   
JRNL        AUTH 2 R.J.KUHN,J.L.SMITH                                           
JRNL        TITL   EXTENDED SURFACE FOR MEMBRANE ASSOCIATION IN ZIKA VIRUS NS1  
JRNL        TITL 2 STRUCTURE.                                                   
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  23   865 2016              
JRNL        REFN                   ESSN 1545-9985                               
JRNL        PMID   27455458                                                     
JRNL        DOI    10.1038/NSMB.3268                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.89 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.89                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.08                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 74473                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.150                           
REMARK   3   R VALUE            (WORKING SET) : 0.149                           
REMARK   3   FREE R VALUE                     : 0.189                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.810                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2089                            
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 48.0955 -  4.6600    1.00     5072   146  0.1456 0.1641        
REMARK   3     2  4.6600 -  3.6992    1.00     4893   141  0.1127 0.1592        
REMARK   3     3  3.6992 -  3.2317    1.00     4852   142  0.1291 0.1756        
REMARK   3     4  3.2317 -  2.9363    1.00     4867   140  0.1381 0.1826        
REMARK   3     5  2.9363 -  2.7258    1.00     4799   141  0.1466 0.1890        
REMARK   3     6  2.7258 -  2.5651    1.00     4828   137  0.1532 0.1890        
REMARK   3     7  2.5651 -  2.4367    1.00     4802   138  0.1537 0.2055        
REMARK   3     8  2.4367 -  2.3306    1.00     4799   137  0.1579 0.2276        
REMARK   3     9  2.3306 -  2.2409    1.00     4779   139  0.1697 0.1883        
REMARK   3    10  2.2409 -  2.1636    1.00     4828   139  0.1704 0.1839        
REMARK   3    11  2.1636 -  2.0959    1.00     4781   134  0.1743 0.2341        
REMARK   3    12  2.0959 -  2.0360    1.00     4772   137  0.1872 0.2359        
REMARK   3    13  2.0360 -  1.9824    1.00     4780   142  0.2129 0.2549        
REMARK   3    14  1.9824 -  1.9340    1.00     4763   140  0.2557 0.3156        
REMARK   3    15  1.9340 -  1.8901    1.00     4769   136  0.3050 0.3598        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.920           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.05                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.61                          
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      :  0.007           5933                                  
REMARK   3   ANGLE     :  0.838           8069                                  
REMARK   3   CHIRALITY :  0.055            850                                  
REMARK   3   PLANARITY :  0.005           1035                                  
REMARK   3   DIHEDRAL  : 18.003           3539                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID -5 THROUGH 180 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.2237 -38.7751 -14.1706              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2155 T22:   0.2311                                     
REMARK   3      T33:   0.2535 T12:   0.0236                                     
REMARK   3      T13:  -0.0313 T23:   0.0080                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8188 L22:   1.1370                                     
REMARK   3      L33:   0.8099 L12:   1.3907                                     
REMARK   3      L13:   0.3973 L23:   0.0046                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0568 S12:  -0.0841 S13:  -0.2635                       
REMARK   3      S21:   0.0821 S22:  -0.0306 S23:  -0.2343                       
REMARK   3      S31:   0.0204 S32:   0.1330 S33:  -0.0199                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 181 THROUGH 352 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -27.1421 -23.9272 -11.8706              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1858 T22:   0.2159                                     
REMARK   3      T33:   0.1965 T12:  -0.0099                                     
REMARK   3      T13:  -0.0162 T23:   0.0228                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4647 L22:   2.1046                                     
REMARK   3      L33:   2.0336 L12:  -0.3311                                     
REMARK   3      L13:  -0.3112 L23:   1.3083                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0044 S12:  -0.0692 S13:   0.0685                       
REMARK   3      S21:   0.0009 S22:   0.0025 S23:   0.0532                       
REMARK   3      S31:  -0.1672 S32:  -0.0659 S33:  -0.0006                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 0 THROUGH 31 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -26.1711 -55.0785 -17.5835              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2462 T22:   0.1855                                     
REMARK   3      T33:   0.2511 T12:  -0.0321                                     
REMARK   3      T13:  -0.0328 T23:   0.0708                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3246 L22:   2.5628                                     
REMARK   3      L33:   4.2982 L12:   0.2773                                     
REMARK   3      L13:   1.3754 L23:   1.0164                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2611 S12:  -0.2718 S13:  -0.2838                       
REMARK   3      S21:   0.1708 S22:  -0.0963 S23:  -0.1454                       
REMARK   3      S31:   0.3299 S32:  -0.3158 S33:  -0.1400                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 32 THROUGH 180 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -56.8414 -51.5902 -31.0621              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1900 T22:   0.2118                                     
REMARK   3      T33:   0.2252 T12:  -0.0172                                     
REMARK   3      T13:   0.0024 T23:   0.0206                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9633 L22:   2.5514                                     
REMARK   3      L33:   1.7238 L12:   0.9270                                     
REMARK   3      L13:  -0.3927 L23:  -0.5591                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0845 S12:  -0.2606 S13:  -0.1545                       
REMARK   3      S21:   0.1607 S22:  -0.0678 S23:   0.2528                       
REMARK   3      S31:   0.1387 S32:  -0.1060 S33:  -0.0162                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 181 THROUGH 352 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -26.2940 -51.0775 -44.0288              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2217 T22:   0.1904                                     
REMARK   3      T33:   0.2229 T12:   0.0008                                     
REMARK   3      T13:  -0.0060 T23:   0.0227                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4988 L22:   1.0594                                     
REMARK   3      L33:   3.6290 L12:  -0.1204                                     
REMARK   3      L13:  -0.4783 L23:   0.9921                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0150 S12:   0.0514 S13:  -0.0827                       
REMARK   3      S21:  -0.1250 S22:  -0.0131 S23:  -0.0415                       
REMARK   3      S31:   0.1519 S32:   0.1342 S33:   0.0338                       
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 5K6K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAY-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000221837.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-APR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0332                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XSCALE, XDS                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 74493                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.890                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.080                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 13.50                              
REMARK 200  R MERGE                    (I) : 0.12500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.2200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.89                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.30                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.61300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.330                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.6.0                                          
REMARK 200 STARTING MODEL: 4O6D                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350 150 MM NH3SO4 100 MM TRIS   
REMARK 280  8.5, PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       48.08000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       65.22000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       73.97500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       48.08000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       65.22000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       73.97500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       48.08000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       65.22000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       73.97500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       48.08000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       65.22000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       73.97500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 7690 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 31630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 18120 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 60510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -133.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      -96.16000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000     -130.44000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 17800 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 60830 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -117.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 563  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 950  LIES ON A SPECIAL POSITION.                          
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     ALA A   -23                                                      
REMARK 465     HIS A   -22                                                      
REMARK 465     HIS A   -21                                                      
REMARK 465     HIS A   -20                                                      
REMARK 465     HIS A   -19                                                      
REMARK 465     HIS A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     GLY A   -14                                                      
REMARK 465     VAL A   -13                                                      
REMARK 465     ASP A   -12                                                      
REMARK 465     LEU A   -11                                                      
REMARK 465     GLY A   -10                                                      
REMARK 465     THR A    -9                                                      
REMARK 465     GLU A    -8                                                      
REMARK 465     ASN A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     HIS A   113                                                      
REMARK 465     GLY A   114                                                      
REMARK 465     TRP A   115                                                      
REMARK 465     LYS A   116                                                      
REMARK 465     ALA A   117                                                      
REMARK 465     TRP A   118                                                      
REMARK 465     GLY A   119                                                      
REMARK 465     LYS A   120                                                      
REMARK 465     ALA B   -23                                                      
REMARK 465     HIS B   -22                                                      
REMARK 465     HIS B   -21                                                      
REMARK 465     HIS B   -20                                                      
REMARK 465     HIS B   -19                                                      
REMARK 465     HIS B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     SER B   -15                                                      
REMARK 465     GLY B   -14                                                      
REMARK 465     VAL B   -13                                                      
REMARK 465     ASP B   -12                                                      
REMARK 465     LEU B   -11                                                      
REMARK 465     GLY B   -10                                                      
REMARK 465     THR B    -9                                                      
REMARK 465     GLU B    -8                                                      
REMARK 465     ASN B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     TYR B    -5                                                      
REMARK 465     PHE B    -4                                                      
REMARK 465     GLN B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     TYR A  -5    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   538     O    HOH B   899              2.08            
REMARK 500   O    HOH A   895     O    HOH A   940              2.08            
REMARK 500   O    HOH B   650     O    HOH B   897              2.14            
REMARK 500   O    HOH B   829     O    HOH B   938              2.14            
REMARK 500   O    HOH B   509     O    HOH B   914              2.15            
REMARK 500   O    HOH B   738     O    HOH B   947              2.15            
REMARK 500   O    LEU A   145     O    HOH A   501              2.16            
REMARK 500   OD2  ASP B    24     O    HOH B   501              2.17            
REMARK 500   O    HOH A   514     O    HOH A   846              2.17            
REMARK 500   O    HOH B   871     O    HOH B   916              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   539     O    HOH B   947     8544     2.11            
REMARK 500   O    HOH B   713     O    HOH B   938     2445     2.17            
REMARK 500   O    HOH B   665     O    HOH B   895     2445     2.17            
REMARK 500   O    HOH B   842     O    HOH B   876     2445     2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 136     -147.97     56.99                                   
REMARK 500    ASP A 197     -157.67   -143.92                                   
REMARK 500    ASN A 207     -121.36    -96.54                                   
REMARK 500    TRP A 232       76.42     48.98                                   
REMARK 500    ASN A 255       45.98   -100.57                                   
REMARK 500    GLU A 278      140.81   -175.72                                   
REMARK 500    GLU A 315       28.17   -157.89                                   
REMARK 500    ASP B 136     -142.39     48.05                                   
REMARK 500    ASP B 197     -155.30   -147.81                                   
REMARK 500    ASN B 207     -128.32    -98.29                                   
REMARK 500    TRP B 232       74.97     52.02                                   
REMARK 500    ASN B 255       41.89    -98.44                                   
REMARK 500    GLU B 278      140.70   -171.03                                   
REMARK 500    GLU B 315       34.58   -157.26                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A1006        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH B1041        DISTANCE =  6.69 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 401 bound   
REMARK 800  to ASN A 130                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 402 bound   
REMARK 800  to ASN A 207                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 401 bound   
REMARK 800  to ASN B 130                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 402 bound   
REMARK 800  to ASN B 207                                                        
DBREF  5K6K A    0   352  UNP    Q32ZE1   POLG_ZIKV      790   1142             
DBREF  5K6K B    0   352  UNP    Q32ZE1   POLG_ZIKV      790   1142             
SEQADV 5K6K ALA A  -23  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS A  -22  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS A  -21  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS A  -20  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS A  -19  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS A  -18  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS A  -17  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K SER A  -16  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K SER A  -15  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K GLY A  -14  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K VAL A  -13  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K ASP A  -12  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K LEU A  -11  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K GLY A  -10  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K THR A   -9  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K GLU A   -8  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K ASN A   -7  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K LEU A   -6  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K TYR A   -5  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K PHE A   -4  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K GLN A   -3  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K SER A   -2  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K ASN A   -1  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K ALA B  -23  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS B  -22  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS B  -21  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS B  -20  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS B  -19  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS B  -18  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K HIS B  -17  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K SER B  -16  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K SER B  -15  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K GLY B  -14  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K VAL B  -13  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K ASP B  -12  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K LEU B  -11  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K GLY B  -10  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K THR B   -9  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K GLU B   -8  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K ASN B   -7  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K LEU B   -6  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K TYR B   -5  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K PHE B   -4  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K GLN B   -3  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K SER B   -2  UNP  Q32ZE1              EXPRESSION TAG                 
SEQADV 5K6K ASN B   -1  UNP  Q32ZE1              EXPRESSION TAG                 
SEQRES   1 A  376  ALA HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  376  GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA ASP VAL          
SEQRES   3 A  376  GLY CYS SER VAL ASP PHE SER LYS LYS GLU THR ARG CYS          
SEQRES   4 A  376  GLY THR GLY VAL PHE ILE TYR ASN ASP VAL GLU ALA TRP          
SEQRES   5 A  376  ARG ASP ARG TYR LYS TYR HIS PRO ASP SER PRO ARG ARG          
SEQRES   6 A  376  LEU ALA ALA ALA VAL LYS GLN ALA TRP GLU GLU GLY ILE          
SEQRES   7 A  376  CYS GLY ILE SER SER VAL SER ARG MET GLU ASN ILE MET          
SEQRES   8 A  376  TRP LYS SER VAL GLU GLY GLU LEU ASN ALA ILE LEU GLU          
SEQRES   9 A  376  GLU ASN GLY VAL GLN LEU THR VAL VAL VAL GLY SER VAL          
SEQRES  10 A  376  LYS ASN PRO MET TRP ARG GLY PRO GLN ARG LEU PRO VAL          
SEQRES  11 A  376  PRO VAL ASN GLU LEU PRO HIS GLY TRP LYS ALA TRP GLY          
SEQRES  12 A  376  LYS SER TYR PHE VAL ARG ALA ALA LYS THR ASN ASN SER          
SEQRES  13 A  376  PHE VAL VAL ASP GLY ASP THR LEU LYS GLU CYS PRO LEU          
SEQRES  14 A  376  GLU HIS ARG ALA TRP ASN SER PHE LEU VAL GLU ASP HIS          
SEQRES  15 A  376  GLY PHE GLY VAL PHE HIS THR SER VAL TRP LEU LYS VAL          
SEQRES  16 A  376  ARG GLU ASP TYR SER LEU GLU CYS ASP PRO ALA VAL ILE          
SEQRES  17 A  376  GLY THR ALA VAL LYS GLY ARG GLU ALA ALA HIS SER ASP          
SEQRES  18 A  376  LEU GLY TYR TRP ILE GLU SER GLU LYS ASN ASP THR TRP          
SEQRES  19 A  376  ARG LEU LYS ARG ALA HIS LEU ILE GLU MET LYS THR CYS          
SEQRES  20 A  376  GLU TRP PRO LYS SER HIS THR LEU TRP THR ASP GLY VAL          
SEQRES  21 A  376  GLU GLU SER ASP LEU ILE ILE PRO LYS SER LEU ALA GLY          
SEQRES  22 A  376  PRO LEU SER HIS HIS ASN THR ARG GLU GLY TYR ARG THR          
SEQRES  23 A  376  GLN VAL LYS GLY PRO TRP HIS SER GLU GLU LEU GLU ILE          
SEQRES  24 A  376  ARG PHE GLU GLU CYS PRO GLY THR LYS VAL TYR VAL GLU          
SEQRES  25 A  376  GLU THR CYS GLY THR ARG GLY PRO SER LEU ARG SER THR          
SEQRES  26 A  376  THR ALA SER GLY ARG VAL ILE GLU GLU TRP CYS CYS ARG          
SEQRES  27 A  376  GLU CYS THR MET PRO PRO LEU SER PHE ARG ALA LYS ASP          
SEQRES  28 A  376  GLY CYS TRP TYR GLY MET GLU ILE ARG PRO ARG LYS GLU          
SEQRES  29 A  376  PRO GLU SER ASN LEU VAL ARG SER MET VAL THR ALA              
SEQRES   1 B  376  ALA HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  376  GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA ASP VAL          
SEQRES   3 B  376  GLY CYS SER VAL ASP PHE SER LYS LYS GLU THR ARG CYS          
SEQRES   4 B  376  GLY THR GLY VAL PHE ILE TYR ASN ASP VAL GLU ALA TRP          
SEQRES   5 B  376  ARG ASP ARG TYR LYS TYR HIS PRO ASP SER PRO ARG ARG          
SEQRES   6 B  376  LEU ALA ALA ALA VAL LYS GLN ALA TRP GLU GLU GLY ILE          
SEQRES   7 B  376  CYS GLY ILE SER SER VAL SER ARG MET GLU ASN ILE MET          
SEQRES   8 B  376  TRP LYS SER VAL GLU GLY GLU LEU ASN ALA ILE LEU GLU          
SEQRES   9 B  376  GLU ASN GLY VAL GLN LEU THR VAL VAL VAL GLY SER VAL          
SEQRES  10 B  376  LYS ASN PRO MET TRP ARG GLY PRO GLN ARG LEU PRO VAL          
SEQRES  11 B  376  PRO VAL ASN GLU LEU PRO HIS GLY TRP LYS ALA TRP GLY          
SEQRES  12 B  376  LYS SER TYR PHE VAL ARG ALA ALA LYS THR ASN ASN SER          
SEQRES  13 B  376  PHE VAL VAL ASP GLY ASP THR LEU LYS GLU CYS PRO LEU          
SEQRES  14 B  376  GLU HIS ARG ALA TRP ASN SER PHE LEU VAL GLU ASP HIS          
SEQRES  15 B  376  GLY PHE GLY VAL PHE HIS THR SER VAL TRP LEU LYS VAL          
SEQRES  16 B  376  ARG GLU ASP TYR SER LEU GLU CYS ASP PRO ALA VAL ILE          
SEQRES  17 B  376  GLY THR ALA VAL LYS GLY ARG GLU ALA ALA HIS SER ASP          
SEQRES  18 B  376  LEU GLY TYR TRP ILE GLU SER GLU LYS ASN ASP THR TRP          
SEQRES  19 B  376  ARG LEU LYS ARG ALA HIS LEU ILE GLU MET LYS THR CYS          
SEQRES  20 B  376  GLU TRP PRO LYS SER HIS THR LEU TRP THR ASP GLY VAL          
SEQRES  21 B  376  GLU GLU SER ASP LEU ILE ILE PRO LYS SER LEU ALA GLY          
SEQRES  22 B  376  PRO LEU SER HIS HIS ASN THR ARG GLU GLY TYR ARG THR          
SEQRES  23 B  376  GLN VAL LYS GLY PRO TRP HIS SER GLU GLU LEU GLU ILE          
SEQRES  24 B  376  ARG PHE GLU GLU CYS PRO GLY THR LYS VAL TYR VAL GLU          
SEQRES  25 B  376  GLU THR CYS GLY THR ARG GLY PRO SER LEU ARG SER THR          
SEQRES  26 B  376  THR ALA SER GLY ARG VAL ILE GLU GLU TRP CYS CYS ARG          
SEQRES  27 B  376  GLU CYS THR MET PRO PRO LEU SER PHE ARG ALA LYS ASP          
SEQRES  28 B  376  GLY CYS TRP TYR GLY MET GLU ILE ARG PRO ARG LYS GLU          
SEQRES  29 B  376  PRO GLU SER ASN LEU VAL ARG SER MET VAL THR ALA              
HET    NAG  A 401      14                                                       
HET    NAG  A 402      14                                                       
HET    SO4  A 403       5                                                       
HET    NAG  B 401      14                                                       
HET    NAG  B 402      14                                                       
HET    SO4  B 403       5                                                       
HET    SO4  B 404       5                                                       
HET    SO4  B 405       5                                                       
HET    SO4  B 406       5                                                       
HET    GOL  B 407       6                                                       
HET    GOL  B 408       6                                                       
HET    GOL  B 409       6                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  NAG    4(C8 H15 N O6)                                               
FORMUL   5  SO4    5(O4 S 2-)                                                   
FORMUL  12  GOL    3(C3 H8 O3)                                                  
FORMUL  15  HOH   *1047(H2 O)                                                   
HELIX    1 AA1 SER A   38  GLU A   52  1                                  15    
HELIX    2 AA2 SER A   61  ASN A   82  1                                  22    
HELIX    3 AA3 PRO A  144  GLU A  146  5                                   3    
HELIX    4 AA4 ASP A  180  VAL A  183  5                                   4    
HELIX    5 AA5 PRO A  226  THR A  230  5                                   5    
HELIX    6 AA6 GLU A  237  LEU A  241  5                                   5    
HELIX    7 AA7 PRO A  244  ALA A  248  5                                   5    
HELIX    8 AA8 SER A  252  THR A  256  5                                   5    
HELIX    9 AA9 PRO A  341  LEU A  345  5                                   5    
HELIX   10 AB1 SER B   38  GLU B   52  1                                  15    
HELIX   11 AB2 SER B   61  ASN B   82  1                                  22    
HELIX   12 AB3 GLY B  119  PHE B  123  5                                   5    
HELIX   13 AB4 PRO B  144  GLU B  146  5                                   3    
HELIX   14 AB5 ASP B  180  VAL B  183  5                                   4    
HELIX   15 AB6 PRO B  226  THR B  230  5                                   5    
HELIX   16 AB7 GLU B  237  LEU B  241  5                                   5    
HELIX   17 AB8 PRO B  244  ALA B  248  5                                   5    
HELIX   18 AB9 SER B  252  THR B  256  5                                   5    
HELIX   19 AC1 PRO B  341  LEU B  345  5                                   5    
SHEET    1 AA1 5 ASP A   1  ASP A   7  0                                        
SHEET    2 AA1 5 GLU A  12  TYR A  22 -1  O  GLU A  12   N  ASP A   7           
SHEET    3 AA1 5 GLU B  12  TYR B  22 -1  O  ILE B  21   N  VAL A  19           
SHEET    4 AA1 5 ASP B   1  ASP B   7 -1  N  ASP B   7   O  GLU B  12           
SHEET    5 AA1 5 ASP A   1  ASP A   7 -1  N  VAL A   6   O  VAL B   2           
SHEET    1 AA2 3 TYR A  32  PRO A  36  0                                        
SHEET    2 AA2 3 THR A 165  VAL A 171  1  O  VAL A 167   N  HIS A  35           
SHEET    3 AA2 3 PHE A 153  GLY A 159 -1  N  GLU A 156   O  TRP A 168           
SHEET    1 AA3 4 THR A  87  VAL A  90  0                                        
SHEET    2 AA3 4 SER A 132  VAL A 135  1  O  PHE A 133   N  THR A  87           
SHEET    3 AA3 4 GLY A  56  ILE A  57  1  N  ILE A  57   O  VAL A 134           
SHEET    4 AA3 4 ARG A 148  ALA A 149  1  O  ALA A 149   N  GLY A  56           
SHEET    1 AA414 GLY A 328  TYR A 331  0                                        
SHEET    2 AA414 LEU A 321  ALA A 325 -1  N  PHE A 323   O  TRP A 330           
SHEET    3 AA414 LEU A 273  PHE A 277 -1  N  GLU A 274   O  ARG A 324           
SHEET    4 AA414 TRP A 210  LEU A 217 -1  N  LEU A 217   O  LEU A 273           
SHEET    5 AA414 TYR A 200  LYS A 206 -1  N  GLU A 203   O  LYS A 213           
SHEET    6 AA414 GLU A 192  SER A 196 -1  N  HIS A 195   O  ILE A 202           
SHEET    7 AA414 GLY A 185  LYS A 189 -1  N  ALA A 187   O  ALA A 194           
SHEET    8 AA414 GLY B 185  LYS B 189 -1  O  VAL B 188   N  THR A 186           
SHEET    9 AA414 GLU B 192  SER B 196 -1  O  ALA B 194   N  ALA B 187           
SHEET   10 AA414 TYR B 200  LYS B 206 -1  O  ILE B 202   N  HIS B 195           
SHEET   11 AA414 TRP B 210  LEU B 217 -1  O  LYS B 213   N  GLU B 203           
SHEET   12 AA414 LEU B 273  PHE B 277 -1  O  ILE B 275   N  ALA B 215           
SHEET   13 AA414 LEU B 321  ALA B 325 -1  O  ARG B 324   N  GLU B 274           
SHEET   14 AA414 GLY B 328  TYR B 331 -1  O  GLY B 328   N  ALA B 325           
SHEET    1 AA5 3 LYS A 284  VAL A 287  0                                        
SHEET    2 AA5 3 GLU A 310  CYS A 313  1  O  TRP A 311   N  LYS A 284           
SHEET    3 AA5 3 ARG A 336  PRO A 337 -1  O  ARG A 336   N  CYS A 312           
SHEET    1 AA6 3 TYR B  32  PRO B  36  0                                        
SHEET    2 AA6 3 THR B 165  VAL B 171  1  O  LEU B 169   N  HIS B  35           
SHEET    3 AA6 3 PHE B 153  GLY B 159 -1  N  GLU B 156   O  TRP B 168           
SHEET    1 AA7 4 THR B  87  VAL B  90  0                                        
SHEET    2 AA7 4 SER B 132  VAL B 135  1  O  VAL B 135   N  VAL B  89           
SHEET    3 AA7 4 GLY B  56  ILE B  57  1  N  ILE B  57   O  VAL B 134           
SHEET    4 AA7 4 ARG B 148  ALA B 149  1  O  ALA B 149   N  GLY B  56           
SHEET    1 AA8 3 LYS B 284  VAL B 287  0                                        
SHEET    2 AA8 3 GLU B 310  CYS B 313  1  O  TRP B 311   N  LYS B 284           
SHEET    3 AA8 3 ARG B 336  PRO B 337 -1  O  ARG B 336   N  CYS B 312           
SSBOND   1 CYS A    4    CYS A   15                          1555   1555  2.05  
SSBOND   2 CYS A   55    CYS A  143                          1555   1555  2.04  
SSBOND   3 CYS A  179    CYS A  223                          1555   1555  2.06  
SSBOND   4 CYS A  280    CYS A  329                          1555   1555  2.05  
SSBOND   5 CYS A  291    CYS A  312                          1555   1555  2.08  
SSBOND   6 CYS A  313    CYS A  316                          1555   1555  2.05  
SSBOND   7 CYS B    4    CYS B   15                          1555   1555  2.03  
SSBOND   8 CYS B   55    CYS B  143                          1555   1555  2.03  
SSBOND   9 CYS B  179    CYS B  223                          1555   1555  2.07  
SSBOND  10 CYS B  280    CYS B  329                          1555   1555  2.06  
SSBOND  11 CYS B  291    CYS B  312                          1555   1555  2.07  
SSBOND  12 CYS B  313    CYS B  316                          1555   1555  2.05  
LINK         ND2 ASN A 130                 C1  NAG A 401     1555   1555  1.43  
LINK         ND2 ASN A 207                 C1  NAG A 402     1555   1555  1.44  
LINK         ND2 ASN B 130                 C1  NAG B 401     1555   1555  1.44  
LINK         ND2 ASN B 207                 C1  NAG B 402     1555   1555  1.44  
CISPEP   1 ASN A   95    PRO A   96          0        -5.82                     
CISPEP   2 MET A  318    PRO A  319          0        -4.47                     
CISPEP   3 ASN B   95    PRO B   96          0        -6.85                     
CISPEP   4 MET B  318    PRO B  319          0        -2.59                     
SITE     1 AC1  4 ARG A 261  ARG A 294  HOH A 507  HOH A 509                    
SITE     1 AC2 10 ALA A 303  SER A 304  PRO B 341  GLU B 342                    
SITE     2 AC2 10 SER B 343  HOH B 544  HOH B 584  HOH B 603                    
SITE     3 AC2 10 HOH B 643  HOH B 660                                          
SITE     1 AC3  5 THR B 302  SER B 304  ARG B 306  HOH B 524                    
SITE     2 AC3  5 HOH B 540                                                     
SITE     1 AC4  5 ARG B 261  ARG B 294  HOH B 507  HOH B 563                    
SITE     2 AC4  5 HOH B 853                                                     
SITE     1 AC5  6 ARG B 261  THR B 293  ARG B 294  ARG B 314                    
SITE     2 AC5  6 HOH B 507  HOH B 734                                          
SITE     1 AC6  6 GLU A 224  LYS A 245  GLU B  52  GLY B  53                    
SITE     2 AC6  6 GLN B 102  HIS B 147                                          
SITE     1 AC7  6 GLY A  53  LYS B 265  THR B 351  HOH B 504                    
SITE     2 AC7  6 HOH B 688  HOH B 861                                          
SITE     1 AC8  4 SER B  92  GLY B 137  ASP B 138  HOH B 666                    
SITE     1 AC9 12 ASN A 130  ARG A 299  ALA A 303  ASP A 327                    
SITE     2 AC9 12 HOH A 520  HOH A 584  HOH A 686  HOH A 706                    
SITE     3 AC9 12 HOH A 714  HOH A 775  HOH A 801  HOH A 940                    
SITE     1 AD1  6 ARG A 191  ASN A 207  ASP A 208  ARG A 211                    
SITE     2 AD1  6 HOH A 526  HOH A 850                                          
SITE     1 AD2  2 ASN B 130  HOH B 838                                          
SITE     1 AD3  4 ASN B 207  ARG B 211  HOH B 502  HOH B 602                    
CRYST1   96.160  130.440  147.950  90.00  90.00  90.00 I 2 2 2      16          
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      0.010399  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007666  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006759        0.00000                         
ATOM      1  N   TYR A  -5     -11.456 -55.993 -25.849  1.00 82.90           N  
ANISOU    1  N   TYR A  -5    10022   9573  11905    101    195  -1359       N  
ATOM      2  CA  TYR A  -5     -10.583 -55.278 -24.922  1.00 75.76           C  
ANISOU    2  CA  TYR A  -5     9103   8660  11020    183    143  -1220       C  
ATOM      3  C   TYR A  -5     -11.208 -53.962 -24.461  1.00 73.11           C  
ANISOU    3  C   TYR A  -5     8873   8480  10426    159    102  -1024       C  
ATOM      4  O   TYR A  -5     -11.045 -53.562 -23.308  1.00 71.79           O  
ANISOU    4  O   TYR A  -5     8727   8279  10269    216     20   -847       O  
ATOM      5  CB  TYR A  -5      -9.221 -55.009 -25.563  1.00 72.23           C  
ANISOU    5  CB  TYR A  -5     8561   8259  10623    199    233  -1391       C  
ATOM      6  N   PHE A  -4     -11.918 -53.287 -25.368  1.00 65.19           N  
ANISOU    6  N   PHE A  -4     7925   7645   9199     68    157  -1059       N  
ATOM      7  CA  PHE A  -4     -12.580 -52.024 -25.054  1.00 62.65           C  
ANISOU    7  CA  PHE A  -4     7688   7455   8660     44    121   -891       C  
ATOM      8  C   PHE A  -4     -14.082 -52.075 -25.301  1.00 50.46           C  
ANISOU    8  C   PHE A  -4     6213   5963   6995    -25    101   -831       C  
ATOM      9  O   PHE A  -4     -14.738 -51.025 -25.300  1.00 49.87           O  
ANISOU    9  O   PHE A  -4     6194   6006   6748    -57     83   -719       O  
ATOM     10  CB  PHE A  -4     -11.952 -50.876 -25.853  1.00 71.29           C  
ANISOU   10  CB  PHE A  -4     8774   8714   9598     -3    184   -941       C  
ATOM     11  CG  PHE A  -4     -10.499 -50.651 -25.539  1.00 74.66           C  
ANISOU   11  CG  PHE A  -4     9135   9110  10124     63    200   -979       C  
ATOM     12  CD1 PHE A  -4      -9.508 -51.329 -26.241  1.00 77.21           C  
ANISOU   12  CD1 PHE A  -4     9361   9403  10571     61    278  -1180       C  
ATOM     13  CD2 PHE A  -4     -10.124 -49.777 -24.529  1.00 69.13           C  
ANISOU   13  CD2 PHE A  -4     8459   8409   9400    121    140   -824       C  
ATOM     14  CE1 PHE A  -4      -8.166 -51.131 -25.946  1.00 79.43           C  
ANISOU   14  CE1 PHE A  -4     9569   9656  10956    123    291  -1213       C  
ATOM     15  CE2 PHE A  -4      -8.786 -49.571 -24.229  1.00 66.87           C  
ANISOU   15  CE2 PHE A  -4     8108   8097   9202    175    147   -851       C  
ATOM     16  CZ  PHE A  -4      -7.805 -50.248 -24.938  1.00 74.36           C  
ANISOU   16  CZ  PHE A  -4     8957   9017  10280    179    220  -1038       C  
ATOM     17  N   GLN A  -3     -14.644 -53.265 -25.499  1.00 38.97           N  
ANISOU   17  N   GLN A  -3     4748   4416   5643    -47     99   -900       N  
ATOM     18  CA  GLN A  -3     -16.069 -53.412 -25.755  1.00 48.35           C  
ANISOU   18  CA  GLN A  -3     5994   5652   6727   -119     79   -848       C  
ATOM     19  C   GLN A  -3     -16.876 -53.234 -24.476  1.00 41.45           C  
ANISOU   19  C   GLN A  -3     5170   4735   5845    -75    -12   -639       C  
ATOM     20  O   GLN A  -3     -16.636 -53.920 -23.475  1.00 39.51           O  
ANISOU   20  O   GLN A  -3     4908   4351   5753    -14    -70   -573       O  
ATOM     21  CB  GLN A  -3     -16.365 -54.780 -26.364  1.00 44.44           C  
ANISOU   21  CB  GLN A  -3     5467   5064   6354   -164    107  -1000       C  
ATOM     22  CG  GLN A  -3     -16.521 -54.749 -27.856  1.00 57.20           C  
ANISOU   22  CG  GLN A  -3     7071   6819   7844   -283    196  -1176       C  
ATOM     23  CD  GLN A  -3     -15.482 -55.565 -28.557  1.00 70.84           C  
ANISOU   23  CD  GLN A  -3     8712   8485   9718   -289    282  -1424       C  
ATOM     24  OE1 GLN A  -3     -14.377 -55.088 -28.821  1.00 84.70           O  
ANISOU   24  OE1 GLN A  -3    10419  10292  11472   -269    336  -1504       O  
ATOM     25  NE2 GLN A  -3     -15.822 -56.814 -28.864  1.00 66.48           N  
ANISOU   25  NE2 GLN A  -3     8131   7818   9308   -319    298  -1559       N  
ATOM     26  N   SER A  -2     -17.854 -52.331 -24.530  1.00 32.07           N  
ANISOU   26  N   SER A  -2     4034   3669   4483   -116    -26   -535       N  
ATOM     27  CA  SER A  -2     -18.723 -52.037 -23.398  1.00 35.37           C  
ANISOU   27  CA  SER A  -2     4491   4079   4868    -89    -93   -361       C  
ATOM     28  C   SER A  -2     -20.211 -52.212 -23.703  1.00 39.29           C  
ANISOU   28  C   SER A  -2     5019   4628   5282   -158   -108   -315       C  
ATOM     29  O   SER A  -2     -21.040 -51.938 -22.826  1.00 34.40           O  
ANISOU   29  O   SER A  -2     4423   4022   4627   -146   -153   -184       O  
ATOM     30  CB  SER A  -2     -18.461 -50.606 -22.913  1.00 35.32           C  
ANISOU   30  CB  SER A  -2     4501   4159   4761    -52    -99   -268       C  
ATOM     31  OG  SER A  -2     -18.341 -49.736 -24.030  1.00 35.16           O  
ANISOU   31  OG  SER A  -2     4479   4257   4625   -101    -54   -323       O  
ATOM     32  N   ASN A  -1     -20.574 -52.643 -24.917  1.00 37.21           N  
ANISOU   32  N   ASN A  -1     4750   4407   4981   -240    -70   -426       N  
ATOM     33  CA  ASN A  -1     -21.964 -52.888 -25.294  1.00 35.75           C  
ANISOU   33  CA  ASN A  -1     4588   4275   4722   -318    -89   -388       C  
ATOM     34  C   ASN A  -1     -22.461 -54.269 -24.893  1.00 34.84           C  
ANISOU   34  C   ASN A  -1     4472   4032   4733   -328   -121   -397       C  
ATOM     35  O   ASN A  -1     -23.652 -54.558 -25.076  1.00 29.86           O  
ANISOU   35  O   ASN A  -1     3859   3436   4051   -392   -143   -355       O  
ATOM     36  CB  ASN A  -1     -22.165 -52.733 -26.812  1.00 32.47           C  
ANISOU   36  CB  ASN A  -1     4165   3982   4189   -427    -41   -496       C  
ATOM     37  CG  ASN A  -1     -22.153 -51.268 -27.273  1.00 30.50           C  
ANISOU   37  CG  ASN A  -1     3919   3882   3789   -451    -38   -427       C  
ATOM     38  OD1 ASN A  -1     -22.210 -50.350 -26.463  1.00 34.33           O  
ANISOU   38  OD1 ASN A  -1     4413   4369   4262   -383    -71   -302       O  
ATOM     39  ND2 ASN A  -1     -22.089 -51.062 -28.585  1.00 29.29           N  
ANISOU   39  ND2 ASN A  -1     3753   3852   3523   -561     -2   -510       N  
ATOM     40  N   ALA A   0     -21.585 -55.132 -24.372  1.00 35.20           N  
ANISOU   40  N   ALA A   0     4491   3928   4955   -272   -131   -443       N  
ATOM     41  CA  ALA A   0     -21.946 -56.518 -24.088  1.00 34.48           C  
ANISOU   41  CA  ALA A   0     4390   3691   5019   -289   -170   -457       C  
ATOM     42  C   ALA A   0     -21.548 -56.931 -22.673  1.00 32.63           C  
ANISOU   42  C   ALA A   0     4144   3327   4925   -217   -246   -326       C  
ATOM     43  O   ALA A   0     -21.183 -58.092 -22.441  1.00 35.77           O  
ANISOU   43  O   ALA A   0     4508   3558   5524   -204   -282   -357       O  
ATOM     44  CB  ALA A   0     -21.321 -57.469 -25.110  1.00 31.36           C  
ANISOU   44  CB  ALA A   0     3952   3213   4749   -319   -115   -674       C  
ATOM     45  N   ASP A   1     -21.594 -55.992 -21.727  1.00 29.05           N  
ANISOU   45  N   ASP A   1     3712   2949   4376   -178   -274   -179       N  
ATOM     46  CA  ASP A   1     -21.501 -56.345 -20.320  1.00 29.50           C  
ANISOU   46  CA  ASP A   1     3764   2930   4514   -148   -355    -26       C  
ATOM     47  C   ASP A   1     -22.700 -57.213 -19.940  1.00 30.12           C  
ANISOU   47  C   ASP A   1     3857   2973   4614   -214   -410     63       C  
ATOM     48  O   ASP A   1     -23.713 -57.252 -20.639  1.00 29.68           O  
ANISOU   48  O   ASP A   1     3822   2981   4474   -274   -383     26       O  
ATOM     49  CB  ASP A   1     -21.445 -55.080 -19.445  1.00 31.88           C  
ANISOU   49  CB  ASP A   1     4086   3352   4676   -116   -359     87       C  
ATOM     50  CG  ASP A   1     -20.097 -54.329 -19.537  1.00 35.80           C  
ANISOU   50  CG  ASP A   1     4562   3857   5182    -49   -326     30       C  
ATOM     51  OD1 ASP A   1     -19.172 -54.800 -20.233  1.00 34.41           O  
ANISOU   51  OD1 ASP A   1     4351   3600   5123    -24   -299    -94       O  
ATOM     52  OD2 ASP A   1     -19.967 -53.267 -18.887  1.00 34.03           O  
ANISOU   52  OD2 ASP A   1     4352   3723   4853    -25   -325    101       O  
ATOM     53  N   VAL A   2     -22.573 -57.955 -18.844  1.00 29.85           N  
ANISOU   53  N   VAL A   2     3808   2838   4697   -215   -496    190       N  
ATOM     54  CA  VAL A   2     -23.689 -58.737 -18.323  1.00 28.81           C  
ANISOU   54  CA  VAL A   2     3687   2684   4577   -290   -559    304       C  
ATOM     55  C   VAL A   2     -23.927 -58.288 -16.893  1.00 31.47           C  
ANISOU   55  C   VAL A   2     4031   3107   4820   -307   -613    491       C  
ATOM     56  O   VAL A   2     -22.978 -57.958 -16.177  1.00 28.83           O  
ANISOU   56  O   VAL A   2     3681   2763   4510   -264   -640    545       O  
ATOM     57  CB  VAL A   2     -23.455 -60.261 -18.404  1.00 36.83           C  
ANISOU   57  CB  VAL A   2     4668   3487   5838   -310   -625    288       C  
ATOM     58  CG1 VAL A   2     -23.561 -60.733 -19.856  1.00 39.73           C  
ANISOU   58  CG1 VAL A   2     5030   3802   6264   -326   -556     78       C  
ATOM     59  CG2 VAL A   2     -22.114 -60.648 -17.824  1.00 35.42           C  
ANISOU   59  CG2 VAL A   2     4439   3164   5854   -246   -684    320       C  
ATOM     60  N   GLY A   3     -25.192 -58.230 -16.493  1.00 29.17           N  
ANISOU   60  N   GLY A   3     3758   2916   4408   -377   -623    581       N  
ATOM     61  CA  GLY A   3     -25.474 -57.778 -15.147  1.00 31.61           C  
ANISOU   61  CA  GLY A   3     4067   3338   4607   -412   -657    735       C  
ATOM     62  C   GLY A   3     -26.931 -57.965 -14.806  1.00 33.96           C  
ANISOU   62  C   GLY A   3     4369   3732   4802   -503   -665    817       C  
ATOM     63  O   GLY A   3     -27.725 -58.475 -15.602  1.00 29.58           O  
ANISOU   63  O   GLY A   3     3822   3150   4269   -537   -654    767       O  
ATOM     64  N   CYS A   4     -27.265 -57.552 -13.588  1.00 27.13           N  
ANISOU   64  N   CYS A   4     3495   2993   3818   -551   -683    937       N  
ATOM     65  CA  CYS A   4     -28.625 -57.616 -13.077  1.00 30.00           C  
ANISOU   65  CA  CYS A   4     3850   3483   4068   -645   -681   1017       C  
ATOM     66  C   CYS A   4     -28.913 -56.306 -12.371  1.00 33.93           C  
ANISOU   66  C   CYS A   4     4333   4171   4387   -640   -612   1012       C  
ATOM     67  O   CYS A   4     -28.009 -55.676 -11.815  1.00 32.15           O  
ANISOU   67  O   CYS A   4     4107   3974   4133   -602   -606   1011       O  
ATOM     68  CB  CYS A   4     -28.848 -58.775 -12.102  1.00 32.26           C  
ANISOU   68  CB  CYS A   4     4121   3729   4407   -756   -789   1191       C  
ATOM     69  SG  CYS A   4     -28.385 -60.411 -12.691  1.00 38.86           S  
ANISOU   69  SG  CYS A   4     4957   4300   5509   -766   -892   1214       S  
ATOM     70  N   SER A   5     -30.179 -55.907 -12.370  1.00 26.40           N  
ANISOU   70  N   SER A   5     3360   3346   3326   -681   -560   1002       N  
ATOM     71  CA  SER A   5     -30.491 -54.615 -11.785  1.00 27.84           C  
ANISOU   71  CA  SER A   5     3514   3694   3370   -666   -482    963       C  
ATOM     72  C   SER A   5     -31.949 -54.589 -11.368  1.00 34.82           C  
ANISOU   72  C   SER A   5     4354   4719   4158   -751   -451    997       C  
ATOM     73  O   SER A   5     -32.773 -55.368 -11.859  1.00 33.13           O  
ANISOU   73  O   SER A   5     4137   4472   3977   -799   -477   1029       O  
ATOM     74  CB  SER A   5     -30.202 -53.472 -12.762  1.00 32.64           C  
ANISOU   74  CB  SER A   5     4127   4291   3983   -553   -409    827       C  
ATOM     75  OG  SER A   5     -31.084 -53.569 -13.865  1.00 32.21           O  
ANISOU   75  OG  SER A   5     4067   4220   3950   -547   -390    781       O  
ATOM     76  N   VAL A   6     -32.241 -53.690 -10.432  1.00 29.80           N  
ANISOU   76  N   VAL A   6     3676   4243   3402   -774   -390    980       N  
ATOM     77  CA  VAL A   6     -33.606 -53.367 -10.043  1.00 34.66           C  
ANISOU   77  CA  VAL A   6     4229   5015   3927   -837   -330    971       C  
ATOM     78  C   VAL A   6     -33.984 -52.146 -10.862  1.00 40.23           C  
ANISOU   78  C   VAL A   6     4902   5732   4653   -730   -247    839       C  
ATOM     79  O   VAL A   6     -33.375 -51.079 -10.717  1.00 37.16           O  
ANISOU   79  O   VAL A   6     4506   5359   4255   -657   -198    757       O  
ATOM     80  CB  VAL A   6     -33.731 -53.099  -8.539  1.00 35.52           C  
ANISOU   80  CB  VAL A   6     4295   5303   3899   -939   -303   1007       C  
ATOM     81  CG1 VAL A   6     -35.185 -52.850  -8.170  1.00 35.72           C  
ANISOU   81  CG1 VAL A   6     4239   5493   3839  -1010   -232    981       C  
ATOM     82  CG2 VAL A   6     -33.162 -54.254  -7.753  1.00 37.91           C  
ANISOU   82  CG2 VAL A   6     4630   5584   4190  -1050   -410   1167       C  
ATOM     83  N   ASP A   7     -34.954 -52.322 -11.756  1.00 33.50           N  
ANISOU   83  N   ASP A   7     4027   4861   3839   -725   -243    828       N  
ATOM     84  CA  ASP A   7     -35.346 -51.299 -12.720  1.00 34.90           C  
ANISOU   84  CA  ASP A   7     4170   5028   4061   -634   -193    737       C  
ATOM     85  C   ASP A   7     -36.628 -50.664 -12.197  1.00 35.25           C  
ANISOU   85  C   ASP A   7     4113   5218   4064   -663   -124    707       C  
ATOM     86  O   ASP A   7     -37.717 -51.209 -12.376  1.00 37.46           O  
ANISOU   86  O   ASP A   7     4354   5541   4338   -725   -134    751       O  
ATOM     87  CB  ASP A   7     -35.537 -51.925 -14.098  1.00 40.17           C  
ANISOU   87  CB  ASP A   7     4873   5590   4798   -625   -243    750       C  
ATOM     88  CG  ASP A   7     -35.597 -50.898 -15.204  1.00 45.40           C  
ANISOU   88  CG  ASP A   7     5515   6229   5506   -539   -218    680       C  
ATOM     89  OD1 ASP A   7     -36.270 -49.857 -15.014  1.00 41.67           O  
ANISOU   89  OD1 ASP A   7     4964   5834   5034   -507   -166    645       O  
ATOM     90  OD2 ASP A   7     -34.968 -51.141 -16.261  1.00 52.66           O  
ANISOU   90  OD2 ASP A   7     6489   7053   6467   -513   -252    662       O  
ATOM     91  N   PHE A   8     -36.499 -49.519 -11.527  1.00 37.86           N  
ANISOU   91  N   PHE A   8     4391   5623   4373   -621    -51    623       N  
ATOM     92  CA  PHE A   8     -37.653 -48.976 -10.824  1.00 40.36           C  
ANISOU   92  CA  PHE A   8     4594   6085   4655   -658     29    571       C  
ATOM     93  C   PHE A   8     -38.719 -48.481 -11.795  1.00 44.92           C  
ANISOU   93  C   PHE A   8     5095   6644   5329   -604     43    545       C  
ATOM     94  O   PHE A   8     -39.920 -48.633 -11.529  1.00 43.69           O  
ANISOU   94  O   PHE A   8     4852   6588   5160   -661     75    550       O  
ATOM     95  CB  PHE A   8     -37.211 -47.866  -9.867  1.00 45.80           C  
ANISOU   95  CB  PHE A   8     5241   6851   5312   -630    111    460       C  
ATOM     96  CG  PHE A   8     -36.498 -48.375  -8.647  1.00 52.46           C  
ANISOU   96  CG  PHE A   8     6128   7778   6027   -728    103    498       C  
ATOM     97  CD1 PHE A   8     -37.201 -49.006  -7.630  1.00 51.44           C  
ANISOU   97  CD1 PHE A   8     5954   7810   5780   -870    122    543       C  
ATOM     98  CD2 PHE A   8     -35.122 -48.234  -8.523  1.00 53.46           C  
ANISOU   98  CD2 PHE A   8     6333   7832   6148   -691     69    501       C  
ATOM     99  CE1 PHE A   8     -36.543 -49.481  -6.500  1.00 52.78           C  
ANISOU   99  CE1 PHE A   8     6161   8073   5822   -983     99    603       C  
ATOM    100  CE2 PHE A   8     -34.455 -48.711  -7.399  1.00 51.51           C  
ANISOU  100  CE2 PHE A   8     6119   7667   5786   -792     46    557       C  
ATOM    101  CZ  PHE A   8     -35.171 -49.333  -6.384  1.00 52.38           C  
ANISOU  101  CZ  PHE A   8     6186   7943   5773   -943     56    615       C  
ATOM    102  N   SER A   9     -38.313 -47.913 -12.936  1.00 41.55           N  
ANISOU  102  N   SER A   9     4693   6100   4996   -508     12    529       N  
ATOM    103  CA  SER A   9     -39.321 -47.366 -13.844  1.00 49.65           C  
ANISOU  103  CA  SER A   9     5634   7115   6118   -467     10    525       C  
ATOM    104  C   SER A   9     -40.011 -48.453 -14.667  1.00 50.99           C  
ANISOU  104  C   SER A   9     5827   7271   6277   -536    -57    619       C  
ATOM    105  O   SER A   9     -41.184 -48.295 -15.030  1.00 47.35           O  
ANISOU  105  O   SER A   9     5273   6855   5862   -550    -55    637       O  
ATOM    106  CB  SER A   9     -38.707 -46.304 -14.766  1.00 46.94           C  
ANISOU  106  CB  SER A   9     5296   6668   5873   -362     -9    493       C  
ATOM    107  OG  SER A   9     -37.829 -46.877 -15.709  1.00 55.06           O  
ANISOU  107  OG  SER A   9     6436   7603   6883   -362    -79    543       O  
ATOM    108  N   LYS A  10     -39.326 -49.559 -14.958  1.00 43.68           N  
ANISOU  108  N   LYS A  10     5013   6279   5303   -583   -118    675       N  
ATOM    109  CA  LYS A  10     -39.965 -50.673 -15.647  1.00 37.41           C  
ANISOU  109  CA  LYS A  10     4243   5469   4501   -662   -177    748       C  
ATOM    110  C   LYS A  10     -40.537 -51.715 -14.690  1.00 41.91           C  
ANISOU  110  C   LYS A  10     4807   6115   5003   -773   -179    807       C  
ATOM    111  O   LYS A  10     -41.040 -52.743 -15.153  1.00 40.29           O  
ANISOU  111  O   LYS A  10     4626   5889   4795   -850   -233    870       O  
ATOM    112  CB  LYS A  10     -38.988 -51.340 -16.626  1.00 37.26           C  
ANISOU  112  CB  LYS A  10     4335   5325   4495   -658   -241    758       C  
ATOM    113  CG  LYS A  10     -38.556 -50.445 -17.791  1.00 35.88           C  
ANISOU  113  CG  LYS A  10     4165   5098   4369   -584   -251    719       C  
ATOM    114  CD  LYS A  10     -38.026 -51.264 -18.973  1.00 37.82           C  
ANISOU  114  CD  LYS A  10     4494   5261   4614   -620   -307    718       C  
ATOM    115  CE  LYS A  10     -37.625 -50.376 -20.156  1.00 43.59           C  
ANISOU  115  CE  LYS A  10     5224   5972   5366   -576   -320    692       C  
ATOM    116  NZ  LYS A  10     -37.394 -51.164 -21.429  1.00 47.26           N  
ANISOU  116  NZ  LYS A  10     5749   6399   5810   -643   -364    677       N  
ATOM    117  N   LYS A  11     -40.479 -51.476 -13.371  1.00 39.64           N  
ANISOU  117  N   LYS A  11     4484   5922   4655   -797   -125    789       N  
ATOM    118  CA  LYS A  11     -41.185 -52.318 -12.400  1.00 43.71           C  
ANISOU  118  CA  LYS A  11     4969   6548   5089   -923   -121    855       C  
ATOM    119  C   LYS A  11     -40.702 -53.769 -12.455  1.00 42.82           C  
ANISOU  119  C   LYS A  11     4957   6349   4964  -1006   -214    960       C  
ATOM    120  O   LYS A  11     -41.499 -54.714 -12.425  1.00 40.04           O  
ANISOU  120  O   LYS A  11     4594   6025   4595  -1110   -252   1039       O  
ATOM    121  CB  LYS A  11     -42.702 -52.250 -12.614  1.00 45.77           C  
ANISOU  121  CB  LYS A  11     5120   6907   5363   -965    -95    861       C  
ATOM    122  CG  LYS A  11     -43.413 -51.104 -11.913  1.00 58.80           C  
ANISOU  122  CG  LYS A  11     6633   8692   7015   -934     11    766       C  
ATOM    123  CD  LYS A  11     -43.078 -49.765 -12.523  1.00 66.77           C  
ANISOU  123  CD  LYS A  11     7608   9629   8133   -791     42    672       C  
ATOM    124  CE  LYS A  11     -44.066 -48.696 -12.082  1.00 75.57           C  
ANISOU  124  CE  LYS A  11     8557  10849   9309   -755    137    574       C  
ATOM    125  NZ  LYS A  11     -43.709 -47.360 -12.641  1.00 77.28           N  
ANISOU  125  NZ  LYS A  11     8731  10971   9659   -616    154    494       N  
ATOM    126  N   GLU A  12     -39.387 -53.954 -12.549  1.00 34.33           N  
ANISOU  126  N   GLU A  12     3972   5155   3915   -961   -254    959       N  
ATOM    127  CA  GLU A  12     -38.847 -55.294 -12.715  1.00 36.64           C  
ANISOU  127  CA  GLU A  12     4348   5328   4246  -1020   -346   1044       C  
ATOM    128  C   GLU A  12     -37.444 -55.352 -12.136  1.00 40.09           C  
ANISOU  128  C   GLU A  12     4845   5696   4690   -991   -373   1056       C  
ATOM    129  O   GLU A  12     -36.728 -54.348 -12.082  1.00 36.54           O  
ANISOU  129  O   GLU A  12     4398   5251   4235   -900   -326    978       O  
ATOM    130  CB  GLU A  12     -38.828 -55.725 -14.199  1.00 37.31           C  
ANISOU  130  CB  GLU A  12     4478   5277   4421   -985   -388   1013       C  
ATOM    131  CG  GLU A  12     -37.985 -54.831 -15.099  1.00 30.06           C  
ANISOU  131  CG  GLU A  12     3588   4287   3545   -863   -363    914       C  
ATOM    132  CD  GLU A  12     -38.121 -55.167 -16.586  1.00 38.39           C  
ANISOU  132  CD  GLU A  12     4673   5259   4655   -858   -393    876       C  
ATOM    133  OE1 GLU A  12     -38.858 -56.120 -16.926  1.00 34.89           O  
ANISOU  133  OE1 GLU A  12     4231   4801   4225   -944   -434    917       O  
ATOM    134  OE2 GLU A  12     -37.495 -54.468 -17.418  1.00 38.56           O  
ANISOU  134  OE2 GLU A  12     4712   5240   4697   -781   -377    804       O  
ATOM    135  N   THR A  13     -37.076 -56.542 -11.682  1.00 32.16           N  
ANISOU  135  N   THR A  13     3882   4625   3712  -1075   -456   1164       N  
ATOM    136  CA  THR A  13     -35.699 -56.892 -11.367  1.00 31.51           C  
ANISOU  136  CA  THR A  13     3857   4430   3685  -1050   -514   1198       C  
ATOM    137  C   THR A  13     -35.306 -57.979 -12.353  1.00 33.70           C  
ANISOU  137  C   THR A  13     4188   4506   4111  -1037   -590   1205       C  
ATOM    138  O   THR A  13     -36.000 -58.995 -12.462  1.00 35.01           O  
ANISOU  138  O   THR A  13     4351   4635   4314  -1128   -644   1277       O  
ATOM    139  CB  THR A  13     -35.569 -57.384  -9.922  1.00 38.67           C  
ANISOU  139  CB  THR A  13     4749   5424   4520  -1171   -563   1335       C  
ATOM    140  OG1 THR A  13     -36.079 -56.384  -9.029  1.00 40.98           O  
ANISOU  140  OG1 THR A  13     4981   5930   4661  -1202   -473   1297       O  
ATOM    141  CG2 THR A  13     -34.109 -57.671  -9.576  1.00 34.33           C  
ANISOU  141  CG2 THR A  13     4245   4758   4040  -1142   -632   1383       C  
ATOM    142  N   ARG A  14     -34.234 -57.756 -13.103  1.00 35.27           N  
ANISOU  142  N   ARG A  14     4427   4579   4395   -932   -586   1117       N  
ATOM    143  CA  ARG A  14     -33.907 -58.691 -14.169  1.00 34.51           C  
ANISOU  143  CA  ARG A  14     4369   4303   4440   -919   -633   1076       C  
ATOM    144  C   ARG A  14     -32.417 -58.633 -14.457  1.00 37.94           C  
ANISOU  144  C   ARG A  14     4836   4606   4975   -826   -645   1013       C  
ATOM    145  O   ARG A  14     -31.682 -57.790 -13.925  1.00 29.09           O  
ANISOU  145  O   ARG A  14     3713   3536   3805   -769   -616   1003       O  
ATOM    146  CB  ARG A  14     -34.733 -58.402 -15.443  1.00 29.62           C  
ANISOU  146  CB  ARG A  14     3745   3709   3801   -903   -585    976       C  
ATOM    147  CG  ARG A  14     -34.776 -56.932 -15.863  1.00 28.02           C  
ANISOU  147  CG  ARG A  14     3521   3611   3512   -817   -501    887       C  
ATOM    148  CD  ARG A  14     -33.551 -56.471 -16.665  1.00 31.81           C  
ANISOU  148  CD  ARG A  14     4037   4004   4044   -719   -479    780       C  
ATOM    149  NE  ARG A  14     -33.219 -57.326 -17.811  1.00 28.92           N  
ANISOU  149  NE  ARG A  14     3705   3511   3774   -731   -504    706       N  
ATOM    150  CZ  ARG A  14     -33.589 -57.115 -19.078  1.00 34.26           C  
ANISOU  150  CZ  ARG A  14     4383   4206   4429   -737   -477    620       C  
ATOM    151  NH1 ARG A  14     -34.339 -56.071 -19.421  1.00 30.10           N  
ANISOU  151  NH1 ARG A  14     3823   3807   3808   -726   -439    619       N  
ATOM    152  NH2 ARG A  14     -33.205 -57.969 -20.016  1.00 29.16           N  
ANISOU  152  NH2 ARG A  14     3764   3450   3865   -763   -492    533       N  
ATOM    153  N   CYS A  15     -31.985 -59.560 -15.306  1.00 28.84           N  
ANISOU  153  N   CYS A  15     3707   3282   3971   -818   -683    959       N  
ATOM    154  CA  CYS A  15     -30.608 -59.701 -15.745  1.00 25.87           C  
ANISOU  154  CA  CYS A  15     3347   2761   3722   -736   -691    877       C  
ATOM    155  C   CYS A  15     -30.577 -59.638 -17.265  1.00 27.37           C  
ANISOU  155  C   CYS A  15     3552   2906   3942   -699   -635    708       C  
ATOM    156  O   CYS A  15     -31.617 -59.675 -17.916  1.00 28.71           O  
ANISOU  156  O   CYS A  15     3722   3137   4052   -750   -613    678       O  
ATOM    157  CB  CYS A  15     -30.002 -61.017 -15.251  1.00 29.02           C  
ANISOU  157  CB  CYS A  15     3740   2979   4309   -772   -796    964       C  
ATOM    158  SG  CYS A  15     -30.098 -61.257 -13.436  1.00 39.39           S  
ANISOU  158  SG  CYS A  15     5030   4364   5572   -862   -889   1203       S  
ATOM    159  N   GLY A  16     -29.386 -59.528 -17.833  1.00 27.32           N  
ANISOU  159  N   GLY A  16     3552   2809   4020   -623   -613    597       N  
ATOM    160  CA  GLY A  16     -29.278 -59.437 -19.274  1.00 28.30           C  
ANISOU  160  CA  GLY A  16     3685   2917   4149   -609   -553    429       C  
ATOM    161  C   GLY A  16     -27.929 -58.879 -19.675  1.00 31.12           C  
ANISOU  161  C   GLY A  16     4041   3242   4542   -519   -510    322       C  
ATOM    162  O   GLY A  16     -27.038 -58.690 -18.845  1.00 30.62           O  
ANISOU  162  O   GLY A  16     3969   3140   4525   -464   -534    378       O  
ATOM    163  N   THR A  17     -27.795 -58.636 -20.972  1.00 28.45           N  
ANISOU  163  N   THR A  17     3708   2930   4172   -521   -448    171       N  
ATOM    164  CA  THR A  17     -26.589 -58.037 -21.516  1.00 25.61           C  
ANISOU  164  CA  THR A  17     3341   2567   3821   -454   -395     57       C  
ATOM    165  C   THR A  17     -26.911 -56.624 -21.987  1.00 24.24           C  
ANISOU  165  C   THR A  17     3178   2570   3463   -446   -343     55       C  
ATOM    166  O   THR A  17     -28.049 -56.325 -22.356  1.00 28.12           O  
ANISOU  166  O   THR A  17     3674   3164   3848   -502   -339     89       O  
ATOM    167  CB  THR A  17     -26.011 -58.886 -22.665  1.00 31.47           C  
ANISOU  167  CB  THR A  17     4068   3207   4680   -476   -360   -132       C  
ATOM    168  OG1 THR A  17     -24.820 -58.266 -23.167  1.00 36.73           O  
ANISOU  168  OG1 THR A  17     4720   3891   5344   -418   -302   -243       O  
ATOM    169  CG2 THR A  17     -27.010 -59.033 -23.804  1.00 31.57           C  
ANISOU  169  CG2 THR A  17     4093   3304   4596   -574   -329   -213       C  
ATOM    170  N   GLY A  18     -25.917 -55.742 -21.939  1.00 22.88           N  
ANISOU  170  N   GLY A  18     3002   2425   3266   -376   -311     29       N  
ATOM    171  CA  GLY A  18     -26.161 -54.383 -22.407  1.00 25.82           C  
ANISOU  171  CA  GLY A  18     3377   2943   3490   -370   -273     36       C  
ATOM    172  C   GLY A  18     -25.064 -53.429 -21.988  1.00 25.82           C  
ANISOU  172  C   GLY A  18     3373   2956   3481   -290   -254     40       C  
ATOM    173  O   GLY A  18     -23.909 -53.823 -21.834  1.00 27.10           O  
ANISOU  173  O   GLY A  18     3527   3028   3742   -247   -252    -15       O  
ATOM    174  N   VAL A  19     -25.452 -52.161 -21.809  1.00 23.16           N  
ANISOU  174  N   VAL A  19     3034   2726   3039   -271   -244    103       N  
ATOM    175  CA  VAL A  19     -24.558 -51.070 -21.424  1.00 28.55           C  
ANISOU  175  CA  VAL A  19     3713   3434   3699   -204   -226    112       C  
ATOM    176  C   VAL A  19     -24.980 -50.555 -20.048  1.00 27.56           C  
ANISOU  176  C   VAL A  19     3584   3337   3552   -172   -246    217       C  
ATOM    177  O   VAL A  19     -26.146 -50.195 -19.845  1.00 28.20           O  
ANISOU  177  O   VAL A  19     3651   3484   3578   -196   -248    274       O  
ATOM    178  CB  VAL A  19     -24.585 -49.915 -22.447  1.00 26.62           C  
ANISOU  178  CB  VAL A  19     3462   3286   3366   -219   -199     86       C  
ATOM    179  CG1 VAL A  19     -23.523 -48.850 -22.093  1.00 27.41           C  
ANISOU  179  CG1 VAL A  19     3559   3396   3461   -154   -183     86       C  
ATOM    180  CG2 VAL A  19     -24.413 -50.412 -23.866  1.00 28.26           C  
ANISOU  180  CG2 VAL A  19     3670   3514   3554   -289   -176    -17       C  
ATOM    181  N   PHE A  20     -24.033 -50.499 -19.116  1.00 25.04           N  
ANISOU  181  N   PHE A  20     3265   2976   3271   -125   -256    236       N  
ATOM    182  CA  PHE A  20     -24.297 -50.075 -17.743  1.00 27.98           C  
ANISOU  182  CA  PHE A  20     3632   3392   3609   -114   -270    320       C  
ATOM    183  C   PHE A  20     -23.483 -48.816 -17.447  1.00 28.31           C  
ANISOU  183  C   PHE A  20     3669   3470   3616    -60   -244    301       C  
ATOM    184  O   PHE A  20     -22.248 -48.857 -17.477  1.00 25.83           O  
ANISOU  184  O   PHE A  20     3360   3106   3348    -26   -249    269       O  
ATOM    185  CB  PHE A  20     -23.944 -51.192 -16.749  1.00 24.44           C  
ANISOU  185  CB  PHE A  20     3185   2874   3226   -134   -323    385       C  
ATOM    186  CG  PHE A  20     -24.617 -52.528 -17.044  1.00 30.15           C  
ANISOU  186  CG  PHE A  20     3911   3532   4013   -190   -359    405       C  
ATOM    187  CD1 PHE A  20     -25.806 -52.879 -16.427  1.00 55.45           C  
ANISOU  187  CD1 PHE A  20     7110   6787   7173   -251   -380    487       C  
ATOM    188  CD2 PHE A  20     -24.044 -53.432 -17.924  1.00 36.99           C  
ANISOU  188  CD2 PHE A  20     4778   4285   4990   -186   -367    329       C  
ATOM    189  CE1 PHE A  20     -26.420 -54.103 -16.698  1.00 55.04           C  
ANISOU  189  CE1 PHE A  20     7060   6669   7184   -309   -418    510       C  
ATOM    190  CE2 PHE A  20     -24.655 -54.660 -18.205  1.00 35.10           C  
ANISOU  190  CE2 PHE A  20     4539   3971   4826   -240   -400    333       C  
ATOM    191  CZ  PHE A  20     -25.841 -54.986 -17.595  1.00 42.30           C  
ANISOU  191  CZ  PHE A  20     5453   4929   5691   -302   -430    432       C  
ATOM    192  N   ILE A  21     -24.171 -47.710 -17.154  1.00 25.03           N  
ANISOU  192  N   ILE A  21     3237   3135   3139    -52   -218    315       N  
ATOM    193  CA  ILE A  21     -23.543 -46.421 -16.855  1.00 24.46           C  
ANISOU  193  CA  ILE A  21     3156   3092   3047     -6   -194    291       C  
ATOM    194  C   ILE A  21     -23.685 -46.195 -15.353  1.00 28.79           C  
ANISOU  194  C   ILE A  21     3692   3690   3558    -16   -190    324       C  
ATOM    195  O   ILE A  21     -24.791 -45.928 -14.865  1.00 27.81           O  
ANISOU  195  O   ILE A  21     3539   3631   3398    -41   -170    338       O  
ATOM    196  CB  ILE A  21     -24.192 -45.265 -17.637  1.00 30.49           C  
ANISOU  196  CB  ILE A  21     3894   3895   3796      6   -171    274       C  
ATOM    197  CG1 ILE A  21     -24.123 -45.483 -19.159  1.00 27.29           C  
ANISOU  197  CG1 ILE A  21     3497   3475   3395    -16   -179    251       C  
ATOM    198  CG2 ILE A  21     -23.599 -43.908 -17.204  1.00 27.17           C  
ANISOU  198  CG2 ILE A  21     3459   3488   3377     51   -150    250       C  
ATOM    199  CD1 ILE A  21     -22.753 -45.812 -19.698  1.00 28.78           C  
ANISOU  199  CD1 ILE A  21     3710   3621   3603     -6   -177    199       C  
ATOM    200  N   TYR A  22     -22.581 -46.303 -14.612  1.00 26.88           N  
ANISOU  200  N   TYR A  22     3462   3431   3320     -8   -209    335       N  
ATOM    201  CA  TYR A  22     -22.627 -46.189 -13.156  1.00 25.21           C  
ANISOU  201  CA  TYR A  22     3240   3289   3050    -45   -212    371       C  
ATOM    202  C   TYR A  22     -22.380 -44.762 -12.693  1.00 26.13           C  
ANISOU  202  C   TYR A  22     3338   3460   3128    -19   -167    311       C  
ATOM    203  O   TYR A  22     -21.565 -44.036 -13.271  1.00 24.68           O  
ANISOU  203  O   TYR A  22     3163   3237   2978     31   -159    268       O  
ATOM    204  CB  TYR A  22     -21.595 -47.110 -12.488  1.00 24.62           C  
ANISOU  204  CB  TYR A  22     3179   3174   3002    -69   -274    436       C  
ATOM    205  CG  TYR A  22     -22.013 -48.559 -12.520  1.00 24.12           C  
ANISOU  205  CG  TYR A  22     3119   3058   2987   -114   -328    510       C  
ATOM    206  CD1 TYR A  22     -22.832 -49.074 -11.534  1.00 27.24           C  
ANISOU  206  CD1 TYR A  22     3503   3525   3323   -196   -351    591       C  
ATOM    207  CD2 TYR A  22     -21.619 -49.404 -13.563  1.00 29.32           C  
ANISOU  207  CD2 TYR A  22     3788   3600   3753    -84   -351    490       C  
ATOM    208  CE1 TYR A  22     -23.236 -50.394 -11.558  1.00 27.96           C  
ANISOU  208  CE1 TYR A  22     3596   3558   3469   -246   -409    671       C  
ATOM    209  CE2 TYR A  22     -22.027 -50.737 -13.597  1.00 29.39           C  
ANISOU  209  CE2 TYR A  22     3796   3542   3830   -127   -402    548       C  
ATOM    210  CZ  TYR A  22     -22.835 -51.222 -12.583  1.00 29.82           C  
ANISOU  210  CZ  TYR A  22     3843   3656   3832   -207   -437    649       C  
ATOM    211  OH  TYR A  22     -23.260 -52.530 -12.564  1.00 30.56           O  
ANISOU  211  OH  TYR A  22     3934   3677   4000   -259   -498    722       O  
ATOM    212  N   ASN A  23     -23.078 -44.381 -11.624  1.00 23.97           N  
ANISOU  212  N   ASN A  23     3037   3284   2788    -64   -136    302       N  
ATOM    213  CA  ASN A  23     -22.808 -43.143 -10.900  1.00 21.32           C  
ANISOU  213  CA  ASN A  23     2679   3006   2417    -57    -90    229       C  
ATOM    214  C   ASN A  23     -21.635 -43.413  -9.963  1.00 25.69           C  
ANISOU  214  C   ASN A  23     3254   3586   2921    -97   -128    266       C  
ATOM    215  O   ASN A  23     -21.808 -43.906  -8.843  1.00 25.37           O  
ANISOU  215  O   ASN A  23     3205   3637   2798   -182   -143    312       O  
ATOM    216  CB  ASN A  23     -24.046 -42.685 -10.139  1.00 24.59           C  
ANISOU  216  CB  ASN A  23     3039   3522   2781    -99    -30    180       C  
ATOM    217  CG  ASN A  23     -23.859 -41.355  -9.443  1.00 27.12           C  
ANISOU  217  CG  ASN A  23     3325   3893   3087    -92     30     70       C  
ATOM    218  OD1 ASN A  23     -22.742 -40.845  -9.325  1.00 24.13           O  
ANISOU  218  OD1 ASN A  23     2969   3486   2711    -72     19     48       O  
ATOM    219  ND2 ASN A  23     -24.963 -40.785  -8.961  1.00 22.82           N  
ANISOU  219  ND2 ASN A  23     2715   3420   2535   -111     99    -11       N  
ATOM    220  N   ASP A  24     -20.428 -43.088 -10.430  1.00 26.18           N  
ANISOU  220  N   ASP A  24     3338   3579   3031    -45   -149    254       N  
ATOM    221  CA  ASP A  24     -19.219 -43.196  -9.626  1.00 29.21           C  
ANISOU  221  CA  ASP A  24     3732   3982   3384    -75   -190    289       C  
ATOM    222  C   ASP A  24     -18.911 -41.912  -8.865  1.00 30.10           C  
ANISOU  222  C   ASP A  24     3830   4167   3438    -90   -145    205       C  
ATOM    223  O   ASP A  24     -17.969 -41.889  -8.068  1.00 36.48           O  
ANISOU  223  O   ASP A  24     4643   5017   4200   -133   -177    230       O  
ATOM    224  CB  ASP A  24     -18.028 -43.567 -10.528  1.00 29.90           C  
ANISOU  224  CB  ASP A  24     3839   3958   3562    -14   -234    311       C  
ATOM    225  CG  ASP A  24     -18.174 -44.954 -11.150  1.00 35.76           C  
ANISOU  225  CG  ASP A  24     4589   4622   4377    -10   -280    376       C  
ATOM    226  OD1 ASP A  24     -18.439 -45.914 -10.392  1.00 32.43           O  
ANISOU  226  OD1 ASP A  24     4162   4220   3938    -72   -329    464       O  
ATOM    227  OD2 ASP A  24     -18.032 -45.082 -12.396  1.00 36.95           O  
ANISOU  227  OD2 ASP A  24     4746   4693   4600     45   -268    338       O  
ATOM    228  N   VAL A  25     -19.662 -40.843  -9.114  1.00 26.86           N  
ANISOU  228  N   VAL A  25     3394   3764   3046    -58    -76    106       N  
ATOM    229  CA  VAL A  25     -19.438 -39.584  -8.415  1.00 23.71           C  
ANISOU  229  CA  VAL A  25     2973   3417   2619    -71    -25      1       C  
ATOM    230  C   VAL A  25     -19.994 -39.650  -6.994  1.00 29.77           C  
ANISOU  230  C   VAL A  25     3712   4336   3265   -177     10    -32       C  
ATOM    231  O   VAL A  25     -19.329 -39.270  -6.028  1.00 28.81           O  
ANISOU  231  O   VAL A  25     3588   4295   3062   -242     14    -65       O  
ATOM    232  CB  VAL A  25     -20.063 -38.424  -9.210  1.00 24.76           C  
ANISOU  232  CB  VAL A  25     3073   3481   2852      3     27    -89       C  
ATOM    233  CG1 VAL A  25     -20.076 -37.175  -8.380  1.00 23.06           C  
ANISOU  233  CG1 VAL A  25     2819   3311   2630    -15     88   -219       C  
ATOM    234  CG2 VAL A  25     -19.311 -38.208 -10.505  1.00 25.90           C  
ANISOU  234  CG2 VAL A  25     3245   3510   3085     77    -12    -54       C  
ATOM    235  N   GLU A  26     -21.229 -40.125  -6.843  1.00 25.82           N  
ANISOU  235  N   GLU A  26     3184   3889   2737   -210     38    -26       N  
ATOM    236  CA  GLU A  26     -21.891 -40.130  -5.551  1.00 28.42           C  
ANISOU  236  CA  GLU A  26     3474   4385   2941   -324     88    -73       C  
ATOM    237  C   GLU A  26     -21.719 -41.458  -4.830  1.00 40.09           C  
ANISOU  237  C   GLU A  26     4975   5951   4308   -435     15     74       C  
ATOM    238  O   GLU A  26     -22.426 -41.724  -3.855  1.00 55.82           O  
ANISOU  238  O   GLU A  26     6934   8097   6179   -552     45     69       O  
ATOM    239  CB  GLU A  26     -23.363 -39.760  -5.724  1.00 25.43           C  
ANISOU  239  CB  GLU A  26     3032   4027   2601   -305    168   -163       C  
ATOM    240  CG  GLU A  26     -23.497 -38.369  -6.410  1.00 29.53           C  
ANISOU  240  CG  GLU A  26     3515   4441   3265   -197    224   -293       C  
ATOM    241  CD  GLU A  26     -24.930 -37.909  -6.551  1.00 29.30           C  
ANISOU  241  CD  GLU A  26     3403   4421   3310   -172    298   -385       C  
ATOM    242  OE1 GLU A  26     -25.633 -38.408  -7.452  1.00 35.26           O  
ANISOU  242  OE1 GLU A  26     4154   5111   4131   -125    270   -309       O  
ATOM    243  OE2 GLU A  26     -25.359 -37.053  -5.757  1.00 32.22           O  
ANISOU  243  OE2 GLU A  26     3701   4863   3676   -202    387   -541       O  
ATOM    244  N   ALA A  27     -20.759 -42.267  -5.265  1.00 37.06           N  
ANISOU  244  N   ALA A  27     4638   5474   3970   -408    -82    203       N  
ATOM    245  CA  ALA A  27     -20.447 -43.525  -4.613  1.00 39.59           C  
ANISOU  245  CA  ALA A  27     4972   5843   4227   -507   -175    364       C  
ATOM    246  C   ALA A  27     -19.716 -43.268  -3.295  1.00 46.72           C  
ANISOU  246  C   ALA A  27     5866   6892   4993   -630   -196    380       C  
ATOM    247  O   ALA A  27     -19.177 -42.181  -3.047  1.00 44.15           O  
ANISOU  247  O   ALA A  27     5536   6597   4644   -618   -148    266       O  
ATOM    248  CB  ALA A  27     -19.609 -44.398  -5.544  1.00 32.99           C  
ANISOU  248  CB  ALA A  27     4171   4839   3524   -427   -266    473       C  
ATOM    249  N   TRP A  28     -19.696 -44.288  -2.437  1.00 48.28           N  
ANISOU  249  N   TRP A  28     6058   7185   5100   -762   -277    531       N  
ATOM    250  CA  TRP A  28     -19.137 -44.091  -1.098  1.00 53.80           C  
ANISOU  250  CA  TRP A  28     6743   8063   5637   -916   -304    562       C  
ATOM    251  C   TRP A  28     -17.609 -44.040  -1.082  1.00 50.80           C  
ANISOU  251  C   TRP A  28     6381   7615   5305   -891   -391    632       C  
ATOM    252  O   TRP A  28     -17.027 -43.577  -0.091  1.00 44.59           O  
ANISOU  252  O   TRP A  28     5583   6971   4389  -1004   -401    623       O  
ATOM    253  CB  TRP A  28     -19.629 -45.193  -0.151  1.00 51.28           C  
ANISOU  253  CB  TRP A  28     6404   7886   5194  -1092   -378    729       C  
ATOM    254  CG  TRP A  28     -19.083 -46.561  -0.456  1.00 60.11           C  
ANISOU  254  CG  TRP A  28     7539   8871   6430  -1083   -530    955       C  
ATOM    255  CD1 TRP A  28     -19.439 -47.374  -1.493  1.00 56.82           C  
ANISOU  255  CD1 TRP A  28     7137   8272   6179   -975   -561   1008       C  
ATOM    256  CD2 TRP A  28     -18.092 -47.281   0.296  1.00 71.97           C  
ANISOU  256  CD2 TRP A  28     9032  10404   7911  -1191   -677   1155       C  
ATOM    257  NE1 TRP A  28     -18.727 -48.549  -1.440  1.00 58.98           N  
ANISOU  257  NE1 TRP A  28     7410   8447   6555  -1000   -710   1210       N  
ATOM    258  CE2 TRP A  28     -17.896 -48.519  -0.350  1.00 72.26           C  
ANISOU  258  CE2 TRP A  28     9072  10250   8133  -1129   -791   1315       C  
ATOM    259  CE3 TRP A  28     -17.354 -46.999   1.453  1.00 75.18           C  
ANISOU  259  CE3 TRP A  28     9419  10979   8165  -1341   -729   1215       C  
ATOM    260  CZ2 TRP A  28     -16.994 -49.477   0.123  1.00 77.85           C  
ANISOU  260  CZ2 TRP A  28     9758  10913   8908  -1200   -959   1540       C  
ATOM    261  CZ3 TRP A  28     -16.453 -47.951   1.919  1.00 74.99           C  
ANISOU  261  CZ3 TRP A  28     9378  10927   8186  -1421   -903   1455       C  
ATOM    262  CH2 TRP A  28     -16.281 -49.172   1.253  1.00 76.49           C  
ANISOU  262  CH2 TRP A  28     9564  10907   8590  -1344  -1018   1618       C  
ATOM    263  N   ARG A  29     -16.950 -44.494  -2.147  1.00 56.52           N  
ANISOU  263  N   ARG A  29     7128   8137   6210   -755   -449    691       N  
ATOM    264  CA  ARG A  29     -15.499 -44.607  -2.154  1.00 58.98           C  
ANISOU  264  CA  ARG A  29     7441   8377   6589   -731   -540    771       C  
ATOM    265  C   ARG A  29     -14.975 -44.378  -3.561  1.00 57.30           C  
ANISOU  265  C   ARG A  29     7247   7965   6558   -551   -517    702       C  
ATOM    266  O   ARG A  29     -15.715 -44.474  -4.544  1.00 53.21           O  
ANISOU  266  O   ARG A  29     6742   7353   6121   -460   -465    643       O  
ATOM    267  CB  ARG A  29     -15.040 -45.983  -1.669  1.00 57.91           C  
ANISOU  267  CB  ARG A  29     7288   8225   6491   -813   -692   1001       C  
ATOM    268  CG  ARG A  29     -15.160 -47.084  -2.714  1.00 62.89           C  
ANISOU  268  CG  ARG A  29     7922   8655   7321   -706   -743   1076       C  
ATOM    269  CD  ARG A  29     -14.690 -48.394  -2.111  1.00 72.79           C  
ANISOU  269  CD  ARG A  29     9142   9879   8635   -796   -904   1309       C  
ATOM    270  NE  ARG A  29     -14.797 -49.548  -3.001  1.00 69.99           N  
ANISOU  270  NE  ARG A  29     8780   9323   8490   -709   -961   1378       N  
ATOM    271  CZ  ARG A  29     -13.783 -50.031  -3.712  1.00 57.85           C  
ANISOU  271  CZ  ARG A  29     7218   7598   7162   -601  -1021   1404       C  
ATOM    272  NH1 ARG A  29     -12.593 -49.442  -3.652  1.00 41.53           N  
ANISOU  272  NH1 ARG A  29     5135   5526   5120   -563  -1034   1379       N  
ATOM    273  NH2 ARG A  29     -13.957 -51.102  -4.478  1.00 55.77           N  
ANISOU  273  NH2 ARG A  29     6941   7157   7090   -535  -1062   1443       N  
ATOM    274  N   ASP A  30     -13.681 -44.069  -3.641  1.00 47.88           N  
ANISOU  274  N   ASP A  30     6050   6724   5417   -514   -559    712       N  
ATOM    275  CA  ASP A  30     -12.957 -44.101  -4.907  1.00 51.37           C  
ANISOU  275  CA  ASP A  30     6497   6990   6031   -369   -560    680       C  
ATOM    276  C   ASP A  30     -12.582 -45.550  -5.191  1.00 40.29           C  
ANISOU  276  C   ASP A  30     5070   5468   4769   -350   -666    828       C  
ATOM    277  O   ASP A  30     -11.752 -46.129  -4.488  1.00 43.30           O  
ANISOU  277  O   ASP A  30     5420   5859   5174   -411   -774    964       O  
ATOM    278  CB  ASP A  30     -11.704 -43.228  -4.852  1.00 44.53           C  
ANISOU  278  CB  ASP A  30     5624   6125   5170   -346   -563    634       C  
ATOM    279  CG  ASP A  30     -11.962 -41.796  -5.272  1.00 65.09           C  
ANISOU  279  CG  ASP A  30     8250   8744   7738   -295   -451    460       C  
ATOM    280  OD1 ASP A  30     -12.951 -41.550  -5.995  1.00 70.48           O  
ANISOU  280  OD1 ASP A  30     8947   9387   8447   -237   -378    379       O  
ATOM    281  OD2 ASP A  30     -11.157 -40.915  -4.892  1.00 69.29           O  
ANISOU  281  OD2 ASP A  30     8778   9320   8228   -316   -445    411       O  
ATOM    282  N  AARG A  31     -13.189 -46.139  -6.215  0.50 35.76           N  
ANISOU  282  N  AARG A  31     4507   4780   4302   -271   -641    801       N  
ATOM    283  N  BARG A  31     -13.191 -46.145  -6.212  0.50 35.76           N  
ANISOU  283  N  BARG A  31     4507   4780   4302   -272   -641    802       N  
ATOM    284  CA AARG A  31     -12.801 -47.477  -6.633  0.50 38.02           C  
ANISOU  284  CA AARG A  31     4764   4922   4759   -238   -729    904       C  
ATOM    285  CA BARG A  31     -12.790 -47.482  -6.626  0.50 37.99           C  
ANISOU  285  CA BARG A  31     4759   4918   4756   -238   -730    906       C  
ATOM    286  C  AARG A  31     -11.751 -47.472  -7.739  0.50 35.05           C  
ANISOU  286  C  AARG A  31     4368   4406   4545   -118   -718    834       C  
ATOM    287  C  BARG A  31     -11.723 -47.468  -7.715  0.50 34.96           C  
ANISOU  287  C  BARG A  31     4354   4395   4533   -119   -720    836       C  
ATOM    288  O  AARG A  31     -11.210 -48.534  -8.059  0.50 35.76           O  
ANISOU  288  O  AARG A  31     4415   4366   4807    -83   -788    898       O  
ATOM    289  O  BARG A  31     -11.149 -48.521  -8.006  0.50 35.80           O  
ANISOU  289  O  BARG A  31     4418   4373   4811    -85   -792    903       O  
ATOM    290  CB AARG A  31     -14.030 -48.271  -7.095  0.50 37.54           C  
ANISOU  290  CB AARG A  31     4719   4816   4729   -238   -713    913       C  
ATOM    291  CB BARG A  31     -14.002 -48.284  -7.117  0.50 37.44           C  
ANISOU  291  CB BARG A  31     4705   4799   4722   -235   -714    912       C  
ATOM    292  CG AARG A  31     -14.778 -47.667  -8.272  0.50 33.67           C  
ANISOU  292  CG AARG A  31     4260   4297   4234   -154   -598    758       C  
ATOM    293  CG BARG A  31     -14.557 -47.812  -8.447  0.50 33.30           C  
ANISOU  293  CG BARG A  31     4208   4217   4226   -137   -608    759       C  
ATOM    294  CD AARG A  31     -15.780 -48.665  -8.858  0.50 32.68           C  
ANISOU  294  CD AARG A  31     4141   4100   4174   -151   -602    777       C  
ATOM    295  CD BARG A  31     -15.622 -48.758  -8.994  0.50 32.95           C  
ANISOU  295  CD BARG A  31     4173   4111   4237   -138   -608    775       C  
ATOM    296  NE AARG A  31     -15.135 -49.934  -9.193  0.50 28.48           N  
ANISOU  296  NE AARG A  31     3577   3416   3827   -124   -687    849       N  
ATOM    297  NE BARG A  31     -16.760 -48.899  -8.090  0.50 33.68           N  
ANISOU  297  NE BARG A  31     4273   4320   4202   -241   -613    842       N  
ATOM    298  CZ AARG A  31     -15.256 -51.054  -8.491  0.50 28.66           C  
ANISOU  298  CZ AARG A  31     3576   3404   3910   -195   -790    999       C  
ATOM    299  CZ BARG A  31     -16.978 -49.961  -7.318  0.50 37.33           C  
ANISOU  299  CZ BARG A  31     4718   4786   4679   -331   -706    992       C  
ATOM    300  NH1AARG A  31     -16.015 -51.081  -7.402  0.50 36.96           N  
ANISOU  300  NH1AARG A  31     4636   4587   4819   -312   -819   1099       N  
ATOM    301  NH1BARG A  31     -16.137 -50.989  -7.341  0.50 36.43           N  
ANISOU  301  NH1BARG A  31     4573   4541   4728   -320   -811   1095       N  
ATOM    302  NH2AARG A  31     -14.615 -52.147  -8.874  0.50 23.99           N  
ANISOU  302  NH2AARG A  31     2942   2645   3527   -156   -866   1047       N  
ATOM    303  NH2BARG A  31     -18.044 -49.995  -6.527  0.50 37.37           N  
ANISOU  303  NH2BARG A  31     4728   4924   4547   -436   -697   1040       N  
ATOM    304  N   TYR A  32     -11.451 -46.311  -8.319  1.00 29.12           N  
ANISOU  304  N   TYR A  32     3636   3678   3751    -60   -632    703       N  
ATOM    305  CA  TYR A  32     -10.453 -46.173  -9.375  1.00 30.17           C  
ANISOU  305  CA  TYR A  32     3745   3711   4007     36   -609    626       C  
ATOM    306  C   TYR A  32      -9.233 -45.401  -8.884  1.00 32.33           C  
ANISOU  306  C   TYR A  32     3997   4031   4255     28   -630    630       C  
ATOM    307  O   TYR A  32      -9.344 -44.483  -8.065  1.00 35.33           O  
ANISOU  307  O   TYR A  32     4401   4529   4493    -33   -615    623       O  
ATOM    308  CB  TYR A  32     -11.044 -45.453 -10.593  1.00 25.87           C  
ANISOU  308  CB  TYR A  32     3235   3157   3437     96   -502    486       C  
ATOM    309  CG  TYR A  32     -12.267 -46.148 -11.124  1.00 31.95           C  
ANISOU  309  CG  TYR A  32     4025   3893   4222     97   -480    478       C  
ATOM    310  CD1 TYR A  32     -12.169 -47.413 -11.696  1.00 27.83           C  
ANISOU  310  CD1 TYR A  32     3476   3255   3844    124   -515    496       C  
ATOM    311  CD2 TYR A  32     -13.528 -45.559 -11.027  1.00 27.66           C  
ANISOU  311  CD2 TYR A  32     3519   3427   3564     68   -425    446       C  
ATOM    312  CE1 TYR A  32     -13.299 -48.073 -12.171  1.00 27.83           C  
ANISOU  312  CE1 TYR A  32     3495   3225   3855    114   -498    487       C  
ATOM    313  CE2 TYR A  32     -14.658 -46.200 -11.506  1.00 26.02           C  
ANISOU  313  CE2 TYR A  32     3324   3195   3368     63   -410    445       C  
ATOM    314  CZ  TYR A  32     -14.540 -47.460 -12.074  1.00 28.31           C  
ANISOU  314  CZ  TYR A  32     3597   3377   3785     82   -448    469       C  
ATOM    315  OH  TYR A  32     -15.667 -48.105 -12.532  1.00 28.17           O  
ANISOU  315  OH  TYR A  32     3592   3335   3775     66   -435    467       O  
ATOM    316  N   LYS A  33      -8.061 -45.786  -9.394  1.00 32.07           N  
ANISOU  316  N   LYS A  33     3912   3905   4369     87   -662    630       N  
ATOM    317  CA  LYS A  33      -6.817 -45.047  -9.190  1.00 31.39           C  
ANISOU  317  CA  LYS A  33     3797   3849   4280     94   -674    618       C  
ATOM    318  C   LYS A  33      -6.127 -44.865 -10.535  1.00 32.08           C  
ANISOU  318  C   LYS A  33     3857   3860   4472    185   -611    502       C  
ATOM    319  O   LYS A  33      -5.837 -45.851 -11.223  1.00 33.26           O  
ANISOU  319  O   LYS A  33     3957   3899   4782    238   -621    487       O  
ATOM    320  CB  LYS A  33      -5.888 -45.772  -8.210  1.00 34.26           C  
ANISOU  320  CB  LYS A  33     4096   4199   4723     51   -801    769       C  
ATOM    321  CG  LYS A  33      -6.289 -45.642  -6.746  1.00 39.28           C  
ANISOU  321  CG  LYS A  33     4753   4967   5203    -77   -867    887       C  
ATOM    322  CD  LYS A  33      -5.383 -46.498  -5.862  1.00 49.04           C  
ANISOU  322  CD  LYS A  33     5915   6182   6535   -131  -1016   1069       C  
ATOM    323  CE  LYS A  33      -5.739 -46.363  -4.390  1.00 55.09           C  
ANISOU  323  CE  LYS A  33     6700   7114   7117   -289  -1086   1196       C  
ATOM    324  NZ  LYS A  33      -5.471 -44.988  -3.891  1.00 71.33           N  
ANISOU  324  NZ  LYS A  33     8792   9320   8989   -344  -1029   1110       N  
ATOM    325  N   TYR A  34      -5.875 -43.610 -10.908  1.00 28.57           N  
ANISOU  325  N   TYR A  34     3439   3474   3940    193   -544    414       N  
ATOM    326  CA  TYR A  34      -5.015 -43.321 -12.047  1.00 29.10           C  
ANISOU  326  CA  TYR A  34     3472   3503   4083    251   -493    320       C  
ATOM    327  C   TYR A  34      -3.569 -43.689 -11.729  1.00 29.67           C  
ANISOU  327  C   TYR A  34     3461   3541   4272    267   -557    366       C  
ATOM    328  O   TYR A  34      -3.055 -43.379 -10.650  1.00 31.08           O  
ANISOU  328  O   TYR A  34     3630   3773   4406    219   -623    451       O  
ATOM    329  CB  TYR A  34      -5.075 -41.837 -12.409  1.00 26.40           C  
ANISOU  329  CB  TYR A  34     3175   3234   3623    240   -426    244       C  
ATOM    330  CG  TYR A  34      -6.303 -41.357 -13.156  1.00 32.12           C  
ANISOU  330  CG  TYR A  34     3956   3972   4277    242   -356    181       C  
ATOM    331  CD1 TYR A  34      -7.479 -42.096 -13.185  1.00 33.97           C  
ANISOU  331  CD1 TYR A  34     4216   4184   4508    240   -353    198       C  
ATOM    332  CD2 TYR A  34      -6.277 -40.139 -13.829  1.00 28.30           C  
ANISOU  332  CD2 TYR A  34     3494   3521   3738    240   -304    118       C  
ATOM    333  CE1 TYR A  34      -8.606 -41.621 -13.889  1.00 28.41           C  
ANISOU  333  CE1 TYR A  34     3553   3495   3746    239   -297    150       C  
ATOM    334  CE2 TYR A  34      -7.379 -39.663 -14.522  1.00 29.16           C  
ANISOU  334  CE2 TYR A  34     3642   3637   3801    238   -257     82       C  
ATOM    335  CZ  TYR A  34      -8.532 -40.409 -14.556  1.00 27.99           C  
ANISOU  335  CZ  TYR A  34     3515   3471   3650    239   -253     96       C  
ATOM    336  OH  TYR A  34      -9.614 -39.917 -15.236  1.00 30.86           O  
ANISOU  336  OH  TYR A  34     3907   3844   3975    234   -215     70       O  
ATOM    337  N   HIS A  35      -2.896 -44.314 -12.693  1.00 27.53           N  
ANISOU  337  N   HIS A  35     3120   3188   4150    328   -532    300       N  
ATOM    338  CA  HIS A  35      -1.484 -44.642 -12.578  1.00 28.89           C  
ANISOU  338  CA  HIS A  35     3192   3317   4466    357   -579    321       C  
ATOM    339  C   HIS A  35      -0.836 -44.341 -13.921  1.00 32.14           C  
ANISOU  339  C   HIS A  35     3562   3726   4924    400   -484    174       C  
ATOM    340  O   HIS A  35      -1.431 -44.633 -14.968  1.00 31.10           O  
ANISOU  340  O   HIS A  35     3445   3573   4800    419   -408     72       O  
ATOM    341  CB  HIS A  35      -1.238 -46.120 -12.235  1.00 29.27           C  
ANISOU  341  CB  HIS A  35     3158   3242   4722    387   -666    399       C  
ATOM    342  CG  HIS A  35      -1.776 -46.542 -10.904  1.00 41.16           C  
ANISOU  342  CG  HIS A  35     4690   4759   6188    323   -777    570       C  
ATOM    343  ND1 HIS A  35      -1.246 -46.098  -9.711  1.00 46.68           N  
ANISOU  343  ND1 HIS A  35     5384   5540   6813    257   -864    695       N  
ATOM    344  CD2 HIS A  35      -2.784 -47.386 -10.578  1.00 43.45           C  
ANISOU  344  CD2 HIS A  35     5009   5005   6493    300   -818    640       C  
ATOM    345  CE1 HIS A  35      -1.913 -46.640  -8.707  1.00 47.23           C  
ANISOU  345  CE1 HIS A  35     5476   5627   6841    187   -951    835       C  
ATOM    346  NE2 HIS A  35      -2.848 -47.430  -9.205  1.00 38.66           N  
ANISOU  346  NE2 HIS A  35     4412   4463   5814    214   -926    809       N  
ATOM    347  N   PRO A  36       0.376 -43.787 -13.933  1.00 32.12           N  
ANISOU  347  N   PRO A  36     3501   3757   4945    404   -486    160       N  
ATOM    348  CA  PRO A  36       1.104 -43.669 -15.203  1.00 29.81           C  
ANISOU  348  CA  PRO A  36     3146   3471   4712    434   -397     20       C  
ATOM    349  C   PRO A  36       1.359 -45.047 -15.795  1.00 34.07           C  
ANISOU  349  C   PRO A  36     3585   3894   5466    494   -383    -53       C  
ATOM    350  O   PRO A  36       1.712 -45.993 -15.088  1.00 33.30           O  
ANISOU  350  O   PRO A  36     3416   3696   5541    527   -471     28       O  
ATOM    351  CB  PRO A  36       2.420 -42.981 -14.816  1.00 31.19           C  
ANISOU  351  CB  PRO A  36     3260   3694   4896    423   -427     49       C  
ATOM    352  CG  PRO A  36       2.237 -42.499 -13.387  1.00 39.97           C  
ANISOU  352  CG  PRO A  36     4431   4846   5909    374   -522    193       C  
ATOM    353  CD  PRO A  36       1.183 -43.369 -12.772  1.00 31.37           C  
ANISOU  353  CD  PRO A  36     3382   3702   4833    371   -575    272       C  
ATOM    354  N   ASP A  37       1.163 -45.152 -17.110  1.00 37.40           N  
ANISOU  354  N   ASP A  37     3996   4331   5883    499   -274   -208       N  
ATOM    355  CA  ASP A  37       1.530 -46.370 -17.826  1.00 38.06           C  
ANISOU  355  CA  ASP A  37     3968   4313   6178    550   -235   -329       C  
ATOM    356  C   ASP A  37       2.962 -46.780 -17.514  1.00 36.34           C  
ANISOU  356  C   ASP A  37     3604   4032   6171    601   -274   -329       C  
ATOM    357  O   ASP A  37       3.270 -47.973 -17.439  1.00 37.43           O  
ANISOU  357  O   ASP A  37     3637   4030   6556    660   -308   -351       O  
ATOM    358  CB  ASP A  37       1.347 -46.150 -19.330  1.00 54.72           C  
ANISOU  358  CB  ASP A  37     6080   6504   8208    518    -98   -513       C  
ATOM    359  CG  ASP A  37       1.506 -47.423 -20.134  1.00 71.66           C  
ANISOU  359  CG  ASP A  37     8121   8554  10553    556    -38   -675       C  
ATOM    360  OD1 ASP A  37       0.502 -48.150 -20.308  1.00 74.04           O  
ANISOU  360  OD1 ASP A  37     8466   8791  10875    556    -35   -695       O  
ATOM    361  OD2 ASP A  37       2.633 -47.689 -20.601  1.00 78.74           O  
ANISOU  361  OD2 ASP A  37     8887   9440  11592    584     13   -795       O  
ATOM    362  N   SER A  38       3.842 -45.811 -17.308  1.00 39.38           N  
ANISOU  362  N   SER A  38     3971   4509   6480    579   -279   -300       N  
ATOM    363  CA  SER A  38       5.231 -46.066 -16.960  1.00 38.89           C  
ANISOU  363  CA  SER A  38     3766   4404   6605    621   -323   -285       C  
ATOM    364  C   SER A  38       5.769 -44.867 -16.193  1.00 40.27           C  
ANISOU  364  C   SER A  38     3984   4686   6632    572   -378   -167       C  
ATOM    365  O   SER A  38       5.915 -43.782 -16.775  1.00 37.99           O  
ANISOU  365  O   SER A  38     3740   4520   6174    524   -304   -228       O  
ATOM    366  CB  SER A  38       6.070 -46.320 -18.215  1.00 43.59           C  
ANISOU  366  CB  SER A  38     4233   5013   7316    645   -201   -495       C  
ATOM    367  OG  SER A  38       7.448 -46.373 -17.896  1.00 43.62           O  
ANISOU  367  OG  SER A  38     4093   4995   7485    682   -237   -482       O  
ATOM    368  N   PRO A  39       6.046 -45.008 -14.891  1.00 39.00           N  
ANISOU  368  N   PRO A  39     3810   4487   6521    570   -513      8       N  
ATOM    369  CA  PRO A  39       6.703 -43.909 -14.165  1.00 36.57           C  
ANISOU  369  CA  PRO A  39     3525   4283   6087    516   -563    101       C  
ATOM    370  C   PRO A  39       7.999 -43.439 -14.817  1.00 36.85           C  
ANISOU  370  C   PRO A  39     3452   4373   6176    525   -505      6       C  
ATOM    371  O   PRO A  39       8.248 -42.231 -14.858  1.00 33.53           O  
ANISOU  371  O   PRO A  39     3089   4069   5583    466   -477      5       O  
ATOM    372  CB  PRO A  39       6.944 -44.514 -12.771  1.00 38.94           C  
ANISOU  372  CB  PRO A  39     3784   4521   6489    510   -723    294       C  
ATOM    373  CG  PRO A  39       5.861 -45.534 -12.622  1.00 44.89           C  
ANISOU  373  CG  PRO A  39     4576   5176   7305    530   -754    332       C  
ATOM    374  CD  PRO A  39       5.693 -46.128 -14.000  1.00 44.23           C  
ANISOU  374  CD  PRO A  39     4446   5023   7336    595   -632    140       C  
ATOM    375  N   ARG A  40       8.823 -44.355 -15.346  1.00 35.02           N  
ANISOU  375  N   ARG A  40     3060   4058   6190    594   -481    -82       N  
ATOM    376  CA  ARG A  40      10.080 -43.946 -15.972  1.00 42.47           C  
ANISOU  376  CA  ARG A  40     3883   5064   7190    597   -416   -184       C  
ATOM    377  C   ARG A  40       9.840 -43.147 -17.248  1.00 41.53           C  
ANISOU  377  C   ARG A  40     3821   5071   6888    547   -266   -344       C  
ATOM    378  O   ARG A  40      10.594 -42.214 -17.553  1.00 37.68           O  
ANISOU  378  O   ARG A  40     3312   4697   6308    498   -227   -372       O  
ATOM    379  CB  ARG A  40      10.950 -45.166 -16.277  1.00 45.22           C  
ANISOU  379  CB  ARG A  40     4028   5285   7868    687   -413   -266       C  
ATOM    380  CG  ARG A  40      11.530 -45.821 -15.043  1.00 59.60           C  
ANISOU  380  CG  ARG A  40     5753   6994   9899    725   -582    -81       C  
ATOM    381  CD  ARG A  40      12.719 -46.712 -15.358  1.00 69.13           C  
ANISOU  381  CD  ARG A  40     6726   8090  11451    812   -581   -163       C  
ATOM    382  NE  ARG A  40      13.462 -47.013 -14.136  1.00 81.03           N  
ANISOU  382  NE  ARG A  40     8136   9527  13123    824   -760     50       N  
ATOM    383  CZ  ARG A  40      14.578 -46.392 -13.759  1.00 87.70           C  
ANISOU  383  CZ  ARG A  40     8901  10451  13972    799   -806    114       C  
ATOM    384  NH1 ARG A  40      15.173 -46.730 -12.622  1.00 93.37           N  
ANISOU  384  NH1 ARG A  40     9579  11116  14781    778   -966    320       N  
ATOM    385  NH2 ARG A  40      15.110 -45.444 -14.521  1.00 85.11           N  
ANISOU  385  NH2 ARG A  40     8572  10267  13499    765   -682    -24       N  
ATOM    386  N   ARG A  41       8.823 -43.520 -18.027  1.00 38.95           N  
ANISOU  386  N   ARG A  41     3558   4729   6511    547   -187   -443       N  
ATOM    387  CA  ARG A  41       8.484 -42.735 -19.209  1.00 36.76           C  
ANISOU  387  CA  ARG A  41     3344   4585   6038    476    -63   -564       C  
ATOM    388  C   ARG A  41       7.979 -41.353 -18.814  1.00 32.74           C  
ANISOU  388  C   ARG A  41     2987   4172   5281    400    -99   -447       C  
ATOM    389  O   ARG A  41       8.346 -40.347 -19.436  1.00 34.73           O  
ANISOU  389  O   ARG A  41     3252   4544   5400    330    -44   -483       O  
ATOM    390  CB  ARG A  41       7.443 -43.476 -20.049  1.00 41.28           C  
ANISOU  390  CB  ARG A  41     3953   5122   6608    482     13   -678       C  
ATOM    391  CG  ARG A  41       7.227 -42.891 -21.432  1.00 60.08           C  
ANISOU  391  CG  ARG A  41     6361   7650   8818    397    143   -817       C  
ATOM    392  CD  ARG A  41       6.333 -43.787 -22.288  1.00 74.14           C  
ANISOU  392  CD  ARG A  41     8150   9399  10619    397    219   -949       C  
ATOM    393  NE  ARG A  41       6.645 -45.203 -22.101  1.00 85.15           N  
ANISOU  393  NE  ARG A  41     9423  10637  12294    491    213  -1030       N  
ATOM    394  CZ  ARG A  41       7.682 -45.823 -22.660  1.00 91.63           C  
ANISOU  394  CZ  ARG A  41    10071  11443  13303    523    288  -1199       C  
ATOM    395  NH1 ARG A  41       8.519 -45.153 -23.442  1.00 89.82           N  
ANISOU  395  NH1 ARG A  41     9774  11368  12986    457    382  -1305       N  
ATOM    396  NH2 ARG A  41       7.887 -47.115 -22.433  1.00 94.28           N  
ANISOU  396  NH2 ARG A  41    10291  11605  13928    616    269  -1263       N  
ATOM    397  N   LEU A  42       7.155 -41.281 -17.766  1.00 29.53           N  
ANISOU  397  N   LEU A  42     2688   3713   4820    405   -192   -309       N  
ATOM    398  CA  LEU A  42       6.661 -39.992 -17.292  1.00 30.51           C  
ANISOU  398  CA  LEU A  42     2944   3910   4740    339   -224   -217       C  
ATOM    399  C   LEU A  42       7.802 -39.109 -16.800  1.00 29.82           C  
ANISOU  399  C   LEU A  42     2815   3884   4630    303   -265   -164       C  
ATOM    400  O   LEU A  42       7.839 -37.909 -17.092  1.00 30.28           O  
ANISOU  400  O   LEU A  42     2932   4028   4544    236   -240   -164       O  
ATOM    401  CB  LEU A  42       5.628 -40.203 -16.183  1.00 29.13           C  
ANISOU  401  CB  LEU A  42     2867   3675   4527    348   -307   -101       C  
ATOM    402  CG  LEU A  42       4.987 -38.936 -15.601  1.00 31.19           C  
ANISOU  402  CG  LEU A  42     3256   3996   4600    285   -333    -31       C  
ATOM    403  CD1 LEU A  42       4.385 -38.069 -16.707  1.00 25.97           C  
ANISOU  403  CD1 LEU A  42     2661   3395   3812    242   -250   -102       C  
ATOM    404  CD2 LEU A  42       3.925 -39.293 -14.565  1.00 31.94           C  
ANISOU  404  CD2 LEU A  42     3429   4046   4658    288   -397     56       C  
ATOM    405  N   ALA A  43       8.733 -39.682 -16.031  1.00 31.92           N  
ANISOU  405  N   ALA A  43     2978   4104   5046    341   -339   -107       N  
ATOM    406  CA  ALA A  43       9.910 -38.936 -15.606  1.00 33.03           C  
ANISOU  406  CA  ALA A  43     3062   4307   5179    304   -379    -60       C  
ATOM    407  C   ALA A  43      10.642 -38.330 -16.800  1.00 35.53           C  
ANISOU  407  C   ALA A  43     3320   4719   5462    268   -277   -176       C  
ATOM    408  O   ALA A  43      11.066 -37.164 -16.764  1.00 30.46           O  
ANISOU  408  O   ALA A  43     2710   4161   4701    198   -281   -148       O  
ATOM    409  CB  ALA A  43      10.844 -39.855 -14.814  1.00 31.73           C  
ANISOU  409  CB  ALA A  43     2762   4073   5223    357   -472     12       C  
ATOM    410  N   ALA A  44      10.823 -39.128 -17.861  1.00 30.76           N  
ANISOU  410  N   ALA A  44     2619   4104   4963    305   -184   -313       N  
ATOM    411  CA  ALA A  44      11.476 -38.631 -19.067  1.00 32.22           C  
ANISOU  411  CA  ALA A  44     2739   4405   5097    250    -75   -435       C  
ATOM    412  C   ALA A  44      10.674 -37.500 -19.703  1.00 31.12           C  
ANISOU  412  C   ALA A  44     2738   4360   4727    157    -33   -429       C  
ATOM    413  O   ALA A  44      11.253 -36.528 -20.206  1.00 30.68           O  
ANISOU  413  O   ALA A  44     2671   4413   4572     75     -2   -437       O  
ATOM    414  CB  ALA A  44      11.678 -39.774 -20.064  1.00 33.66           C  
ANISOU  414  CB  ALA A  44     2795   4568   5428    297     27   -608       C  
ATOM    415  N   ALA A  45       9.342 -37.613 -19.697  1.00 31.90           N  
ANISOU  415  N   ALA A  45     2958   4412   4751    163    -39   -405       N  
ATOM    416  CA  ALA A  45       8.499 -36.556 -20.255  1.00 32.83           C  
ANISOU  416  CA  ALA A  45     3197   4598   4679     80    -16   -380       C  
ATOM    417  C   ALA A  45       8.644 -35.266 -19.457  1.00 32.24           C  
ANISOU  417  C   ALA A  45     3197   4537   4514     32    -92   -263       C  
ATOM    418  O   ALA A  45       8.740 -34.175 -20.033  1.00 30.49           O  
ANISOU  418  O   ALA A  45     3007   4393   4182    -54    -75   -249       O  
ATOM    419  CB  ALA A  45       7.036 -37.008 -20.276  1.00 31.53           C  
ANISOU  419  CB  ALA A  45     3133   4368   4478    107    -17   -371       C  
ATOM    420  N   VAL A  46       8.670 -35.383 -18.124  1.00 29.77           N  
ANISOU  420  N   VAL A  46     2908   4152   4250     77   -180   -179       N  
ATOM    421  CA  VAL A  46       8.836 -34.226 -17.245  1.00 28.18           C  
ANISOU  421  CA  VAL A  46     2772   3964   3972     27   -250    -91       C  
ATOM    422  C   VAL A  46      10.193 -33.566 -17.469  1.00 27.25           C  
ANISOU  422  C   VAL A  46     2570   3924   3859    -27   -247    -96       C  
ATOM    423  O   VAL A  46      10.296 -32.340 -17.599  1.00 29.85           O  
ANISOU  423  O   VAL A  46     2949   4297   4095   -105   -256    -66       O  
ATOM    424  CB  VAL A  46       8.652 -34.662 -15.777  1.00 30.92           C  
ANISOU  424  CB  VAL A  46     3144   4245   4361     67   -340    -12       C  
ATOM    425  CG1 VAL A  46       9.102 -33.572 -14.812  1.00 29.38           C  
ANISOU  425  CG1 VAL A  46     2986   4080   4098      4   -407     54       C  
ATOM    426  CG2 VAL A  46       7.190 -35.083 -15.535  1.00 27.83           C  
ANISOU  426  CG2 VAL A  46     2849   3792   3933     99   -342     -1       C  
ATOM    427  N   LYS A  47      11.261 -34.367 -17.500  1.00 27.61           N  
ANISOU  427  N   LYS A  47     2479   3980   4031     13   -239   -130       N  
ATOM    428  CA  LYS A  47      12.595 -33.819 -17.727  1.00 32.57           C  
ANISOU  428  CA  LYS A  47     3010   4691   4674    -38   -231   -140       C  
ATOM    429  C   LYS A  47      12.654 -33.027 -19.033  1.00 36.40           C  
ANISOU  429  C   LYS A  47     3501   5279   5050   -128   -149   -196       C  
ATOM    430  O   LYS A  47      13.125 -31.881 -19.060  1.00 30.92           O  
ANISOU  430  O   LYS A  47     2827   4645   4277   -213   -170   -150       O  
ATOM    431  CB  LYS A  47      13.629 -34.949 -17.735  1.00 32.14           C  
ANISOU  431  CB  LYS A  47     2786   4623   4804     31   -220   -190       C  
ATOM    432  CG  LYS A  47      14.975 -34.573 -18.345  1.00 36.80           C  
ANISOU  432  CG  LYS A  47     3243   5317   5421    -18   -174   -243       C  
ATOM    433  CD  LYS A  47      15.892 -35.802 -18.435  1.00 36.47           C  
ANISOU  433  CD  LYS A  47     3012   5244   5600     66   -151   -318       C  
ATOM    434  CE  LYS A  47      17.358 -35.414 -18.642  1.00 46.90           C  
ANISOU  434  CE  LYS A  47     4187   6661   6973     24   -135   -342       C  
ATOM    435  NZ  LYS A  47      17.616 -34.843 -19.988  1.00 52.25           N  
ANISOU  435  NZ  LYS A  47     4833   7480   7537    -68    -12   -453       N  
ATOM    436  N   GLN A  48      12.174 -33.619 -20.131  1.00 33.71           N  
ANISOU  436  N   GLN A  48     3141   4967   4700   -123    -59   -290       N  
ATOM    437  CA  GLN A  48      12.190 -32.902 -21.405  1.00 35.66           C  
ANISOU  437  CA  GLN A  48     3390   5337   4824   -234     12   -328       C  
ATOM    438  C   GLN A  48      11.270 -31.685 -21.364  1.00 32.01           C  
ANISOU  438  C   GLN A  48     3075   4860   4229   -304    -39   -226       C  
ATOM    439  O   GLN A  48      11.602 -30.628 -21.916  1.00 30.46           O  
ANISOU  439  O   GLN A  48     2886   4744   3943   -413    -39   -186       O  
ATOM    440  CB  GLN A  48      11.790 -33.831 -22.553  1.00 40.31           C  
ANISOU  440  CB  GLN A  48     3930   5972   5415   -231    118   -457       C  
ATOM    441  CG  GLN A  48      11.842 -33.149 -23.933  1.00 42.11           C  
ANISOU  441  CG  GLN A  48     4147   6361   5492   -374    191   -492       C  
ATOM    442  CD  GLN A  48      11.493 -34.092 -25.072  1.00 46.71           C  
ANISOU  442  CD  GLN A  48     4674   7015   6060   -392    303   -640       C  
ATOM    443  OE1 GLN A  48      11.625 -35.311 -24.945  1.00 43.22           O  
ANISOU  443  OE1 GLN A  48     4152   6510   5759   -294    347   -753       O  
ATOM    444  NE2 GLN A  48      11.040 -33.530 -26.193  1.00 36.93           N  
ANISOU  444  NE2 GLN A  48     3471   5906   4654   -528    344   -636       N  
ATOM    445  N   ALA A  49      10.107 -31.816 -20.725  1.00 30.95           N  
ANISOU  445  N   ALA A  49     3049   4618   4092   -246    -84   -182       N  
ATOM    446  CA  ALA A  49       9.223 -30.666 -20.582  1.00 25.66           C  
ANISOU  446  CA  ALA A  49     2502   3911   3335   -298   -134    -96       C  
ATOM    447  C   ALA A  49       9.952 -29.524 -19.889  1.00 28.15           C  
ANISOU  447  C   ALA A  49     2829   4224   3643   -350   -199    -28       C  
ATOM    448  O   ALA A  49       9.919 -28.376 -20.351  1.00 29.58           O  
ANISOU  448  O   ALA A  49     3046   4431   3763   -443   -218     24       O  
ATOM    449  CB  ALA A  49       7.964 -31.059 -19.803  1.00 27.84           C  
ANISOU  449  CB  ALA A  49     2873   4075   3630   -219   -168    -75       C  
ATOM    450  N   TRP A  50      10.650 -29.833 -18.792  1.00 26.25           N  
ANISOU  450  N   TRP A  50     2551   3953   3469   -300   -242    -22       N  
ATOM    451  CA  TRP A  50      11.379 -28.796 -18.072  1.00 31.41           C  
ANISOU  451  CA  TRP A  50     3213   4610   4111   -357   -305     32       C  
ATOM    452  C   TRP A  50      12.404 -28.131 -18.980  1.00 33.89           C  
ANISOU  452  C   TRP A  50     3454   5030   4394   -454   -278     34       C  
ATOM    453  O   TRP A  50      12.554 -26.902 -18.969  1.00 31.41           O  
ANISOU  453  O   TRP A  50     3180   4716   4037   -541   -318     89       O  
ATOM    454  CB  TRP A  50      12.052 -29.394 -16.841  1.00 32.37           C  
ANISOU  454  CB  TRP A  50     3286   4710   4303   -302   -357     44       C  
ATOM    455  CG  TRP A  50      12.899 -28.434 -16.097  1.00 32.14           C  
ANISOU  455  CG  TRP A  50     3253   4701   4257   -369   -420     90       C  
ATOM    456  CD1 TRP A  50      14.256 -28.283 -16.202  1.00 37.74           C  
ANISOU  456  CD1 TRP A  50     3857   5487   4997   -411   -427     96       C  
ATOM    457  CD2 TRP A  50      12.462 -27.478 -15.120  1.00 36.16           C  
ANISOU  457  CD2 TRP A  50     3862   5158   4721   -411   -482    123       C  
ATOM    458  NE1 TRP A  50      14.687 -27.293 -15.346  1.00 39.41           N  
ANISOU  458  NE1 TRP A  50     4102   5695   5176   -479   -497    142       N  
ATOM    459  CE2 TRP A  50      13.607 -26.783 -14.672  1.00 36.23           C  
ANISOU  459  CE2 TRP A  50     3824   5212   4727   -482   -528    150       C  
ATOM    460  CE3 TRP A  50      11.213 -27.143 -14.580  1.00 37.68           C  
ANISOU  460  CE3 TRP A  50     4167   5271   4878   -398   -496    118       C  
ATOM    461  CZ2 TRP A  50      13.542 -25.775 -13.706  1.00 45.30           C  
ANISOU  461  CZ2 TRP A  50     5044   6330   5839   -545   -587    165       C  
ATOM    462  CZ3 TRP A  50      11.149 -26.142 -13.623  1.00 42.02           C  
ANISOU  462  CZ3 TRP A  50     4777   5790   5398   -456   -547    122       C  
ATOM    463  CH2 TRP A  50      12.309 -25.471 -13.193  1.00 39.96           C  
ANISOU  463  CH2 TRP A  50     4475   5574   5133   -531   -592    141       C  
ATOM    464  N   GLU A  51      13.092 -28.927 -19.800  1.00 34.90           N  
ANISOU  464  N   GLU A  51     3466   5246   4549   -448   -206    -33       N  
ATOM    465  CA  GLU A  51      14.101 -28.388 -20.701  1.00 37.29           C  
ANISOU  465  CA  GLU A  51     3682   5676   4810   -553   -168    -43       C  
ATOM    466  C   GLU A  51      13.499 -27.541 -21.810  1.00 34.13           C  
ANISOU  466  C   GLU A  51     3339   5331   4297   -666   -149     -4       C  
ATOM    467  O   GLU A  51      14.214 -26.730 -22.412  1.00 40.76           O  
ANISOU  467  O   GLU A  51     4138   6269   5081   -785   -147     31       O  
ATOM    468  CB  GLU A  51      14.924 -29.537 -21.277  1.00 33.99           C  
ANISOU  468  CB  GLU A  51     3112   5342   4461   -515    -81   -153       C  
ATOM    469  CG  GLU A  51      15.793 -30.189 -20.214  1.00 48.59           C  
ANISOU  469  CG  GLU A  51     4874   7144   6446   -426   -123   -158       C  
ATOM    470  CD  GLU A  51      16.300 -31.559 -20.606  1.00 56.23           C  
ANISOU  470  CD  GLU A  51     5694   8130   7543   -345    -48   -275       C  
ATOM    471  OE1 GLU A  51      15.789 -32.127 -21.597  1.00 57.78           O  
ANISOU  471  OE1 GLU A  51     5875   8362   7718   -345     42   -371       O  
ATOM    472  OE2 GLU A  51      17.210 -32.062 -19.910  1.00 56.53           O  
ANISOU  472  OE2 GLU A  51     5624   8143   7714   -286    -84   -273       O  
ATOM    473  N   GLU A  52      12.213 -27.701 -22.089  1.00 33.10           N  
ANISOU  473  N   GLU A  52     3298   5144   4135   -641   -145      4       N  
ATOM    474  CA  GLU A  52      11.513 -26.882 -23.069  1.00 33.48           C  
ANISOU  474  CA  GLU A  52     3403   5228   4089   -750   -151     70       C  
ATOM    475  C   GLU A  52      10.875 -25.650 -22.452  1.00 36.83           C  
ANISOU  475  C   GLU A  52     3936   5531   4527   -773   -249    177       C  
ATOM    476  O   GLU A  52      10.140 -24.936 -23.141  1.00 37.42           O  
ANISOU  476  O   GLU A  52     4062   5598   4559   -851   -278    254       O  
ATOM    477  CB  GLU A  52      10.437 -27.704 -23.771  1.00 36.90           C  
ANISOU  477  CB  GLU A  52     3863   5669   4488   -721    -99     24       C  
ATOM    478  CG  GLU A  52      10.998 -28.796 -24.649  1.00 49.50           C  
ANISOU  478  CG  GLU A  52     5345   7398   6065   -730     10   -102       C  
ATOM    479  CD  GLU A  52       9.925 -29.711 -25.232  1.00 56.27           C  
ANISOU  479  CD  GLU A  52     6229   8252   6897   -695     63   -165       C  
ATOM    480  OE1 GLU A  52       8.725 -29.542 -24.892  1.00 53.22           O  
ANISOU  480  OE1 GLU A  52     5951   7758   6512   -654     10   -100       O  
ATOM    481  OE2 GLU A  52      10.294 -30.605 -26.028  1.00 51.75           O  
ANISOU  481  OE2 GLU A  52     5563   7788   6311   -713    162   -291       O  
ATOM    482  N   GLY A  53      11.107 -25.397 -21.169  1.00 31.00           N  
ANISOU  482  N   GLY A  53     3228   4696   3855   -713   -302    181       N  
ATOM    483  CA  GLY A  53      10.533 -24.233 -20.529  1.00 28.90           C  
ANISOU  483  CA  GLY A  53     3054   4309   3619   -734   -382    248       C  
ATOM    484  C   GLY A  53       9.158 -24.443 -19.940  1.00 31.96           C  
ANISOU  484  C   GLY A  53     3532   4573   4040   -645   -396    234       C  
ATOM    485  O   GLY A  53       8.495 -23.460 -19.582  1.00 30.32           O  
ANISOU  485  O   GLY A  53     3391   4257   3871   -664   -451    274       O  
ATOM    486  N   ILE A  54       8.702 -25.686 -19.844  1.00 25.49           N  
ANISOU  486  N   ILE A  54     2707   3761   3219   -552   -348    174       N  
ATOM    487  CA  ILE A  54       7.452 -26.018 -19.174  1.00 25.90           C  
ANISOU  487  CA  ILE A  54     2835   3710   3297   -466   -358    156       C  
ATOM    488  C   ILE A  54       7.784 -26.252 -17.705  1.00 28.82           C  
ANISOU  488  C   ILE A  54     3214   4036   3699   -409   -386    123       C  
ATOM    489  O   ILE A  54       8.499 -27.197 -17.367  1.00 31.29           O  
ANISOU  489  O   ILE A  54     3467   4398   4024   -366   -370     94       O  
ATOM    490  CB  ILE A  54       6.794 -27.253 -19.800  1.00 28.59           C  
ANISOU  490  CB  ILE A  54     3165   4081   3618   -409   -298    116       C  
ATOM    491  CG1 ILE A  54       6.549 -27.016 -21.299  1.00 31.28           C  
ANISOU  491  CG1 ILE A  54     3488   4497   3898   -495   -271    150       C  
ATOM    492  CG2 ILE A  54       5.473 -27.603 -19.068  1.00 26.57           C  
ANISOU  492  CG2 ILE A  54     2986   3725   3387   -326   -310    104       C  
ATOM    493  CD1 ILE A  54       5.967 -28.230 -22.021  1.00 34.45           C  
ANISOU  493  CD1 ILE A  54     3873   4947   4270   -458   -205     93       C  
ATOM    494  N   CYS A  55       7.290 -25.386 -16.830  1.00 25.57           N  
ANISOU  494  N   CYS A  55     2868   3539   3309   -418   -430    126       N  
ATOM    495  CA  CYS A  55       7.723 -25.425 -15.441  1.00 26.01           C  
ANISOU  495  CA  CYS A  55     2929   3584   3368   -404   -462     96       C  
ATOM    496  C   CYS A  55       6.754 -26.161 -14.530  1.00 29.65           C  
ANISOU  496  C   CYS A  55     3436   4007   3823   -333   -457     61       C  
ATOM    497  O   CYS A  55       6.970 -26.183 -13.316  1.00 24.55           O  
ANISOU  497  O   CYS A  55     2800   3368   3161   -340   -487     41       O  
ATOM    498  CB  CYS A  55       7.955 -23.999 -14.910  1.00 29.89           C  
ANISOU  498  CB  CYS A  55     3452   4024   3880   -480   -509     95       C  
ATOM    499  SG  CYS A  55       6.579 -22.819 -15.172  1.00 43.05           S  
ANISOU  499  SG  CYS A  55     5192   5554   5610   -494   -522     91       S  
ATOM    500  N   GLY A  56       5.694 -26.754 -15.065  1.00 27.58           N  
ANISOU  500  N   GLY A  56     3199   3717   3562   -279   -422     57       N  
ATOM    501  CA  GLY A  56       4.779 -27.467 -14.203  1.00 25.64           C  
ANISOU  501  CA  GLY A  56     2993   3444   3306   -222   -417     30       C  
ATOM    502  C   GLY A  56       3.523 -27.897 -14.929  1.00 27.79           C  
ANISOU  502  C   GLY A  56     3296   3678   3584   -175   -381     28       C  
ATOM    503  O   GLY A  56       3.445 -27.882 -16.163  1.00 27.04           O  
ANISOU  503  O   GLY A  56     3185   3596   3493   -186   -358     51       O  
ATOM    504  N   ILE A  57       2.537 -28.270 -14.118  1.00 25.89           N  
ANISOU  504  N   ILE A  57     3098   3405   3333   -137   -377      2       N  
ATOM    505  CA  ILE A  57       1.331 -28.950 -14.570  1.00 23.57           C  
ANISOU  505  CA  ILE A  57     2830   3085   3042    -86   -347      1       C  
ATOM    506  C   ILE A  57       0.126 -28.276 -13.938  1.00 24.24           C  
ANISOU  506  C   ILE A  57     2966   3107   3137    -84   -344    -36       C  
ATOM    507  O   ILE A  57       0.158 -27.903 -12.756  1.00 27.29           O  
ANISOU  507  O   ILE A  57     3368   3496   3506   -107   -356    -79       O  
ATOM    508  CB  ILE A  57       1.351 -30.449 -14.181  1.00 27.12           C  
ANISOU  508  CB  ILE A  57     3258   3567   3480    -35   -342      7       C  
ATOM    509  CG1 ILE A  57       2.539 -31.184 -14.813  1.00 28.65           C  
ANISOU  509  CG1 ILE A  57     3379   3807   3700    -26   -337     22       C  
ATOM    510  CG2 ILE A  57       0.033 -31.118 -14.521  1.00 27.56           C  
ANISOU  510  CG2 ILE A  57     3345   3591   3535      9   -313      3       C  
ATOM    511  CD1 ILE A  57       2.378 -31.422 -16.300  1.00 28.35           C  
ANISOU  511  CD1 ILE A  57     3320   3783   3669    -23   -290     12       C  
ATOM    512  N   SER A  58      -0.937 -28.130 -14.721  1.00 23.28           N  
ANISOU  512  N   SER A  58     2862   2937   3045    -63   -327    -25       N  
ATOM    513  CA  SER A  58      -2.286 -27.913 -14.209  1.00 30.51           C  
ANISOU  513  CA  SER A  58     3811   3799   3985    -38   -312    -64       C  
ATOM    514  C   SER A  58      -3.082 -29.172 -14.525  1.00 28.91           C  
ANISOU  514  C   SER A  58     3613   3617   3752     11   -288    -46       C  
ATOM    515  O   SER A  58      -3.343 -29.460 -15.697  1.00 26.95           O  
ANISOU  515  O   SER A  58     3358   3371   3513     18   -280     -5       O  
ATOM    516  CB  SER A  58      -2.928 -26.682 -14.843  1.00 31.28           C  
ANISOU  516  CB  SER A  58     3909   3807   4169    -54   -326    -55       C  
ATOM    517  OG  SER A  58      -2.191 -25.517 -14.515  1.00 38.23           O  
ANISOU  517  OG  SER A  58     4782   4650   5093   -103   -353    -75       O  
ATOM    518  N   SER A  59      -3.431 -29.938 -13.489  1.00 23.88           N  
ANISOU  518  N   SER A  59     2990   3010   3075     29   -279    -73       N  
ATOM    519  CA  SER A  59      -4.163 -31.184 -13.696  1.00 24.89           C  
ANISOU  519  CA  SER A  59     3122   3151   3182     70   -263    -51       C  
ATOM    520  C   SER A  59      -5.520 -30.893 -14.333  1.00 22.70           C  
ANISOU  520  C   SER A  59     2860   2825   2940     90   -242    -54       C  
ATOM    521  O   SER A  59      -6.154 -29.875 -14.049  1.00 24.09           O  
ANISOU  521  O   SER A  59     3042   2952   3159     82   -238    -89       O  
ATOM    522  CB  SER A  59      -4.372 -31.915 -12.365  1.00 27.73           C  
ANISOU  522  CB  SER A  59     3492   3554   3492     65   -269    -63       C  
ATOM    523  OG  SER A  59      -3.155 -32.369 -11.783  1.00 27.27           O  
ANISOU  523  OG  SER A  59     3409   3543   3410     44   -305    -34       O  
ATOM    524  N  AVAL A  60      -5.970 -31.805 -15.195  0.50 23.08           N  
ANISOU  524  N  AVAL A  60     2907   2881   2981    114   -230    -21       N  
ATOM    525  N  BVAL A  60      -5.980 -31.804 -15.189  0.50 23.18           N  
ANISOU  525  N  BVAL A  60     2919   2893   2993    114   -230    -21       N  
ATOM    526  CA AVAL A  60      -7.301 -31.654 -15.777  0.50 26.72           C  
ANISOU  526  CA AVAL A  60     3377   3306   3470    127   -219    -11       C  
ATOM    527  CA BVAL A  60      -7.310 -31.591 -15.750  0.50 26.75           C  
ANISOU  527  CA BVAL A  60     3380   3307   3475    127   -220    -12       C  
ATOM    528  C  AVAL A  60      -8.371 -32.030 -14.768  0.50 28.78           C  
ANISOU  528  C  AVAL A  60     3652   3564   3718    149   -201    -45       C  
ATOM    529  C  BVAL A  60      -8.390 -32.045 -14.781  0.50 28.76           C  
ANISOU  529  C  BVAL A  60     3650   3562   3716    150   -201    -44       C  
ATOM    530  O  AVAL A  60      -9.433 -31.399 -14.709  0.50 29.58           O  
ANISOU  530  O  AVAL A  60     3750   3624   3865    158   -191    -65       O  
ATOM    531  O  BVAL A  60      -9.484 -31.469 -14.759  0.50 30.04           O  
ANISOU  531  O  BVAL A  60     3808   3683   3921    159   -190    -62       O  
ATOM    532  CB AVAL A  60      -7.438 -32.501 -17.050  0.50 26.08           C  
ANISOU  532  CB AVAL A  60     3288   3251   3370    127   -211     27       C  
ATOM    533  CB BVAL A  60      -7.472 -32.287 -17.111  0.50 27.29           C  
ANISOU  533  CB BVAL A  60     3441   3398   3530    123   -214     30       C  
ATOM    534  CG1AVAL A  60      -8.675 -32.068 -17.867  0.50 17.17           C  
ANISOU  534  CG1AVAL A  60     2161   2092   2271    119   -217     61       C  
ATOM    535  CG1BVAL A  60      -6.504 -31.717 -18.078  0.50 31.32           C  
ANISOU  535  CG1BVAL A  60     3929   3931   4038     79   -226     57       C  
ATOM    536  CG2AVAL A  60      -6.197 -32.394 -17.850  0.50 30.08           C  
ANISOU  536  CG2AVAL A  60     3770   3795   3864     94   -215     40       C  
ATOM    537  CG2BVAL A  60      -7.282 -33.778 -16.996  0.50 27.13           C  
ANISOU  537  CG2BVAL A  60     3419   3412   3477    148   -197     19       C  
ATOM    538  N   SER A  61      -8.112 -33.060 -13.964  1.00 26.00           N  
ANISOU  538  N   SER A  61     3307   3258   3315    153   -201    -46       N  
ATOM    539  CA  SER A  61      -9.142 -33.671 -13.146  1.00 24.90           C  
ANISOU  539  CA  SER A  61     3178   3139   3144    157   -185    -60       C  
ATOM    540  C   SER A  61      -8.609 -33.947 -11.751  1.00 30.15           C  
ANISOU  540  C   SER A  61     3845   3863   3749    121   -199    -71       C  
ATOM    541  O   SER A  61      -7.400 -34.022 -11.528  1.00 26.58           O  
ANISOU  541  O   SER A  61     3384   3432   3286    105   -229    -50       O  
ATOM    542  CB  SER A  61      -9.625 -34.969 -13.780  1.00 24.95           C  
ANISOU  542  CB  SER A  61     3188   3147   3147    180   -186    -16       C  
ATOM    543  OG  SER A  61      -8.601 -35.946 -13.709  1.00 27.84           O  
ANISOU  543  OG  SER A  61     3543   3529   3507    182   -210     15       O  
ATOM    544  N   ARG A  62      -9.544 -34.091 -10.808  1.00 24.57           N  
ANISOU  544  N   ARG A  62     3143   3195   2997     97   -179   -100       N  
ATOM    545  CA  ARG A  62      -9.182 -34.525  -9.464  1.00 22.38           C  
ANISOU  545  CA  ARG A  62     2866   3004   2635     36   -199    -92       C  
ATOM    546  C   ARG A  62      -8.357 -35.808  -9.502  1.00 22.33           C  
ANISOU  546  C   ARG A  62     2852   3007   2625     39   -257      8       C  
ATOM    547  O   ARG A  62      -7.373 -35.945  -8.767  1.00 25.75           O  
ANISOU  547  O   ARG A  62     3272   3487   3025     -4   -301     43       O  
ATOM    548  CB  ARG A  62     -10.452 -34.728  -8.630  1.00 28.27           C  
ANISOU  548  CB  ARG A  62     3611   3808   3321      0   -164   -128       C  
ATOM    549  CG  ARG A  62     -10.245 -34.794  -7.137  1.00 37.43           C  
ANISOU  549  CG  ARG A  62     4767   5087   4367    -96   -173   -144       C  
ATOM    550  CD  ARG A  62     -11.553 -35.162  -6.459  1.00 42.04           C  
ANISOU  550  CD  ARG A  62     5344   5745   4885   -140   -133   -173       C  
ATOM    551  NE  ARG A  62     -12.043 -36.411  -7.019  1.00 42.20           N  
ANISOU  551  NE  ARG A  62     5372   5734   4928   -105   -162    -71       N  
ATOM    552  CZ  ARG A  62     -11.944 -37.593  -6.422  1.00 38.49           C  
ANISOU  552  CZ  ARG A  62     4903   5324   4399   -160   -217     34       C  
ATOM    553  NH1 ARG A  62     -11.410 -37.702  -5.214  1.00 40.52           N  
ANISOU  553  NH1 ARG A  62     5152   5693   4550   -262   -254     66       N  
ATOM    554  NH2 ARG A  62     -12.400 -38.669  -7.037  1.00 31.48           N  
ANISOU  554  NH2 ARG A  62     4020   4383   3560   -121   -242    114       N  
ATOM    555  N   MET A  63      -8.749 -36.766 -10.350  1.00 26.98           N  
ANISOU  555  N   MET A  63     3440   3549   3262     86   -261     53       N  
ATOM    556  CA  MET A  63      -8.063 -38.057 -10.378  1.00 29.45           C  
ANISOU  556  CA  MET A  63     3732   3846   3610     95   -314    135       C  
ATOM    557  C   MET A  63      -6.618 -37.904 -10.846  1.00 30.33           C  
ANISOU  557  C   MET A  63     3814   3931   3778    116   -338    142       C  
ATOM    558  O   MET A  63      -5.725 -38.618 -10.375  1.00 26.42           O  
ANISOU  558  O   MET A  63     3285   3441   3314    106   -395    205       O  
ATOM    559  CB  MET A  63      -8.817 -39.034 -11.288  1.00 32.05           C  
ANISOU  559  CB  MET A  63     4064   4120   3994    138   -302    152       C  
ATOM    560  CG  MET A  63     -10.195 -39.446 -10.780  1.00 36.86           C  
ANISOU  560  CG  MET A  63     4693   4758   4554    111   -290    165       C  
ATOM    561  SD  MET A  63     -10.085 -40.664  -9.469  1.00 42.24           S  
ANISOU  561  SD  MET A  63     5360   5486   5202     47   -365    274       S  
ATOM    562  CE  MET A  63      -9.527 -42.075 -10.418  1.00 35.15           C  
ANISOU  562  CE  MET A  63     4432   4475   4448    106   -408    327       C  
ATOM    563  N   GLU A  64      -6.370 -36.987 -11.780  1.00 32.26           N  
ANISOU  563  N   GLU A  64     4062   4150   4046    141   -300     86       N  
ATOM    564  CA  GLU A  64      -5.001 -36.772 -12.238  1.00 27.66           C  
ANISOU  564  CA  GLU A  64     3445   3559   3507    151   -315     86       C  
ATOM    565  C   GLU A  64      -4.128 -36.201 -11.125  1.00 23.72           C  
ANISOU  565  C   GLU A  64     2935   3110   2966    102   -353    100       C  
ATOM    566  O   GLU A  64      -2.988 -36.640 -10.927  1.00 25.89           O  
ANISOU  566  O   GLU A  64     3167   3392   3279    100   -397    143       O  
ATOM    567  CB  GLU A  64      -4.983 -35.845 -13.453  1.00 27.19           C  
ANISOU  567  CB  GLU A  64     3391   3479   3463    163   -272     39       C  
ATOM    568  CG  GLU A  64      -3.557 -35.637 -13.959  1.00 27.95           C  
ANISOU  568  CG  GLU A  64     3443   3583   3593    162   -281     37       C  
ATOM    569  CD  GLU A  64      -3.455 -34.613 -15.045  1.00 30.31           C  
ANISOU  569  CD  GLU A  64     3746   3881   3890    146   -251     10       C  
ATOM    570  OE1 GLU A  64      -4.467 -34.344 -15.726  1.00 26.68           O  
ANISOU  570  OE1 GLU A  64     3312   3403   3422    147   -228      4       O  
ATOM    571  OE2 GLU A  64      -2.349 -34.078 -15.215  1.00 30.44           O  
ANISOU  571  OE2 GLU A  64     3733   3918   3915    125   -260      7       O  
ATOM    572  N   ASN A  65      -4.645 -35.224 -10.382  1.00 23.32           N  
ANISOU  572  N   ASN A  65     2917   3096   2849     58   -336     57       N  
ATOM    573  CA  ASN A  65      -3.874 -34.658  -9.279  1.00 27.57           C  
ANISOU  573  CA  ASN A  65     3449   3697   3331     -7   -369     55       C  
ATOM    574  C   ASN A  65      -3.549 -35.713  -8.221  1.00 28.81           C  
ANISOU  574  C   ASN A  65     3583   3914   3450    -53   -435    143       C  
ATOM    575  O   ASN A  65      -2.437 -35.737  -7.683  1.00 30.08           O  
ANISOU  575  O   ASN A  65     3711   4113   3605    -91   -491    190       O  
ATOM    576  CB  ASN A  65      -4.637 -33.489  -8.662  1.00 24.99           C  
ANISOU  576  CB  ASN A  65     3152   3396   2947    -51   -326    -37       C  
ATOM    577  CG  ASN A  65      -4.019 -33.011  -7.352  1.00 31.54           C  
ANISOU  577  CG  ASN A  65     3978   4315   3692   -143   -352    -57       C  
ATOM    578  OD1 ASN A  65      -4.353 -33.524  -6.300  1.00 30.48           O  
ANISOU  578  OD1 ASN A  65     3845   4267   3471   -208   -371    -35       O  
ATOM    579  ND2 ASN A  65      -3.111 -32.029  -7.422  1.00 27.63           N  
ANISOU  579  ND2 ASN A  65     3474   3809   3213   -163   -358    -95       N  
ATOM    580  N   ILE A  66      -4.510 -36.584  -7.899  1.00 25.50           N  
ANISOU  580  N   ILE A  66     3175   3505   3007    -59   -439    180       N  
ATOM    581  CA  ILE A  66      -4.252 -37.663  -6.941  1.00 30.22           C  
ANISOU  581  CA  ILE A  66     3747   4154   3581   -113   -520    294       C  
ATOM    582  C   ILE A  66      -3.148 -38.574  -7.458  1.00 28.77           C  
ANISOU  582  C   ILE A  66     3505   3901   3526    -60   -582    377       C  
ATOM    583  O   ILE A  66      -2.295 -39.047  -6.688  1.00 26.31           O  
ANISOU  583  O   ILE A  66     3148   3623   3224   -108   -669    476       O  
ATOM    584  CB  ILE A  66      -5.545 -38.454  -6.663  1.00 31.04           C  
ANISOU  584  CB  ILE A  66     3871   4272   3650   -129   -512    324       C  
ATOM    585  CG1 ILE A  66      -6.534 -37.613  -5.852  1.00 31.63           C  
ANISOU  585  CG1 ILE A  66     3982   4444   3593   -202   -455    239       C  
ATOM    586  CG2 ILE A  66      -5.232 -39.791  -5.965  1.00 32.91           C  
ANISOU  586  CG2 ILE A  66     4072   4525   3908   -174   -614    475       C  
ATOM    587  CD1 ILE A  66      -7.973 -38.156  -5.896  1.00 36.04           C  
ANISOU  587  CD1 ILE A  66     4559   5006   4129   -199   -418    234       C  
ATOM    588  N  AMET A  67      -3.139 -38.823  -8.771  0.50 25.08           N  
ANISOU  588  N  AMET A  67     3028   3339   3163     31   -539    334       N  
ATOM    589  N  BMET A  67      -3.148 -38.832  -8.769  0.50 25.08           N  
ANISOU  589  N  BMET A  67     3027   3339   3162     31   -539    334       N  
ATOM    590  CA AMET A  67      -2.091 -39.642  -9.377  0.50 29.02           C  
ANISOU  590  CA AMET A  67     3456   3768   3803     87   -576    372       C  
ATOM    591  CA BMET A  67      -2.094 -39.637  -9.384  0.50 29.06           C  
ANISOU  591  CA BMET A  67     3462   3773   3808     87   -575    371       C  
ATOM    592  C  AMET A  67      -0.721 -39.006  -9.197  0.50 28.27           C  
ANISOU  592  C  AMET A  67     3317   3703   3720     70   -604    376       C  
ATOM    593  C  BMET A  67      -0.729 -39.000  -9.177  0.50 28.27           C  
ANISOU  593  C  BMET A  67     3319   3705   3719     68   -605    377       C  
ATOM    594  O  AMET A  67       0.238 -39.672  -8.788  0.50 30.66           O  
ANISOU  594  O  AMET A  67     3549   3994   4106     66   -682    460       O  
ATOM    595  O  BMET A  67       0.219 -39.660  -8.735  0.50 30.45           O  
ANISOU  595  O  BMET A  67     3525   3972   4075     62   -684    463       O  
ATOM    596  CB AMET A  67      -2.374 -39.852 -10.866  0.50 22.89           C  
ANISOU  596  CB AMET A  67     2678   2916   3104    165   -503    290       C  
ATOM    597  CB BMET A  67      -2.369 -39.815 -10.879  0.50 22.57           C  
ANISOU  597  CB BMET A  67     2638   2877   3061    165   -501    288       C  
ATOM    598  CG AMET A  67      -1.380 -40.809 -11.530  0.50 26.66           C  
ANISOU  598  CG AMET A  67     3069   3320   3741    222   -522    295       C  
ATOM    599  CG BMET A  67      -1.333 -40.689 -11.601  0.50 26.50           C  
ANISOU  599  CG BMET A  67     3050   3304   3716    223   -515    286       C  
ATOM    600  SD AMET A  67      -1.371 -40.740 -13.331  0.50 25.91           S  
ANISOU  600  SD AMET A  67     2959   3187   3697    279   -420    166       S  
ATOM    601  SD BMET A  67       0.166 -39.832 -12.139  0.50 39.57           S  
ANISOU  601  SD BMET A  67     4649   4986   5400    230   -495    235       S  
ATOM    602  CE AMET A  67      -0.543 -39.168 -13.578  0.50 36.67           C  
ANISOU  602  CE AMET A  67     4330   4624   4979    246   -389    123       C  
ATOM    603  CE BMET A  67      -0.421 -38.965 -13.591  0.50 40.73           C  
ANISOU  603  CE BMET A  67     4844   5147   5483    241   -386    119       C  
ATOM    604  N   TRP A  68      -0.603 -37.718  -9.526  1.00 28.93           N  
ANISOU  604  N   TRP A  68     3435   3819   3739     57   -548    293       N  
ATOM    605  CA  TRP A  68       0.667 -37.023  -9.347  1.00 30.51           C  
ANISOU  605  CA  TRP A  68     3597   4054   3942     30   -574    294       C  
ATOM    606  C   TRP A  68       1.165 -37.140  -7.912  1.00 31.00           C  
ANISOU  606  C   TRP A  68     3640   4191   3947    -53   -664    385       C  
ATOM    607  O   TRP A  68       2.342 -37.442  -7.672  1.00 26.38           O  
ANISOU  607  O   TRP A  68     2983   3613   3428    -61   -730    451       O  
ATOM    608  CB  TRP A  68       0.519 -35.558  -9.743  1.00 23.12           C  
ANISOU  608  CB  TRP A  68     2711   3136   2939     11   -511    202       C  
ATOM    609  CG  TRP A  68       0.504 -35.303 -11.237  1.00 29.23           C  
ANISOU  609  CG  TRP A  68     3480   3858   3769     68   -446    142       C  
ATOM    610  CD1 TRP A  68      -0.579 -34.975 -11.999  1.00 27.13           C  
ANISOU  610  CD1 TRP A  68     3262   3562   3485     89   -387     92       C  
ATOM    611  CD2 TRP A  68       1.631 -35.324 -12.129  1.00 24.54           C  
ANISOU  611  CD2 TRP A  68     2822   3256   3246     91   -435    129       C  
ATOM    612  NE1 TRP A  68      -0.199 -34.803 -13.315  1.00 27.01           N  
ANISOU  612  NE1 TRP A  68     3222   3529   3512    113   -348     60       N  
ATOM    613  CE2 TRP A  68       1.154 -35.003 -13.416  1.00 29.09           C  
ANISOU  613  CE2 TRP A  68     3417   3811   3825    112   -369     72       C  
ATOM    614  CE3 TRP A  68       3.000 -35.578 -11.958  1.00 29.80           C  
ANISOU  614  CE3 TRP A  68     3408   3940   3974     89   -477    161       C  
ATOM    615  CZ2 TRP A  68       1.994 -34.931 -14.535  1.00 27.86           C  
ANISOU  615  CZ2 TRP A  68     3206   3668   3711    119   -335     39       C  
ATOM    616  CZ3 TRP A  68       3.838 -35.507 -13.067  1.00 28.12           C  
ANISOU  616  CZ3 TRP A  68     3135   3727   3821    110   -437    118       C  
ATOM    617  CH2 TRP A  68       3.330 -35.194 -14.341  1.00 27.39           C  
ANISOU  617  CH2 TRP A  68     3067   3630   3712    120   -362     53       C  
ATOM    618  N   LYS A  69       0.273 -36.937  -6.940  1.00 28.63           N  
ANISOU  618  N   LYS A  69     3394   3959   3524   -126   -668    389       N  
ATOM    619  CA  LYS A  69       0.678 -37.037  -5.542  1.00 34.92           C  
ANISOU  619  CA  LYS A  69     4174   4860   4235   -236   -754    477       C  
ATOM    620  C   LYS A  69       1.225 -38.425  -5.228  1.00 35.95           C  
ANISOU  620  C   LYS A  69     4230   4964   4467   -231   -863    633       C  
ATOM    621  O   LYS A  69       2.222 -38.556  -4.509  1.00 33.24           O  
ANISOU  621  O   LYS A  69     3830   4671   4129   -292   -957    731       O  
ATOM    622  CB  LYS A  69      -0.503 -36.690  -4.637  1.00 35.20           C  
ANISOU  622  CB  LYS A  69     4273   4988   4115   -323   -723    436       C  
ATOM    623  CG  LYS A  69      -0.117 -36.181  -3.260  1.00 55.69           C  
ANISOU  623  CG  LYS A  69     6868   7730   6564   -469   -772    457       C  
ATOM    624  CD  LYS A  69       0.877 -35.020  -3.361  1.00 69.60           C  
ANISOU  624  CD  LYS A  69     8622   9503   8320   -485   -758    383       C  
ATOM    625  CE  LYS A  69       1.273 -34.475  -1.988  1.00 72.24           C  
ANISOU  625  CE  LYS A  69     8956   9994   8497   -646   -804    386       C  
ATOM    626  NZ  LYS A  69       2.500 -33.617  -2.054  1.00 67.91           N  
ANISOU  626  NZ  LYS A  69     8384   9452   7966   -667   -824    359       N  
ATOM    627  N   SER A  70       0.619 -39.473  -5.799  1.00 32.86           N  
ANISOU  627  N   SER A  70     3829   4481   4176   -159   -858    662       N  
ATOM    628  CA  SER A  70       1.028 -40.832  -5.460  1.00 33.17           C  
ANISOU  628  CA  SER A  70     3791   4469   4343   -155   -970    814       C  
ATOM    629  C   SER A  70       2.358 -41.216  -6.100  1.00 34.46           C  
ANISOU  629  C   SER A  70     3853   4543   4699    -76  -1006    835       C  
ATOM    630  O   SER A  70       3.082 -42.046  -5.545  1.00 32.93           O  
ANISOU  630  O   SER A  70     3571   4323   4616    -95  -1125    977       O  
ATOM    631  CB  SER A  70      -0.050 -41.833  -5.873  1.00 38.40           C  
ANISOU  631  CB  SER A  70     4472   5050   5069   -107   -953    827       C  
ATOM    632  OG  SER A  70      -0.181 -41.877  -7.288  1.00 45.25           O  
ANISOU  632  OG  SER A  70     5340   5811   6041     11   -858    705       O  
ATOM    633  N   VAL A  71       2.707 -40.620  -7.242  1.00 29.43           N  
ANISOU  633  N   VAL A  71     3215   3862   4106      3   -909    701       N  
ATOM    634  CA  VAL A  71       3.917 -40.990  -7.974  1.00 30.96           C  
ANISOU  634  CA  VAL A  71     3301   3980   4483     78   -919    689       C  
ATOM    635  C   VAL A  71       5.055 -39.994  -7.762  1.00 37.60           C  
ANISOU  635  C   VAL A  71     4112   4896   5278     38   -931    678       C  
ATOM    636  O   VAL A  71       6.176 -40.230  -8.236  1.00 36.85           O  
ANISOU  636  O   VAL A  71     3914   4758   5328     87   -944    675       O  
ATOM    637  CB  VAL A  71       3.588 -41.147  -9.476  1.00 34.14           C  
ANISOU  637  CB  VAL A  71     3706   4300   4965    177   -802    547       C  
ATOM    638  CG1 VAL A  71       3.434 -39.772 -10.150  1.00 24.36           C  
ANISOU  638  CG1 VAL A  71     2538   3124   3592    165   -699    424       C  
ATOM    639  CG2 VAL A  71       4.611 -42.017 -10.183  1.00 45.15           C  
ANISOU  639  CG2 VAL A  71     4969   5599   6587    258   -812    529       C  
ATOM    640  N   GLU A  72       4.798 -38.903  -7.031  1.00 29.16           N  
ANISOU  640  N   GLU A  72     3123   3937   4020    -55   -925    665       N  
ATOM    641  CA  GLU A  72       5.779 -37.837  -6.817  1.00 34.04           C  
ANISOU  641  CA  GLU A  72     3726   4627   4580   -107   -931    642       C  
ATOM    642  C   GLU A  72       7.113 -38.368  -6.302  1.00 36.99           C  
ANISOU  642  C   GLU A  72     3980   5009   5067   -125  -1046    765       C  
ATOM    643  O   GLU A  72       8.178 -38.050  -6.846  1.00 31.85           O  
ANISOU  643  O   GLU A  72     3258   4346   4497    -92  -1033    732       O  
ATOM    644  CB  GLU A  72       5.197 -36.825  -5.825  1.00 29.65           C  
ANISOU  644  CB  GLU A  72     3264   4184   3817   -222   -926    619       C  
ATOM    645  CG  GLU A  72       6.095 -35.652  -5.466  1.00 40.82           C  
ANISOU  645  CG  GLU A  72     4677   5677   5157   -295   -935    586       C  
ATOM    646  CD  GLU A  72       5.534 -34.864  -4.292  1.00 49.42           C  
ANISOU  646  CD  GLU A  72     5841   6881   6054   -425   -940    559       C  
ATOM    647  OE1 GLU A  72       5.144 -35.499  -3.288  1.00 63.02           O  
ANISOU  647  OE1 GLU A  72     7565   8674   7706   -501  -1008    651       O  
ATOM    648  OE2 GLU A  72       5.456 -33.620  -4.375  1.00 46.89           O  
ANISOU  648  OE2 GLU A  72     5573   6583   5658   -457   -876    442       O  
ATOM    649  N   GLY A  73       7.078 -39.149  -5.224  1.00 32.80           N  
ANISOU  649  N   GLY A  73     3419   4505   4540   -188  -1166    918       N  
ATOM    650  CA  GLY A  73       8.321 -39.627  -4.642  1.00 35.97           C  
ANISOU  650  CA  GLY A  73     3697   4916   5055   -217  -1297   1062       C  
ATOM    651  C   GLY A  73       9.102 -40.502  -5.602  1.00 36.09           C  
ANISOU  651  C   GLY A  73     3581   4791   5340    -86  -1298   1056       C  
ATOM    652  O   GLY A  73      10.329 -40.392  -5.704  1.00 34.97           O  
ANISOU  652  O   GLY A  73     3333   4649   5306    -72  -1336   1078       O  
ATOM    653  N   GLU A  74       8.398 -41.365  -6.337  1.00 34.60           N  
ANISOU  653  N   GLU A  74     3392   4485   5269      9  -1248   1009       N  
ATOM    654  CA  GLU A  74       9.066 -42.260  -7.278  1.00 36.81           C  
ANISOU  654  CA  GLU A  74     3541   4628   5819    132  -1232    969       C  
ATOM    655  C   GLU A  74       9.642 -41.492  -8.461  1.00 28.49           C  
ANISOU  655  C   GLU A  74     2470   3587   4770    188  -1100    792       C  
ATOM    656  O   GLU A  74      10.778 -41.746  -8.872  1.00 33.66           O  
ANISOU  656  O   GLU A  74     2987   4201   5600    239  -1109    775       O  
ATOM    657  CB  GLU A  74       8.093 -43.333  -7.760  1.00 36.37           C  
ANISOU  657  CB  GLU A  74     3498   4450   5871    203  -1205    945       C  
ATOM    658  CG  GLU A  74       8.733 -44.379  -8.663  1.00 53.01           C  
ANISOU  658  CG  GLU A  74     5457   6403   8282    325  -1189    886       C  
ATOM    659  CD  GLU A  74       7.823 -45.566  -8.932  1.00 59.87           C  
ANISOU  659  CD  GLU A  74     6327   7138   9281    379  -1192    888       C  
ATOM    660  OE1 GLU A  74       6.581 -45.398  -8.923  1.00 53.49           O  
ANISOU  660  OE1 GLU A  74     5654   6367   8303    346  -1144    863       O  
ATOM    661  OE2 GLU A  74       8.361 -46.672  -9.145  1.00 71.66           O  
ANISOU  661  OE2 GLU A  74     7679   8485  11065    455  -1246    911       O  
ATOM    662  N   LEU A  75       8.873 -40.556  -9.026  1.00 31.29           N  
ANISOU  662  N   LEU A  75     2951   3997   4940    172   -982    667       N  
ATOM    663  CA  LEU A  75       9.411 -39.693 -10.079  1.00 32.17           C  
ANISOU  663  CA  LEU A  75     3054   4145   5026    193   -871    527       C  
ATOM    664  C   LEU A  75      10.698 -39.009  -9.639  1.00 32.60           C  
ANISOU  664  C   LEU A  75     3038   4273   5075    142   -925    573       C  
ATOM    665  O   LEU A  75      11.669 -38.939 -10.405  1.00 31.97           O  
ANISOU  665  O   LEU A  75     2856   4189   5100    181   -880    504       O  
ATOM    666  CB  LEU A  75       8.376 -38.643 -10.488  1.00 27.63           C  
ANISOU  666  CB  LEU A  75     2627   3624   4245    158   -774    433       C  
ATOM    667  CG  LEU A  75       7.151 -39.108 -11.286  1.00 31.81           C  
ANISOU  667  CG  LEU A  75     3221   4094   4769    209   -693    355       C  
ATOM    668  CD1 LEU A  75       6.314 -37.904 -11.716  1.00 28.67           C  
ANISOU  668  CD1 LEU A  75     2948   3752   4193    169   -611    277       C  
ATOM    669  CD2 LEU A  75       7.545 -39.959 -12.497  1.00 34.68           C  
ANISOU  669  CD2 LEU A  75     3485   4387   5306    293   -626    259       C  
ATOM    670  N   ASN A  76      10.729 -38.498  -8.405  1.00 32.81           N  
ANISOU  670  N   ASN A  76     3114   4380   4973     44  -1017    681       N  
ATOM    671  CA  ASN A  76      11.923 -37.804  -7.934  1.00 30.43           C  
ANISOU  671  CA  ASN A  76     2753   4158   4651    -21  -1074    727       C  
ATOM    672  C   ASN A  76      13.093 -38.755  -7.734  1.00 34.93           C  
ANISOU  672  C   ASN A  76     3145   4678   5449     20  -1173    829       C  
ATOM    673  O   ASN A  76      14.253 -38.355  -7.915  1.00 33.97           O  
ANISOU  673  O   ASN A  76     2929   4593   5384     13  -1181    820       O  
ATOM    674  CB  ASN A  76      11.614 -37.040  -6.643  1.00 34.04           C  
ANISOU  674  CB  ASN A  76     3306   4725   4903   -153  -1144    802       C  
ATOM    675  CG  ASN A  76      10.776 -35.800  -6.901  1.00 29.59           C  
ANISOU  675  CG  ASN A  76     2888   4207   4149   -194  -1039    675       C  
ATOM    676  OD1 ASN A  76      10.822 -35.234  -7.994  1.00 30.33           O  
ANISOU  676  OD1 ASN A  76     2996   4275   4254   -147   -938    560       O  
ATOM    677  ND2 ASN A  76       9.997 -35.385  -5.908  1.00 32.12           N  
ANISOU  677  ND2 ASN A  76     3306   4595   4303   -286  -1065    695       N  
ATOM    678  N   ALA A  77      12.825 -40.003  -7.345  1.00 30.49           N  
ANISOU  678  N   ALA A  77     2525   4027   5033     60  -1257    933       N  
ATOM    679  CA  ALA A  77      13.914 -40.973  -7.250  1.00 36.59           C  
ANISOU  679  CA  ALA A  77     3107   4718   6076    115  -1356   1027       C  
ATOM    680  C   ALA A  77      14.488 -41.291  -8.625  1.00 32.33           C  
ANISOU  680  C   ALA A  77     2454   4097   5733    237  -1238    863       C  
ATOM    681  O   ALA A  77      15.707 -41.392  -8.787  1.00 33.49           O  
ANISOU  681  O   ALA A  77     2446   4235   6044    265  -1265    869       O  
ATOM    682  CB  ALA A  77      13.422 -42.251  -6.577  1.00 38.26           C  
ANISOU  682  CB  ALA A  77     3280   4832   6422    128  -1478   1182       C  
ATOM    683  N   ILE A  78      13.615 -41.455  -9.623  1.00 38.69           N  
ANISOU  683  N   ILE A  78     3329   4853   6520    298  -1106    712       N  
ATOM    684  CA  ILE A  78      14.045 -41.766 -10.986  1.00 39.84           C  
ANISOU  684  CA  ILE A  78     3374   4945   6819    392   -977    532       C  
ATOM    685  C   ILE A  78      14.884 -40.630 -11.548  1.00 34.50           C  
ANISOU  685  C   ILE A  78     2680   4386   6041    352   -897    440       C  
ATOM    686  O   ILE A  78      15.929 -40.854 -12.172  1.00 36.13           O  
ANISOU  686  O   ILE A  78     2730   4584   6415    398   -856    362       O  
ATOM    687  CB  ILE A  78      12.813 -42.051 -11.871  1.00 36.49           C  
ANISOU  687  CB  ILE A  78     3052   4476   6338    432   -858    400       C  
ATOM    688  CG1 ILE A  78      12.099 -43.325 -11.410  1.00 38.83           C  
ANISOU  688  CG1 ILE A  78     3336   4637   6780    479   -938    485       C  
ATOM    689  CG2 ILE A  78      13.203 -42.171 -13.348  1.00 39.38           C  
ANISOU  689  CG2 ILE A  78     3331   4835   6795    492   -705    191       C  
ATOM    690  CD1 ILE A  78      10.772 -43.564 -12.110  1.00 34.35           C  
ANISOU  690  CD1 ILE A  78     2885   4037   6129    501   -838    379       C  
ATOM    691  N   LEU A  79      14.436 -39.393 -11.337  1.00 31.73           N  
ANISOU  691  N   LEU A  79     2483   4145   5426    261   -873    443       N  
ATOM    692  CA  LEU A  79      15.198 -38.240 -11.790  1.00 29.85           C  
ANISOU  692  CA  LEU A  79     2240   4016   5087    206   -814    378       C  
ATOM    693  C   LEU A  79      16.552 -38.182 -11.105  1.00 35.46           C  
ANISOU  693  C   LEU A  79     2814   4760   5898    180   -916    478       C  
ATOM    694  O   LEU A  79      17.569 -37.917 -11.753  1.00 33.75           O  
ANISOU  694  O   LEU A  79     2484   4587   5753    187   -864    405       O  
ATOM    695  CB  LEU A  79      14.400 -36.958 -11.537  1.00 36.91           C  
ANISOU  695  CB  LEU A  79     3321   4991   5713    114   -791    378       C  
ATOM    696  CG  LEU A  79      13.145 -36.796 -12.400  1.00 35.30           C  
ANISOU  696  CG  LEU A  79     3239   4767   5405    132   -682    273       C  
ATOM    697  CD1 LEU A  79      12.244 -35.689 -11.859  1.00 29.87           C  
ANISOU  697  CD1 LEU A  79     2721   4127   4502     52   -689    298       C  
ATOM    698  CD2 LEU A  79      13.524 -36.517 -13.850  1.00 37.01           C  
ANISOU  698  CD2 LEU A  79     3405   5022   5636    145   -555    133       C  
ATOM    699  N   GLU A  80      16.592 -38.464  -9.800  1.00 36.93           N  
ANISOU  699  N   GLU A  80     3001   4939   6092    139  -1066    649       N  
ATOM    700  CA  GLU A  80      17.866 -38.455  -9.086  1.00 40.48           C  
ANISOU  700  CA  GLU A  80     3314   5425   6641    103  -1183    768       C  
ATOM    701  C   GLU A  80      18.777 -39.585  -9.553  1.00 42.43           C  
ANISOU  701  C   GLU A  80     3339   5570   7212    213  -1198    755       C  
ATOM    702  O   GLU A  80      19.995 -39.402  -9.659  1.00 42.40           O  
ANISOU  702  O   GLU A  80     3190   5603   7316    212  -1215    758       O  
ATOM    703  CB  GLU A  80      17.621 -38.561  -7.583  1.00 38.09           C  
ANISOU  703  CB  GLU A  80     3061   5153   6256     13  -1348    965       C  
ATOM    704  CG  GLU A  80      18.882 -38.465  -6.732  1.00 39.98           C  
ANISOU  704  CG  GLU A  80     3173   5453   6565    -53  -1490   1113       C  
ATOM    705  CD  GLU A  80      18.570 -38.617  -5.258  1.00 51.30           C  
ANISOU  705  CD  GLU A  80     4658   6942   7892   -167  -1655   1313       C  
ATOM    706  OE1 GLU A  80      18.325 -39.762  -4.815  1.00 57.64           O  
ANISOU  706  OE1 GLU A  80     5398   7657   8847   -134  -1758   1443       O  
ATOM    707  OE2 GLU A  80      18.536 -37.590  -4.550  1.00 55.39           O  
ANISOU  707  OE2 GLU A  80     5279   7593   8172   -300  -1680   1335       O  
ATOM    708  N   GLU A  81      18.204 -40.763  -9.814  1.00 42.62           N  
ANISOU  708  N   GLU A  81     3325   5459   7411    307  -1193    738       N  
ATOM    709  CA  GLU A  81      18.981 -41.892 -10.320  1.00 44.43           C  
ANISOU  709  CA  GLU A  81     3334   5562   7986    423  -1194    695       C  
ATOM    710  C   GLU A  81      19.682 -41.546 -11.630  1.00 43.68           C  
ANISOU  710  C   GLU A  81     3144   5514   7940    464  -1027    478       C  
ATOM    711  O   GLU A  81      20.785 -42.038 -11.899  1.00 49.10           O  
ANISOU  711  O   GLU A  81     3619   6158   8881    525  -1032    443       O  
ATOM    712  CB  GLU A  81      18.052 -43.099 -10.500  1.00 50.59           C  
ANISOU  712  CB  GLU A  81     4120   6186   8917    507  -1193    678       C  
ATOM    713  CG  GLU A  81      18.702 -44.350 -11.057  1.00 66.86           C  
ANISOU  713  CG  GLU A  81     6021   8089  11295    617  -1154    591       C  
ATOM    714  CD  GLU A  81      17.697 -45.472 -11.299  1.00 73.67           C  
ANISOU  714  CD  GLU A  81     6934   8797  12261    679  -1131    551       C  
ATOM    715  OE1 GLU A  81      16.491 -45.270 -11.024  1.00 63.70           O  
ANISOU  715  OE1 GLU A  81     5806   7557  10840    647  -1156    605       O  
ATOM    716  OE2 GLU A  81      18.114 -46.557 -11.766  1.00 83.87           O  
ANISOU  716  OE2 GLU A  81     8127   9943  13795    754  -1088    461       O  
ATOM    717  N   ASN A  82      19.069 -40.693 -12.448  1.00 46.49           N  
ANISOU  717  N   ASN A  82     3645   5963   8057    423   -883    337       N  
ATOM    718  CA  ASN A  82      19.621 -40.308 -13.738  1.00 50.59           C  
ANISOU  718  CA  ASN A  82     4091   6556   8575    431   -721    138       C  
ATOM    719  C   ASN A  82      20.331 -38.959 -13.696  1.00 48.28           C  
ANISOU  719  C   ASN A  82     3829   6421   8095    326   -712    158       C  
ATOM    720  O   ASN A  82      20.571 -38.362 -14.749  1.00 53.74           O  
ANISOU  720  O   ASN A  82     4513   7208   8698    293   -578     13       O  
ATOM    721  CB  ASN A  82      18.516 -40.307 -14.795  1.00 46.10           C  
ANISOU  721  CB  ASN A  82     3643   5992   7881    439   -574    -22       C  
ATOM    722  CG  ASN A  82      18.041 -41.714 -15.128  1.00 56.85           C  
ANISOU  722  CG  ASN A  82     4930   7200   9471    547   -550    -97       C  
ATOM    723  OD1 ASN A  82      18.700 -42.441 -15.876  1.00 61.52           O  
ANISOU  723  OD1 ASN A  82     5339   7744  10290    618   -472   -244       O  
ATOM    724  ND2 ASN A  82      16.905 -42.111 -14.559  1.00 45.76           N  
ANISOU  724  ND2 ASN A  82     3656   5715   8017    557   -616     -4       N  
ATOM    725  N   GLY A  83      20.669 -38.470 -12.505  1.00 46.38           N  
ANISOU  725  N   GLY A  83     3620   6215   7787    259   -855    336       N  
ATOM    726  CA  GLY A  83      21.462 -37.260 -12.389  1.00 42.23           C  
ANISOU  726  CA  GLY A  83     3102   5824   7118    159   -861    359       C  
ATOM    727  C   GLY A  83      20.769 -35.993 -12.839  1.00 46.59           C  
ANISOU  727  C   GLY A  83     3847   6471   7385     69   -775    295       C  
ATOM    728  O   GLY A  83      21.441 -35.072 -13.313  1.00 53.95           O  
ANISOU  728  O   GLY A  83     4759   7507   8232      0   -724    249       O  
ATOM    729  N   VAL A  84      19.446 -35.910 -12.693  1.00 40.18           N  
ANISOU  729  N   VAL A  84     3213   5621   6434     63   -764    300       N  
ATOM    730  CA  VAL A  84      18.675 -34.767 -13.168  1.00 37.40           C  
ANISOU  730  CA  VAL A  84     3033   5330   5847    -11   -687    242       C  
ATOM    731  C   VAL A  84      18.339 -33.877 -11.976  1.00 44.77           C  
ANISOU  731  C   VAL A  84     4103   6295   6614   -102   -787    355       C  
ATOM    732  O   VAL A  84      17.664 -34.315 -11.033  1.00 42.37           O  
ANISOU  732  O   VAL A  84     3863   5942   6292    -95   -867    439       O  
ATOM    733  CB  VAL A  84      17.403 -35.212 -13.909  1.00 39.99           C  
ANISOU  733  CB  VAL A  84     3454   5599   6140     42   -597    154       C  
ATOM    734  CG1 VAL A  84      16.626 -34.001 -14.392  1.00 36.27           C  
ANISOU  734  CG1 VAL A  84     3145   5184   5451    -37   -535    115       C  
ATOM    735  CG2 VAL A  84      17.759 -36.123 -15.076  1.00 38.10           C  
ANISOU  735  CG2 VAL A  84     3073   5340   6063    118   -491     17       C  
ATOM    736  N   GLN A  85      18.801 -32.624 -12.017  1.00 38.04           N  
ANISOU  736  N   GLN A  85     3290   5527   5636   -199   -780    350       N  
ATOM    737  CA  GLN A  85      18.575 -31.675 -10.930  1.00 45.77           C  
ANISOU  737  CA  GLN A  85     4388   6540   6462   -299   -862    424       C  
ATOM    738  C   GLN A  85      17.161 -31.122 -11.059  1.00 41.44           C  
ANISOU  738  C   GLN A  85     4020   5956   5771   -313   -810    374       C  
ATOM    739  O   GLN A  85      16.935 -29.984 -11.480  1.00 37.33           O  
ANISOU  739  O   GLN A  85     3584   5458   5143   -376   -764    326       O  
ATOM    740  CB  GLN A  85      19.632 -30.571 -10.945  1.00 43.16           C  
ANISOU  740  CB  GLN A  85     4022   6298   6080   -396   -876    430       C  
ATOM    741  CG  GLN A  85      21.008 -30.999 -10.459  1.00 51.95           C  
ANISOU  741  CG  GLN A  85     4964   7456   7319   -402   -960    508       C  
ATOM    742  CD  GLN A  85      20.970 -31.622  -9.064  1.00 57.82           C  
ANISOU  742  CD  GLN A  85     5697   8184   8087   -414  -1098    640       C  
ATOM    743  OE1 GLN A  85      21.355 -32.778  -8.876  1.00 55.47           O  
ANISOU  743  OE1 GLN A  85     5268   7843   7965   -339  -1153    703       O  
ATOM    744  NE2 GLN A  85      20.500 -30.857  -8.083  1.00 54.24           N  
ANISOU  744  NE2 GLN A  85     5376   7770   7464   -517  -1157    679       N  
ATOM    745  N   LEU A  86      16.192 -31.956 -10.688  1.00 33.90           N  
ANISOU  745  N   LEU A  86     3114   4936   4830   -255   -823    393       N  
ATOM    746  CA  LEU A  86      14.796 -31.586 -10.850  1.00 29.18           C  
ANISOU  746  CA  LEU A  86     2667   4299   4121   -254   -770    342       C  
ATOM    747  C   LEU A  86      13.948 -32.315  -9.816  1.00 31.68           C  
ANISOU  747  C   LEU A  86     3037   4581   4420   -239   -833    404       C  
ATOM    748  O   LEU A  86      14.130 -33.514  -9.577  1.00 34.89           O  
ANISOU  748  O   LEU A  86     3359   4952   4946   -179   -880    464       O  
ATOM    749  CB  LEU A  86      14.287 -31.906 -12.261  1.00 27.83           C  
ANISOU  749  CB  LEU A  86     2494   4092   3988   -187   -659    251       C  
ATOM    750  CG  LEU A  86      12.888 -31.372 -12.583  1.00 33.17           C  
ANISOU  750  CG  LEU A  86     3317   4731   4556   -194   -606    205       C  
ATOM    751  CD1 LEU A  86      12.857 -29.837 -12.525  1.00 26.80           C  
ANISOU  751  CD1 LEU A  86     2592   3951   3639   -288   -606    193       C  
ATOM    752  CD2 LEU A  86      12.388 -31.902 -13.941  1.00 33.34           C  
ANISOU  752  CD2 LEU A  86     3324   4730   4615   -135   -508    130       C  
ATOM    753  N   THR A  87      13.011 -31.583  -9.219  1.00 28.20           N  
ANISOU  753  N   THR A  87     2728   4147   3840   -297   -833    387       N  
ATOM    754  CA  THR A  87      12.151 -32.104  -8.165  1.00 29.93           C  
ANISOU  754  CA  THR A  87     3005   4363   4003   -312   -885    438       C  
ATOM    755  C   THR A  87      10.704 -31.814  -8.531  1.00 32.08           C  
ANISOU  755  C   THR A  87     3398   4587   4202   -288   -806    358       C  
ATOM    756  O   THR A  87      10.333 -30.649  -8.723  1.00 28.19           O  
ANISOU  756  O   THR A  87     2983   4095   3631   -331   -759    285       O  
ATOM    757  CB  THR A  87      12.497 -31.480  -6.808  1.00 32.97           C  
ANISOU  757  CB  THR A  87     3415   4836   4274   -436   -970    488       C  
ATOM    758  OG1 THR A  87      13.864 -31.775  -6.478  1.00 30.81           O  
ANISOU  758  OG1 THR A  87     3020   4611   4077   -462  -1056    580       O  
ATOM    759  CG2 THR A  87      11.577 -32.033  -5.727  1.00 33.35           C  
ANISOU  759  CG2 THR A  87     3520   4910   4242   -475  -1019    539       C  
ATOM    760  N   VAL A  88       9.894 -32.867  -8.631  1.00 28.65           N  
ANISOU  760  N   VAL A  88     2971   4103   3811   -220   -797    377       N  
ATOM    761  CA  VAL A  88       8.456 -32.703  -8.818  1.00 26.46           C  
ANISOU  761  CA  VAL A  88     2801   3788   3466   -202   -734    316       C  
ATOM    762  C   VAL A  88       7.835 -32.356  -7.471  1.00 32.45           C  
ANISOU  762  C   VAL A  88     3630   4602   4098   -288   -776    331       C  
ATOM    763  O   VAL A  88       8.079 -33.038  -6.466  1.00 29.55           O  
ANISOU  763  O   VAL A  88     3228   4284   3715   -332   -861    425       O  
ATOM    764  CB  VAL A  88       7.830 -33.978  -9.412  1.00 27.57           C  
ANISOU  764  CB  VAL A  88     2919   3860   3696   -107   -710    326       C  
ATOM    765  CG1 VAL A  88       6.317 -33.840  -9.504  1.00 26.71           C  
ANISOU  765  CG1 VAL A  88     2915   3722   3513    -96   -655    276       C  
ATOM    766  CG2 VAL A  88       8.417 -34.270 -10.787  1.00 24.02           C  
ANISOU  766  CG2 VAL A  88     2395   3374   3358    -38   -649    276       C  
ATOM    767  N   VAL A  89       7.046 -31.282  -7.441  1.00 27.26           N  
ANISOU  767  N   VAL A  89     3062   3941   3354   -324   -720    239       N  
ATOM    768  CA  VAL A  89       6.428 -30.781  -6.214  1.00 33.10           C  
ANISOU  768  CA  VAL A  89     3864   4743   3969   -417   -734    208       C  
ATOM    769  C   VAL A  89       4.931 -30.674  -6.477  1.00 34.10           C  
ANISOU  769  C   VAL A  89     4065   4818   4073   -378   -659    131       C  
ATOM    770  O   VAL A  89       4.494 -29.792  -7.228  1.00 27.13           O  
ANISOU  770  O   VAL A  89     3220   3870   3217   -350   -596     48       O  
ATOM    771  CB  VAL A  89       7.008 -29.422  -5.789  1.00 30.62           C  
ANISOU  771  CB  VAL A  89     3569   4469   3598   -510   -737    141       C  
ATOM    772  CG1 VAL A  89       6.374 -28.938  -4.473  1.00 34.44           C  
ANISOU  772  CG1 VAL A  89     4107   5033   3947   -621   -739     77       C  
ATOM    773  CG2 VAL A  89       8.533 -29.492  -5.673  1.00 27.85           C  
ANISOU  773  CG2 VAL A  89     3136   4168   3279   -546   -810    220       C  
ATOM    774  N   VAL A  90       4.145 -31.563  -5.866  1.00 28.31           N  
ANISOU  774  N   VAL A  90     3346   4113   3297   -382   -675    171       N  
ATOM    775  CA  VAL A  90       2.707 -31.645  -6.119  1.00 30.00           C  
ANISOU  775  CA  VAL A  90     3617   4284   3498   -340   -608    111       C  
ATOM    776  C   VAL A  90       1.958 -31.022  -4.951  1.00 33.76           C  
ANISOU  776  C   VAL A  90     4140   4838   3849   -438   -587     31       C  
ATOM    777  O   VAL A  90       2.123 -31.443  -3.801  1.00 26.91           O  
ANISOU  777  O   VAL A  90     3260   4081   2884   -533   -642     83       O  
ATOM    778  CB  VAL A  90       2.252 -33.098  -6.336  1.00 33.22           C  
ANISOU  778  CB  VAL A  90     4003   4666   3951   -278   -629    199       C  
ATOM    779  CG1 VAL A  90       0.772 -33.134  -6.740  1.00 27.51           C  
ANISOU  779  CG1 VAL A  90     3336   3896   3220   -233   -556    135       C  
ATOM    780  CG2 VAL A  90       3.114 -33.781  -7.392  1.00 30.47           C  
ANISOU  780  CG2 VAL A  90     3590   4250   3735   -192   -644    253       C  
ATOM    781  N   GLY A  91       1.113 -30.036  -5.246  1.00 28.92           N  
ANISOU  781  N   GLY A  91     3571   4171   3245   -424   -510    -94       N  
ATOM    782  CA  GLY A  91       0.229 -29.458  -4.266  1.00 30.56           C  
ANISOU  782  CA  GLY A  91     3811   4438   3361   -502   -465   -207       C  
ATOM    783  C   GLY A  91      -1.221 -29.834  -4.505  1.00 28.42           C  
ANISOU  783  C   GLY A  91     3565   4132   3103   -447   -405   -243       C  
ATOM    784  O   GLY A  91      -1.550 -30.688  -5.330  1.00 29.20           O  
ANISOU  784  O   GLY A  91     3660   4170   3264   -359   -409   -165       O  
ATOM    785  N   SER A  92      -2.098 -29.159  -3.766  1.00 26.66           N  
ANISOU  785  N   SER A  92     3360   3948   2824   -506   -344   -378       N  
ATOM    786  CA  SER A  92      -3.527 -29.421  -3.856  1.00 29.07           C  
ANISOU  786  CA  SER A  92     3677   4233   3136   -467   -282   -428       C  
ATOM    787  C   SER A  92      -4.118 -28.739  -5.087  1.00 29.08           C  
ANISOU  787  C   SER A  92     3684   4075   3290   -356   -235   -478       C  
ATOM    788  O   SER A  92      -3.560 -27.777  -5.621  1.00 32.14           O  
ANISOU  788  O   SER A  92     4069   4380   3764   -338   -237   -512       O  
ATOM    789  CB  SER A  92      -4.241 -28.929  -2.594  1.00 40.33           C  
ANISOU  789  CB  SER A  92     5101   5770   4451   -578   -224   -573       C  
ATOM    790  OG  SER A  92      -3.716 -29.572  -1.443  1.00 45.01           O  
ANISOU  790  OG  SER A  92     5687   6535   4881   -707   -278   -507       O  
ATOM    791  N   VAL A  93      -5.270 -29.237  -5.526  1.00 32.77           N  
ANISOU  791  N   VAL A  93     4156   4504   3791   -294   -199   -470       N  
ATOM    792  CA  VAL A  93      -5.980 -28.618  -6.639  1.00 35.44           C  
ANISOU  792  CA  VAL A  93     4492   4705   4269   -204   -164   -503       C  
ATOM    793  C   VAL A  93      -6.866 -27.509  -6.113  1.00 39.31           C  
ANISOU  793  C   VAL A  93     4964   5163   4807   -226    -96   -671       C  
ATOM    794  O   VAL A  93      -7.442 -27.603  -5.020  1.00 42.39           O  
ANISOU  794  O   VAL A  93     5345   5653   5107   -293    -50   -765       O  
ATOM    795  CB  VAL A  93      -6.808 -29.640  -7.437  1.00 49.80           C  
ANISOU  795  CB  VAL A  93     6316   6493   6111   -129   -162   -417       C  
ATOM    796  CG1 VAL A  93      -5.920 -30.368  -8.394  1.00 53.77           C  
ANISOU  796  CG1 VAL A  93     6822   6971   6638    -84   -216   -290       C  
ATOM    797  CG2 VAL A  93      -7.544 -30.598  -6.519  1.00 56.71           C  
ANISOU  797  CG2 VAL A  93     7193   7475   6878   -172   -148   -411       C  
ATOM    798  N   LYS A  94      -6.933 -26.431  -6.879  1.00 33.87           N  
ANISOU  798  N   LYS A  94     4262   4338   4269   -179    -90   -711       N  
ATOM    799  CA  LYS A  94      -7.895 -25.369  -6.662  1.00 45.74           C  
ANISOU  799  CA  LYS A  94     5732   5759   5890   -170    -30   -864       C  
ATOM    800  C   LYS A  94      -8.891 -25.388  -7.810  1.00 43.80           C  
ANISOU  800  C   LYS A  94     5468   5395   5779    -74    -31   -804       C  
ATOM    801  O   LYS A  94      -8.551 -25.752  -8.941  1.00 39.37           O  
ANISOU  801  O   LYS A  94     4924   4791   5244    -28    -84   -661       O  
ATOM    802  CB  LYS A  94      -7.215 -24.002  -6.564  1.00 55.28           C  
ANISOU  802  CB  LYS A  94     6925   6880   7200   -202    -37   -955       C  
ATOM    803  CG  LYS A  94      -6.702 -23.665  -5.173  1.00 73.48           C  
ANISOU  803  CG  LYS A  94     9229   9299   9392   -314     -6  -1094       C  
ATOM    804  CD  LYS A  94      -5.941 -22.345  -5.182  1.00 85.76           C  
ANISOU  804  CD  LYS A  94    10772  10755  11058   -346    -21  -1175       C  
ATOM    805  CE  LYS A  94      -6.788 -21.211  -5.751  1.00 85.81           C  
ANISOU  805  CE  LYS A  94    10731  10563  11309   -280      4  -1266       C  
ATOM    806  NZ  LYS A  94      -7.579 -20.521  -4.692  1.00 85.38           N  
ANISOU  806  NZ  LYS A  94    10628  10509  11303   -324     97  -1512       N  
ATOM    807  N   ASN A  95     -10.128 -25.036  -7.503  1.00 40.55           N  
ANISOU  807  N   ASN A  95     5015   4947   5445    -54     29   -917       N  
ATOM    808  CA  ASN A  95     -11.157 -24.976  -8.521  1.00 32.67           C  
ANISOU  808  CA  ASN A  95     3988   3838   4589     30     22   -861       C  
ATOM    809  C   ASN A  95     -11.464 -23.526  -8.874  1.00 31.62           C  
ANISOU  809  C   ASN A  95     3798   3529   4686     60     19   -938       C  
ATOM    810  O   ASN A  95     -11.400 -22.650  -8.013  1.00 32.67           O  
ANISOU  810  O   ASN A  95     3899   3637   4876     22     64  -1106       O  
ATOM    811  CB  ASN A  95     -12.410 -25.708  -8.045  1.00 37.69           C  
ANISOU  811  CB  ASN A  95     4602   4547   5173     40     82   -909       C  
ATOM    812  CG  ASN A  95     -12.182 -27.197  -7.908  1.00 43.60           C  
ANISOU  812  CG  ASN A  95     5402   5435   5730     16     64   -795       C  
ATOM    813  OD1 ASN A  95     -12.111 -27.918  -8.898  1.00 40.02           O  
ANISOU  813  OD1 ASN A  95     4974   4960   5272     61     16   -651       O  
ATOM    814  ND2 ASN A  95     -12.047 -27.663  -6.673  1.00 56.36           N  
ANISOU  814  ND2 ASN A  95     7027   7196   7191    -64     98   -860       N  
ATOM    815  N   PRO A  96     -11.781 -23.259 -10.153  1.00 27.91           N  
ANISOU  815  N   PRO A  96     3311   2938   4357    118    -41   -812       N  
ATOM    816  CA  PRO A  96     -11.754 -24.191 -11.293  1.00 27.82           C  
ANISOU  816  CA  PRO A  96     3335   2958   4276    145    -94   -624       C  
ATOM    817  C   PRO A  96     -10.337 -24.653 -11.667  1.00 26.49           C  
ANISOU  817  C   PRO A  96     3224   2862   3978    108   -141   -519       C  
ATOM    818  O   PRO A  96      -9.367 -23.931 -11.434  1.00 25.17           O  
ANISOU  818  O   PRO A  96     3064   2672   3830     70   -160   -547       O  
ATOM    819  CB  PRO A  96     -12.368 -23.369 -12.442  1.00 30.26           C  
ANISOU  819  CB  PRO A  96     3593   3111   4794    186   -152   -541       C  
ATOM    820  CG  PRO A  96     -13.137 -22.253 -11.761  1.00 30.30           C  
ANISOU  820  CG  PRO A  96     3521   2994   4998    207   -112   -702       C  
ATOM    821  CD  PRO A  96     -12.370 -21.950 -10.504  1.00 30.22           C  
ANISOU  821  CD  PRO A  96     3530   3043   4910    154    -56   -864       C  
ATOM    822  N   MET A  97     -10.225 -25.846 -12.246  1.00 21.07           N  
ANISOU  822  N   MET A  97     2572   2258   3175    119   -156   -407       N  
ATOM    823  CA  MET A  97      -8.940 -26.389 -12.690  1.00 23.03           C  
ANISOU  823  CA  MET A  97     2858   2572   3321     93   -192   -317       C  
ATOM    824  C   MET A  97      -8.648 -25.839 -14.084  1.00 25.81           C  
ANISOU  824  C   MET A  97     3197   2855   3754     89   -249   -207       C  
ATOM    825  O   MET A  97      -8.890 -26.481 -15.106  1.00 24.84           O  
ANISOU  825  O   MET A  97     3080   2757   3602     99   -267   -111       O  
ATOM    826  CB  MET A  97      -8.965 -27.916 -12.675  1.00 20.60           C  
ANISOU  826  CB  MET A  97     2578   2369   2881    104   -180   -266       C  
ATOM    827  CG  MET A  97      -9.219 -28.486 -11.264  1.00 26.35           C  
ANISOU  827  CG  MET A  97     3315   3182   3515     83   -139   -347       C  
ATOM    828  SD  MET A  97      -9.323 -30.303 -11.147  1.00 31.48           S  
ANISOU  828  SD  MET A  97     3990   3932   4040     91   -142   -271       S  
ATOM    829  CE  MET A  97      -7.627 -30.770 -11.441  1.00 41.27           C  
ANISOU  829  CE  MET A  97     5239   5207   5234     74   -190   -196       C  
ATOM    830  N   TRP A  98      -8.091 -24.633 -14.107  1.00 25.37           N  
ANISOU  830  N   TRP A  98     3124   2721   3793     60   -280   -221       N  
ATOM    831  CA  TRP A  98      -7.933 -23.868 -15.338  1.00 24.33           C  
ANISOU  831  CA  TRP A  98     2972   2514   3761     37   -345   -108       C  
ATOM    832  C   TRP A  98      -6.975 -24.563 -16.299  1.00 28.79           C  
ANISOU  832  C   TRP A  98     3557   3178   4204      1   -368      0       C  
ATOM    833  O   TRP A  98      -6.076 -25.304 -15.889  1.00 24.58           O  
ANISOU  833  O   TRP A  98     3047   2740   3553     -7   -342    -26       O  
ATOM    834  CB  TRP A  98      -7.400 -22.474 -15.025  1.00 27.42           C  
ANISOU  834  CB  TRP A  98     3340   2800   4280      3   -377   -149       C  
ATOM    835  CG  TRP A  98      -8.198 -21.680 -14.037  1.00 33.81           C  
ANISOU  835  CG  TRP A  98     4115   3503   5227     31   -343   -294       C  
ATOM    836  CD1 TRP A  98      -7.811 -21.312 -12.772  1.00 26.82           C  
ANISOU  836  CD1 TRP A  98     3233   2628   4327     11   -297   -449       C  
ATOM    837  CD2 TRP A  98      -9.498 -21.110 -14.241  1.00 29.61           C  
ANISOU  837  CD2 TRP A  98     3526   2843   4880     76   -351   -309       C  
ATOM    838  NE1 TRP A  98      -8.799 -20.565 -12.181  1.00 29.54           N  
ANISOU  838  NE1 TRP A  98     3527   2862   4833     40   -262   -581       N  
ATOM    839  CE2 TRP A  98      -9.844 -20.427 -13.057  1.00 31.18           C  
ANISOU  839  CE2 TRP A  98     3692   2975   5179     88   -296   -497       C  
ATOM    840  CE3 TRP A  98     -10.413 -21.131 -15.303  1.00 32.49           C  
ANISOU  840  CE3 TRP A  98     3857   3149   5337    101   -400   -184       C  
ATOM    841  CZ2 TRP A  98     -11.057 -19.754 -12.909  1.00 33.74           C  
ANISOU  841  CZ2 TRP A  98     3942   3162   5715    137   -282   -576       C  
ATOM    842  CZ3 TRP A  98     -11.620 -20.462 -15.156  1.00 32.42           C  
ANISOU  842  CZ3 TRP A  98     3777   3003   5539    149   -401   -237       C  
ATOM    843  CH2 TRP A  98     -11.929 -19.782 -13.965  1.00 34.88           C  
ANISOU  843  CH2 TRP A  98     4047   3236   5968    173   -338   -438       C  
ATOM    844  N   ARG A  99      -7.188 -24.321 -17.598  1.00 26.71           N  
ANISOU  844  N   ARG A  99     3274   2896   3977    -30   -418    121       N  
ATOM    845  CA  ARG A  99      -6.316 -24.836 -18.648  1.00 23.62           C  
ANISOU  845  CA  ARG A  99     2889   2609   3477    -85   -432    210       C  
ATOM    846  C   ARG A  99      -4.918 -24.229 -18.568  1.00 30.88           C  
ANISOU  846  C   ARG A  99     3804   3546   4382   -140   -452    214       C  
ATOM    847  O   ARG A  99      -4.711 -23.127 -18.048  1.00 31.87           O  
ANISOU  847  O   ARG A  99     3920   3579   4611   -153   -481    188       O  
ATOM    848  CB  ARG A  99      -6.873 -24.492 -20.029  1.00 29.02           C  
ANISOU  848  CB  ARG A  99     3547   3282   4199   -137   -491    344       C  
ATOM    849  CG  ARG A  99      -8.225 -25.023 -20.300  1.00 26.27           C  
ANISOU  849  CG  ARG A  99     3193   2921   3866    -99   -485    363       C  
ATOM    850  CD  ARG A  99      -8.800 -24.385 -21.565  1.00 23.97           C  
ANISOU  850  CD  ARG A  99     2865   2602   3641   -167   -568    516       C  
ATOM    851  NE  ARG A  99     -10.154 -24.867 -21.754  1.00 28.67           N  
ANISOU  851  NE  ARG A  99     3448   3182   4262   -129   -567    533       N  
ATOM    852  CZ  ARG A  99     -10.984 -24.423 -22.678  1.00 35.00           C  
ANISOU  852  CZ  ARG A  99     4210   3950   5140   -174   -643    665       C  
ATOM    853  NH1 ARG A  99     -10.591 -23.458 -23.504  1.00 29.68           N  
ANISOU  853  NH1 ARG A  99     3504   3251   4523   -267   -734    802       N  
ATOM    854  NH2 ARG A  99     -12.200 -24.955 -22.775  1.00 33.66           N  
ANISOU  854  NH2 ARG A  99     4027   3775   4985   -136   -637    672       N  
ATOM    855  N   GLY A 100      -3.957 -24.955 -19.130  1.00 26.70           N  
ANISOU  855  N   GLY A 100     3275   3138   3734   -174   -434    240       N  
ATOM    856  CA  GLY A 100      -2.684 -24.387 -19.505  1.00 27.18           C  
ANISOU  856  CA  GLY A 100     3317   3237   3774   -248   -460    280       C  
ATOM    857  C   GLY A 100      -2.418 -24.687 -20.962  1.00 26.61           C  
ANISOU  857  C   GLY A 100     3220   3267   3622   -324   -470    374       C  
ATOM    858  O   GLY A 100      -2.963 -25.644 -21.513  1.00 27.25           O  
ANISOU  858  O   GLY A 100     3304   3413   3638   -310   -437    374       O  
ATOM    859  N   PRO A 101      -1.581 -23.880 -21.620  1.00 27.60           N  
ANISOU  859  N   PRO A 101     3318   3421   3746   -421   -513    451       N  
ATOM    860  CA  PRO A 101      -1.405 -24.025 -23.069  1.00 26.46           C  
ANISOU  860  CA  PRO A 101     3144   3396   3513   -525   -525    547       C  
ATOM    861  C   PRO A 101      -0.281 -24.953 -23.490  1.00 31.46           C  
ANISOU  861  C   PRO A 101     3749   4191   4014   -557   -456    490       C  
ATOM    862  O   PRO A 101      -0.169 -25.236 -24.690  1.00 30.31           O  
ANISOU  862  O   PRO A 101     3573   4171   3772   -651   -444    537       O  
ATOM    863  CB  PRO A 101      -1.109 -22.583 -23.514  1.00 26.76           C  
ANISOU  863  CB  PRO A 101     3160   3377   3629   -628   -617    671       C  
ATOM    864  CG  PRO A 101      -0.333 -22.012 -22.362  1.00 29.19           C  
ANISOU  864  CG  PRO A 101     3478   3606   4008   -589   -616    597       C  
ATOM    865  CD  PRO A 101      -0.904 -22.678 -21.099  1.00 23.85           C  
ANISOU  865  CD  PRO A 101     2838   2867   3358   -455   -560    462       C  
ATOM    866  N   GLN A 102       0.553 -25.417 -22.564  1.00 25.61           N  
ANISOU  866  N   GLN A 102     3006   3456   3268   -492   -411    390       N  
ATOM    867  CA  GLN A 102       1.646 -26.308 -22.923  1.00 24.45           C  
ANISOU  867  CA  GLN A 102     2812   3444   3033   -510   -347    328       C  
ATOM    868  C   GLN A 102       1.175 -27.757 -22.872  1.00 25.82           C  
ANISOU  868  C   GLN A 102     2988   3646   3176   -429   -281    241       C  
ATOM    869  O   GLN A 102       0.087 -28.072 -22.381  1.00 26.51           O  
ANISOU  869  O   GLN A 102     3119   3652   3299   -356   -286    230       O  
ATOM    870  CB  GLN A 102       2.848 -26.095 -21.998  1.00 24.31           C  
ANISOU  870  CB  GLN A 102     2774   3417   3043   -488   -346    282       C  
ATOM    871  CG  GLN A 102       3.218 -24.625 -21.771  1.00 25.65           C  
ANISOU  871  CG  GLN A 102     2952   3522   3269   -555   -417    354       C  
ATOM    872  CD  GLN A 102       3.592 -23.899 -23.055  1.00 36.54           C  
ANISOU  872  CD  GLN A 102     4296   4984   4604   -695   -449    459       C  
ATOM    873  OE1 GLN A 102       3.912 -24.525 -24.075  1.00 31.66           O  
ANISOU  873  OE1 GLN A 102     3634   4510   3885   -757   -402    456       O  
ATOM    874  NE2 GLN A 102       3.552 -22.569 -23.013  1.00 29.20           N  
ANISOU  874  NE2 GLN A 102     3378   3965   3751   -758   -530    550       N  
ATOM    875  N   ARG A 103       2.012 -28.652 -23.383  1.00 27.91           N  
ANISOU  875  N   ARG A 103     3196   4024   3385   -444   -216    172       N  
ATOM    876  CA  ARG A 103       1.693 -30.072 -23.379  1.00 24.04           C  
ANISOU  876  CA  ARG A 103     2695   3549   2891   -371   -155     81       C  
ATOM    877  C   ARG A 103       2.967 -30.854 -23.098  1.00 28.07           C  
ANISOU  877  C   ARG A 103     3132   4106   3425   -335   -106    -10       C  
ATOM    878  O   ARG A 103       4.031 -30.504 -23.614  1.00 28.38           O  
ANISOU  878  O   ARG A 103     3112   4238   3435   -408    -87    -18       O  
ATOM    879  CB  ARG A 103       1.083 -30.505 -24.726  1.00 25.44           C  
ANISOU  879  CB  ARG A 103     2859   3822   2985   -446   -118     77       C  
ATOM    880  CG  ARG A 103      -0.254 -29.843 -25.057  1.00 25.64           C  
ANISOU  880  CG  ARG A 103     2942   3800   3000   -481   -178    181       C  
ATOM    881  CD  ARG A 103      -1.342 -30.338 -24.107  1.00 24.31           C  
ANISOU  881  CD  ARG A 103     2830   3508   2901   -361   -188    161       C  
ATOM    882  NE  ARG A 103      -2.697 -29.897 -24.453  1.00 25.37           N  
ANISOU  882  NE  ARG A 103     3002   3597   3041   -382   -235    244       N  
ATOM    883  CZ  ARG A 103      -3.201 -28.689 -24.195  1.00 23.09           C  
ANISOU  883  CZ  ARG A 103     2735   3219   2818   -394   -308    339       C  
ATOM    884  NH1 ARG A 103      -2.462 -27.747 -23.602  1.00 21.73           N  
ANISOU  884  NH1 ARG A 103     2560   2995   2701   -398   -342    358       N  
ATOM    885  NH2 ARG A 103      -4.462 -28.422 -24.520  1.00 24.29           N  
ANISOU  885  NH2 ARG A 103     2906   3325   2998   -403   -351    410       N  
ATOM    886  N   LEU A 104       2.867 -31.903 -22.280  1.00 25.57           N  
ANISOU  886  N   LEU A 104     2814   3726   3175   -229    -91    -69       N  
ATOM    887  CA  LEU A 104       4.024 -32.770 -22.077  1.00 23.41           C  
ANISOU  887  CA  LEU A 104     2454   3482   2959   -188    -53   -149       C  
ATOM    888  C   LEU A 104       4.437 -33.387 -23.410  1.00 29.43           C  
ANISOU  888  C   LEU A 104     3137   4361   3685   -246     32   -241       C  
ATOM    889  O   LEU A 104       3.575 -33.824 -24.180  1.00 29.13           O  
ANISOU  889  O   LEU A 104     3119   4349   3598   -271     67   -270       O  
ATOM    890  CB  LEU A 104       3.724 -33.895 -21.085  1.00 25.31           C  
ANISOU  890  CB  LEU A 104     2699   3628   3290    -75    -65   -177       C  
ATOM    891  CG  LEU A 104       3.524 -33.490 -19.626  1.00 28.68           C  
ANISOU  891  CG  LEU A 104     3183   3970   3745    -29   -138   -109       C  
ATOM    892  CD1 LEU A 104       3.213 -34.725 -18.760  1.00 28.84           C  
ANISOU  892  CD1 LEU A 104     3198   3919   3841     58   -155   -120       C  
ATOM    893  CD2 LEU A 104       4.755 -32.746 -19.130  1.00 26.87           C  
ANISOU  893  CD2 LEU A 104     2914   3768   3526    -60   -171    -84       C  
ATOM    894  N   PRO A 105       5.733 -33.451 -23.708  1.00 31.77           N  
ANISOU  894  N   PRO A 105     3335   4737   3999   -277     72   -299       N  
ATOM    895  CA  PRO A 105       6.174 -34.134 -24.927  1.00 33.95           C  
ANISOU  895  CA  PRO A 105     3517   5136   4246   -334    172   -423       C  
ATOM    896  C   PRO A 105       6.207 -35.640 -24.726  1.00 31.20           C  
ANISOU  896  C   PRO A 105     3107   4721   4025   -229    222   -547       C  
ATOM    897  O   PRO A 105       6.412 -36.141 -23.619  1.00 34.55           O  
ANISOU  897  O   PRO A 105     3523   5028   4578   -120    175   -528       O  
ATOM    898  CB  PRO A 105       7.587 -33.586 -25.147  1.00 30.59           C  
ANISOU  898  CB  PRO A 105     2999   4811   3812   -399    194   -440       C  
ATOM    899  CG  PRO A 105       8.091 -33.331 -23.702  1.00 30.22           C  
ANISOU  899  CG  PRO A 105     2966   4647   3869   -307    112   -368       C  
ATOM    900  CD  PRO A 105       6.859 -32.893 -22.929  1.00 28.19           C  
ANISOU  900  CD  PRO A 105     2843   4274   3593   -267     32   -263       C  
ATOM    901  N   VAL A 106       5.979 -36.363 -25.816  1.00 31.63           N  
ANISOU  901  N   VAL A 106     3116   4856   4048   -275    311   -671       N  
ATOM    902  CA  VAL A 106       6.259 -37.793 -25.832  1.00 32.83           C  
ANISOU  902  CA  VAL A 106     3174   4952   4347   -190    375   -823       C  
ATOM    903  C   VAL A 106       7.777 -37.919 -25.868  1.00 42.06           C  
ANISOU  903  C   VAL A 106     4199   6173   5611   -184    422   -911       C  
ATOM    904  O   VAL A 106       8.402 -37.531 -26.867  1.00 42.29           O  
ANISOU  904  O   VAL A 106     4158   6366   5543   -298    500   -987       O  
ATOM    905  CB  VAL A 106       5.588 -38.491 -27.021  1.00 36.46           C  
ANISOU  905  CB  VAL A 106     3621   5490   4742   -256    467   -955       C  
ATOM    906  CG1 VAL A 106       5.989 -39.957 -27.060  1.00 41.79           C  
ANISOU  906  CG1 VAL A 106     4182   6093   5605   -168    539  -1136       C  
ATOM    907  CG2 VAL A 106       4.068 -38.326 -26.935  1.00 36.82           C  
ANISOU  907  CG2 VAL A 106     3804   5483   4701   -261    408   -850       C  
ATOM    908  N   PRO A 107       8.406 -38.426 -24.806  1.00 49.94           N  
ANISOU  908  N   PRO A 107     5141   7044   6790    -65    372   -894       N  
ATOM    909  CA  PRO A 107       9.866 -38.302 -24.664  1.00 57.65           C  
ANISOU  909  CA  PRO A 107     5984   8063   7856    -59    389   -933       C  
ATOM    910  C   PRO A 107      10.616 -38.906 -25.842  1.00 66.87           C  
ANISOU  910  C   PRO A 107     6997   9348   9062   -107    529  -1146       C  
ATOM    911  O   PRO A 107      10.430 -40.076 -26.189  1.00 59.84           O  
ANISOU  911  O   PRO A 107     6038   8403   8296    -54    596  -1297       O  
ATOM    912  CB  PRO A 107      10.158 -39.047 -23.356  1.00 60.10           C  
ANISOU  912  CB  PRO A 107     6258   8199   8378     82    303   -877       C  
ATOM    913  CG  PRO A 107       8.944 -39.899 -23.102  1.00 58.15           C  
ANISOU  913  CG  PRO A 107     6089   7829   8175    147    278   -870       C  
ATOM    914  CD  PRO A 107       7.798 -39.115 -23.657  1.00 53.66           C  
ANISOU  914  CD  PRO A 107     5664   7336   7388     58    287   -819       C  
ATOM    915  N   VAL A 108      11.465 -38.074 -26.459  1.00 75.98           N  
ANISOU  915  N   VAL A 108     8093  10669  10107   -219    577  -1165       N  
ATOM    916  CA  VAL A 108      12.291 -38.509 -27.584  1.00 89.24           C  
ANISOU  916  CA  VAL A 108     9611  12499  11797   -291    722  -1378       C  
ATOM    917  C   VAL A 108      13.205 -39.653 -27.161  1.00 96.68           C  
ANISOU  917  C   VAL A 108    10380  13328  13028   -156    756  -1515       C  
ATOM    918  O   VAL A 108      13.249 -40.710 -27.804  1.00 98.04           O  
ANISOU  918  O   VAL A 108    10442  13496  13313   -133    865  -1726       O  
ATOM    919  CB  VAL A 108      13.099 -37.321 -28.143  1.00 89.35           C  
ANISOU  919  CB  VAL A 108     9594  12712  11644   -441    747  -1338       C  
ATOM    920  CG1 VAL A 108      13.917 -37.748 -29.354  1.00 89.86           C  
ANISOU  920  CG1 VAL A 108     9485  12966  11691   -539    911  -1572       C  
ATOM    921  CG2 VAL A 108      12.179 -36.165 -28.496  1.00 87.53           C  
ANISOU  921  CG2 VAL A 108     9528  12560  11167   -569    688  -1174       C  
ATOM    922  N   ASN A 109      13.952 -39.455 -26.076  1.00 96.44           N  
ANISOU  922  N   ASN A 109    10312  13200  13129    -71    659  -1398       N  
ATOM    923  CA  ASN A 109      14.849 -40.467 -25.530  1.00 98.50           C  
ANISOU  923  CA  ASN A 109    10401  13333  13690     61    656  -1480       C  
ATOM    924  C   ASN A 109      14.349 -40.902 -24.157  1.00 97.22           C  
ANISOU  924  C   ASN A 109    10316  12953  13669    193    504  -1310       C  
ATOM    925  O   ASN A 109      14.131 -40.064 -23.274  1.00 94.53           O  
ANISOU  925  O   ASN A 109    10100  12592  13226    182    386  -1108       O  
ATOM    926  CB  ASN A 109      16.282 -39.936 -25.425  1.00 96.29           C  
ANISOU  926  CB  ASN A 109     9983  13145  13459     35    664  -1480       C  
ATOM    927  CG  ASN A 109      16.809 -39.391 -26.743  1.00 93.38           C  
ANISOU  927  CG  ASN A 109     9540  13021  12920   -121    809  -1628       C  
ATOM    928  OD1 ASN A 109      17.121 -40.149 -27.662  1.00101.14           O  
ANISOU  928  OD1 ASN A 109    10378  14073  13977   -138    953  -1866       O  
ATOM    929  ND2 ASN A 109      16.923 -38.070 -26.834  1.00 84.66           N  
ANISOU  929  ND2 ASN A 109     8526  12052  11589   -245    771  -1490       N  
ATOM    930  N   GLU A 110      14.170 -42.208 -23.981  1.00 97.85           N  
ANISOU  930  N   GLU A 110    10317  12874  13986    304    507  -1396       N  
ATOM    931  CA  GLU A 110      13.763 -42.756 -22.695  1.00100.46           C  
ANISOU  931  CA  GLU A 110    10697  13004  14467    416    359  -1231       C  
ATOM    932  C   GLU A 110      14.962 -42.863 -21.747  1.00104.83           C  
ANISOU  932  C   GLU A 110    11116  13485  15227    486    264  -1139       C  
ATOM    933  O   GLU A 110      16.113 -42.998 -22.178  1.00105.94           O  
ANISOU  933  O   GLU A 110    11076  13677  15500    493    333  -1262       O  
ATOM    934  CB  GLU A 110      13.100 -44.123 -22.900  1.00 99.13           C  
ANISOU  934  CB  GLU A 110    10493  12686  14487    498    388  -1344       C  
ATOM    935  CG  GLU A 110      12.877 -44.945 -21.633  1.00103.68           C  
ANISOU  935  CG  GLU A 110    11068  13045  15283    613    235  -1188       C  
ATOM    936  CD  GLU A 110      11.866 -44.322 -20.682  1.00101.27           C  
ANISOU  936  CD  GLU A 110    10971  12726  14783    586    111   -957       C  
ATOM    937  OE1 GLU A 110      10.731 -44.837 -20.609  1.00103.85           O  
ANISOU  937  OE1 GLU A 110    11395  12973  15089    603     93   -937       O  
ATOM    938  OE2 GLU A 110      12.202 -43.322 -20.007  1.00 94.03           O  
ANISOU  938  OE2 GLU A 110    10113  11878  13735    544     37   -807       O  
ATOM    939  N   LEU A 111      14.674 -42.775 -20.414  1.00 98.85           N  
ANISOU  939  N   LEU A 111    10446  12622  14488    527    100   -913       N  
ATOM    940  CA  LEU A 111      15.654 -42.882 -19.333  1.00 87.21           C  
ANISOU  940  CA  LEU A 111     8867  11077  13190    579    -27   -776       C  
ATOM    941  C   LEU A 111      15.932 -44.349 -18.999  1.00 89.95           C  
ANISOU  941  C   LEU A 111     9052  11227  13896    703    -76   -803       C  
ATOM    942  O   LEU A 111      15.009 -45.170 -18.989  1.00 92.79           O  
ANISOU  942  O   LEU A 111     9462  11468  14325    748    -87   -816       O  
ATOM    943  CB  LEU A 111      15.151 -42.167 -18.078  1.00 70.86           C  
ANISOU  943  CB  LEU A 111     6962   9001  10960    543   -176   -534       C  
ATOM    944  CG  LEU A 111      14.976 -40.652 -18.129  1.00 60.41           C  
ANISOU  944  CG  LEU A 111     5786   7834   9331    430   -163   -475       C  
ATOM    945  CD1 LEU A 111      14.280 -40.166 -16.868  1.00 52.58           C  
ANISOU  945  CD1 LEU A 111     4952   6812   8213    404   -297   -276       C  
ATOM    946  CD2 LEU A 111      16.328 -39.970 -18.307  1.00 65.82           C  
ANISOU  946  CD2 LEU A 111     6354   8630  10025    386   -143   -496       C  
ATOM    947  N   PRO A 112      17.197 -44.705 -18.707  1.00 85.62           N  
ANISOU  947  N   PRO A 112     8301  10632  13599    758   -116   -801       N  
ATOM    948  CA  PRO A 112      17.587 -46.076 -18.353  1.00 86.59           C  
ANISOU  948  CA  PRO A 112     8317  10550  14034    852   -178   -791       C  
ATOM    949  C   PRO A 112      17.559 -46.354 -16.850  1.00 90.83           C  
ANISOU  949  C   PRO A 112     8891  10968  14652    873   -392   -508       C  
ATOM    950  O   PRO A 112      16.513 -46.212 -16.218  1.00 90.37           O  
ANISOU  950  O   PRO A 112     8958  10891  14488    859   -479   -371       O  
ATOM    951  CB  PRO A 112      19.015 -46.167 -18.885  1.00 84.03           C  
ANISOU  951  CB  PRO A 112     7833  10264  13828    855   -101   -916       C  
ATOM    952  CG  PRO A 112      19.546 -44.780 -18.701  1.00 80.29           C  
ANISOU  952  CG  PRO A 112     7348   9983  13174    783   -112   -845       C  
ATOM    953  CD  PRO A 112      18.373 -43.831 -18.870  1.00 81.17           C  
ANISOU  953  CD  PRO A 112     7647  10214  12979    704    -84   -818       C  
ATOM    954  N   SER A 121      13.355 -48.075  -6.689  1.00 77.60           N  
ANISOU  954  N   SER A 121     7928   9093  12463    386  -1674   1397       N  
ATOM    955  CA  SER A 121      12.937 -46.699  -6.958  1.00 85.51           C  
ANISOU  955  CA  SER A 121     9016  10268  13204    364  -1607   1315       C  
ATOM    956  C   SER A 121      11.773 -46.277  -6.064  1.00 90.90           C  
ANISOU  956  C   SER A 121     9855  11070  13614    250  -1669   1437       C  
ATOM    957  O   SER A 121      11.741 -45.153  -5.558  1.00 78.76           O  
ANISOU  957  O   SER A 121     8385   9704  11837    159  -1691   1472       O  
ATOM    958  CB  SER A 121      12.543 -46.521  -8.430  1.00 80.94           C  
ANISOU  958  CB  SER A 121     8423   9652  12679    483  -1443   1071       C  
ATOM    959  OG  SER A 121      13.683 -46.446  -9.270  1.00 82.67           O  
ANISOU  959  OG  SER A 121     8507   9844  13061    557  -1360    928       O  
ATOM    960  N   TYR A 122      10.810 -47.182  -5.873  1.00102.46           N  
ANISOU  960  N   TYR A 122    11372  12446  15112    245  -1693   1490       N  
ATOM    961  CA  TYR A 122       9.675 -46.890  -5.006  1.00105.75           C  
ANISOU  961  CA  TYR A 122    11929  12979  15273    128  -1743   1599       C  
ATOM    962  C   TYR A 122      10.093 -46.628  -3.564  1.00100.03           C  
ANISOU  962  C   TYR A 122    11227  12386  14393    -37  -1867   1795       C  
ATOM    963  O   TYR A 122       9.277 -46.126  -2.782  1.00 98.44           O  
ANISOU  963  O   TYR A 122    11139  12332  13930   -159  -1893   1860       O  
ATOM    964  CB  TYR A 122       8.663 -48.044  -5.061  1.00112.23           C  
ANISOU  964  CB  TYR A 122    12783  13672  16187    146  -1750   1629       C  
ATOM    965  CG  TYR A 122       7.352 -47.759  -4.353  1.00115.61           C  
ANISOU  965  CG  TYR A 122    13352  14223  16351     38  -1775   1708       C  
ATOM    966  CD1 TYR A 122       6.443 -46.843  -4.874  1.00116.53           C  
ANISOU  966  CD1 TYR A 122    13587  14434  16257     52  -1658   1563       C  
ATOM    967  CD2 TYR A 122       7.020 -48.409  -3.169  1.00115.46           C  
ANISOU  967  CD2 TYR A 122    13361  14231  16276    -98  -1882   1899       C  
ATOM    968  CE1 TYR A 122       5.243 -46.577  -4.234  1.00114.58           C  
ANISOU  968  CE1 TYR A 122    13474  14302  15761    -53  -1649   1600       C  
ATOM    969  CE2 TYR A 122       5.819 -48.150  -2.521  1.00114.81           C  
ANISOU  969  CE2 TYR A 122    13400  14280  15942   -208  -1889   1953       C  
ATOM    970  CZ  TYR A 122       4.936 -47.233  -3.060  1.00113.32           C  
ANISOU  970  CZ  TYR A 122    13308  14183  15567   -175  -1796   1819       C  
ATOM    971  OH  TYR A 122       3.744 -46.970  -2.425  1.00110.17           O  
ANISOU  971  OH  TYR A 122    13026  13916  14917   -287  -1786   1850       O  
ATOM    972  N   PHE A 123      11.340 -46.932  -3.196  1.00 88.19           N  
ANISOU  972  N   PHE A 123     9619  10846  13042    -53  -1936   1881       N  
ATOM    973  CA  PHE A 123      11.791 -46.782  -1.824  1.00 81.68           C  
ANISOU  973  CA  PHE A 123     8806  10139  12089   -220  -2056   2075       C  
ATOM    974  C   PHE A 123      12.792 -45.652  -1.619  1.00 71.71           C  
ANISOU  974  C   PHE A 123     7521   9014  10711   -264  -2060   2056       C  
ATOM    975  O   PHE A 123      13.030 -45.269  -0.471  1.00 74.41           O  
ANISOU  975  O   PHE A 123     7899   9497  10878   -423  -2140   2189       O  
ATOM    976  CB  PHE A 123      12.395 -48.105  -1.326  1.00 85.06           C  
ANISOU  976  CB  PHE A 123     9129  10415  12775   -240  -2165   2238       C  
ATOM    977  CG  PHE A 123      11.469 -49.281  -1.476  1.00 90.15           C  
ANISOU  977  CG  PHE A 123     9785  10915  13552   -213  -2175   2266       C  
ATOM    978  CD1 PHE A 123      10.368 -49.421  -0.645  1.00 92.98           C  
ANISOU  978  CD1 PHE A 123    10247  11365  13714   -345  -2218   2377       C  
ATOM    979  CD2 PHE A 123      11.690 -50.236  -2.455  1.00 93.81           C  
ANISOU  979  CD2 PHE A 123    10153  11159  14332    -66  -2133   2167       C  
ATOM    980  CE1 PHE A 123       9.506 -50.496  -0.785  1.00 98.03           C  
ANISOU  980  CE1 PHE A 123    10895  11877  14475   -328  -2230   2406       C  
ATOM    981  CE2 PHE A 123      10.832 -51.315  -2.600  1.00 98.61           C  
ANISOU  981  CE2 PHE A 123    10771  11631  15064    -49  -2143   2185       C  
ATOM    982  CZ  PHE A 123       9.739 -51.445  -1.763  1.00 99.71           C  
ANISOU  982  CZ  PHE A 123    11015  11861  15009   -179  -2196   2312       C  
ATOM    983  N   VAL A 124      13.365 -45.093  -2.686  1.00 60.76           N  
ANISOU  983  N   VAL A 124     6075   7601   9408   -143  -1971   1891       N  
ATOM    984  CA  VAL A 124      14.412 -44.086  -2.532  1.00 64.26           C  
ANISOU  984  CA  VAL A 124     6481   8163   9772   -186  -1979   1877       C  
ATOM    985  C   VAL A 124      13.832 -42.794  -1.963  1.00 59.03           C  
ANISOU  985  C   VAL A 124     5952   7714   8764   -318  -1968   1858       C  
ATOM    986  O   VAL A 124      12.723 -42.375  -2.322  1.00 56.09           O  
ANISOU  986  O   VAL A 124     5678   7383   8251   -307  -1901   1762       O  
ATOM    987  CB  VAL A 124      15.109 -43.843  -3.884  1.00 63.02           C  
ANISOU  987  CB  VAL A 124     6219   7931   9793    -33  -1874   1694       C  
ATOM    988  CG1 VAL A 124      16.040 -42.623  -3.822  1.00 58.19           C  
ANISOU  988  CG1 VAL A 124     5582   7463   9063    -88  -1868   1662       C  
ATOM    989  CG2 VAL A 124      15.866 -45.092  -4.326  1.00 62.14           C  
ANISOU  989  CG2 VAL A 124     5964   7623  10024     77  -1881   1697       C  
ATOM    990  N   ARG A 125      14.578 -42.158  -1.055  1.00 50.94           N  
ANISOU  990  N   ARG A 125     4929   6822   7602   -450  -2033   1943       N  
ATOM    991  CA  ARG A 125      14.226 -40.844  -0.509  1.00 49.48           C  
ANISOU  991  CA  ARG A 125     4859   6841   7101   -586  -2014   1893       C  
ATOM    992  C   ARG A 125      15.114 -39.803  -1.193  1.00 42.82           C  
ANISOU  992  C   ARG A 125     3966   6041   6264   -548  -1963   1773       C  
ATOM    993  O   ARG A 125      16.254 -39.583  -0.781  1.00 47.04           O  
ANISOU  993  O   ARG A 125     4433   6615   6827   -599  -2016   1837       O  
ATOM    994  CB  ARG A 125      14.402 -40.834   1.010  1.00 54.67           C  
ANISOU  994  CB  ARG A 125     5558   7629   7586   -783  -2109   2055       C  
ATOM    995  CG  ARG A 125      14.125 -39.487   1.693  1.00 52.34           C  
ANISOU  995  CG  ARG A 125     5377   7548   6964   -943  -2079   1981       C  
ATOM    996  CD  ARG A 125      14.372 -39.562   3.205  1.00 56.82           C  
ANISOU  996  CD  ARG A 125     5967   8249   7372  -1147  -2163   2137       C  
ATOM    997  NE  ARG A 125      15.777 -39.815   3.521  1.00 59.81           N  
ANISOU  997  NE  ARG A 125     6233   8600   7892  -1166  -2251   2267       N  
ATOM    998  CZ  ARG A 125      16.216 -40.315   4.674  1.00 62.56           C  
ANISOU  998  CZ  ARG A 125     6552   9002   8215  -1311  -2354   2460       C  
ATOM    999  NH1 ARG A 125      15.366 -40.639   5.643  1.00 64.75           N  
ANISOU  999  NH1 ARG A 125     6901   9373   8328  -1459  -2377   2547       N  
ATOM   1000  NH2 ARG A 125      17.513 -40.504   4.855  1.00 53.84           N  
ANISOU 1000  NH2 ARG A 125     5339   7863   7255  -1316  -2433   2571       N  
ATOM   1001  N   ALA A 126      14.600 -39.171  -2.252  1.00 41.77           N  
ANISOU 1001  N   ALA A 126     3895   5881   6093   -461  -1818   1575       N  
ATOM   1002  CA  ALA A 126      15.414 -38.271  -3.066  1.00 45.01           C  
ANISOU 1002  CA  ALA A 126     4280   6300   6521   -415  -1721   1433       C  
ATOM   1003  C   ALA A 126      15.622 -36.931  -2.366  1.00 45.44           C  
ANISOU 1003  C   ALA A 126     4422   6519   6323   -567  -1722   1403       C  
ATOM   1004  O   ALA A 126      14.667 -36.328  -1.868  1.00 42.94           O  
ANISOU 1004  O   ALA A 126     4250   6281   5783   -655  -1679   1346       O  
ATOM   1005  CB  ALA A 126      14.763 -38.045  -4.435  1.00 36.61           C  
ANISOU 1005  CB  ALA A 126     3285   5147   5479   -289  -1536   1223       C  
ATOM   1006  N   ALA A 127      16.869 -36.461  -2.338  1.00 38.63           N  
ANISOU 1006  N   ALA A 127     3465   5705   5506   -598  -1765   1429       N  
ATOM   1007  CA  ALA A 127      17.142 -35.114  -1.851  1.00 42.41           C  
ANISOU 1007  CA  ALA A 127     4024   6322   5768   -734  -1749   1369       C  
ATOM   1008  C   ALA A 127      16.463 -34.077  -2.742  1.00 42.38           C  
ANISOU 1008  C   ALA A 127     4152   6291   5658   -691  -1572   1151       C  
ATOM   1009  O   ALA A 127      16.415 -34.220  -3.970  1.00 39.34           O  
ANISOU 1009  O   ALA A 127     3746   5803   5398   -558  -1467   1050       O  
ATOM   1010  CB  ALA A 127      18.651 -34.855  -1.801  1.00 42.94           C  
ANISOU 1010  CB  ALA A 127     3952   6433   5930   -763  -1825   1435       C  
ATOM   1011  N   LYS A 128      15.928 -33.028  -2.120  1.00 36.51           N  
ANISOU 1011  N   LYS A 128     3539   5644   4691   -813  -1542   1076       N  
ATOM   1012  CA  LYS A 128      15.291 -31.967  -2.888  1.00 44.06           C  
ANISOU 1012  CA  LYS A 128     4610   6563   5568   -783  -1394    887       C  
ATOM   1013  C   LYS A 128      16.341 -31.168  -3.652  1.00 38.99           C  
ANISOU 1013  C   LYS A 128     3915   5913   4986   -768  -1356    827       C  
ATOM   1014  O   LYS A 128      17.410 -30.857  -3.125  1.00 36.49           O  
ANISOU 1014  O   LYS A 128     3528   5677   4660   -854  -1439    894       O  
ATOM   1015  CB  LYS A 128      14.496 -31.042  -1.975  1.00 49.61           C  
ANISOU 1015  CB  LYS A 128     5445   7357   6049   -918  -1374    808       C  
ATOM   1016  CG  LYS A 128      13.351 -31.718  -1.254  1.00 65.83           C  
ANISOU 1016  CG  LYS A 128     7559   9438   8016   -948  -1391    845       C  
ATOM   1017  CD  LYS A 128      12.395 -30.689  -0.687  1.00 78.73           C  
ANISOU 1017  CD  LYS A 128     9323  11136   9456  -1049  -1316    699       C  
ATOM   1018  CE  LYS A 128      11.487 -31.269   0.398  1.00 82.00           C  
ANISOU 1018  CE  LYS A 128     9777  11646   9732  -1145  -1357    751       C  
ATOM   1019  NZ  LYS A 128      12.176 -31.466   1.716  1.00 74.38           N  
ANISOU 1019  NZ  LYS A 128     8760  10852   8648  -1324  -1496    888       N  
ATOM   1020  N   THR A 129      16.033 -30.838  -4.898  1.00 30.76           N  
ANISOU 1020  N   THR A 129     2904   4787   3998   -671  -1234    709       N  
ATOM   1021  CA  THR A 129      16.927 -30.041  -5.730  1.00 35.48           C  
ANISOU 1021  CA  THR A 129     3457   5385   4639   -669  -1188    650       C  
ATOM   1022  C   THR A 129      16.441 -28.598  -5.790  1.00 37.33           C  
ANISOU 1022  C   THR A 129     3817   5627   4738   -744  -1123    534       C  
ATOM   1023  O   THR A 129      15.350 -28.261  -5.325  1.00 35.44           O  
ANISOU 1023  O   THR A 129     3694   5377   4395   -776  -1095    476       O  
ATOM   1024  CB  THR A 129      17.000 -30.599  -7.155  1.00 32.23           C  
ANISOU 1024  CB  THR A 129     2979   4892   4374   -534  -1099    601       C  
ATOM   1025  OG1 THR A 129      15.817 -30.205  -7.859  1.00 31.12           O  
ANISOU 1025  OG1 THR A 129     2959   4692   4173   -496   -994    496       O  
ATOM   1026  CG2 THR A 129      17.116 -32.129  -7.143  1.00 33.29           C  
ANISOU 1026  CG2 THR A 129     3004   4976   4670   -438  -1145    684       C  
ATOM   1027  N   ASN A 130      17.249 -27.749  -6.428  1.00 29.57           N  
ANISOU 1027  N   ASN A 130     2804   4654   3778   -771  -1095    496       N  
ATOM   1028  CA  ASN A 130      16.922 -26.336  -6.535  1.00 32.29           C  
ANISOU 1028  CA  ASN A 130     3250   4984   4033   -846  -1048    398       C  
ATOM   1029  C   ASN A 130      15.910 -26.026  -7.632  1.00 35.40           C  
ANISOU 1029  C   ASN A 130     3722   5282   4447   -772   -944    313       C  
ATOM   1030  O   ASN A 130      15.494 -24.869  -7.752  1.00 36.18           O  
ANISOU 1030  O   ASN A 130     3904   5342   4501   -825   -911    238       O  
ATOM   1031  CB  ASN A 130      18.188 -25.524  -6.788  1.00 29.98           C  
ANISOU 1031  CB  ASN A 130     2892   4739   3759   -919  -1072    408       C  
ATOM   1032  CG  ASN A 130      18.087 -24.123  -6.247  1.00 42.24           C  
ANISOU 1032  CG  ASN A 130     4536   6298   5215  -1043  -1079    336       C  
ATOM   1033  OD1 ASN A 130      17.511 -23.890  -5.179  1.00 30.56           O  
ANISOU 1033  OD1 ASN A 130     3130   4842   3638  -1113  -1105    299       O  
ATOM   1034  ND2 ASN A 130      18.639 -23.175  -6.979  1.00 35.22           N  
ANISOU 1034  ND2 ASN A 130     3637   5391   4354  -1081  -1054    307       N  
ATOM   1035  N   ASN A 131      15.509 -27.008  -8.437  1.00 32.13           N  
ANISOU 1035  N   ASN A 131     3275   4823   4107   -658   -897    323       N  
ATOM   1036  CA  ASN A 131      14.582 -26.780  -9.540  1.00 26.54           C  
ANISOU 1036  CA  ASN A 131     2630   4041   3412   -599   -806    257       C  
ATOM   1037  C   ASN A 131      13.292 -27.544  -9.280  1.00 27.16           C  
ANISOU 1037  C   ASN A 131     2774   4071   3475   -532   -785    244       C  
ATOM   1038  O   ASN A 131      13.311 -28.775  -9.184  1.00 34.62           O  
ANISOU 1038  O   ASN A 131     3662   5017   4475   -466   -803    293       O  
ATOM   1039  CB  ASN A 131      15.207 -27.217 -10.868  1.00 32.32           C  
ANISOU 1039  CB  ASN A 131     3267   4782   4231   -542   -753    260       C  
ATOM   1040  CG  ASN A 131      16.494 -26.480 -11.162  1.00 39.61           C  
ANISOU 1040  CG  ASN A 131     4116   5767   5166   -616   -769    275       C  
ATOM   1041  OD1 ASN A 131      16.540 -25.251 -11.102  1.00 37.69           O  
ANISOU 1041  OD1 ASN A 131     3933   5520   4869   -703   -778    256       O  
ATOM   1042  ND2 ASN A 131      17.554 -27.226 -11.458  1.00 38.09           N  
ANISOU 1042  ND2 ASN A 131     3784   5627   5059   -584   -775    305       N  
ATOM   1043  N   SER A 132      12.176 -26.823  -9.183  1.00 28.20           N  
ANISOU 1043  N   SER A 132     3015   4150   3548   -549   -749    179       N  
ATOM   1044  CA  SER A 132      10.888 -27.416  -8.832  1.00 25.01           C  
ANISOU 1044  CA  SER A 132     2676   3710   3117   -501   -727    160       C  
ATOM   1045  C   SER A 132       9.963 -27.433 -10.040  1.00 34.08           C  
ANISOU 1045  C   SER A 132     3863   4783   4304   -428   -651    121       C  
ATOM   1046  O   SER A 132       9.624 -26.375 -10.582  1.00 31.51           O  
ANISOU 1046  O   SER A 132     3584   4411   3978   -454   -620     77       O  
ATOM   1047  CB  SER A 132      10.228 -26.661  -7.684  1.00 29.05           C  
ANISOU 1047  CB  SER A 132     3269   4231   3535   -581   -741    101       C  
ATOM   1048  OG  SER A 132      11.080 -26.658  -6.555  1.00 34.04           O  
ANISOU 1048  OG  SER A 132     3867   4957   4110   -671   -816    140       O  
ATOM   1049  N   PHE A 133       9.543 -28.635 -10.436  1.00 24.78           N  
ANISOU 1049  N   PHE A 133     2660   3589   3166   -343   -630    144       N  
ATOM   1050  CA  PHE A 133       8.485 -28.839 -11.429  1.00 27.41           C  
ANISOU 1050  CA  PHE A 133     3034   3863   3518   -281   -563    110       C  
ATOM   1051  C   PHE A 133       7.170 -28.955 -10.657  1.00 29.76           C  
ANISOU 1051  C   PHE A 133     3413   4128   3766   -271   -560     86       C  
ATOM   1052  O   PHE A 133       6.902 -29.974 -10.015  1.00 30.51           O  
ANISOU 1052  O   PHE A 133     3499   4240   3856   -244   -584    121       O  
ATOM   1053  CB  PHE A 133       8.803 -30.085 -12.253  1.00 29.78           C  
ANISOU 1053  CB  PHE A 133     3256   4168   3893   -206   -538    129       C  
ATOM   1054  CG  PHE A 133       7.883 -30.312 -13.417  1.00 30.38           C  
ANISOU 1054  CG  PHE A 133     3362   4205   3977   -159   -468     92       C  
ATOM   1055  CD1 PHE A 133       8.136 -29.719 -14.650  1.00 25.53           C  
ANISOU 1055  CD1 PHE A 133     2730   3608   3360   -187   -423     71       C  
ATOM   1056  CD2 PHE A 133       6.787 -31.147 -13.297  1.00 29.37           C  
ANISOU 1056  CD2 PHE A 133     3273   4035   3853   -103   -454     87       C  
ATOM   1057  CE1 PHE A 133       7.295 -29.943 -15.738  1.00 24.29           C  
ANISOU 1057  CE1 PHE A 133     2596   3435   3196   -165   -367     46       C  
ATOM   1058  CE2 PHE A 133       5.940 -31.367 -14.383  1.00 30.00           C  
ANISOU 1058  CE2 PHE A 133     3376   4087   3934    -70   -394     55       C  
ATOM   1059  CZ  PHE A 133       6.195 -30.755 -15.601  1.00 25.03           C  
ANISOU 1059  CZ  PHE A 133     2731   3484   3295   -104   -353     36       C  
ATOM   1060  N   VAL A 134       6.352 -27.901 -10.674  1.00 27.16           N  
ANISOU 1060  N   VAL A 134     3155   3753   3412   -298   -533     29       N  
ATOM   1061  CA  VAL A 134       5.232 -27.802  -9.739  1.00 27.93           C  
ANISOU 1061  CA  VAL A 134     3316   3837   3461   -309   -525    -18       C  
ATOM   1062  C   VAL A 134       3.958 -28.317 -10.394  1.00 31.12           C  
ANISOU 1062  C   VAL A 134     3752   4184   3887   -237   -477    -28       C  
ATOM   1063  O   VAL A 134       3.628 -27.946 -11.527  1.00 30.32           O  
ANISOU 1063  O   VAL A 134     3658   4031   3832   -209   -445    -32       O  
ATOM   1064  CB  VAL A 134       5.051 -26.364  -9.217  1.00 29.14           C  
ANISOU 1064  CB  VAL A 134     3511   3961   3599   -381   -521    -99       C  
ATOM   1065  CG1 VAL A 134       6.188 -25.996  -8.235  1.00 29.54           C  
ANISOU 1065  CG1 VAL A 134     3537   4089   3599   -471   -574    -97       C  
ATOM   1066  CG2 VAL A 134       4.990 -25.367 -10.359  1.00 32.69           C  
ANISOU 1066  CG2 VAL A 134     3969   4328   4125   -376   -501   -109       C  
ATOM   1067  N   VAL A 135       3.240 -29.168  -9.678  1.00 26.17           N  
ANISOU 1067  N   VAL A 135     3142   3579   3221   -219   -479    -22       N  
ATOM   1068  CA  VAL A 135       1.967 -29.713 -10.134  1.00 20.57           C  
ANISOU 1068  CA  VAL A 135     2464   2827   2526   -158   -438    -32       C  
ATOM   1069  C   VAL A 135       0.887 -29.119  -9.244  1.00 30.24           C  
ANISOU 1069  C   VAL A 135     3739   4046   3704   -192   -415   -107       C  
ATOM   1070  O   VAL A 135       0.882 -29.362  -8.030  1.00 27.15           O  
ANISOU 1070  O   VAL A 135     3352   3727   3237   -247   -436   -115       O  
ATOM   1071  CB  VAL A 135       1.964 -31.250 -10.067  1.00 26.07           C  
ANISOU 1071  CB  VAL A 135     3130   3546   3229   -113   -458     34       C  
ATOM   1072  CG1 VAL A 135       0.615 -31.811 -10.493  1.00 27.02           C  
ANISOU 1072  CG1 VAL A 135     3285   3624   3358    -61   -417     22       C  
ATOM   1073  CG2 VAL A 135       3.097 -31.820 -10.926  1.00 24.50           C  
ANISOU 1073  CG2 VAL A 135     2861   3347   3101    -78   -469     78       C  
ATOM   1074  N   ASP A 136      -0.008 -28.327  -9.832  1.00 23.65           N  
ANISOU 1074  N   ASP A 136     2932   3135   2919   -169   -374   -161       N  
ATOM   1075  CA  ASP A 136      -1.095 -27.699  -9.063  1.00 27.26           C  
ANISOU 1075  CA  ASP A 136     3419   3574   3364   -192   -339   -257       C  
ATOM   1076  C   ASP A 136      -0.480 -26.869  -7.928  1.00 30.99           C  
ANISOU 1076  C   ASP A 136     3892   4094   3791   -282   -351   -331       C  
ATOM   1077  O   ASP A 136       0.629 -26.337  -8.060  1.00 32.64           O  
ANISOU 1077  O   ASP A 136     4084   4304   4013   -317   -385   -313       O  
ATOM   1078  CB  ASP A 136      -2.077 -28.775  -8.610  1.00 25.18           C  
ANISOU 1078  CB  ASP A 136     3167   3353   3046   -169   -320   -246       C  
ATOM   1079  CG  ASP A 136      -2.655 -29.560  -9.783  1.00 31.53           C  
ANISOU 1079  CG  ASP A 136     3972   4108   3901    -89   -308   -183       C  
ATOM   1080  OD1 ASP A 136      -3.010 -28.920 -10.802  1.00 30.45           O  
ANISOU 1080  OD1 ASP A 136     3837   3893   3840    -57   -291   -189       O  
ATOM   1081  OD2 ASP A 136      -2.727 -30.807  -9.702  1.00 27.13           O  
ANISOU 1081  OD2 ASP A 136     3407   3588   3311    -67   -322   -122       O  
ATOM   1082  N   GLY A 137      -1.177 -26.771  -6.794  1.00 29.34           N  
ANISOU 1082  N   GLY A 137     3696   3937   3515   -332   -322   -422       N  
ATOM   1083  CA  GLY A 137      -0.665 -26.040  -5.655  1.00 28.91           C  
ANISOU 1083  CA  GLY A 137     3640   3949   3395   -437   -326   -513       C  
ATOM   1084  C   GLY A 137      -0.794 -24.534  -5.813  1.00 34.66           C  
ANISOU 1084  C   GLY A 137     4368   4571   4228   -451   -295   -637       C  
ATOM   1085  O   GLY A 137      -1.241 -24.006  -6.831  1.00 38.14           O  
ANISOU 1085  O   GLY A 137     4807   4881   4802   -381   -283   -631       O  
ATOM   1086  N   ASP A 138      -0.361 -23.831  -4.771  1.00 32.41           N  
ANISOU 1086  N   ASP A 138     4081   4344   3888   -554   -290   -745       N  
ATOM   1087  CA  ASP A 138      -0.398 -22.369  -4.729  1.00 32.55           C  
ANISOU 1087  CA  ASP A 138     4093   4256   4019   -583   -264   -885       C  
ATOM   1088  C   ASP A 138       0.961 -21.843  -5.195  1.00 33.69           C  
ANISOU 1088  C   ASP A 138     4231   4370   4199   -611   -328   -813       C  
ATOM   1089  O   ASP A 138       1.755 -21.276  -4.439  1.00 39.08           O  
ANISOU 1089  O   ASP A 138     4910   5107   4832   -711   -345   -877       O  
ATOM   1090  CB  ASP A 138      -0.765 -21.900  -3.323  1.00 32.31           C  
ANISOU 1090  CB  ASP A 138     4058   4312   3906   -692   -209  -1075       C  
ATOM   1091  CG  ASP A 138      -0.895 -20.398  -3.214  1.00 45.30           C  
ANISOU 1091  CG  ASP A 138     5687   5829   5696   -720   -172  -1253       C  
ATOM   1092  OD1 ASP A 138      -1.174 -19.755  -4.240  1.00 43.19           O  
ANISOU 1092  OD1 ASP A 138     5409   5382   5619   -635   -181  -1229       O  
ATOM   1093  OD2 ASP A 138      -0.729 -19.858  -2.094  1.00 45.31           O  
ANISOU 1093  OD2 ASP A 138     5681   5909   5626   -836   -138  -1417       O  
ATOM   1094  N   THR A 139       1.227 -22.063  -6.492  1.00 30.67           N  
ANISOU 1094  N   THR A 139     3844   3914   3896   -531   -361   -676       N  
ATOM   1095  CA  THR A 139       2.569 -21.905  -7.045  1.00 36.94           C  
ANISOU 1095  CA  THR A 139     4622   4716   4697   -554   -420   -575       C  
ATOM   1096  C   THR A 139       2.568 -21.077  -8.327  1.00 37.15           C  
ANISOU 1096  C   THR A 139     4641   4602   4874   -516   -436   -527       C  
ATOM   1097  O   THR A 139       3.511 -21.177  -9.120  1.00 32.88           O  
ANISOU 1097  O   THR A 139     4081   4077   4335   -518   -476   -417       O  
ATOM   1098  CB  THR A 139       3.206 -23.277  -7.315  1.00 36.38           C  
ANISOU 1098  CB  THR A 139     4535   4751   4538   -521   -453   -432       C  
ATOM   1099  OG1 THR A 139       2.298 -24.072  -8.082  1.00 34.10           O  
ANISOU 1099  OG1 THR A 139     4253   4427   4276   -427   -426   -380       O  
ATOM   1100  CG2 THR A 139       3.501 -24.009  -6.007  1.00 40.35           C  
ANISOU 1100  CG2 THR A 139     5033   5398   4898   -588   -472   -439       C  
ATOM   1101  N   LEU A 140       1.525 -20.273  -8.551  1.00 35.77           N  
ANISOU 1101  N   LEU A 140     4469   4293   4828   -487   -408   -603       N  
ATOM   1102  CA  LEU A 140       1.412 -19.534  -9.805  1.00 41.52           C  
ANISOU 1102  CA  LEU A 140     5185   4887   5706   -460   -441   -526       C  
ATOM   1103  C   LEU A 140       2.491 -18.476  -9.939  1.00 46.50           C  
ANISOU 1103  C   LEU A 140     5801   5469   6396   -538   -491   -514       C  
ATOM   1104  O   LEU A 140       2.846 -18.099 -11.060  1.00 47.14           O  
ANISOU 1104  O   LEU A 140     5867   5496   6548   -543   -537   -396       O  
ATOM   1105  CB  LEU A 140       0.044 -18.873  -9.908  1.00 42.15           C  
ANISOU 1105  CB  LEU A 140     5255   4819   5940   -414   -414   -604       C  
ATOM   1106  CG  LEU A 140      -1.135 -19.824 -10.026  1.00 51.97           C  
ANISOU 1106  CG  LEU A 140     6505   6090   7149   -335   -370   -596       C  
ATOM   1107  CD1 LEU A 140      -2.438 -19.041 -10.059  1.00 55.01           C  
ANISOU 1107  CD1 LEU A 140     6865   6322   7713   -294   -346   -684       C  
ATOM   1108  CD2 LEU A 140      -0.955 -20.662 -11.270  1.00 50.54           C  
ANISOU 1108  CD2 LEU A 140     6328   5952   6922   -294   -399   -424       C  
ATOM   1109  N   LYS A 141       2.998 -17.966  -8.816  1.00 46.40           N  
ANISOU 1109  N   LYS A 141     5793   5486   6352   -613   -486   -634       N  
ATOM   1110  CA  LYS A 141       4.033 -16.943  -8.878  1.00 52.53           C  
ANISOU 1110  CA  LYS A 141     6555   6215   7187   -695   -536   -630       C  
ATOM   1111  C   LYS A 141       5.303 -17.512  -9.492  1.00 53.68           C  
ANISOU 1111  C   LYS A 141     6686   6475   7234   -718   -580   -477       C  
ATOM   1112  O   LYS A 141       5.885 -16.916 -10.406  1.00 54.98           O  
ANISOU 1112  O   LYS A 141     6832   6587   7471   -748   -627   -382       O  
ATOM   1113  CB  LYS A 141       4.303 -16.383  -7.480  1.00 54.96           C  
ANISOU 1113  CB  LYS A 141     6870   6554   7459   -783   -515   -805       C  
ATOM   1114  CG  LYS A 141       4.302 -14.865  -7.397  1.00 67.74           C  
ANISOU 1114  CG  LYS A 141     8475   8001   9262   -837   -532   -911       C  
ATOM   1115  CD  LYS A 141       4.441 -14.400  -5.951  1.00 82.60           C  
ANISOU 1115  CD  LYS A 141    10361   9931  11091   -932   -492  -1122       C  
ATOM   1116  CE  LYS A 141       4.544 -12.881  -5.852  1.00 88.17           C  
ANISOU 1116  CE  LYS A 141    11047  10453  12000   -992   -510  -1245       C  
ATOM   1117  NZ  LYS A 141       4.812 -12.425  -4.455  1.00 84.13           N  
ANISOU 1117  NZ  LYS A 141    10538  10009  11419  -1107   -468  -1466       N  
ATOM   1118  N   GLU A 142       5.735 -18.683  -9.017  1.00 41.28           N  
ANISOU 1118  N   GLU A 142     5114   5062   5508   -708   -569   -448       N  
ATOM   1119  CA  GLU A 142       6.965 -19.268  -9.533  1.00 43.48           C  
ANISOU 1119  CA  GLU A 142     5359   5446   5716   -723   -605   -323       C  
ATOM   1120  C   GLU A 142       6.765 -19.979 -10.873  1.00 45.44           C  
ANISOU 1120  C   GLU A 142     5589   5697   5977   -649   -596   -203       C  
ATOM   1121  O   GLU A 142       7.729 -20.117 -11.629  1.00 43.16           O  
ANISOU 1121  O   GLU A 142     5261   5465   5674   -671   -618   -112       O  
ATOM   1122  CB  GLU A 142       7.552 -20.236  -8.511  1.00 48.99           C  
ANISOU 1122  CB  GLU A 142     6045   6295   6275   -743   -611   -326       C  
ATOM   1123  CG  GLU A 142       6.824 -21.551  -8.396  1.00 45.18           C  
ANISOU 1123  CG  GLU A 142     5569   5869   5729   -664   -580   -299       C  
ATOM   1124  CD  GLU A 142       7.169 -22.277  -7.109  1.00 64.94           C  
ANISOU 1124  CD  GLU A 142     8064   8501   8109   -710   -600   -313       C  
ATOM   1125  OE1 GLU A 142       6.395 -22.150  -6.129  1.00 68.40           O  
ANISOU 1125  OE1 GLU A 142     8536   8957   8497   -744   -573   -415       O  
ATOM   1126  OE2 GLU A 142       8.224 -22.954  -7.076  1.00 62.86           O  
ANISOU 1126  OE2 GLU A 142     7752   8328   7802   -722   -645   -219       O  
ATOM   1127  N   CYS A 143       5.553 -20.454 -11.176  1.00 39.44           N  
ANISOU 1127  N   CYS A 143     4852   4894   5238   -572   -559   -210       N  
ATOM   1128  CA  CYS A 143       5.256 -21.078 -12.468  1.00 34.26           C  
ANISOU 1128  CA  CYS A 143     4182   4244   4589   -517   -548   -112       C  
ATOM   1129  C   CYS A 143       3.885 -20.616 -12.932  1.00 30.59           C  
ANISOU 1129  C   CYS A 143     3743   3657   4221   -477   -536   -124       C  
ATOM   1130  O   CYS A 143       2.858 -21.187 -12.546  1.00 34.42           O  
ANISOU 1130  O   CYS A 143     4250   4134   4695   -416   -498   -173       O  
ATOM   1131  CB  CYS A 143       5.309 -22.604 -12.395  1.00 37.22           C  
ANISOU 1131  CB  CYS A 143     4544   4727   4871   -455   -520    -85       C  
ATOM   1132  SG  CYS A 143       5.024 -23.436 -14.012  1.00 41.02           S  
ANISOU 1132  SG  CYS A 143     5000   5233   5352   -403   -493      6       S  
ATOM   1133  N   PRO A 144       3.828 -19.563 -13.743  1.00 35.31           N  
ANISOU 1133  N   PRO A 144     4331   4158   4928   -517   -574    -71       N  
ATOM   1134  CA  PRO A 144       2.534 -19.058 -14.215  1.00 29.72           C  
ANISOU 1134  CA  PRO A 144     3632   3319   4342   -482   -580    -63       C  
ATOM   1135  C   PRO A 144       1.802 -20.074 -15.079  1.00 28.99           C  
ANISOU 1135  C   PRO A 144     3541   3277   4198   -423   -556      8       C  
ATOM   1136  O   PRO A 144       2.394 -20.999 -15.645  1.00 27.35           O  
ANISOU 1136  O   PRO A 144     3319   3190   3881   -422   -540     66       O  
ATOM   1137  CB  PRO A 144       2.919 -17.814 -15.027  1.00 32.53           C  
ANISOU 1137  CB  PRO A 144     3964   3579   4817   -559   -651     25       C  
ATOM   1138  CG  PRO A 144       4.220 -17.385 -14.426  1.00 42.40           C  
ANISOU 1138  CG  PRO A 144     5207   4873   6030   -630   -668     -9       C  
ATOM   1139  CD  PRO A 144       4.935 -18.648 -14.056  1.00 37.73           C  
ANISOU 1139  CD  PRO A 144     4613   4454   5267   -607   -625    -22       C  
ATOM   1140  N   LEU A 145       0.487 -19.866 -15.187  1.00 30.68           N  
ANISOU 1140  N   LEU A 145     3762   3389   4506   -375   -551     -7       N  
ATOM   1141  CA  LEU A 145      -0.369 -20.779 -15.940  1.00 35.33           C  
ANISOU 1141  CA  LEU A 145     4353   4017   5053   -324   -530     51       C  
ATOM   1142  C   LEU A 145       0.073 -20.911 -17.391  1.00 33.58           C  
ANISOU 1142  C   LEU A 145     4110   3860   4789   -377   -563    193       C  
ATOM   1143  O   LEU A 145      -0.045 -21.988 -17.982  1.00 31.31           O  
ANISOU 1143  O   LEU A 145     3822   3674   4401   -356   -529    224       O  
ATOM   1144  CB  LEU A 145      -1.815 -20.296 -15.890  1.00 41.85           C  
ANISOU 1144  CB  LEU A 145     5176   4710   6016   -277   -535     25       C  
ATOM   1145  CG  LEU A 145      -2.491 -20.435 -14.535  1.00 62.40           C  
ANISOU 1145  CG  LEU A 145     7793   7286   8632   -224   -478   -133       C  
ATOM   1146  CD1 LEU A 145      -3.905 -19.880 -14.578  1.00 62.89           C  
ANISOU 1146  CD1 LEU A 145     7830   7209   8856   -177   -479   -165       C  
ATOM   1147  CD2 LEU A 145      -2.490 -21.896 -14.127  1.00 71.13           C  
ANISOU 1147  CD2 LEU A 145     8923   8532   9570   -184   -423   -156       C  
ATOM   1148  N   GLU A 146       0.563 -19.820 -17.988  1.00 33.98           N  
ANISOU 1148  N   GLU A 146     4138   3859   4916   -459   -627    276       N  
ATOM   1149  CA  GLU A 146       0.930 -19.846 -19.399  1.00 34.43           C  
ANISOU 1149  CA  GLU A 146     4168   3996   4919   -539   -662    418       C  
ATOM   1150  C   GLU A 146       2.129 -20.743 -19.678  1.00 29.57           C  
ANISOU 1150  C   GLU A 146     3535   3556   4143   -567   -615    411       C  
ATOM   1151  O   GLU A 146       2.411 -21.029 -20.846  1.00 29.87           O  
ANISOU 1151  O   GLU A 146     3545   3702   4103   -634   -616    495       O  
ATOM   1152  CB  GLU A 146       1.215 -18.424 -19.896  1.00 32.72           C  
ANISOU 1152  CB  GLU A 146     3926   3682   4826   -637   -754    523       C  
ATOM   1153  CG  GLU A 146       2.414 -17.793 -19.239  1.00 42.65           C  
ANISOU 1153  CG  GLU A 146     5178   4932   6093   -684   -766    478       C  
ATOM   1154  CD  GLU A 146       2.549 -16.325 -19.561  1.00 68.88           C  
ANISOU 1154  CD  GLU A 146     8478   8118   9576   -773   -864    571       C  
ATOM   1155  OE1 GLU A 146       2.480 -15.961 -20.760  1.00 70.51           O  
ANISOU 1155  OE1 GLU A 146     8656   8340   9795   -861   -930    735       O  
ATOM   1156  OE2 GLU A 146       2.720 -15.537 -18.605  1.00 75.09           O  
ANISOU 1156  OE2 GLU A 146     9271   8781  10477   -764   -878    480       O  
ATOM   1157  N   HIS A 147       2.831 -21.209 -18.645  1.00 27.51           N  
ANISOU 1157  N   HIS A 147     3281   3335   3836   -525   -574    310       N  
ATOM   1158  CA  HIS A 147       3.974 -22.096 -18.829  1.00 26.53           C  
ANISOU 1158  CA  HIS A 147     3123   3361   3597   -538   -533    296       C  
ATOM   1159  C   HIS A 147       3.743 -23.485 -18.258  1.00 29.08           C  
ANISOU 1159  C   HIS A 147     3454   3735   3860   -442   -472    217       C  
ATOM   1160  O   HIS A 147       4.709 -24.217 -18.024  1.00 30.04           O  
ANISOU 1160  O   HIS A 147     3540   3946   3927   -432   -445    186       O  
ATOM   1161  CB  HIS A 147       5.216 -21.461 -18.216  1.00 25.66           C  
ANISOU 1161  CB  HIS A 147     2994   3263   3494   -590   -557    279       C  
ATOM   1162  CG  HIS A 147       5.633 -20.221 -18.937  1.00 31.90           C  
ANISOU 1162  CG  HIS A 147     3765   4021   4336   -700   -620    374       C  
ATOM   1163  ND1 HIS A 147       5.815 -19.009 -18.306  1.00 41.11           N  
ANISOU 1163  ND1 HIS A 147     4945   5072   5604   -741   -675    365       N  
ATOM   1164  CD2 HIS A 147       5.855 -19.999 -20.254  1.00 33.29           C  
ANISOU 1164  CD2 HIS A 147     3906   4267   4476   -792   -640    484       C  
ATOM   1165  CE1 HIS A 147       6.159 -18.098 -19.200  1.00 37.19           C  
ANISOU 1165  CE1 HIS A 147     4423   4561   5146   -847   -735    479       C  
ATOM   1166  NE2 HIS A 147       6.195 -18.673 -20.389  1.00 39.35           N  
ANISOU 1166  NE2 HIS A 147     4667   4958   5328   -886   -716    559       N  
ATOM   1167  N   ARG A 148       2.488 -23.864 -18.041  1.00 24.74           N  
ANISOU 1167  N   ARG A 148     2942   3127   3332   -375   -457    192       N  
ATOM   1168  CA  ARG A 148       2.150 -25.182 -17.519  1.00 22.95           C  
ANISOU 1168  CA  ARG A 148     2723   2938   3057   -293   -410    133       C  
ATOM   1169  C   ARG A 148       1.480 -26.041 -18.584  1.00 24.82           C  
ANISOU 1169  C   ARG A 148     2954   3219   3256   -275   -378    161       C  
ATOM   1170  O   ARG A 148       0.715 -25.546 -19.419  1.00 27.59           O  
ANISOU 1170  O   ARG A 148     3314   3540   3630   -307   -397    219       O  
ATOM   1171  CB  ARG A 148       1.212 -25.077 -16.309  1.00 27.89           C  
ANISOU 1171  CB  ARG A 148     3394   3483   3720   -239   -409     69       C  
ATOM   1172  CG  ARG A 148       1.744 -24.249 -15.163  1.00 30.04           C  
ANISOU 1172  CG  ARG A 148     3674   3721   4017   -269   -432     15       C  
ATOM   1173  CD  ARG A 148       0.949 -24.508 -13.889  1.00 32.89           C  
ANISOU 1173  CD  ARG A 148     4068   4058   4372   -227   -411    -71       C  
ATOM   1174  NE  ARG A 148       1.510 -23.748 -12.773  1.00 38.23           N  
ANISOU 1174  NE  ARG A 148     4749   4726   5051   -276   -427   -139       N  
ATOM   1175  CZ  ARG A 148       1.487 -24.132 -11.497  1.00 33.02           C  
ANISOU 1175  CZ  ARG A 148     4102   4116   4328   -281   -415   -208       C  
ATOM   1176  NH1 ARG A 148       0.927 -25.284 -11.134  1.00 35.02           N  
ANISOU 1176  NH1 ARG A 148     4364   4423   4520   -237   -391   -206       N  
ATOM   1177  NH2 ARG A 148       2.041 -23.357 -10.577  1.00 32.14           N  
ANISOU 1177  NH2 ARG A 148     3992   4009   4211   -346   -430   -274       N  
ATOM   1178  N   ALA A 149       1.755 -27.341 -18.530  1.00 25.47           N  
ANISOU 1178  N   ALA A 149     3016   3369   3294   -227   -334    120       N  
ATOM   1179  CA  ALA A 149       1.097 -28.302 -19.400  1.00 23.66           C  
ANISOU 1179  CA  ALA A 149     2781   3177   3031   -207   -296    118       C  
ATOM   1180  C   ALA A 149      -0.223 -28.756 -18.786  1.00 31.56           C  
ANISOU 1180  C   ALA A 149     3830   4109   4052   -137   -292     98       C  
ATOM   1181  O   ALA A 149      -0.370 -28.830 -17.559  1.00 27.22           O  
ANISOU 1181  O   ALA A 149     3303   3517   3521    -93   -300     63       O  
ATOM   1182  CB  ALA A 149       1.999 -29.513 -19.658  1.00 24.94           C  
ANISOU 1182  CB  ALA A 149     2885   3423   3167   -186   -249     69       C  
ATOM   1183  N   TRP A 150      -1.189 -29.059 -19.657  1.00 24.99           N  
ANISOU 1183  N   TRP A 150     3009   3282   3206   -140   -279    121       N  
ATOM   1184  CA  TRP A 150      -2.541 -29.416 -19.242  1.00 21.66           C  
ANISOU 1184  CA  TRP A 150     2625   2800   2805    -84   -275    111       C  
ATOM   1185  C   TRP A 150      -3.133 -30.345 -20.292  1.00 23.73           C  
ANISOU 1185  C   TRP A 150     2880   3112   3024    -90   -245    117       C  
ATOM   1186  O   TRP A 150      -2.926 -30.135 -21.487  1.00 22.39           O  
ANISOU 1186  O   TRP A 150     2687   3006   2815   -162   -244    154       O  
ATOM   1187  CB  TRP A 150      -3.395 -28.144 -19.051  1.00 24.26           C  
ANISOU 1187  CB  TRP A 150     2978   3038   3204    -97   -317    147       C  
ATOM   1188  CG  TRP A 150      -4.893 -28.304 -18.893  1.00 23.88           C  
ANISOU 1188  CG  TRP A 150     2951   2931   3191    -53   -315    145       C  
ATOM   1189  CD1 TRP A 150      -5.586 -28.424 -17.712  1.00 25.29           C  
ANISOU 1189  CD1 TRP A 150     3151   3061   3398      4   -299     84       C  
ATOM   1190  CD2 TRP A 150      -5.881 -28.313 -19.939  1.00 21.37           C  
ANISOU 1190  CD2 TRP A 150     2629   2611   2881    -74   -330    209       C  
ATOM   1191  NE1 TRP A 150      -6.944 -28.525 -17.965  1.00 24.16           N  
ANISOU 1191  NE1 TRP A 150     3012   2879   3290     28   -298    100       N  
ATOM   1192  CE2 TRP A 150      -7.147 -28.464 -19.321  1.00 23.33           C  
ANISOU 1192  CE2 TRP A 150     2891   2796   3176    -16   -322    182       C  
ATOM   1193  CE3 TRP A 150      -5.819 -28.206 -21.342  1.00 20.40           C  
ANISOU 1193  CE3 TRP A 150     2485   2548   2720   -151   -351    290       C  
ATOM   1194  CZ2 TRP A 150      -8.337 -28.522 -20.051  1.00 23.29           C  
ANISOU 1194  CZ2 TRP A 150     2879   2775   3196    -21   -339    237       C  
ATOM   1195  CZ3 TRP A 150      -6.998 -28.275 -22.069  1.00 22.31           C  
ANISOU 1195  CZ3 TRP A 150     2723   2782   2971   -168   -373    350       C  
ATOM   1196  CH2 TRP A 150      -8.251 -28.424 -21.418  1.00 22.00           C  
ANISOU 1196  CH2 TRP A 150     2698   2666   2995    -97   -370    326       C  
ATOM   1197  N   ASN A 151      -3.833 -31.387 -19.838  1.00 25.16           N  
ANISOU 1197  N   ASN A 151     3079   3276   3205    -27   -221     80       N  
ATOM   1198  CA  ASN A 151      -4.550 -32.311 -20.726  1.00 24.10           C  
ANISOU 1198  CA  ASN A 151     2942   3177   3037    -31   -193     73       C  
ATOM   1199  C   ASN A 151      -3.588 -33.101 -21.603  1.00 26.50           C  
ANISOU 1199  C   ASN A 151     3198   3568   3302    -64   -149     26       C  
ATOM   1200  O   ASN A 151      -3.905 -33.420 -22.749  1.00 25.35           O  
ANISOU 1200  O   ASN A 151     3038   3487   3105   -119   -125     21       O  
ATOM   1201  CB  ASN A 151      -5.605 -31.582 -21.583  1.00 23.50           C  
ANISOU 1201  CB  ASN A 151     2879   3094   2956    -82   -222    144       C  
ATOM   1202  CG  ASN A 151      -6.773 -32.499 -21.999  1.00 28.67           C  
ANISOU 1202  CG  ASN A 151     3547   3757   3588    -67   -204    138       C  
ATOM   1203  OD1 ASN A 151      -7.123 -33.435 -21.279  1.00 28.75           O  
ANISOU 1203  OD1 ASN A 151     3573   3739   3612     -2   -181     90       O  
ATOM   1204  ND2 ASN A 151      -7.386 -32.213 -23.160  1.00 23.50           N  
ANISOU 1204  ND2 ASN A 151     2885   3146   2898   -140   -223    199       N  
ATOM   1205  N   SER A 152      -2.415 -33.442 -21.046  1.00 25.87           N  
ANISOU 1205  N   SER A 152     3084   3496   3249    -36   -137    -17       N  
ATOM   1206  CA  SER A 152      -1.394 -34.190 -21.770  1.00 24.12           C  
ANISOU 1206  CA  SER A 152     2796   3349   3022    -56    -87    -85       C  
ATOM   1207  C   SER A 152      -1.633 -35.697 -21.780  1.00 28.77           C  
ANISOU 1207  C   SER A 152     3362   3916   3653      0    -49   -158       C  
ATOM   1208  O   SER A 152      -1.000 -36.398 -22.568  1.00 30.23           O  
ANISOU 1208  O   SER A 152     3482   4157   3845    -20      6   -240       O  
ATOM   1209  CB  SER A 152      -0.008 -33.932 -21.162  1.00 28.26           C  
ANISOU 1209  CB  SER A 152     3274   3881   3583    -46    -97    -96       C  
ATOM   1210  OG  SER A 152       0.287 -32.544 -21.092  1.00 29.48           O  
ANISOU 1210  OG  SER A 152     3446   4043   3711   -101   -136    -33       O  
ATOM   1211  N   PHE A 153      -2.487 -36.215 -20.905  1.00 24.72           N  
ANISOU 1211  N   PHE A 153     2891   3324   3176     64    -75   -137       N  
ATOM   1212  CA  PHE A 153      -2.665 -37.649 -20.730  1.00 26.76           C  
ANISOU 1212  CA  PHE A 153     3127   3539   3499    119    -57   -189       C  
ATOM   1213  C   PHE A 153      -3.884 -38.169 -21.491  1.00 28.59           C  
ANISOU 1213  C   PHE A 153     3390   3778   3696     99    -32   -208       C  
ATOM   1214  O   PHE A 153      -4.868 -37.456 -21.694  1.00 25.23           O  
ANISOU 1214  O   PHE A 153     3016   3362   3207     67    -50   -151       O  
ATOM   1215  CB  PHE A 153      -2.843 -37.996 -19.252  1.00 24.75           C  
ANISOU 1215  CB  PHE A 153     2897   3208   3300    181   -111   -138       C  
ATOM   1216  CG  PHE A 153      -1.591 -37.845 -18.422  1.00 25.48           C  
ANISOU 1216  CG  PHE A 153     2945   3295   3440    199   -143   -121       C  
ATOM   1217  CD1 PHE A 153      -0.403 -38.459 -18.802  1.00 24.43           C  
ANISOU 1217  CD1 PHE A 153     2724   3171   3386    214   -121   -177       C  
ATOM   1218  CD2 PHE A 153      -1.611 -37.094 -17.265  1.00 32.65           C  
ANISOU 1218  CD2 PHE A 153     3892   4193   4320    196   -194    -59       C  
ATOM   1219  CE1 PHE A 153       0.749 -38.323 -18.031  1.00 33.21           C  
ANISOU 1219  CE1 PHE A 153     3786   4279   4552    228   -160   -149       C  
ATOM   1220  CE2 PHE A 153      -0.464 -36.956 -16.486  1.00 37.39           C  
ANISOU 1220  CE2 PHE A 153     4451   4800   4954    198   -232    -36       C  
ATOM   1221  CZ  PHE A 153       0.713 -37.565 -16.876  1.00 34.57           C  
ANISOU 1221  CZ  PHE A 153     4006   4449   4679    216   -220    -70       C  
ATOM   1222  N   LEU A 154      -3.814 -39.437 -21.877  1.00 29.50           N  
ANISOU 1222  N   LEU A 154     3465   3876   3868    120      6   -289       N  
ATOM   1223  CA  LEU A 154      -4.974 -40.209 -22.303  1.00 26.62           C  
ANISOU 1223  CA  LEU A 154     3127   3494   3492    114     21   -311       C  
ATOM   1224  C   LEU A 154      -4.991 -41.522 -21.538  1.00 30.00           C  
ANISOU 1224  C   LEU A 154     3535   3821   4043    188      5   -332       C  
ATOM   1225  O   LEU A 154      -3.945 -42.156 -21.359  1.00 29.36           O  
ANISOU 1225  O   LEU A 154     3383   3702   4070    226     13   -385       O  
ATOM   1226  CB  LEU A 154      -4.957 -40.513 -23.812  1.00 30.51           C  
ANISOU 1226  CB  LEU A 154     3586   4078   3929     36     90   -408       C  
ATOM   1227  CG  LEU A 154      -5.559 -39.464 -24.744  1.00 38.46           C  
ANISOU 1227  CG  LEU A 154     4627   5188   4798    -64     87   -354       C  
ATOM   1228  CD1 LEU A 154      -5.389 -39.866 -26.209  1.00 36.26           C  
ANISOU 1228  CD1 LEU A 154     4302   5030   4444   -167    158   -458       C  
ATOM   1229  CD2 LEU A 154      -7.028 -39.268 -24.394  1.00 28.08           C  
ANISOU 1229  CD2 LEU A 154     3382   3828   3460    -51     38   -262       C  
ATOM   1230  N   VAL A 155      -6.179 -41.923 -21.087  1.00 26.85           N  
ANISOU 1230  N   VAL A 155     3189   3374   3640    205    -24   -283       N  
ATOM   1231  CA  VAL A 155      -6.345 -43.262 -20.532  1.00 27.86           C  
ANISOU 1231  CA  VAL A 155     3297   3406   3884    254    -46   -293       C  
ATOM   1232  C   VAL A 155      -6.028 -44.284 -21.610  1.00 30.25           C  
ANISOU 1232  C   VAL A 155     3537   3698   4260    244     16   -428       C  
ATOM   1233  O   VAL A 155      -6.674 -44.312 -22.663  1.00 30.54           O  
ANISOU 1233  O   VAL A 155     3589   3794   4219    186     64   -488       O  
ATOM   1234  CB  VAL A 155      -7.761 -43.456 -19.994  1.00 29.47           C  
ANISOU 1234  CB  VAL A 155     3567   3583   4049    254    -80   -219       C  
ATOM   1235  CG1 VAL A 155      -7.976 -44.932 -19.584  1.00 27.32           C  
ANISOU 1235  CG1 VAL A 155     3270   3209   3901    288   -106   -224       C  
ATOM   1236  CG2 VAL A 155      -8.006 -42.521 -18.853  1.00 25.07           C  
ANISOU 1236  CG2 VAL A 155     3054   3039   3433    261   -128   -118       C  
ATOM   1237  N   GLU A 156      -5.038 -45.139 -21.341  1.00 30.22           N  
ANISOU 1237  N   GLU A 156     3453   3616   4415    295     13   -480       N  
ATOM   1238  CA  GLU A 156      -4.644 -46.203 -22.258  1.00 35.57           C  
ANISOU 1238  CA  GLU A 156     4050   4260   5206    296     78   -638       C  
ATOM   1239  C   GLU A 156      -5.474 -47.470 -22.071  1.00 38.46           C  
ANISOU 1239  C   GLU A 156     4421   4510   5682    320     54   -648       C  
ATOM   1240  O   GLU A 156      -5.857 -48.100 -23.058  1.00 34.76           O  
ANISOU 1240  O   GLU A 156     3935   4050   5223    284    118   -776       O  
ATOM   1241  CB  GLU A 156      -3.162 -46.525 -22.068  1.00 36.74           C  
ANISOU 1241  CB  GLU A 156     4087   4359   5513    347     85   -697       C  
ATOM   1242  CG  GLU A 156      -2.646 -47.718 -22.867  1.00 51.19           C  
ANISOU 1242  CG  GLU A 156     5807   6126   7517    364    154   -883       C  
ATOM   1243  CD  GLU A 156      -2.154 -47.335 -24.254  1.00 70.14           C  
ANISOU 1243  CD  GLU A 156     8160   8669   9823    288    274  -1055       C  
ATOM   1244  OE1 GLU A 156      -1.297 -48.058 -24.804  1.00 77.44           O  
ANISOU 1244  OE1 GLU A 156     8964   9564  10897    304    344  -1227       O  
ATOM   1245  OE2 GLU A 156      -2.619 -46.308 -24.794  1.00 80.62           O  
ANISOU 1245  OE2 GLU A 156     9560  10140  10931    204    296  -1017       O  
ATOM   1246  N   ASP A 157      -5.769 -47.852 -20.826  1.00 33.84           N  
ANISOU 1246  N   ASP A 157     3859   3828   5171    367    -38   -513       N  
ATOM   1247  CA  ASP A 157      -6.501 -49.081 -20.534  1.00 30.08           C  
ANISOU 1247  CA  ASP A 157     3383   3233   4815    385    -78   -498       C  
ATOM   1248  C   ASP A 157      -6.881 -49.050 -19.058  1.00 33.11           C  
ANISOU 1248  C   ASP A 157     3810   3573   5196    403   -186   -307       C  
ATOM   1249  O   ASP A 157      -6.397 -48.213 -18.295  1.00 34.42           O  
ANISOU 1249  O   ASP A 157     3989   3790   5298    408   -224   -216       O  
ATOM   1250  CB  ASP A 157      -5.660 -50.325 -20.854  1.00 36.49           C  
ANISOU 1250  CB  ASP A 157     4077   3911   5876    432    -63   -619       C  
ATOM   1251  CG  ASP A 157      -6.506 -51.570 -21.095  1.00 46.47           C  
ANISOU 1251  CG  ASP A 157     5339   5063   7255    427    -69   -667       C  
ATOM   1252  OD1 ASP A 157      -7.741 -51.538 -20.864  1.00 48.15           O  
ANISOU 1252  OD1 ASP A 157     5641   5299   7353    390    -99   -580       O  
ATOM   1253  OD2 ASP A 157      -5.923 -52.590 -21.514  1.00 53.90           O  
ANISOU 1253  OD2 ASP A 157     6179   5885   8415    461    -44   -799       O  
ATOM   1254  N   HIS A 158      -7.763 -49.964 -18.671  1.00 32.77           N  
ANISOU 1254  N   HIS A 158     3788   3448   5214    398   -235   -250       N  
ATOM   1255  CA  HIS A 158      -8.051 -50.267 -17.280  1.00 30.53           C  
ANISOU 1255  CA  HIS A 158     3524   3118   4960    398   -343    -74       C  
ATOM   1256  C   HIS A 158      -7.345 -51.562 -16.893  1.00 34.99           C  
ANISOU 1256  C   HIS A 158     3993   3515   5787    440   -417    -48       C  
ATOM   1257  O   HIS A 158      -7.016 -52.395 -17.744  1.00 34.73           O  
ANISOU 1257  O   HIS A 158     3890   3383   5923    470   -375   -185       O  
ATOM   1258  CB  HIS A 158      -9.561 -50.394 -17.039  1.00 30.76           C  
ANISOU 1258  CB  HIS A 158     3634   3177   4878    351   -358     -6       C  
ATOM   1259  CG  HIS A 158     -10.287 -49.081 -16.978  1.00 27.10           C  
ANISOU 1259  CG  HIS A 158     3251   2858   4188    315   -320     20       C  
ATOM   1260  ND1 HIS A 158     -10.508 -48.297 -18.092  1.00 27.19           N  
ANISOU 1260  ND1 HIS A 158     3287   2953   4091    300   -236    -82       N  
ATOM   1261  CD2 HIS A 158     -10.834 -48.410 -15.935  1.00 25.27           C  
ANISOU 1261  CD2 HIS A 158     3069   2700   3832    286   -358    134       C  
ATOM   1262  CE1 HIS A 158     -11.165 -47.203 -17.740  1.00 28.02           C  
ANISOU 1262  CE1 HIS A 158     3451   3154   4042    275   -231    -24       C  
ATOM   1263  NE2 HIS A 158     -11.383 -47.250 -16.436  1.00 29.03           N  
ANISOU 1263  NE2 HIS A 158     3594   3278   4157    269   -295     91       N  
ATOM   1264  N   GLY A 159      -7.112 -51.727 -15.598  1.00 30.91           N  
ANISOU 1264  N   GLY A 159     3465   2968   5313    434   -530    127       N  
ATOM   1265  CA  GLY A 159      -6.466 -52.929 -15.092  1.00 29.67           C  
ANISOU 1265  CA  GLY A 159     3209   2643   5423    466   -631    200       C  
ATOM   1266  C   GLY A 159      -7.153 -53.438 -13.842  1.00 34.94           C  
ANISOU 1266  C   GLY A 159     3907   3288   6081    409   -758    413       C  
ATOM   1267  O   GLY A 159      -7.577 -52.658 -12.986  1.00 30.79           O  
ANISOU 1267  O   GLY A 159     3452   2899   5348    349   -785    528       O  
ATOM   1268  N   PHE A 160      -7.261 -54.757 -13.746  1.00 39.97           N  
ANISOU 1268  N   PHE A 160     4483   3754   6949    418   -835    460       N  
ATOM   1269  CA  PHE A 160      -7.919 -55.367 -12.605  1.00 39.17           C  
ANISOU 1269  CA  PHE A 160     4401   3628   6852    346   -967    678       C  
ATOM   1270  C   PHE A 160      -7.119 -55.144 -11.325  1.00 42.02           C  
ANISOU 1270  C   PHE A 160     4724   4028   7216    310  -1093    879       C  
ATOM   1271  O   PHE A 160      -5.888 -55.225 -11.312  1.00 37.07           O  
ANISOU 1271  O   PHE A 160     4001   3328   6757    365  -1130    876       O  
ATOM   1272  CB  PHE A 160      -8.110 -56.866 -12.840  1.00 41.89           C  
ANISOU 1272  CB  PHE A 160     4677   3754   7484    363  -1034    689       C  
ATOM   1273  CG  PHE A 160      -8.561 -57.617 -11.614  1.00 44.90           C  
ANISOU 1273  CG  PHE A 160     5053   4089   7917    281  -1199    948       C  
ATOM   1274  CD1 PHE A 160      -7.635 -58.142 -10.719  1.00 49.05           C  
ANISOU 1274  CD1 PHE A 160     5480   4515   8640    275  -1355   1133       C  
ATOM   1275  CD2 PHE A 160      -9.914 -57.784 -11.346  1.00 44.66           C  
ANISOU 1275  CD2 PHE A 160     5110   4126   7734    197  -1206   1019       C  
ATOM   1276  CE1 PHE A 160      -8.047 -58.818  -9.586  1.00 50.28           C  
ANISOU 1276  CE1 PHE A 160     5633   4693   8777    155  -1487   1356       C  
ATOM   1277  CE2 PHE A 160     -10.332 -58.472 -10.209  1.00 43.47           C  
ANISOU 1277  CE2 PHE A 160     4950   3953   7614    100  -1359   1266       C  
ATOM   1278  CZ  PHE A 160      -9.394 -58.982  -9.333  1.00 48.19           C  
ANISOU 1278  CZ  PHE A 160     5455   4484   8370     75  -1501   1437       C  
ATOM   1279  N   GLY A 161      -7.833 -54.903 -10.232  1.00 45.64           N  
ANISOU 1279  N   GLY A 161     5246   4609   7485    207  -1162   1053       N  
ATOM   1280  CA  GLY A 161      -7.226 -54.885  -8.910  1.00 42.68           C  
ANISOU 1280  CA  GLY A 161     4832   4282   7101    136  -1304   1272       C  
ATOM   1281  C   GLY A 161      -8.231 -55.337  -7.875  1.00 47.17           C  
ANISOU 1281  C   GLY A 161     5444   4916   7562      7  -1402   1471       C  
ATOM   1282  O   GLY A 161      -9.440 -55.130  -8.026  1.00 40.33           O  
ANISOU 1282  O   GLY A 161     4664   4138   6523    -33  -1328   1422       O  
ATOM   1283  N   VAL A 162      -7.721 -55.965  -6.809  1.00 49.30           N  
ANISOU 1283  N   VAL A 162     5644   5150   7937    -67  -1577   1707       N  
ATOM   1284  CA  VAL A 162      -8.589 -56.472  -5.747  1.00 49.03           C  
ANISOU 1284  CA  VAL A 162     5639   5210   7780   -225  -1662   1890       C  
ATOM   1285  C   VAL A 162      -9.324 -55.326  -5.063  1.00 46.90           C  
ANISOU 1285  C   VAL A 162     5468   5201   7151   -324  -1614   1918       C  
ATOM   1286  O   VAL A 162     -10.546 -55.370  -4.878  1.00 50.26           O  
ANISOU 1286  O   VAL A 162     5958   5718   7419   -400  -1578   1928       O  
ATOM   1287  CB  VAL A 162      -7.777 -57.292  -4.728  1.00 55.67           C  
ANISOU 1287  CB  VAL A 162     6381   6023   8748   -323  -1798   2061       C  
ATOM   1288  CG1 VAL A 162      -8.710 -57.956  -3.735  1.00 58.86           C  
ANISOU 1288  CG1 VAL A 162     6799   6513   9051   -493  -1882   2235       C  
ATOM   1289  CG2 VAL A 162      -6.907 -58.332  -5.425  1.00 57.18           C  
ANISOU 1289  CG2 VAL A 162     6457   5964   9303   -220  -1828   1998       C  
ATOM   1290  N   PHE A 163      -8.589 -54.282  -4.675  1.00 45.38           N  
ANISOU 1290  N   PHE A 163     5282   5144   6817   -334  -1587   1889       N  
ATOM   1291  CA  PHE A 163      -9.138 -53.191  -3.879  1.00 49.00           C  
ANISOU 1291  CA  PHE A 163     5816   5862   6940   -447  -1526   1880       C  
ATOM   1292  C   PHE A 163      -9.398 -51.926  -4.682  1.00 45.46           C  
ANISOU 1292  C   PHE A 163     5439   5488   6345   -359  -1337   1626       C  
ATOM   1293  O   PHE A 163     -10.221 -51.104  -4.264  1.00 48.03           O  
ANISOU 1293  O   PHE A 163     5830   5994   6426   -431  -1257   1570       O  
ATOM   1294  CB  PHE A 163      -8.189 -52.861  -2.722  1.00 52.34           C  
ANISOU 1294  CB  PHE A 163     6196   6406   7286   -553  -1640   2038       C  
ATOM   1295  CG  PHE A 163      -7.898 -54.033  -1.830  1.00 62.40           C  
ANISOU 1295  CG  PHE A 163     7393   7633   8682   -669  -1776   2231       C  
ATOM   1296  CD1 PHE A 163      -8.755 -54.360  -0.792  1.00 67.78           C  
ANISOU 1296  CD1 PHE A 163     8092   8464   9196   -850  -1814   2352       C  
ATOM   1297  CD2 PHE A 163      -6.769 -54.811  -2.030  1.00 68.71           C  
ANISOU 1297  CD2 PHE A 163     8092   8245   9772   -606  -1853   2273       C  
ATOM   1298  CE1 PHE A 163      -8.491 -55.443   0.032  1.00 68.13           C  
ANISOU 1298  CE1 PHE A 163     8056   8469   9361   -971  -1941   2529       C  
ATOM   1299  CE2 PHE A 163      -6.500 -55.897  -1.208  1.00 70.20           C  
ANISOU 1299  CE2 PHE A 163     8198   8385  10089   -721  -1981   2448       C  
ATOM   1300  CZ  PHE A 163      -7.361 -56.212  -0.178  1.00 70.20           C  
ANISOU 1300  CZ  PHE A 163     8218   8533   9921   -906  -2031   2584       C  
ATOM   1301  N   HIS A 164      -8.706 -51.743  -5.802  1.00 40.84           N  
ANISOU 1301  N   HIS A 164     4833   4775   5911   -214  -1268   1475       N  
ATOM   1302  CA  HIS A 164      -8.911 -50.602  -6.680  1.00 33.24           C  
ANISOU 1302  CA  HIS A 164     3930   3866   4835   -136  -1106   1255       C  
ATOM   1303  C   HIS A 164      -8.711 -51.074  -8.112  1.00 34.71           C  
ANISOU 1303  C   HIS A 164     4091   3877   5221     -3  -1043   1116       C  
ATOM   1304  O   HIS A 164      -7.880 -51.947  -8.375  1.00 39.36           O  
ANISOU 1304  O   HIS A 164     4598   4309   6048     50  -1113   1152       O  
ATOM   1305  CB  HIS A 164      -7.950 -49.449  -6.356  1.00 44.01           C  
ANISOU 1305  CB  HIS A 164     5291   5331   6099   -137  -1083   1213       C  
ATOM   1306  CG  HIS A 164      -8.138 -48.880  -4.984  1.00 60.09           C  
ANISOU 1306  CG  HIS A 164     7352   7562   7917   -280  -1125   1313       C  
ATOM   1307  ND1 HIS A 164      -9.011 -47.845  -4.723  1.00 60.06           N  
ANISOU 1307  ND1 HIS A 164     7418   7714   7687   -331  -1021   1211       N  
ATOM   1308  CD2 HIS A 164      -7.580 -49.211  -3.794  1.00 65.27           C  
ANISOU 1308  CD2 HIS A 164     7965   8288   8548   -396  -1260   1501       C  
ATOM   1309  CE1 HIS A 164      -8.978 -47.559  -3.433  1.00 57.63           C  
ANISOU 1309  CE1 HIS A 164     7110   7573   7213   -473  -1076   1308       C  
ATOM   1310  NE2 HIS A 164      -8.119 -48.373  -2.847  1.00 62.02           N  
ANISOU 1310  NE2 HIS A 164     7601   8090   7873   -523  -1225   1493       N  
ATOM   1311  N   THR A 165      -9.500 -50.520  -9.022  1.00 30.74           N  
ANISOU 1311  N   THR A 165     3649   3403   4628     40   -914    956       N  
ATOM   1312  CA  THR A 165      -9.319 -50.752 -10.448  1.00 29.52           C  
ANISOU 1312  CA  THR A 165     3477   3130   4607    142   -835    797       C  
ATOM   1313  C   THR A 165      -8.339 -49.723 -10.988  1.00 30.64           C  
ANISOU 1313  C   THR A 165     3608   3311   4721    200   -764    681       C  
ATOM   1314  O   THR A 165      -8.533 -48.519 -10.796  1.00 29.13           O  
ANISOU 1314  O   THR A 165     3472   3251   4348    176   -708    643       O  
ATOM   1315  CB  THR A 165     -10.657 -50.662 -11.182  1.00 30.54           C  
ANISOU 1315  CB  THR A 165     3672   3287   4643    140   -745    704       C  
ATOM   1316  OG1 THR A 165     -11.490 -51.747 -10.769  1.00 31.61           O  
ANISOU 1316  OG1 THR A 165     3808   3370   4832     88   -814    810       O  
ATOM   1317  CG2 THR A 165     -10.459 -50.727 -12.724  1.00 26.45           C  
ANISOU 1317  CG2 THR A 165     3141   2690   4217    222   -651    525       C  
ATOM   1318  N   SER A 166      -7.282 -50.194 -11.651  1.00 31.60           N  
ANISOU 1318  N   SER A 166     3652   3316   5037    272   -767    620       N  
ATOM   1319  CA  SER A 166      -6.276 -49.291 -12.202  1.00 32.15           C  
ANISOU 1319  CA  SER A 166     3701   3426   5090    318   -703    514       C  
ATOM   1320  C   SER A 166      -6.780 -48.608 -13.468  1.00 28.75           C  
ANISOU 1320  C   SER A 166     3320   3043   4561    344   -571    345       C  
ATOM   1321  O   SER A 166      -7.483 -49.211 -14.286  1.00 28.93           O  
ANISOU 1321  O   SER A 166     3354   3013   4627    356   -527    270       O  
ATOM   1322  CB  SER A 166      -4.979 -50.048 -12.513  1.00 34.39           C  
ANISOU 1322  CB  SER A 166     3867   3578   5623    383   -742    493       C  
ATOM   1323  OG  SER A 166      -4.401 -50.604 -11.340  1.00 38.60           O  
ANISOU 1323  OG  SER A 166     4339   4065   6260    354   -883    674       O  
ATOM   1324  N   VAL A 167      -6.408 -47.337 -13.628  1.00 25.48           N  
ANISOU 1324  N   VAL A 167     2934   2732   4016    341   -516    294       N  
ATOM   1325  CA  VAL A 167      -6.632 -46.582 -14.857  1.00 30.64           C  
ANISOU 1325  CA  VAL A 167     3619   3436   4589    354   -408    157       C  
ATOM   1326  C   VAL A 167      -5.261 -46.086 -15.335  1.00 29.35           C  
ANISOU 1326  C   VAL A 167     3395   3284   4473    384   -379     88       C  
ATOM   1327  O   VAL A 167      -4.665 -45.189 -14.721  1.00 35.52           O  
ANISOU 1327  O   VAL A 167     4182   4129   5184    368   -401    132       O  
ATOM   1328  CB  VAL A 167      -7.622 -45.426 -14.646  1.00 28.39           C  
ANISOU 1328  CB  VAL A 167     3420   3259   4108    312   -374    170       C  
ATOM   1329  CG1 VAL A 167      -8.010 -44.807 -15.983  1.00 27.60           C  
ANISOU 1329  CG1 VAL A 167     3345   3198   3944    314   -285     59       C  
ATOM   1330  CG2 VAL A 167      -8.868 -45.932 -13.916  1.00 29.65           C  
ANISOU 1330  CG2 VAL A 167     3622   3421   4221    276   -411    251       C  
ATOM   1331  N   TRP A 168      -4.751 -46.680 -16.415  1.00 27.94           N  
ANISOU 1331  N   TRP A 168     3152   3049   4414    418   -326    -31       N  
ATOM   1332  CA  TRP A 168      -3.397 -46.398 -16.896  1.00 31.60           C  
ANISOU 1332  CA  TRP A 168     3537   3523   4947    444   -294   -108       C  
ATOM   1333  C   TRP A 168      -3.385 -45.202 -17.846  1.00 30.71           C  
ANISOU 1333  C   TRP A 168     3462   3529   4677    409   -206   -193       C  
ATOM   1334  O   TRP A 168      -4.091 -45.200 -18.861  1.00 29.82           O  
ANISOU 1334  O   TRP A 168     3379   3450   4501    383   -139   -276       O  
ATOM   1335  CB  TRP A 168      -2.808 -47.616 -17.610  1.00 38.05           C  
ANISOU 1335  CB  TRP A 168     4247   4230   5980    490   -268   -219       C  
ATOM   1336  CG  TRP A 168      -2.830 -48.889 -16.802  1.00 46.61           C  
ANISOU 1336  CG  TRP A 168     5280   5167   7263    525   -365   -130       C  
ATOM   1337  CD1 TRP A 168      -3.658 -49.963 -16.984  1.00 40.28           C  
ANISOU 1337  CD1 TRP A 168     4482   4267   6556    529   -376   -144       C  
ATOM   1338  CD2 TRP A 168      -1.986 -49.215 -15.695  1.00 39.02           C  
ANISOU 1338  CD2 TRP A 168     4250   4140   6435    547   -478      4       C  
ATOM   1339  NE1 TRP A 168      -3.377 -50.939 -16.058  1.00 44.48           N  
ANISOU 1339  NE1 TRP A 168     4951   4665   7283    554   -493    -22       N  
ATOM   1340  CE2 TRP A 168      -2.357 -50.505 -15.253  1.00 41.68           C  
ANISOU 1340  CE2 TRP A 168     4550   4333   6954    563   -561     78       C  
ATOM   1341  CE3 TRP A 168      -0.949 -48.546 -15.036  1.00 43.50           C  
ANISOU 1341  CE3 TRP A 168     4781   4759   6989    546   -525     78       C  
ATOM   1342  CZ2 TRP A 168      -1.729 -51.137 -14.179  1.00 40.68           C  
ANISOU 1342  CZ2 TRP A 168     4346   4112   6997    574   -698    239       C  
ATOM   1343  CZ3 TRP A 168      -0.323 -49.176 -13.973  1.00 47.03           C  
ANISOU 1343  CZ3 TRP A 168     5153   5122   7594    556   -656    228       C  
ATOM   1344  CH2 TRP A 168      -0.716 -50.459 -13.554  1.00 48.70           C  
ANISOU 1344  CH2 TRP A 168     5324   5191   7987    568   -745    315       C  
ATOM   1345  N   LEU A 169      -2.547 -44.213 -17.535  1.00 28.66           N  
ANISOU 1345  N   LEU A 169     3194   3333   4363    399   -215   -165       N  
ATOM   1346  CA  LEU A 169      -2.444 -42.975 -18.301  1.00 30.13           C  
ANISOU 1346  CA  LEU A 169     3412   3625   4409    356   -153   -214       C  
ATOM   1347  C   LEU A 169      -1.143 -42.931 -19.097  1.00 39.71           C  
ANISOU 1347  C   LEU A 169     4532   4869   5686    358   -101   -313       C  
ATOM   1348  O   LEU A 169      -0.067 -43.252 -18.574  1.00 31.91           O  
ANISOU 1348  O   LEU A 169     3465   3841   4820    394   -136   -299       O  
ATOM   1349  CB  LEU A 169      -2.516 -41.756 -17.375  1.00 28.89           C  
ANISOU 1349  CB  LEU A 169     3318   3521   4139    329   -198   -117       C  
ATOM   1350  CG  LEU A 169      -3.917 -41.179 -17.139  1.00 43.45           C  
ANISOU 1350  CG  LEU A 169     5258   5390   5863    301   -201    -72       C  
ATOM   1351  CD1 LEU A 169      -4.813 -42.182 -16.436  1.00 39.45           C  
ANISOU 1351  CD1 LEU A 169     4772   4824   5393    318   -241    -19       C  
ATOM   1352  CD2 LEU A 169      -3.840 -39.875 -16.357  1.00 45.73           C  
ANISOU 1352  CD2 LEU A 169     5589   5727   6061    273   -227    -19       C  
ATOM   1353  N   LYS A 170      -1.248 -42.509 -20.361  1.00 32.88           N  
ANISOU 1353  N   LYS A 170     3669   4088   4735    307    -19   -407       N  
ATOM   1354  CA  LYS A 170      -0.107 -42.351 -21.253  1.00 29.43           C  
ANISOU 1354  CA  LYS A 170     3144   3718   4319    283     48   -515       C  
ATOM   1355  C   LYS A 170      -0.041 -40.907 -21.748  1.00 27.45           C  
ANISOU 1355  C   LYS A 170     2939   3590   3900    205     66   -484       C  
ATOM   1356  O   LYS A 170      -1.075 -40.265 -21.934  1.00 27.62           O  
ANISOU 1356  O   LYS A 170     3048   3644   3801    162     56   -427       O  
ATOM   1357  CB  LYS A 170      -0.233 -43.321 -22.431  1.00 36.82           C  
ANISOU 1357  CB  LYS A 170     4022   4661   5307    267    135   -674       C  
ATOM   1358  CG  LYS A 170       0.752 -43.102 -23.547  1.00 51.87           C  
ANISOU 1358  CG  LYS A 170     5839   6677   7192    212    228   -812       C  
ATOM   1359  CD  LYS A 170       0.580 -44.167 -24.624  1.00 66.36           C  
ANISOU 1359  CD  LYS A 170     7611   8520   9084    189    322   -996       C  
ATOM   1360  CE  LYS A 170       1.541 -45.327 -24.424  1.00 65.72           C  
ANISOU 1360  CE  LYS A 170     7392   8324   9255    273    344  -1113       C  
ATOM   1361  NZ  LYS A 170       2.779 -45.121 -25.220  1.00 67.92           N  
ANISOU 1361  NZ  LYS A 170     7549   8709   9548    233    438  -1260       N  
ATOM   1362  N   VAL A 171       1.173 -40.371 -21.907  1.00 29.88           N  
ANISOU 1362  N   VAL A 171     3182   3956   4214    184     84   -508       N  
ATOM   1363  CA  VAL A 171       1.321 -39.061 -22.543  1.00 31.22           C  
ANISOU 1363  CA  VAL A 171     3382   4243   4238     95    101   -481       C  
ATOM   1364  C   VAL A 171       0.928 -39.181 -24.010  1.00 29.14           C  
ANISOU 1364  C   VAL A 171     3106   4082   3882      8    182   -573       C  
ATOM   1365  O   VAL A 171       1.444 -40.040 -24.735  1.00 29.99           O  
ANISOU 1365  O   VAL A 171     3125   4223   4046      0    259   -715       O  
ATOM   1366  CB  VAL A 171       2.761 -38.539 -22.403  1.00 31.79           C  
ANISOU 1366  CB  VAL A 171     3377   4361   4340     83    103   -488       C  
ATOM   1367  CG1 VAL A 171       2.916 -37.183 -23.135  1.00 27.61           C  
ANISOU 1367  CG1 VAL A 171     2875   3952   3663    -26    115   -450       C  
ATOM   1368  CG2 VAL A 171       3.160 -38.425 -20.928  1.00 31.09           C  
ANISOU 1368  CG2 VAL A 171     3297   4186   4328    151     16   -391       C  
ATOM   1369  N   ARG A 172       0.035 -38.309 -24.460  1.00 27.67           N  
ANISOU 1369  N   ARG A 172     3001   3953   3561    -65    163   -496       N  
ATOM   1370  CA  ARG A 172      -0.481 -38.360 -25.823  1.00 28.91           C  
ANISOU 1370  CA  ARG A 172     3155   4225   3605   -171    220   -552       C  
ATOM   1371  C   ARG A 172       0.369 -37.517 -26.779  1.00 28.96           C  
ANISOU 1371  C   ARG A 172     3112   4387   3506   -293    257   -566       C  
ATOM   1372  O   ARG A 172       1.075 -36.591 -26.374  1.00 28.50           O  
ANISOU 1372  O   ARG A 172     3050   4336   3443   -301    219   -492       O  
ATOM   1373  CB  ARG A 172      -1.921 -37.855 -25.847  1.00 28.03           C  
ANISOU 1373  CB  ARG A 172     3142   4094   3414   -197    165   -440       C  
ATOM   1374  CG  ARG A 172      -1.982 -36.353 -25.617  1.00 27.44           C  
ANISOU 1374  CG  ARG A 172     3114   4031   3280   -238     97   -299       C  
ATOM   1375  CD  ARG A 172      -3.289 -35.944 -25.065  1.00 33.35           C  
ANISOU 1375  CD  ARG A 172     3944   4696   4030   -204     31   -195       C  
ATOM   1376  NE  ARG A 172      -4.369 -36.119 -26.018  1.00 36.56           N  
ANISOU 1376  NE  ARG A 172     4373   5158   4360   -275     37   -180       N  
ATOM   1377  CZ  ARG A 172      -5.647 -36.002 -25.670  1.00 43.39           C  
ANISOU 1377  CZ  ARG A 172     5295   5955   5236   -244     -9   -107       C  
ATOM   1378  NH1 ARG A 172      -5.975 -35.722 -24.389  1.00 34.76           N  
ANISOU 1378  NH1 ARG A 172     4241   4746   4222   -148    -53    -60       N  
ATOM   1379  NH2 ARG A 172      -6.586 -36.164 -26.590  1.00 30.29           N  
ANISOU 1379  NH2 ARG A 172     3647   4356   3506   -318    -10    -87       N  
ATOM   1380  N   GLU A 173       0.273 -37.844 -28.074  1.00 28.88           N  
ANISOU 1380  N   GLU A 173     3062   4513   3397   -405    331   -661       N  
ATOM   1381  CA  GLU A 173       0.995 -37.096 -29.099  1.00 35.41           C  
ANISOU 1381  CA  GLU A 173     3838   5522   4094   -554    369   -671       C  
ATOM   1382  C   GLU A 173       0.252 -35.837 -29.558  1.00 38.75           C  
ANISOU 1382  C   GLU A 173     4334   6011   4377   -670    292   -494       C  
ATOM   1383  O   GLU A 173       0.893 -34.851 -29.952  1.00 39.60           O  
ANISOU 1383  O   GLU A 173     4420   6220   4408   -771    274   -424       O  
ATOM   1384  CB  GLU A 173       1.271 -38.008 -30.305  1.00 44.03           C  
ANISOU 1384  CB  GLU A 173     4842   6758   5129   -648    491   -867       C  
ATOM   1385  CG  GLU A 173       1.897 -37.301 -31.500  1.00 72.60           C  
ANISOU 1385  CG  GLU A 173     8404  10607   8573   -839    540   -882       C  
ATOM   1386  CD  GLU A 173       3.156 -36.524 -31.133  1.00 89.89           C  
ANISOU 1386  CD  GLU A 173    10542  12821  10792   -838    528   -842       C  
ATOM   1387  OE1 GLU A 173       4.015 -37.085 -30.418  1.00 94.68           O  
ANISOU 1387  OE1 GLU A 173    11083  13334  11557   -714    559   -935       O  
ATOM   1388  OE2 GLU A 173       3.278 -35.349 -31.549  1.00 91.09           O  
ANISOU 1388  OE2 GLU A 173    10715  13080  10816   -964    479   -705       O  
ATOM   1389  N   ASP A 174      -1.077 -35.843 -29.520  1.00 36.66           N  
ANISOU 1389  N   ASP A 174     4148   5690   4093   -660    239   -413       N  
ATOM   1390  CA  ASP A 174      -1.887 -34.830 -30.188  1.00 38.41           C  
ANISOU 1390  CA  ASP A 174     4417   5982   4196   -784    167   -255       C  
ATOM   1391  C   ASP A 174      -2.371 -33.775 -29.196  1.00 34.66           C  
ANISOU 1391  C   ASP A 174     4011   5357   3802   -707     57    -88       C  
ATOM   1392  O   ASP A 174      -2.636 -34.075 -28.028  1.00 32.49           O  
ANISOU 1392  O   ASP A 174     3772   4927   3644   -560     38    -97       O  
ATOM   1393  CB  ASP A 174      -3.083 -35.486 -30.883  1.00 36.86           C  
ANISOU 1393  CB  ASP A 174     4246   5829   3931   -837    178   -274       C  
ATOM   1394  CG  ASP A 174      -3.987 -36.213 -29.904  1.00 51.60           C  
ANISOU 1394  CG  ASP A 174     6168   7519   5919   -679    158   -287       C  
ATOM   1395  OD1 ASP A 174      -3.455 -36.843 -28.963  1.00 48.29           O  
ANISOU 1395  OD1 ASP A 174     5736   6988   5625   -545    185   -369       O  
ATOM   1396  OD2 ASP A 174      -5.227 -36.145 -30.058  1.00 67.58           O  
ANISOU 1396  OD2 ASP A 174     8241   9520   7915   -697    107   -203       O  
ATOM   1397  N   TYR A 175      -2.458 -32.529 -29.661  1.00 32.19           N  
ANISOU 1397  N   TYR A 175     3707   5093   3430   -816    -16     63       N  
ATOM   1398  CA  TYR A 175      -2.997 -31.438 -28.852  1.00 33.99           C  
ANISOU 1398  CA  TYR A 175     3989   5174   3751   -758   -120    210       C  
ATOM   1399  C   TYR A 175      -4.522 -31.499 -28.871  1.00 33.21           C  
ANISOU 1399  C   TYR A 175     3938   5007   3674   -735   -172    284       C  
ATOM   1400  O   TYR A 175      -5.131 -31.619 -29.939  1.00 28.17           O  
ANISOU 1400  O   TYR A 175     3290   4478   2936   -853   -182    328       O  
ATOM   1401  CB  TYR A 175      -2.507 -30.092 -29.400  1.00 36.58           C  
ANISOU 1401  CB  TYR A 175     4297   5563   4038   -889   -189    350       C  
ATOM   1402  CG  TYR A 175      -2.997 -28.850 -28.664  1.00 27.63           C  
ANISOU 1402  CG  TYR A 175     3204   4268   3028   -843   -298    492       C  
ATOM   1403  CD1 TYR A 175      -4.323 -28.412 -28.789  1.00 28.88           C  
ANISOU 1403  CD1 TYR A 175     3391   4349   3234   -846   -377    610       C  
ATOM   1404  CD2 TYR A 175      -2.130 -28.093 -27.891  1.00 29.26           C  
ANISOU 1404  CD2 TYR A 175     3408   4399   3311   -803   -320    502       C  
ATOM   1405  CE1 TYR A 175      -4.770 -27.279 -28.146  1.00 26.80           C  
ANISOU 1405  CE1 TYR A 175     3146   3926   3111   -801   -469    717       C  
ATOM   1406  CE2 TYR A 175      -2.564 -26.942 -27.233  1.00 32.11           C  
ANISOU 1406  CE2 TYR A 175     3798   4606   3798   -767   -412    607       C  
ATOM   1407  CZ  TYR A 175      -3.891 -26.542 -27.369  1.00 30.89           C  
ANISOU 1407  CZ  TYR A 175     3664   4365   3708   -763   -483    707       C  
ATOM   1408  OH  TYR A 175      -4.331 -25.397 -26.738  1.00 32.46           O  
ANISOU 1408  OH  TYR A 175     3874   4397   4061   -723   -567    790       O  
ATOM   1409  N   SER A 176      -5.142 -31.390 -27.696  1.00 29.71           N  
ANISOU 1409  N   SER A 176     3540   4396   3354   -597   -205    299       N  
ATOM   1410  CA  SER A 176      -6.596 -31.455 -27.596  1.00 27.51           C  
ANISOU 1410  CA  SER A 176     3295   4044   3112   -563   -248    358       C  
ATOM   1411  C   SER A 176      -7.086 -30.636 -26.407  1.00 24.22           C  
ANISOU 1411  C   SER A 176     2910   3459   2835   -457   -306    412       C  
ATOM   1412  O   SER A 176      -6.401 -30.526 -25.387  1.00 23.91           O  
ANISOU 1412  O   SER A 176     2878   3350   2855   -376   -288    354       O  
ATOM   1413  CB  SER A 176      -7.084 -32.906 -27.442  1.00 26.28           C  
ANISOU 1413  CB  SER A 176     3153   3890   2941   -496   -180    239       C  
ATOM   1414  OG  SER A 176      -8.495 -32.951 -27.407  1.00 29.83           O  
ANISOU 1414  OG  SER A 176     3630   4285   3419   -475   -222    302       O  
ATOM   1415  N   LEU A 177      -8.286 -30.070 -26.550  1.00 23.89           N  
ANISOU 1415  N   LEU A 177     2874   3355   2848   -466   -375    516       N  
ATOM   1416  CA  LEU A 177      -9.013 -29.453 -25.436  1.00 26.67           C  
ANISOU 1416  CA  LEU A 177     3243   3547   3344   -360   -412    533       C  
ATOM   1417  C   LEU A 177     -10.081 -30.369 -24.858  1.00 25.51           C  
ANISOU 1417  C   LEU A 177     3119   3356   3216   -270   -377    472       C  
ATOM   1418  O   LEU A 177     -10.751 -29.995 -23.887  1.00 25.29           O  
ANISOU 1418  O   LEU A 177     3099   3215   3295   -186   -390    460       O  
ATOM   1419  CB  LEU A 177      -9.680 -28.155 -25.895  1.00 21.52           C  
ANISOU 1419  CB  LEU A 177     2562   2828   2785   -418   -515    687       C  
ATOM   1420  CG  LEU A 177      -8.749 -27.147 -26.557  1.00 21.92           C  
ANISOU 1420  CG  LEU A 177     2587   2918   2825   -530   -571    784       C  
ATOM   1421  CD1 LEU A 177      -9.546 -25.920 -27.060  1.00 32.04           C  
ANISOU 1421  CD1 LEU A 177     3829   4114   4229   -592   -695    963       C  
ATOM   1422  CD2 LEU A 177      -7.630 -26.740 -25.612  1.00 22.23           C  
ANISOU 1422  CD2 LEU A 177     2637   2902   2909   -475   -542    706       C  
ATOM   1423  N   GLU A 178     -10.256 -31.549 -25.440  1.00 23.62           N  
ANISOU 1423  N   GLU A 178     2886   3209   2880   -295   -331    423       N  
ATOM   1424  CA  GLU A 178     -11.396 -32.407 -25.143  1.00 26.28           C  
ANISOU 1424  CA  GLU A 178     3241   3518   3228   -239   -312    392       C  
ATOM   1425  C   GLU A 178     -11.197 -33.175 -23.845  1.00 19.68           C  
ANISOU 1425  C   GLU A 178     2431   2621   2425   -126   -258    284       C  
ATOM   1426  O   GLU A 178     -10.079 -33.596 -23.528  1.00 25.24           O  
ANISOU 1426  O   GLU A 178     3137   3347   3108   -108   -218    213       O  
ATOM   1427  CB  GLU A 178     -11.577 -33.385 -26.299  1.00 26.58           C  
ANISOU 1427  CB  GLU A 178     3273   3678   3149   -324   -283    372       C  
ATOM   1428  CG  GLU A 178     -12.584 -34.467 -26.121  1.00 32.03           C  
ANISOU 1428  CG  GLU A 178     3981   4354   3835   -282   -257    326       C  
ATOM   1429  CD  GLU A 178     -12.533 -35.432 -27.296  1.00 42.05           C  
ANISOU 1429  CD  GLU A 178     5240   5750   4985   -380   -218    276       C  
ATOM   1430  OE1 GLU A 178     -11.702 -36.366 -27.261  1.00 39.45           O  
ANISOU 1430  OE1 GLU A 178     4909   5451   4629   -363   -147    152       O  
ATOM   1431  OE2 GLU A 178     -13.281 -35.213 -28.273  1.00 34.97           O  
ANISOU 1431  OE2 GLU A 178     4330   4927   4030   -481   -261    359       O  
ATOM   1432  N   CYS A 179     -12.291 -33.381 -23.099  1.00 23.91           N  
ANISOU 1432  N   CYS A 179     2979   3089   3015    -60   -261    280       N  
ATOM   1433  CA  CYS A 179     -12.241 -34.275 -21.942  1.00 26.00           C  
ANISOU 1433  CA  CYS A 179     3268   3321   3290     20   -217    197       C  
ATOM   1434  C   CYS A 179     -12.053 -35.710 -22.416  1.00 24.98           C  
ANISOU 1434  C   CYS A 179     3145   3247   3099      8   -176    141       C  
ATOM   1435  O   CYS A 179     -12.618 -36.118 -23.432  1.00 28.39           O  
ANISOU 1435  O   CYS A 179     3570   3731   3484    -49   -176    157       O  
ATOM   1436  CB  CYS A 179     -13.523 -34.183 -21.107  1.00 24.10           C  
ANISOU 1436  CB  CYS A 179     3030   3019   3107     73   -224    204       C  
ATOM   1437  SG  CYS A 179     -13.925 -32.522 -20.510  1.00 27.02           S  
ANISOU 1437  SG  CYS A 179     3374   3300   3592     97   -262    234       S  
ATOM   1438  N   ASP A 180     -11.260 -36.477 -21.676  1.00 22.28           N  
ANISOU 1438  N   ASP A 180     2808   2890   2767     55   -147     76       N  
ATOM   1439  CA  ASP A 180     -10.961 -37.866 -22.040  1.00 24.87           C  
ANISOU 1439  CA  ASP A 180     3128   3241   3080     54   -110      9       C  
ATOM   1440  C   ASP A 180     -12.225 -38.722 -22.100  1.00 24.79           C  
ANISOU 1440  C   ASP A 180     3135   3217   3068     59   -108     12       C  
ATOM   1441  O   ASP A 180     -12.845 -38.983 -21.063  1.00 26.87           O  
ANISOU 1441  O   ASP A 180     3415   3430   3363    108   -120     29       O  
ATOM   1442  CB  ASP A 180      -9.969 -38.459 -21.035  1.00 26.29           C  
ANISOU 1442  CB  ASP A 180     3299   3381   3310    113   -101    -34       C  
ATOM   1443  CG  ASP A 180      -9.325 -39.751 -21.525  1.00 30.15           C  
ANISOU 1443  CG  ASP A 180     3755   3874   3827    114    -65   -113       C  
ATOM   1444  OD1 ASP A 180      -9.912 -40.466 -22.372  1.00 30.97           O  
ANISOU 1444  OD1 ASP A 180     3857   4000   3912     81    -41   -151       O  
ATOM   1445  OD2 ASP A 180      -8.209 -40.042 -21.064  1.00 31.03           O  
ANISOU 1445  OD2 ASP A 180     3835   3964   3990    146    -62   -144       O  
ATOM   1446  N   PRO A 181     -12.610 -39.220 -23.283  1.00 25.06           N  
ANISOU 1446  N   PRO A 181     2645   3519   3357    -32    -30   -164       N  
ATOM   1447  CA  PRO A 181     -13.851 -40.007 -23.391  1.00 25.67           C  
ANISOU 1447  CA  PRO A 181     2856   3532   3366    -14    -65    -51       C  
ATOM   1448  C   PRO A 181     -13.745 -41.412 -22.828  1.00 22.44           C  
ANISOU 1448  C   PRO A 181     2490   3109   2928    101   -142    -48       C  
ATOM   1449  O   PRO A 181     -14.775 -42.090 -22.699  1.00 25.44           O  
ANISOU 1449  O   PRO A 181     2981   3432   3254    107   -167     35       O  
ATOM   1450  CB  PRO A 181     -14.103 -40.048 -24.905  1.00 27.48           C  
ANISOU 1450  CB  PRO A 181     3143   3722   3577    -84     19    -28       C  
ATOM   1451  CG  PRO A 181     -12.728 -39.974 -25.506  1.00 27.89           C  
ANISOU 1451  CG  PRO A 181     3099   3815   3682    -92     89   -137       C  
ATOM   1452  CD  PRO A 181     -11.927 -39.068 -24.579  1.00 26.18           C  
ANISOU 1452  CD  PRO A 181     2756   3663   3528    -96     79   -221       C  
ATOM   1453  N   ALA A 182     -12.543 -41.876 -22.491  1.00 23.06           N  
ANISOU 1453  N   ALA A 182     2488   3235   3040    193   -180   -145       N  
ATOM   1454  CA  ALA A 182     -12.392 -43.224 -21.963  1.00 22.90           C  
ANISOU 1454  CA  ALA A 182     2537   3187   2978    324   -260   -143       C  
ATOM   1455  C   ALA A 182     -13.140 -43.414 -20.656  1.00 27.82           C  
ANISOU 1455  C   ALA A 182     3257   3772   3539    373   -336    -75       C  
ATOM   1456  O   ALA A 182     -13.446 -44.556 -20.293  1.00 30.50           O  
ANISOU 1456  O   ALA A 182     3722   4050   3817    451   -378    -33       O  
ATOM   1457  CB  ALA A 182     -10.908 -43.550 -21.745  1.00 25.10           C  
ANISOU 1457  CB  ALA A 182     2696   3535   3307    438   -307   -280       C  
ATOM   1458  N   VAL A 183     -13.416 -42.328 -19.931  1.00 27.90           N  
ANISOU 1458  N   VAL A 183     3227   3812   3561    327   -345    -65       N  
ATOM   1459  CA  VAL A 183     -14.063 -42.402 -18.627  1.00 23.60           C  
ANISOU 1459  CA  VAL A 183     2774   3237   2957    371   -405    -10       C  
ATOM   1460  C   VAL A 183     -15.406 -41.673 -18.621  1.00 24.16           C  
ANISOU 1460  C   VAL A 183     2891   3277   3014    253   -351     80       C  
ATOM   1461  O   VAL A 183     -15.951 -41.382 -17.556  1.00 28.68           O  
ANISOU 1461  O   VAL A 183     3511   3836   3550    261   -379    115       O  
ATOM   1462  CB  VAL A 183     -13.130 -41.874 -17.518  1.00 30.02           C  
ANISOU 1462  CB  VAL A 183     3504   4116   3786    457   -489    -97       C  
ATOM   1463  CG1 VAL A 183     -11.919 -42.792 -17.386  1.00 30.64           C  
ANISOU 1463  CG1 VAL A 183     3552   4222   3867    609   -568   -194       C  
ATOM   1464  CG2 VAL A 183     -12.691 -40.436 -17.814  1.00 26.75           C  
ANISOU 1464  CG2 VAL A 183     2935   3774   3455    360   -442   -162       C  
ATOM   1465  N   ILE A 184     -15.969 -41.402 -19.807  1.00 21.98           N  
ANISOU 1465  N   ILE A 184     2606   2986   2759    152   -278    113       N  
ATOM   1466  CA  ILE A 184     -17.275 -40.763 -19.932  1.00 21.56           C  
ANISOU 1466  CA  ILE A 184     2589   2907   2695     58   -240    184       C  
ATOM   1467  C   ILE A 184     -18.327 -41.836 -20.165  1.00 26.48           C  
ANISOU 1467  C   ILE A 184     3321   3464   3274     42   -227    246       C  
ATOM   1468  O   ILE A 184     -18.132 -42.749 -20.983  1.00 25.52           O  
ANISOU 1468  O   ILE A 184     3235   3316   3146     55   -214    240       O  
ATOM   1469  CB  ILE A 184     -17.297 -39.738 -21.083  1.00 21.84           C  
ANISOU 1469  CB  ILE A 184     2568   2963   2769    -29   -180    174       C  
ATOM   1470  CG1 ILE A 184     -16.341 -38.583 -20.781  1.00 25.76           C  
ANISOU 1470  CG1 ILE A 184     2963   3513   3311    -41   -172    107       C  
ATOM   1471  CG2 ILE A 184     -18.736 -39.234 -21.310  1.00 22.31           C  
ANISOU 1471  CG2 ILE A 184     2674   2993   2810    -99   -162    240       C  
ATOM   1472  CD1 ILE A 184     -16.298 -37.496 -21.852  1.00 24.40           C  
ANISOU 1472  CD1 ILE A 184     2769   3340   3163   -132    -96     98       C  
ATOM   1473  N   GLY A 185     -19.453 -41.714 -19.454  1.00 21.69           N  
ANISOU 1473  N   GLY A 185     2766   2832   2643      7   -221    294       N  
ATOM   1474  CA  GLY A 185     -20.648 -42.515 -19.700  1.00 22.24           C  
ANISOU 1474  CA  GLY A 185     2916   2845   2688    -43   -190    337       C  
ATOM   1475  C   GLY A 185     -21.884 -41.631 -19.762  1.00 29.30           C  
ANISOU 1475  C   GLY A 185     3776   3755   3603   -124   -165    357       C  
ATOM   1476  O   GLY A 185     -22.120 -40.818 -18.858  1.00 21.89           O  
ANISOU 1476  O   GLY A 185     2813   2837   2665   -126   -171    363       O  
ATOM   1477  N   THR A 186     -22.667 -41.749 -20.835  1.00 23.73           N  
ANISOU 1477  N   THR A 186     3063   3041   2912   -182   -147    360       N  
ATOM   1478  CA  THR A 186     -23.888 -40.966 -20.997  1.00 22.40           C  
ANISOU 1478  CA  THR A 186     2854   2892   2765   -240   -141    362       C  
ATOM   1479  C   THR A 186     -25.001 -41.919 -21.389  1.00 24.37           C  
ANISOU 1479  C   THR A 186     3136   3109   3015   -294   -120    355       C  
ATOM   1480  O   THR A 186     -24.809 -42.753 -22.278  1.00 21.74           O  
ANISOU 1480  O   THR A 186     2838   2749   2673   -298   -119    346       O  
ATOM   1481  CB  THR A 186     -23.728 -39.876 -22.068  1.00 24.13           C  
ANISOU 1481  CB  THR A 186     3025   3143   3000   -246   -156    352       C  
ATOM   1482  OG1 THR A 186     -22.799 -38.885 -21.618  1.00 23.54           O  
ANISOU 1482  OG1 THR A 186     2915   3095   2933   -219   -159    347       O  
ATOM   1483  CG2 THR A 186     -25.078 -39.207 -22.397  1.00 22.46           C  
ANISOU 1483  CG2 THR A 186     2784   2947   2802   -280   -170    345       C  
ATOM   1484  N   ALA A 187     -26.167 -41.788 -20.754  1.00 19.76           N  
ANISOU 1484  N   ALA A 187     2534   2528   2447   -342    -96    346       N  
ATOM   1485  CA  ALA A 187     -27.287 -42.656 -21.097  1.00 19.13           C  
ANISOU 1485  CA  ALA A 187     2463   2423   2382   -411    -66    316       C  
ATOM   1486  C   ALA A 187     -28.611 -41.926 -20.914  1.00 26.15           C  
ANISOU 1486  C   ALA A 187     3265   3356   3315   -457    -63    276       C  
ATOM   1487  O   ALA A 187     -28.756 -41.056 -20.049  1.00 23.29           O  
ANISOU 1487  O   ALA A 187     2871   3020   2958   -443    -56    284       O  
ATOM   1488  CB  ALA A 187     -27.296 -43.937 -20.254  1.00 20.28           C  
ANISOU 1488  CB  ALA A 187     2714   2495   2495   -437     -3    328       C  
ATOM   1489  N   VAL A 188     -29.580 -42.299 -21.741  1.00 22.35           N  
ANISOU 1489  N   VAL A 188     2741   2886   2866   -507    -72    221       N  
ATOM   1490  CA  VAL A 188     -30.958 -41.866 -21.571  1.00 19.32           C  
ANISOU 1490  CA  VAL A 188     2259   2548   2535   -553    -67    154       C  
ATOM   1491  C   VAL A 188     -31.849 -43.092 -21.667  1.00 23.20           C  
ANISOU 1491  C   VAL A 188     2748   3010   3056   -651     -8     91       C  
ATOM   1492  O   VAL A 188     -31.615 -43.993 -22.483  1.00 23.33           O  
ANISOU 1492  O   VAL A 188     2814   2991   3059   -668    -17     83       O  
ATOM   1493  CB  VAL A 188     -31.366 -40.781 -22.599  1.00 20.29           C  
ANISOU 1493  CB  VAL A 188     2302   2732   2676   -499   -162    120       C  
ATOM   1494  CG1 VAL A 188     -31.011 -41.200 -24.045  1.00 21.52           C  
ANISOU 1494  CG1 VAL A 188     2497   2875   2806   -476   -220    114       C  
ATOM   1495  CG2 VAL A 188     -32.857 -40.455 -22.484  1.00 23.00           C  
ANISOU 1495  CG2 VAL A 188     2526   3131   3082   -532   -172     26       C  
ATOM   1496  N   LYS A 189     -32.866 -43.134 -20.822  1.00 21.84           N  
ANISOU 1496  N   LYS A 189     2524   2849   2927   -723     63     37       N  
ATOM   1497  CA  LYS A 189     -33.789 -44.252 -20.829  1.00 23.68           C  
ANISOU 1497  CA  LYS A 189     2747   3052   3199   -841    143    -41       C  
ATOM   1498  C   LYS A 189     -35.146 -43.693 -20.439  1.00 29.46           C  
ANISOU 1498  C   LYS A 189     3329   3854   4010   -897    172   -144       C  
ATOM   1499  O   LYS A 189     -35.290 -43.150 -19.338  1.00 23.94           O  
ANISOU 1499  O   LYS A 189     2625   3161   3310   -899    231   -128       O  
ATOM   1500  CB  LYS A 189     -33.295 -45.315 -19.847  1.00 27.76           C  
ANISOU 1500  CB  LYS A 189     3426   3463   3660   -893    260     15       C  
ATOM   1501  CG  LYS A 189     -34.090 -46.582 -19.727  1.00 37.01           C  
ANISOU 1501  CG  LYS A 189     4639   4569   4855  -1031    376    -53       C  
ATOM   1502  CD  LYS A 189     -33.388 -47.474 -18.709  1.00 42.83           C  
ANISOU 1502  CD  LYS A 189     5588   5182   5505  -1043    477     29       C  
ATOM   1503  CE  LYS A 189     -34.133 -48.750 -18.453  1.00 45.48           C  
ANISOU 1503  CE  LYS A 189     6011   5424   5848  -1192    621    -30       C  
ATOM   1504  NZ  LYS A 189     -33.459 -49.520 -17.368  1.00 50.53           N  
ANISOU 1504  NZ  LYS A 189     6892   5928   6379  -1182    717     57       N  
ATOM   1505  N   GLY A 190     -36.121 -43.787 -21.340  1.00 24.80           N  
ANISOU 1505  N   GLY A 190     2612   3322   3489   -931    123   -261       N  
ATOM   1506  CA  GLY A 190     -37.436 -43.248 -21.018  1.00 26.06           C  
ANISOU 1506  CA  GLY A 190     2601   3562   3737   -972    141   -384       C  
ATOM   1507  C   GLY A 190     -37.388 -41.744 -20.777  1.00 32.66           C  
ANISOU 1507  C   GLY A 190     3375   4465   4570   -854     60   -358       C  
ATOM   1508  O   GLY A 190     -37.036 -40.959 -21.672  1.00 28.06           O  
ANISOU 1508  O   GLY A 190     2784   3918   3961   -737    -76   -332       O  
ATOM   1509  N   ARG A 191     -37.738 -41.328 -19.551  1.00 25.12           N  
ANISOU 1509  N   ARG A 191     2394   3517   3632   -885    153   -363       N  
ATOM   1510  CA  ARG A 191     -37.863 -39.923 -19.169  1.00 21.87           C  
ANISOU 1510  CA  ARG A 191     1917   3165   3226   -787     96   -355       C  
ATOM   1511  C   ARG A 191     -36.690 -39.393 -18.348  1.00 26.77           C  
ANISOU 1511  C   ARG A 191     2675   3733   3763   -727    114   -214       C  
ATOM   1512  O   ARG A 191     -36.755 -38.252 -17.870  1.00 26.24           O  
ANISOU 1512  O   ARG A 191     2571   3702   3696   -659     87   -205       O  
ATOM   1513  CB  ARG A 191     -39.149 -39.696 -18.368  1.00 27.21           C  
ANISOU 1513  CB  ARG A 191     2450   3899   3989   -855    184   -481       C  
ATOM   1514  CG  ARG A 191     -40.421 -40.042 -19.091  1.00 50.32           C  
ANISOU 1514  CG  ARG A 191     5195   6903   7021   -907    158   -657       C  
ATOM   1515  CD  ARG A 191     -41.633 -39.824 -18.194  1.00 58.73           C  
ANISOU 1515  CD  ARG A 191     6107   8029   8181   -984    268   -793       C  
ATOM   1516  NE  ARG A 191     -42.378 -38.618 -18.556  1.00 74.90           N  
ANISOU 1516  NE  ARG A 191     7984  10187  10287   -860    139   -892       N  
ATOM   1517  CZ  ARG A 191     -42.307 -37.464 -17.896  1.00 76.70           C  
ANISOU 1517  CZ  ARG A 191     8209  10437  10496   -768    123   -854       C  
ATOM   1518  NH1 ARG A 191     -43.021 -36.418 -18.297  1.00 64.89           N  
ANISOU 1518  NH1 ARG A 191     6570   9034   9050   -644     -2   -952       N  
ATOM   1519  NH2 ARG A 191     -41.526 -37.359 -16.827  1.00 84.67           N  
ANISOU 1519  NH2 ARG A 191     9366  11371  11432   -791    226   -723       N  
ATOM   1520  N   GLU A 192     -35.617 -40.166 -18.169  1.00 25.21           N  
ANISOU 1520  N   GLU A 192     2630   3454   3495   -743    152   -115       N  
ATOM   1521  CA  GLU A 192     -34.461 -39.654 -17.444  1.00 26.10           C  
ANISOU 1521  CA  GLU A 192     2854   3529   3533   -676    148     -3       C  
ATOM   1522  C   GLU A 192     -33.167 -39.956 -18.191  1.00 23.73           C  
ANISOU 1522  C   GLU A 192     2651   3189   3175   -618     80     80       C  
ATOM   1523  O   GLU A 192     -33.056 -40.958 -18.891  1.00 22.70           O  
ANISOU 1523  O   GLU A 192     2557   3026   3041   -653     82     72       O  
ATOM   1524  CB  GLU A 192     -34.393 -40.237 -16.030  1.00 28.09           C  
ANISOU 1524  CB  GLU A 192     3207   3718   3746   -740    280     27       C  
ATOM   1525  CG  GLU A 192     -35.556 -39.783 -15.158  1.00 49.17           C  
ANISOU 1525  CG  GLU A 192     5790   6427   6468   -795    366    -51       C  
ATOM   1526  CD  GLU A 192     -35.211 -39.789 -13.681  1.00 75.84           C  
ANISOU 1526  CD  GLU A 192     9291   9746   9776   -807    466      6       C  
ATOM   1527  OE1 GLU A 192     -34.781 -40.848 -13.170  1.00 84.39           O  
ANISOU 1527  OE1 GLU A 192    10531  10738  10794   -853    547     52       O  
ATOM   1528  OE2 GLU A 192     -35.364 -38.729 -13.035  1.00 78.36           O  
ANISOU 1528  OE2 GLU A 192     9568  10105  10099   -762    459      2       O  
ATOM   1529  N   ALA A 193     -32.176 -39.089 -17.996  1.00 23.71           N  
ANISOU 1529  N   ALA A 193     2689   3189   3131   -534     29    149       N  
ATOM   1530  CA  ALA A 193     -30.871 -39.234 -18.621  1.00 22.29           C  
ANISOU 1530  CA  ALA A 193     2583   2981   2905   -480    -23    212       C  
ATOM   1531  C   ALA A 193     -29.786 -38.769 -17.663  1.00 26.55           C  
ANISOU 1531  C   ALA A 193     3187   3502   3397   -430    -19    274       C  
ATOM   1532  O   ALA A 193     -30.041 -38.016 -16.712  1.00 22.05           O  
ANISOU 1532  O   ALA A 193     2600   2951   2829   -421      1    273       O  
ATOM   1533  CB  ALA A 193     -30.760 -38.433 -19.937  1.00 19.70           C  
ANISOU 1533  CB  ALA A 193     2210   2689   2586   -425   -117    203       C  
ATOM   1534  N   ALA A 194     -28.560 -39.204 -17.949  1.00 21.15           N  
ANISOU 1534  N   ALA A 194     2570   2789   2676   -392    -43    316       N  
ATOM   1535  CA  ALA A 194     -27.384 -38.754 -17.207  1.00 23.80           C  
ANISOU 1535  CA  ALA A 194     2947   3121   2976   -333    -60    354       C  
ATOM   1536  C   ALA A 194     -26.206 -38.629 -18.160  1.00 24.92           C  
ANISOU 1536  C   ALA A 194     3086   3269   3113   -289   -110    365       C  
ATOM   1537  O   ALA A 194     -25.983 -39.522 -18.985  1.00 23.91           O  
ANISOU 1537  O   ALA A 194     2986   3119   2980   -296   -112    364       O  
ATOM   1538  CB  ALA A 194     -27.045 -39.724 -16.063  1.00 23.12           C  
ANISOU 1538  CB  ALA A 194     2966   2981   2836   -326    -17    377       C  
ATOM   1539  N   HIS A 195     -25.483 -37.503 -18.063  1.00 22.72           N  
ANISOU 1539  N   HIS A 195     2776   3018   2837   -254   -139    367       N  
ATOM   1540  CA  HIS A 195     -24.167 -37.314 -18.674  1.00 20.52           C  
ANISOU 1540  CA  HIS A 195     2493   2746   2557   -222   -162    364       C  
ATOM   1541  C   HIS A 195     -23.154 -37.393 -17.537  1.00 25.00           C  
ANISOU 1541  C   HIS A 195     3077   3317   3105   -175   -175    360       C  
ATOM   1542  O   HIS A 195     -23.268 -36.635 -16.567  1.00 25.86           O  
ANISOU 1542  O   HIS A 195     3176   3442   3210   -166   -179    358       O  
ATOM   1543  CB  HIS A 195     -24.060 -35.947 -19.373  1.00 19.38           C  
ANISOU 1543  CB  HIS A 195     2310   2621   2430   -228   -172    355       C  
ATOM   1544  CG  HIS A 195     -24.874 -35.811 -20.632  1.00 24.72           C  
ANISOU 1544  CG  HIS A 195     2992   3292   3110   -246   -182    353       C  
ATOM   1545  ND1 HIS A 195     -26.245 -35.652 -20.631  1.00 23.34           N  
ANISOU 1545  ND1 HIS A 195     2796   3126   2947   -257   -195    343       N  
ATOM   1546  CD2 HIS A 195     -24.494 -35.777 -21.936  1.00 20.96           C  
ANISOU 1546  CD2 HIS A 195     2541   2801   2622   -248   -184    351       C  
ATOM   1547  CE1 HIS A 195     -26.675 -35.534 -21.880  1.00 23.24           C  
ANISOU 1547  CE1 HIS A 195     2795   3108   2926   -253   -223    332       C  
ATOM   1548  NE2 HIS A 195     -25.633 -35.611 -22.691  1.00 19.49           N  
ANISOU 1548  NE2 HIS A 195     2362   2613   2430   -249   -213    343       N  
ATOM   1549  N   SER A 196     -22.184 -38.311 -17.623  1.00 18.87           N  
ANISOU 1549  N   SER A 196     2328   2529   2313   -134   -189    351       N  
ATOM   1550  CA  SER A 196     -21.348 -38.577 -16.458  1.00 20.52           C  
ANISOU 1550  CA  SER A 196     2567   2740   2492    -65   -222    337       C  
ATOM   1551  C   SER A 196     -19.901 -38.868 -16.837  1.00 23.47           C  
ANISOU 1551  C   SER A 196     2905   3135   2878     -7   -257    292       C  
ATOM   1552  O   SER A 196     -19.610 -39.366 -17.925  1.00 26.06           O  
ANISOU 1552  O   SER A 196     3222   3457   3223    -17   -242    284       O  
ATOM   1553  CB  SER A 196     -21.888 -39.766 -15.647  1.00 19.71           C  
ANISOU 1553  CB  SER A 196     2580   2580   2331    -45   -207    368       C  
ATOM   1554  OG  SER A 196     -21.594 -41.000 -16.294  1.00 25.54           O  
ANISOU 1554  OG  SER A 196     3371   3279   3054    -26   -205    371       O  
ATOM   1555  N   ASP A 197     -19.000 -38.569 -15.907  1.00 22.97           N  
ANISOU 1555  N   ASP A 197     2819   3101   2807     58   -305    250       N  
ATOM   1556  CA  ASP A 197     -17.659 -39.155 -15.891  1.00 22.84           C  
ANISOU 1556  CA  ASP A 197     2776   3108   2794    145   -357    189       C  
ATOM   1557  C   ASP A 197     -17.274 -39.366 -14.429  1.00 26.48           C  
ANISOU 1557  C   ASP A 197     3293   3569   3200    244   -429    170       C  
ATOM   1558  O   ASP A 197     -18.138 -39.458 -13.551  1.00 26.80           O  
ANISOU 1558  O   ASP A 197     3433   3567   3184    241   -420    222       O  
ATOM   1559  CB  ASP A 197     -16.649 -38.306 -16.677  1.00 24.20           C  
ANISOU 1559  CB  ASP A 197     2815   3341   3040    115   -344    115       C  
ATOM   1560  CG  ASP A 197     -16.474 -36.898 -16.125  1.00 31.72           C  
ANISOU 1560  CG  ASP A 197     3696   4334   4024     77   -345     79       C  
ATOM   1561  OD1 ASP A 197     -16.906 -36.576 -15.001  1.00 24.35           O  
ANISOU 1561  OD1 ASP A 197     2803   3396   3055     99   -377     98       O  
ATOM   1562  OD2 ASP A 197     -15.863 -36.099 -16.841  1.00 43.81           O  
ANISOU 1562  OD2 ASP A 197     5139   5896   5612     20   -305     27       O  
ATOM   1563  N   LEU A 198     -15.967 -39.452 -14.136  1.00 22.57           N  
ANISOU 1563  N   LEU A 198     2737   3121   2718    339   -504     83       N  
ATOM   1564  CA  LEU A 198     -15.572 -39.708 -12.752  1.00 23.57           C  
ANISOU 1564  CA  LEU A 198     2935   3245   2777    458   -595     58       C  
ATOM   1565  C   LEU A 198     -15.708 -38.488 -11.846  1.00 23.76           C  
ANISOU 1565  C   LEU A 198     2921   3304   2804    432   -611     39       C  
ATOM   1566  O   LEU A 198     -15.565 -38.629 -10.618  1.00 24.14           O  
ANISOU 1566  O   LEU A 198     3053   3341   2777    526   -684     28       O  
ATOM   1567  CB  LEU A 198     -14.127 -40.236 -12.689  1.00 28.61           C  
ANISOU 1567  CB  LEU A 198     3512   3931   3428    593   -693    -49       C  
ATOM   1568  CG  LEU A 198     -13.880 -41.553 -13.442  1.00 34.04           C  
ANISOU 1568  CG  LEU A 198     4256   4577   4100    650   -691    -40       C  
ATOM   1569  CD1 LEU A 198     -12.405 -41.965 -13.375  1.00 30.27           C  
ANISOU 1569  CD1 LEU A 198     3690   4162   3648    796   -794   -168       C  
ATOM   1570  CD2 LEU A 198     -14.777 -42.639 -12.867  1.00 29.22           C  
ANISOU 1570  CD2 LEU A 198     3872   3856   3376    691   -682     60       C  
ATOM   1571  N   GLY A 199     -15.963 -37.307 -12.405  1.00 21.92           N  
ANISOU 1571  N   GLY A 199     2583   3105   2642    316   -549     34       N  
ATOM   1572  CA  GLY A 199     -16.114 -36.114 -11.597  1.00 22.90           C  
ANISOU 1572  CA  GLY A 199     2677   3255   2771    287   -558     15       C  
ATOM   1573  C   GLY A 199     -17.478 -35.448 -11.683  1.00 24.97           C  
ANISOU 1573  C   GLY A 199     2980   3479   3027    185   -476     98       C  
ATOM   1574  O   GLY A 199     -17.847 -34.710 -10.773  1.00 24.53           O  
ANISOU 1574  O   GLY A 199     2948   3426   2948    181   -484    101       O  
ATOM   1575  N   TYR A 200     -18.235 -35.687 -12.759  1.00 21.59           N  
ANISOU 1575  N   TYR A 200     2560   3021   2622    112   -405    156       N  
ATOM   1576  CA  TYR A 200     -19.521 -35.041 -12.997  1.00 18.80           C  
ANISOU 1576  CA  TYR A 200     2224   2644   2276     29   -339    214       C  
ATOM   1577  C   TYR A 200     -20.620 -36.094 -13.056  1.00 21.64           C  
ANISOU 1577  C   TYR A 200     2677   2950   2594     17   -301    281       C  
ATOM   1578  O   TYR A 200     -20.481 -37.093 -13.765  1.00 22.55           O  
ANISOU 1578  O   TYR A 200     2815   3045   2708     25   -295    292       O  
ATOM   1579  CB  TYR A 200     -19.544 -34.263 -14.335  1.00 17.49           C  
ANISOU 1579  CB  TYR A 200     1984   2489   2173    -49   -292    208       C  
ATOM   1580  CG  TYR A 200     -18.759 -32.972 -14.400  1.00 23.04           C  
ANISOU 1580  CG  TYR A 200     2609   3224   2921    -81   -289    147       C  
ATOM   1581  CD1 TYR A 200     -17.942 -32.564 -13.349  1.00 22.96           C  
ANISOU 1581  CD1 TYR A 200     2563   3249   2911    -41   -339     82       C  
ATOM   1582  CD2 TYR A 200     -18.849 -32.149 -15.518  1.00 22.46           C  
ANISOU 1582  CD2 TYR A 200     2512   3138   2884   -154   -232    148       C  
ATOM   1583  CE1 TYR A 200     -17.218 -31.375 -13.419  1.00 22.68           C  
ANISOU 1583  CE1 TYR A 200     2452   3240   2925    -89   -325     12       C  
ATOM   1584  CE2 TYR A 200     -18.130 -30.952 -15.597  1.00 22.81           C  
ANISOU 1584  CE2 TYR A 200     2506   3195   2966   -200   -207     89       C  
ATOM   1585  CZ  TYR A 200     -17.324 -30.572 -14.549  1.00 24.45           C  
ANISOU 1585  CZ  TYR A 200     2662   3442   3188   -176   -249     18       C  
ATOM   1586  OH  TYR A 200     -16.629 -29.389 -14.633  1.00 23.34           O  
ANISOU 1586  OH  TYR A 200     2469   3309   3091   -239   -213    -53       O  
ATOM   1587  N   TRP A 201     -21.740 -35.833 -12.385  1.00 23.98           N  
ANISOU 1587  N   TRP A 201     3021   3226   2865    -13   -265    316       N  
ATOM   1588  CA  TRP A 201     -22.962 -36.620 -12.561  1.00 21.55           C  
ANISOU 1588  CA  TRP A 201     2772   2874   2541    -59   -204    360       C  
ATOM   1589  C   TRP A 201     -24.088 -35.632 -12.836  1.00 24.09           C  
ANISOU 1589  C   TRP A 201     3034   3214   2905   -124   -164    364       C  
ATOM   1590  O   TRP A 201     -24.498 -34.883 -11.942  1.00 24.35           O  
ANISOU 1590  O   TRP A 201     3071   3255   2926   -125   -152    359       O  
ATOM   1591  CB  TRP A 201     -23.254 -37.505 -11.334  1.00 23.06           C  
ANISOU 1591  CB  TRP A 201     3099   3012   2651    -26   -184    383       C  
ATOM   1592  CG  TRP A 201     -24.517 -38.342 -11.471  1.00 24.00           C  
ANISOU 1592  CG  TRP A 201     3278   3081   2761    -97    -97    412       C  
ATOM   1593  CD1 TRP A 201     -25.752 -38.070 -10.920  1.00 24.92           C  
ANISOU 1593  CD1 TRP A 201     3405   3186   2877   -161    -21    416       C  
ATOM   1594  CD2 TRP A 201     -24.675 -39.563 -12.219  1.00 21.04           C  
ANISOU 1594  CD2 TRP A 201     2949   2662   2384   -121    -70    426       C  
ATOM   1595  NE1 TRP A 201     -26.653 -39.045 -11.282  1.00 24.19           N  
ANISOU 1595  NE1 TRP A 201     3350   3050   2790   -231     54    421       N  
ATOM   1596  CE2 TRP A 201     -26.025 -39.966 -12.083  1.00 24.11           C  
ANISOU 1596  CE2 TRP A 201     3368   3016   2777   -210     24    431       C  
ATOM   1597  CE3 TRP A 201     -23.810 -40.351 -12.994  1.00 22.02           C  
ANISOU 1597  CE3 TRP A 201     3086   2774   2508    -79   -112    424       C  
ATOM   1598  CZ2 TRP A 201     -26.521 -41.132 -12.677  1.00 29.36           C  
ANISOU 1598  CZ2 TRP A 201     4083   3630   3444   -265     77    434       C  
ATOM   1599  CZ3 TRP A 201     -24.312 -41.503 -13.606  1.00 26.06           C  
ANISOU 1599  CZ3 TRP A 201     3655   3231   3014   -124    -64    437       C  
ATOM   1600  CH2 TRP A 201     -25.652 -41.886 -13.437  1.00 24.91           C  
ANISOU 1600  CH2 TRP A 201     3546   3047   2872   -219     29    442       C  
ATOM   1601  N   ILE A 202     -24.556 -35.593 -14.082  1.00 20.21           N  
ANISOU 1601  N   ILE A 202     2491   2730   2458   -167   -151    366       N  
ATOM   1602  CA  ILE A 202     -25.444 -34.540 -14.558  1.00 22.44           C  
ANISOU 1602  CA  ILE A 202     2712   3033   2779   -201   -140    358       C  
ATOM   1603  C   ILE A 202     -26.741 -35.183 -15.023  1.00 28.42           C  
ANISOU 1603  C   ILE A 202     3461   3782   3555   -245   -104    356       C  
ATOM   1604  O   ILE A 202     -26.768 -35.828 -16.078  1.00 22.56           O  
ANISOU 1604  O   ILE A 202     2714   3033   2827   -261   -112    356       O  
ATOM   1605  CB  ILE A 202     -24.811 -33.730 -15.695  1.00 22.33           C  
ANISOU 1605  CB  ILE A 202     2657   3033   2794   -200   -168    347       C  
ATOM   1606  CG1 ILE A 202     -23.490 -33.083 -15.228  1.00 22.17           C  
ANISOU 1606  CG1 ILE A 202     2625   3026   2771   -175   -190    325       C  
ATOM   1607  CG2 ILE A 202     -25.817 -32.706 -16.217  1.00 22.13           C  
ANISOU 1607  CG2 ILE A 202     2603   3015   2792   -212   -168    341       C  
ATOM   1608  CD1 ILE A 202     -22.557 -32.668 -16.358  1.00 21.81           C  
ANISOU 1608  CD1 ILE A 202     2553   2982   2750   -190   -190    306       C  
ATOM   1609  N   GLU A 203     -27.822 -34.983 -14.263  1.00 22.29           N  
ANISOU 1609  N   GLU A 203     2674   3011   2784   -269    -63    342       N  
ATOM   1610  CA  GLU A 203     -29.106 -35.620 -14.534  1.00 24.26           C  
ANISOU 1610  CA  GLU A 203     2895   3261   3063   -324    -17    314       C  
ATOM   1611  C   GLU A 203     -30.049 -34.671 -15.254  1.00 26.71           C  
ANISOU 1611  C   GLU A 203     3110   3613   3424   -319    -47    274       C  
ATOM   1612  O   GLU A 203     -30.172 -33.502 -14.881  1.00 24.22           O  
ANISOU 1612  O   GLU A 203     2770   3319   3115   -286    -64    266       O  
ATOM   1613  CB  GLU A 203     -29.791 -36.080 -13.244  1.00 24.49           C  
ANISOU 1613  CB  GLU A 203     2969   3267   3070   -362     67    305       C  
ATOM   1614  CG  GLU A 203     -29.045 -37.187 -12.488  1.00 25.80           C  
ANISOU 1614  CG  GLU A 203     3267   3371   3164   -356     99    344       C  
ATOM   1615  CD  GLU A 203     -29.810 -37.663 -11.252  1.00 30.58           C  
ANISOU 1615  CD  GLU A 203     3953   3935   3730   -404    203    337       C  
ATOM   1616  OE1 GLU A 203     -29.186 -38.261 -10.365  1.00 33.23           O  
ANISOU 1616  OE1 GLU A 203     4429   4214   3985   -374    221    372       O  
ATOM   1617  OE2 GLU A 203     -31.035 -37.457 -11.172  1.00 40.83           O  
ANISOU 1617  OE2 GLU A 203     5181   5255   5076   -468    270    289       O  
ATOM   1618  N   SER A 204     -30.778 -35.204 -16.228  1.00 20.62           N  
ANISOU 1618  N   SER A 204     2293   2853   2687   -347    -57    239       N  
ATOM   1619  CA  SER A 204     -31.813 -34.453 -16.916  1.00 21.18           C  
ANISOU 1619  CA  SER A 204     2276   2969   2804   -326   -100    183       C  
ATOM   1620  C   SER A 204     -33.092 -35.270 -16.922  1.00 21.31           C  
ANISOU 1620  C   SER A 204     2219   3008   2870   -389    -55    109       C  
ATOM   1621  O   SER A 204     -33.089 -36.482 -16.655  1.00 21.60           O  
ANISOU 1621  O   SER A 204     2294   3012   2902   -459     12    112       O  
ATOM   1622  CB  SER A 204     -31.392 -34.120 -18.354  1.00 23.78           C  
ANISOU 1622  CB  SER A 204     2619   3296   3122   -279   -182    194       C  
ATOM   1623  OG  SER A 204     -30.919 -35.303 -18.978  1.00 24.22           O  
ANISOU 1623  OG  SER A 204     2713   3326   3165   -314   -175    211       O  
ATOM   1624  N   GLU A 205     -34.199 -34.598 -17.223  1.00 21.05           N  
ANISOU 1624  N   GLU A 205     2082   3028   2888   -364    -91     33       N  
ATOM   1625  CA  GLU A 205     -35.488 -35.267 -17.188  1.00 21.69           C  
ANISOU 1625  CA  GLU A 205     2059   3146   3036   -431    -44    -68       C  
ATOM   1626  C   GLU A 205     -36.399 -34.629 -18.217  1.00 21.47           C  
ANISOU 1626  C   GLU A 205     1920   3181   3055   -363   -149   -157       C  
ATOM   1627  O   GLU A 205     -36.231 -33.465 -18.591  1.00 24.59           O  
ANISOU 1627  O   GLU A 205     2330   3586   3428   -261   -237   -139       O  
ATOM   1628  CB  GLU A 205     -36.145 -35.160 -15.803  1.00 27.22           C  
ANISOU 1628  CB  GLU A 205     2725   3858   3761   -482     66   -106       C  
ATOM   1629  CG  GLU A 205     -36.506 -33.702 -15.481  1.00 28.79           C  
ANISOU 1629  CG  GLU A 205     2866   4099   3973   -396     20   -130       C  
ATOM   1630  CD  GLU A 205     -36.923 -33.453 -14.030  1.00 35.36           C  
ANISOU 1630  CD  GLU A 205     3691   4933   4811   -434    131   -150       C  
ATOM   1631  OE1 GLU A 205     -37.055 -32.263 -13.651  1.00 33.53           O  
ANISOU 1631  OE1 GLU A 205     3436   4724   4578   -361     99   -158       O  
ATOM   1632  OE2 GLU A 205     -37.117 -34.429 -13.280  1.00 34.24           O  
ANISOU 1632  OE2 GLU A 205     3583   4761   4665   -536    255   -158       O  
ATOM   1633  N   LYS A 206     -37.396 -35.394 -18.635  1.00 25.56           N  
ANISOU 1633  N   LYS A 206     2335   3739   3638   -420   -140   -262       N  
ATOM   1634  CA  LYS A 206     -38.449 -34.884 -19.505  1.00 28.87           C  
ANISOU 1634  CA  LYS A 206     2626   4232   4112   -349   -249   -380       C  
ATOM   1635  C   LYS A 206     -39.590 -34.373 -18.630  1.00 31.85           C  
ANISOU 1635  C   LYS A 206     2861   4675   4565   -356   -200   -489       C  
ATOM   1636  O   LYS A 206     -40.291 -35.160 -17.990  1.00 31.55           O  
ANISOU 1636  O   LYS A 206     2740   4656   4591   -474    -81   -570       O  
ATOM   1637  CB  LYS A 206     -38.943 -35.967 -20.455  1.00 28.50           C  
ANISOU 1637  CB  LYS A 206     2521   4204   4102   -404   -277   -461       C  
ATOM   1638  CG  LYS A 206     -40.155 -35.558 -21.288  1.00 34.62           C  
ANISOU 1638  CG  LYS A 206     3142   5070   4943   -328   -399   -615       C  
ATOM   1639  CD  LYS A 206     -39.856 -34.345 -22.153  1.00 31.39           C  
ANISOU 1639  CD  LYS A 206     2801   4660   4467   -155   -559   -575       C  
ATOM   1640  CE  LYS A 206     -41.067 -34.011 -23.038  1.00 42.29           C  
ANISOU 1640  CE  LYS A 206     4043   6128   5898    -54   -707   -737       C  
ATOM   1641  NZ  LYS A 206     -41.283 -35.028 -24.110  1.00 44.10           N  
ANISOU 1641  NZ  LYS A 206     4249   6370   6137    -90   -765   -803       N  
ATOM   1642  N   ASN A 207     -39.760 -33.058 -18.591  1.00 37.06           N  
ANISOU 1642  N   ASN A 207     3504   5362   5216   -233   -280   -496       N  
ATOM   1643  CA  ASN A 207     -40.953 -32.444 -18.023  1.00 40.01           C  
ANISOU 1643  CA  ASN A 207     3721   5812   5668   -203   -268   -626       C  
ATOM   1644  C   ASN A 207     -41.891 -32.154 -19.189  1.00 46.01           C  
ANISOU 1644  C   ASN A 207     4358   6649   6477    -97   -424   -760       C  
ATOM   1645  O   ASN A 207     -42.259 -33.073 -19.930  1.00 46.42           O  
ANISOU 1645  O   ASN A 207     4345   6727   6566   -149   -450   -833       O  
ATOM   1646  CB  ASN A 207     -40.563 -31.184 -17.246  1.00 49.98           C  
ANISOU 1646  CB  ASN A 207     5053   7052   6887   -121   -266   -557       C  
ATOM   1647  CG  ASN A 207     -41.689 -30.624 -16.398  1.00 54.65           C  
ANISOU 1647  CG  ASN A 207     5497   7713   7555   -106   -216   -681       C  
ATOM   1648  OD1 ASN A 207     -42.350 -29.667 -16.788  1.00 65.77           O  
ANISOU 1648  OD1 ASN A 207     6828   9172   8988     27   -328   -762       O  
ATOM   1649  ND2 ASN A 207     -41.900 -31.203 -15.230  1.00 72.11           N  
ANISOU 1649  ND2 ASN A 207     7681   9920   9796   -236    -47   -697       N  
ATOM   1650  N   ASP A 208     -42.270 -30.889 -19.385  1.00 44.21           N  
ANISOU 1650  N   ASP A 208     4106   6451   6240     61   -538   -797       N  
ATOM   1651  CA  ASP A 208     -42.874 -30.506 -20.660  1.00 49.08           C  
ANISOU 1651  CA  ASP A 208     4676   7115   6859    206   -725   -892       C  
ATOM   1652  C   ASP A 208     -41.833 -30.551 -21.766  1.00 45.07           C  
ANISOU 1652  C   ASP A 208     4361   6525   6237    254   -813   -764       C  
ATOM   1653  O   ASP A 208     -42.131 -30.910 -22.911  1.00 47.44           O  
ANISOU 1653  O   ASP A 208     4648   6848   6529    305   -930   -825       O  
ATOM   1654  CB  ASP A 208     -43.485 -29.107 -20.565  1.00 60.59           C  
ANISOU 1654  CB  ASP A 208     6096   8608   8317    383   -828   -956       C  
ATOM   1655  CG  ASP A 208     -44.576 -29.015 -19.517  1.00 80.77           C  
ANISOU 1655  CG  ASP A 208     8444  11254  10991    345   -740  -1102       C  
ATOM   1656  OD1 ASP A 208     -45.201 -30.054 -19.205  1.00 82.14           O  
ANISOU 1656  OD1 ASP A 208     8459  11487  11263    202   -638  -1210       O  
ATOM   1657  OD2 ASP A 208     -44.808 -27.897 -19.008  1.00 93.26           O  
ANISOU 1657  OD2 ASP A 208    10026  12842  12567    454   -764  -1114       O  
ATOM   1658  N   THR A 209     -40.606 -30.185 -21.433  1.00 38.87           N  
ANISOU 1658  N   THR A 209     3755   5648   5366    237   -755   -598       N  
ATOM   1659  CA  THR A 209     -39.455 -30.319 -22.299  1.00 32.46           C  
ANISOU 1659  CA  THR A 209     3126   4753   4455    244   -788   -472       C  
ATOM   1660  C   THR A 209     -38.371 -31.044 -21.514  1.00 30.44           C  
ANISOU 1660  C   THR A 209     2941   4441   4183    100   -639   -354       C  
ATOM   1661  O   THR A 209     -38.462 -31.199 -20.290  1.00 29.30           O  
ANISOU 1661  O   THR A 209     2742   4308   4081     20   -525   -354       O  
ATOM   1662  CB  THR A 209     -38.962 -28.946 -22.755  1.00 43.04           C  
ANISOU 1662  CB  THR A 209     4625   6029   5699    388   -875   -400       C  
ATOM   1663  OG1 THR A 209     -38.535 -28.214 -21.600  1.00 47.55           O  
ANISOU 1663  OG1 THR A 209     5229   6571   6267    367   -786   -337       O  
ATOM   1664  CG2 THR A 209     -40.082 -28.181 -23.441  1.00 45.01           C  
ANISOU 1664  CG2 THR A 209     4822   6326   5952    559  -1036   -521       C  
ATOM   1665  N   TRP A 210     -37.327 -31.477 -22.215  1.00 27.70           N  
ANISOU 1665  N   TRP A 210     2725   4032   3769     76   -642   -259       N  
ATOM   1666  CA  TRP A 210     -36.147 -31.978 -21.523  1.00 27.93           C  
ANISOU 1666  CA  TRP A 210     2837   4005   3770    -23   -527   -148       C  
ATOM   1667  C   TRP A 210     -35.416 -30.829 -20.837  1.00 32.26           C  
ANISOU 1667  C   TRP A 210     3470   4512   4276     16   -502    -70       C  
ATOM   1668  O   TRP A 210     -35.305 -29.731 -21.385  1.00 25.42           O  
ANISOU 1668  O   TRP A 210     2678   3618   3361    115   -576    -54       O  
ATOM   1669  CB  TRP A 210     -35.226 -32.693 -22.505  1.00 25.08           C  
ANISOU 1669  CB  TRP A 210     2580   3596   3355    -48   -540    -85       C  
ATOM   1670  CG  TRP A 210     -35.651 -34.109 -22.712  1.00 27.20           C  
ANISOU 1670  CG  TRP A 210     2780   3887   3669   -137   -509   -139       C  
ATOM   1671  CD1 TRP A 210     -36.518 -34.589 -23.666  1.00 22.84           C  
ANISOU 1671  CD1 TRP A 210     2159   3375   3144   -120   -588   -236       C  
ATOM   1672  CD2 TRP A 210     -35.269 -35.226 -21.908  1.00 21.11           C  
ANISOU 1672  CD2 TRP A 210     2010   3092   2917   -254   -392   -108       C  
ATOM   1673  NE1 TRP A 210     -36.681 -35.945 -23.509  1.00 24.82           N  
ANISOU 1673  NE1 TRP A 210     2365   3628   3438   -237   -514   -268       N  
ATOM   1674  CE2 TRP A 210     -35.920 -36.363 -22.439  1.00 27.75           C  
ANISOU 1674  CE2 TRP A 210     2791   3953   3799   -318   -391   -185       C  
ATOM   1675  CE3 TRP A 210     -34.432 -35.377 -20.789  1.00 21.89           C  
ANISOU 1675  CE3 TRP A 210     2170   3151   2996   -304   -294    -28       C  
ATOM   1676  CZ2 TRP A 210     -35.765 -37.636 -21.885  1.00 23.35           C  
ANISOU 1676  CZ2 TRP A 210     2249   3364   3260   -435   -281   -176       C  
ATOM   1677  CZ3 TRP A 210     -34.275 -36.645 -20.238  1.00 22.18           C  
ANISOU 1677  CZ3 TRP A 210     2227   3160   3043   -402   -200    -17       C  
ATOM   1678  CH2 TRP A 210     -34.936 -37.759 -20.793  1.00 21.90           C  
ANISOU 1678  CH2 TRP A 210     2147   3131   3044   -469   -188    -87       C  
ATOM   1679  N   ARG A 211     -34.916 -31.079 -19.630  1.00 25.15           N  
ANISOU 1679  N   ARG A 211     2573   3599   3384    -60   -398    -25       N  
ATOM   1680  CA  ARG A 211     -34.300 -30.000 -18.877  1.00 25.67           C  
ANISOU 1680  CA  ARG A 211     2702   3634   3418    -29   -376     29       C  
ATOM   1681  C   ARG A 211     -33.359 -30.598 -17.853  1.00 24.40           C  
ANISOU 1681  C   ARG A 211     2582   3446   3243   -112   -280     93       C  
ATOM   1682  O   ARG A 211     -33.490 -31.764 -17.460  1.00 20.93           O  
ANISOU 1682  O   ARG A 211     2114   3015   2825   -188   -219     84       O  
ATOM   1683  CB  ARG A 211     -35.345 -29.142 -18.162  1.00 31.11           C  
ANISOU 1683  CB  ARG A 211     3310   4364   4146     22   -381    -40       C  
ATOM   1684  CG  ARG A 211     -35.948 -29.898 -16.976  1.00 28.65           C  
ANISOU 1684  CG  ARG A 211     2904   4092   3890    -66   -277    -85       C  
ATOM   1685  CD  ARG A 211     -37.174 -29.239 -16.442  1.00 31.82           C  
ANISOU 1685  CD  ARG A 211     3192   4550   4347    -23   -276   -185       C  
ATOM   1686  NE  ARG A 211     -37.699 -29.957 -15.284  1.00 28.93           N  
ANISOU 1686  NE  ARG A 211     2756   4210   4026   -123   -149   -227       N  
ATOM   1687  CZ  ARG A 211     -38.766 -29.555 -14.604  1.00 38.75           C  
ANISOU 1687  CZ  ARG A 211     3888   5506   5327   -114   -108   -325       C  
ATOM   1688  NH1 ARG A 211     -39.402 -28.455 -14.990  1.00 35.81           N  
ANISOU 1688  NH1 ARG A 211     3458   5172   4978      7   -203   -389       N  
ATOM   1689  NH2 ARG A 211     -39.195 -30.244 -13.549  1.00 35.48           N  
ANISOU 1689  NH2 ARG A 211     3433   5102   4943   -221     32   -361       N  
ATOM   1690  N   LEU A 212     -32.424 -29.766 -17.406  1.00 23.88           N  
ANISOU 1690  N   LEU A 212     2590   3344   3138    -93   -271    149       N  
ATOM   1691  CA  LEU A 212     -31.525 -30.155 -16.335  1.00 24.92           C  
ANISOU 1691  CA  LEU A 212     2760   3458   3252   -146   -204    195       C  
ATOM   1692  C   LEU A 212     -32.333 -30.402 -15.068  1.00 26.49           C  
ANISOU 1692  C   LEU A 212     2907   3683   3475   -178   -137    159       C  
ATOM   1693  O   LEU A 212     -33.197 -29.595 -14.699  1.00 23.86           O  
ANISOU 1693  O   LEU A 212     2524   3376   3167   -143   -140    112       O  
ATOM   1694  CB  LEU A 212     -30.469 -29.064 -16.105  1.00 23.17           C  
ANISOU 1694  CB  LEU A 212     2609   3201   2994   -119   -214    235       C  
ATOM   1695  CG  LEU A 212     -29.482 -29.320 -14.954  1.00 25.78           C  
ANISOU 1695  CG  LEU A 212     2972   3521   3302   -153   -169    265       C  
ATOM   1696  CD1 LEU A 212     -28.518 -30.472 -15.315  1.00 22.40           C  
ANISOU 1696  CD1 LEU A 212     2571   3080   2860   -185   -163    295       C  
ATOM   1697  CD2 LEU A 212     -28.717 -28.041 -14.550  1.00 25.18           C  
ANISOU 1697  CD2 LEU A 212     2938   3423   3207   -131   -178    274       C  
ATOM   1698  N   LYS A 213     -32.096 -31.553 -14.439  1.00 21.76           N  
ANISOU 1698  N   LYS A 213     2333   3071   2865   -241    -72    177       N  
ATOM   1699  CA  LYS A 213     -32.785 -31.922 -13.205  1.00 21.20           C  
ANISOU 1699  CA  LYS A 213     2248   3006   2799   -286     17    149       C  
ATOM   1700  C   LYS A 213     -31.931 -31.655 -11.967  1.00 27.02           C  
ANISOU 1700  C   LYS A 213     3074   3714   3479   -277     47    195       C  
ATOM   1701  O   LYS A 213     -32.385 -31.024 -11.006  1.00 23.90           O  
ANISOU 1701  O   LYS A 213     2674   3328   3080   -269     86    172       O  
ATOM   1702  CB  LYS A 213     -33.180 -33.405 -13.268  1.00 25.82           C  
ANISOU 1702  CB  LYS A 213     2836   3578   3396   -365     82    133       C  
ATOM   1703  CG  LYS A 213     -33.814 -33.960 -12.013  1.00 28.40           C  
ANISOU 1703  CG  LYS A 213     3186   3889   3714   -432    203    107       C  
ATOM   1704  CD  LYS A 213     -33.883 -35.481 -12.099  1.00 27.48           C  
ANISOU 1704  CD  LYS A 213     3126   3729   3587   -515    274    111       C  
ATOM   1705  CE  LYS A 213     -34.354 -36.081 -10.784  1.00 41.75           C  
ANISOU 1705  CE  LYS A 213     5009   5493   5360   -588    416     99       C  
ATOM   1706  NZ  LYS A 213     -34.031 -37.534 -10.716  1.00 51.15           N  
ANISOU 1706  NZ  LYS A 213     6326   6607   6504   -650    481    131       N  
ATOM   1707  N   ARG A 214     -30.697 -32.139 -11.967  1.00 22.61           N  
ANISOU 1707  N   ARG A 214     2595   3122   2875   -270     24    249       N  
ATOM   1708  CA  ARG A 214     -29.804 -31.993 -10.825  1.00 24.13           C  
ANISOU 1708  CA  ARG A 214     2870   3291   3008   -248     31    279       C  
ATOM   1709  C   ARG A 214     -28.414 -32.355 -11.316  1.00 26.50           C  
ANISOU 1709  C   ARG A 214     3209   3575   3283   -223    -28    314       C  
ATOM   1710  O   ARG A 214     -28.266 -33.032 -12.339  1.00 24.22           O  
ANISOU 1710  O   ARG A 214     2906   3282   3013   -237    -44    322       O  
ATOM   1711  CB  ARG A 214     -30.227 -32.890  -9.645  1.00 27.82           C  
ANISOU 1711  CB  ARG A 214     3414   3727   3428   -284    120    281       C  
ATOM   1712  CG  ARG A 214     -30.139 -34.389  -9.917  1.00 32.58           C  
ANISOU 1712  CG  ARG A 214     4078   4290   4011   -324    155    300       C  
ATOM   1713  CD  ARG A 214     -30.388 -35.223  -8.651  1.00 43.38           C  
ANISOU 1713  CD  ARG A 214     5576   5601   5307   -355    252    311       C  
ATOM   1714  NE  ARG A 214     -29.357 -34.971  -7.656  1.00 33.71           N  
ANISOU 1714  NE  ARG A 214     4457   4352   3998   -283    210    343       N  
ATOM   1715  CZ  ARG A 214     -28.320 -35.768  -7.409  1.00 36.31           C  
ANISOU 1715  CZ  ARG A 214     4903   4638   4256   -233    168    379       C  
ATOM   1716  NH1 ARG A 214     -27.441 -35.415  -6.484  1.00 34.81           N  
ANISOU 1716  NH1 ARG A 214     4791   4439   3995   -156    112    388       N  
ATOM   1717  NH2 ARG A 214     -28.160 -36.917  -8.059  1.00 27.12           N  
ANISOU 1717  NH2 ARG A 214     3777   3438   3089   -250    175    396       N  
ATOM   1718  N   ALA A 215     -27.396 -31.879 -10.599  1.00 20.16           N  
ANISOU 1718  N   ALA A 215     2448   2769   2445   -185    -61    321       N  
ATOM   1719  CA  ALA A 215     -26.035 -32.283 -10.914  1.00 19.21           C  
ANISOU 1719  CA  ALA A 215     2348   2643   2308   -157   -113    331       C  
ATOM   1720  C   ALA A 215     -25.246 -32.386  -9.619  1.00 26.67           C  
ANISOU 1720  C   ALA A 215     3364   3579   3191   -110   -136    326       C  
ATOM   1721  O   ALA A 215     -25.497 -31.643  -8.667  1.00 27.55           O  
ANISOU 1721  O   ALA A 215     3494   3694   3280    -99   -127    313       O  
ATOM   1722  CB  ALA A 215     -25.336 -31.307 -11.873  1.00 18.24           C  
ANISOU 1722  CB  ALA A 215     2165   2538   2227   -154   -156    316       C  
ATOM   1723  N   HIS A 216     -24.309 -33.333  -9.582  1.00 21.44           N  
ANISOU 1723  N   HIS A 216     2747   2903   2495    -71   -173    331       N  
ATOM   1724  CA  HIS A 216     -23.312 -33.382  -8.522  1.00 21.17           C  
ANISOU 1724  CA  HIS A 216     2771   2869   2401      1   -231    309       C  
ATOM   1725  C   HIS A 216     -21.928 -33.341  -9.150  1.00 27.81           C  
ANISOU 1725  C   HIS A 216     3544   3745   3278     36   -304    268       C  
ATOM   1726  O   HIS A 216     -21.605 -34.179 -10.000  1.00 26.93           O  
ANISOU 1726  O   HIS A 216     3422   3628   3184     38   -308    277       O  
ATOM   1727  CB  HIS A 216     -23.451 -34.625  -7.644  1.00 21.87           C  
ANISOU 1727  CB  HIS A 216     3007   2904   2399     43   -215    337       C  
ATOM   1728  CG  HIS A 216     -22.741 -34.482  -6.334  1.00 36.79           C  
ANISOU 1728  CG  HIS A 216     4984   4789   4207    129   -276    313       C  
ATOM   1729  ND1 HIS A 216     -23.308 -33.844  -5.251  1.00 48.98           N  
ANISOU 1729  ND1 HIS A 216     6585   6322   5704    126   -245    313       N  
ATOM   1730  CD2 HIS A 216     -21.490 -34.833  -5.950  1.00 42.46           C  
ANISOU 1730  CD2 HIS A 216     5734   5518   4883    229   -378    277       C  
ATOM   1731  CE1 HIS A 216     -22.450 -33.838  -4.245  1.00 44.17           C  
ANISOU 1731  CE1 HIS A 216     6054   5711   5016    220   -326    283       C  
ATOM   1732  NE2 HIS A 216     -21.337 -34.428  -4.643  1.00 35.95           N  
ANISOU 1732  NE2 HIS A 216     4994   4687   3979    289   -415    256       N  
ATOM   1733  N   LEU A 217     -21.109 -32.381  -8.715  1.00 22.69           N  
ANISOU 1733  N   LEU A 217     2845   3133   2643     58   -355    213       N  
ATOM   1734  CA  LEU A 217     -19.765 -32.189  -9.247  1.00 21.68           C  
ANISOU 1734  CA  LEU A 217     2627   3048   2564     76   -410    147       C  
ATOM   1735  C   LEU A 217     -18.762 -32.295  -8.109  1.00 27.96           C  
ANISOU 1735  C   LEU A 217     3442   3868   3313    168   -502     82       C  
ATOM   1736  O   LEU A 217     -18.870 -31.566  -7.114  1.00 27.53           O  
ANISOU 1736  O   LEU A 217     3415   3819   3227    183   -523     61       O  
ATOM   1737  CB  LEU A 217     -19.647 -30.825  -9.940  1.00 22.91           C  
ANISOU 1737  CB  LEU A 217     2690   3223   2793     -1   -378    116       C  
ATOM   1738  CG  LEU A 217     -20.773 -30.423 -10.915  1.00 30.31           C  
ANISOU 1738  CG  LEU A 217     3626   4130   3758    -72   -305    174       C  
ATOM   1739  CD1 LEU A 217     -20.511 -29.024 -11.468  1.00 26.42           C  
ANISOU 1739  CD1 LEU A 217     3084   3639   3315   -129   -279    141       C  
ATOM   1740  CD2 LEU A 217     -20.952 -31.420 -12.043  1.00 34.29           C  
ANISOU 1740  CD2 LEU A 217     4131   4621   4275    -85   -282    210       C  
ATOM   1741  N   ILE A 218     -17.784 -33.187  -8.248  1.00 21.39           N  
ANISOU 1741  N   ILE A 218     2599   3055   2475    242   -567     42       N  
ATOM   1742  CA  ILE A 218     -16.736 -33.289  -7.239  1.00 23.41           C  
ANISOU 1742  CA  ILE A 218     2859   3345   2690    353   -681    -42       C  
ATOM   1743  C   ILE A 218     -15.406 -32.761  -7.763  1.00 29.09           C  
ANISOU 1743  C   ILE A 218     3408   4141   3504    347   -728   -164       C  
ATOM   1744  O   ILE A 218     -14.360 -32.966  -7.132  1.00 24.03           O  
ANISOU 1744  O   ILE A 218     2732   3548   2851    450   -838   -263       O  
ATOM   1745  CB  ILE A 218     -16.601 -34.720  -6.692  1.00 28.16           C  
ANISOU 1745  CB  ILE A 218     3602   3905   3192    477   -740    -16       C  
ATOM   1746  CG1 ILE A 218     -16.260 -35.723  -7.808  1.00 24.43           C  
ANISOU 1746  CG1 ILE A 218     3099   3427   2757    486   -728     -7       C  
ATOM   1747  CG2 ILE A 218     -17.881 -35.105  -5.929  1.00 24.43           C  
ANISOU 1747  CG2 ILE A 218     3313   3351   2619    468   -676     85       C  
ATOM   1748  CD1 ILE A 218     -15.968 -37.158  -7.276  1.00 23.56           C  
ANISOU 1748  CD1 ILE A 218     3143   3266   2543    627   -797      8       C  
ATOM   1749  N   GLU A 219     -15.432 -32.079  -8.905  1.00 25.58           N  
ANISOU 1749  N   GLU A 219     2862   3707   3151    230   -643   -167       N  
ATOM   1750  CA  GLU A 219     -14.325 -31.303  -9.448  1.00 24.94           C  
ANISOU 1750  CA  GLU A 219     2623   3686   3168    177   -640   -285       C  
ATOM   1751  C   GLU A 219     -14.961 -30.225 -10.321  1.00 21.16           C  
ANISOU 1751  C   GLU A 219     2128   3173   2739     37   -522   -240       C  
ATOM   1752  O   GLU A 219     -16.147 -30.297 -10.642  1.00 24.08           O  
ANISOU 1752  O   GLU A 219     2585   3488   3075      5   -465   -129       O  
ATOM   1753  CB  GLU A 219     -13.359 -32.183 -10.256  1.00 21.78           C  
ANISOU 1753  CB  GLU A 219     2139   3322   2814    214   -658   -346       C  
ATOM   1754  CG  GLU A 219     -14.025 -32.720 -11.555  1.00 21.85           C  
ANISOU 1754  CG  GLU A 219     2188   3281   2832    151   -561   -248       C  
ATOM   1755  CD  GLU A 219     -13.268 -33.857 -12.208  1.00 24.01           C  
ANISOU 1755  CD  GLU A 219     2423   3576   3125    213   -585   -287       C  
ATOM   1756  OE1 GLU A 219     -13.776 -34.409 -13.208  1.00 26.27           O  
ANISOU 1756  OE1 GLU A 219     2751   3820   3410    173   -519   -212       O  
ATOM   1757  OE2 GLU A 219     -12.187 -34.213 -11.723  1.00 27.62           O  
ANISOU 1757  OE2 GLU A 219     2807   4090   3596    309   -677   -397       O  
ATOM   1758  N   MET A 220     -14.181 -29.207 -10.678  1.00 25.12           N  
ANISOU 1758  N   MET A 220     2524   3704   3318    -44   -486   -336       N  
ATOM   1759  CA  MET A 220     -14.630 -28.195 -11.641  1.00 26.27           C  
ANISOU 1759  CA  MET A 220     2678   3801   3501   -170   -370   -300       C  
ATOM   1760  C   MET A 220     -13.569 -28.185 -12.730  1.00 25.36           C  
ANISOU 1760  C   MET A 220     2461   3711   3465   -237   -309   -385       C  
ATOM   1761  O   MET A 220     -12.537 -27.532 -12.566  1.00 26.29           O  
ANISOU 1761  O   MET A 220     2471   3870   3648   -284   -302   -516       O  
ATOM   1762  CB  MET A 220     -14.776 -26.804 -11.004  1.00 32.29           C  
ANISOU 1762  CB  MET A 220     3449   4548   4270   -226   -353   -332       C  
ATOM   1763  CG  MET A 220     -15.424 -26.793  -9.626  1.00 37.60           C  
ANISOU 1763  CG  MET A 220     4195   5221   4872   -148   -428   -299       C  
ATOM   1764  SD  MET A 220     -17.180 -27.143  -9.686  1.00 41.36           S  
ANISOU 1764  SD  MET A 220     4808   5632   5276   -128   -390   -138       S  
ATOM   1765  CE  MET A 220     -17.387 -28.059  -8.141  1.00 40.54           C  
ANISOU 1765  CE  MET A 220     4778   5546   5081     -4   -486   -124       C  
ATOM   1766  N   LYS A 221     -13.789 -28.922 -13.812  1.00 25.56           N  
ANISOU 1766  N   LYS A 221     2512   3711   3487   -245   -262   -325       N  
ATOM   1767  CA  LYS A 221     -12.758 -29.021 -14.834  1.00 26.78           C  
ANISOU 1767  CA  LYS A 221     2575   3889   3710   -303   -195   -410       C  
ATOM   1768  C   LYS A 221     -13.128 -28.160 -16.041  1.00 22.38           C  
ANISOU 1768  C   LYS A 221     2084   3259   3161   -427    -61   -365       C  
ATOM   1769  O   LYS A 221     -14.255 -27.693 -16.172  1.00 25.92           O  
ANISOU 1769  O   LYS A 221     2648   3643   3556   -441    -41   -260       O  
ATOM   1770  CB  LYS A 221     -12.522 -30.480 -15.231  1.00 25.11           C  
ANISOU 1770  CB  LYS A 221     2351   3703   3488   -217   -236   -397       C  
ATOM   1771  CG  LYS A 221     -13.753 -31.237 -15.607  1.00 29.36           C  
ANISOU 1771  CG  LYS A 221     3019   4183   3955   -184   -237   -251       C  
ATOM   1772  CD  LYS A 221     -13.383 -32.650 -16.067  1.00 34.28           C  
ANISOU 1772  CD  LYS A 221     3632   4822   4572   -110   -266   -253       C  
ATOM   1773  CE  LYS A 221     -14.614 -33.373 -16.595  1.00 26.10           C  
ANISOU 1773  CE  LYS A 221     2719   3723   3474   -102   -250   -120       C  
ATOM   1774  NZ  LYS A 221     -15.561 -33.679 -15.485  1.00 26.26           N  
ANISOU 1774  NZ  LYS A 221     2825   3722   3429    -41   -314    -48       N  
ATOM   1775  N   THR A 222     -12.144 -27.933 -16.912  1.00 23.05           N  
ANISOU 1775  N   THR A 222     2097   3352   3308   -512     34   -457       N  
ATOM   1776  CA  THR A 222     -12.270 -26.940 -17.978  1.00 28.00           C  
ANISOU 1776  CA  THR A 222     2806   3898   3934   -640    176   -438       C  
ATOM   1777  C   THR A 222     -11.989 -27.512 -19.358  1.00 27.97           C  
ANISOU 1777  C   THR A 222     2825   3871   3932   -677    266   -428       C  
ATOM   1778  O   THR A 222     -11.726 -26.738 -20.295  1.00 22.70           O  
ANISOU 1778  O   THR A 222     2217   3138   3269   -792    404   -448       O  
ATOM   1779  CB  THR A 222     -11.337 -25.747 -17.750  1.00 21.47           C  
ANISOU 1779  CB  THR A 222     1906   3074   3176   -756    256   -571       C  
ATOM   1780  OG1 THR A 222      -9.968 -26.184 -17.682  1.00 23.09           O  
ANISOU 1780  OG1 THR A 222     1929   3371   3473   -770    261   -734       O  
ATOM   1781  CG2 THR A 222     -11.724 -24.994 -16.470  1.00 25.43           C  
ANISOU 1781  CG2 THR A 222     2417   3581   3664   -731    179   -573       C  
ATOM   1782  N   CYS A 223     -11.978 -28.832 -19.499  1.00 22.13           N  
ANISOU 1782  N   CYS A 223     2052   3173   3183   -585    201   -406       N  
ATOM   1783  CA  CYS A 223     -11.867 -29.426 -20.823  1.00 24.46           C  
ANISOU 1783  CA  CYS A 223     2390   3438   3466   -610    280   -382       C  
ATOM   1784  C   CYS A 223     -13.229 -29.347 -21.513  1.00 22.15           C  
ANISOU 1784  C   CYS A 223     2275   3058   3082   -603    287   -232       C  
ATOM   1785  O   CYS A 223     -14.231 -28.975 -20.902  1.00 22.17           O  
ANISOU 1785  O   CYS A 223     2344   3037   3044   -567    224   -154       O  
ATOM   1786  CB  CYS A 223     -11.355 -30.869 -20.713  1.00 27.27           C  
ANISOU 1786  CB  CYS A 223     2653   3865   3843   -508    203   -420       C  
ATOM   1787  SG  CYS A 223     -12.247 -31.894 -19.488  1.00 26.23           S  
ANISOU 1787  SG  CYS A 223     2556   3758   3654   -351     27   -330       S  
ATOM   1788  N   GLU A 224     -13.269 -29.679 -22.806  1.00 21.46           N  
ANISOU 1788  N   GLU A 224     2264   2925   2965   -633    363   -201       N  
ATOM   1789  CA  GLU A 224     -14.516 -29.644 -23.571  1.00 23.33           C  
ANISOU 1789  CA  GLU A 224     2665   3086   3114   -615    357    -77       C  
ATOM   1790  C   GLU A 224     -15.171 -31.019 -23.557  1.00 23.86           C  
ANISOU 1790  C   GLU A 224     2730   3181   3155   -517    258    -15       C  
ATOM   1791  O   GLU A 224     -14.560 -32.005 -23.987  1.00 22.80           O  
ANISOU 1791  O   GLU A 224     2548   3077   3040   -497    268    -51       O  
ATOM   1792  CB  GLU A 224     -14.253 -29.201 -25.014  1.00 19.31           C  
ANISOU 1792  CB  GLU A 224     2273   2498   2566   -698    491    -78       C  
ATOM   1793  CG  GLU A 224     -13.778 -27.738 -25.084  1.00 22.08           C  
ANISOU 1793  CG  GLU A 224     2676   2789   2925   -809    610   -126       C  
ATOM   1794  CD  GLU A 224     -13.698 -27.204 -26.504  1.00 30.00           C  
ANISOU 1794  CD  GLU A 224     3856   3683   3859   -888    751   -107       C  
ATOM   1795  OE1 GLU A 224     -13.750 -28.013 -27.458  1.00 30.08           O  
ANISOU 1795  OE1 GLU A 224     3916   3682   3830   -865    767    -80       O  
ATOM   1796  OE2 GLU A 224     -13.596 -25.970 -26.647  1.00 30.87           O  
ANISOU 1796  OE2 GLU A 224     4073   3711   3944   -971    847   -118       O  
ATOM   1797  N   TRP A 225     -16.409 -31.083 -23.087  1.00 22.12           N  
ANISOU 1797  N   TRP A 225     2563   2948   2893   -462    173     69       N  
ATOM   1798  CA  TRP A 225     -17.162 -32.338 -23.126  1.00 24.41           C  
ANISOU 1798  CA  TRP A 225     2869   3251   3157   -391     98    125       C  
ATOM   1799  C   TRP A 225     -17.451 -32.701 -24.583  1.00 23.92           C  
ANISOU 1799  C   TRP A 225     2900   3141   3049   -406    140    157       C  
ATOM   1800  O   TRP A 225     -18.075 -31.900 -25.294  1.00 21.42           O  
ANISOU 1800  O   TRP A 225     2690   2766   2682   -429    165    196       O  
ATOM   1801  CB  TRP A 225     -18.460 -32.196 -22.338  1.00 19.89           C  
ANISOU 1801  CB  TRP A 225     2325   2674   2558   -350     23    189       C  
ATOM   1802  CG  TRP A 225     -19.145 -33.509 -22.038  1.00 21.59           C  
ANISOU 1802  CG  TRP A 225     2537   2905   2759   -293    -42    226       C  
ATOM   1803  CD1 TRP A 225     -19.803 -34.314 -22.932  1.00 26.90           C  
ANISOU 1803  CD1 TRP A 225     3263   3554   3402   -283    -51    261       C  
ATOM   1804  CD2 TRP A 225     -19.254 -34.160 -20.759  1.00 21.53           C  
ANISOU 1804  CD2 TRP A 225     2490   2930   2760   -244    -99    227       C  
ATOM   1805  NE1 TRP A 225     -20.309 -35.426 -22.289  1.00 23.41           N  
ANISOU 1805  NE1 TRP A 225     2811   3126   2959   -245    -99    281       N  
ATOM   1806  CE2 TRP A 225     -19.982 -35.364 -20.960  1.00 22.53           C  
ANISOU 1806  CE2 TRP A 225     2654   3042   2863   -218   -125    266       C  
ATOM   1807  CE3 TRP A 225     -18.794 -33.852 -19.467  1.00 23.38           C  
ANISOU 1807  CE3 TRP A 225     2676   3197   3012   -219   -129    196       C  
ATOM   1808  CZ2 TRP A 225     -20.273 -36.258 -19.913  1.00 20.09           C  
ANISOU 1808  CZ2 TRP A 225     2354   2739   2542   -176   -163    280       C  
ATOM   1809  CZ3 TRP A 225     -19.088 -34.736 -18.423  1.00 29.70           C  
ANISOU 1809  CZ3 TRP A 225     3487   4006   3790   -162   -181    213       C  
ATOM   1810  CH2 TRP A 225     -19.827 -35.926 -18.657  1.00 24.46           C  
ANISOU 1810  CH2 TRP A 225     2880   3316   3098   -144   -190    258       C  
ATOM   1811  N   PRO A 226     -17.033 -33.876 -25.068  1.00 24.93           N  
ANISOU 1811  N   PRO A 226     3006   3285   3181   -382    141    141       N  
ATOM   1812  CA  PRO A 226     -17.157 -34.169 -26.509  1.00 20.28           C  
ANISOU 1812  CA  PRO A 226     2512   2648   2544   -402    190    160       C  
ATOM   1813  C   PRO A 226     -18.600 -34.416 -26.929  1.00 21.72           C  
ANISOU 1813  C   PRO A 226     2786   2798   2667   -366    121    234       C  
ATOM   1814  O   PRO A 226     -19.362 -35.118 -26.251  1.00 20.79           O  
ANISOU 1814  O   PRO A 226     2635   2705   2559   -323     42    260       O  
ATOM   1815  CB  PRO A 226     -16.305 -35.434 -26.698  1.00 22.08           C  
ANISOU 1815  CB  PRO A 226     2676   2911   2802   -374    198    114       C  
ATOM   1816  CG  PRO A 226     -16.386 -36.138 -25.335  1.00 24.93           C  
ANISOU 1816  CG  PRO A 226     2953   3323   3198   -307    105    112       C  
ATOM   1817  CD  PRO A 226     -16.352 -34.961 -24.327  1.00 21.38           C  
ANISOU 1817  CD  PRO A 226     2458   2891   2774   -328     97     99       C  
ATOM   1818  N   LYS A 227     -18.968 -33.828 -28.070  1.00 22.12           N  
ANISOU 1818  N   LYS A 227     2961   2790   2655   -385    155    257       N  
ATOM   1819  CA  LYS A 227     -20.312 -34.031 -28.611  1.00 20.83           C  
ANISOU 1819  CA  LYS A 227     2878   2602   2435   -341     77    305       C  
ATOM   1820  C   LYS A 227     -20.600 -35.499 -28.901  1.00 21.12           C  
ANISOU 1820  C   LYS A 227     2891   2658   2474   -314     32    305       C  
ATOM   1821  O   LYS A 227     -21.758 -35.921 -28.823  1.00 23.03           O  
ANISOU 1821  O   LYS A 227     3135   2909   2707   -282    -48    325       O  
ATOM   1822  CB  LYS A 227     -20.495 -33.195 -29.872  1.00 26.00           C  
ANISOU 1822  CB  LYS A 227     3695   3181   3004   -349    115    321       C  
ATOM   1823  CG  LYS A 227     -20.585 -31.713 -29.620  1.00 29.27           C  
ANISOU 1823  CG  LYS A 227     4173   3553   3397   -363    142    332       C  
ATOM   1824  CD  LYS A 227     -20.377 -31.011 -30.951  1.00 32.63           C  
ANISOU 1824  CD  LYS A 227     4792   3883   3724   -380    215    343       C  
ATOM   1825  CE  LYS A 227     -20.920 -29.627 -30.952  1.00 28.86           C  
ANISOU 1825  CE  LYS A 227     4440   3338   3188   -359    207    369       C  
ATOM   1826  NZ  LYS A 227     -20.801 -29.053 -32.330  1.00 31.08           N  
ANISOU 1826  NZ  LYS A 227     4955   3507   3346   -361    274    387       N  
ATOM   1827  N   SER A 228     -19.562 -36.296 -29.200  1.00 23.61           N  
ANISOU 1827  N   SER A 228     3179   2983   2808   -327     87    272       N  
ATOM   1828  CA  SER A 228     -19.743 -37.730 -29.436  1.00 27.12           C  
ANISOU 1828  CA  SER A 228     3614   3437   3254   -299     51    270       C  
ATOM   1829  C   SER A 228     -20.448 -38.409 -28.280  1.00 27.43           C  
ANISOU 1829  C   SER A 228     3585   3506   3329   -272    -22    286       C  
ATOM   1830  O   SER A 228     -21.203 -39.369 -28.494  1.00 23.33           O  
ANISOU 1830  O   SER A 228     3089   2978   2798   -261    -66    295       O  
ATOM   1831  CB  SER A 228     -18.391 -38.415 -29.664  1.00 25.54           C  
ANISOU 1831  CB  SER A 228     3375   3248   3081   -303    119    222       C  
ATOM   1832  OG  SER A 228     -17.530 -38.217 -28.548  1.00 24.81           O  
ANISOU 1832  OG  SER A 228     3172   3202   3053   -298    131    185       O  
ATOM   1833  N   HIS A 229     -20.198 -37.941 -27.055  1.00 23.77           N  
ANISOU 1833  N   HIS A 229     3049   3074   2907   -268    -29    283       N  
ATOM   1834  CA  HIS A 229     -20.748 -38.521 -25.835  1.00 20.17           C  
ANISOU 1834  CA  HIS A 229     2550   2638   2475   -245    -80    297       C  
ATOM   1835  C   HIS A 229     -21.837 -37.629 -25.244  1.00 20.66           C  
ANISOU 1835  C   HIS A 229     2603   2707   2538   -254   -114    321       C  
ATOM   1836  O   HIS A 229     -22.004 -37.565 -24.020  1.00 22.99           O  
ANISOU 1836  O   HIS A 229     2857   3023   2855   -244   -130    327       O  
ATOM   1837  CB  HIS A 229     -19.641 -38.756 -24.795  1.00 18.30           C  
ANISOU 1837  CB  HIS A 229     2248   2431   2273   -215    -73    268       C  
ATOM   1838  CG  HIS A 229     -18.654 -39.820 -25.177  1.00 23.76           C  
ANISOU 1838  CG  HIS A 229     2937   3122   2971   -183    -57    233       C  
ATOM   1839  ND1 HIS A 229     -17.902 -39.764 -26.333  1.00 25.84           N  
ANISOU 1839  ND1 HIS A 229     3208   3380   3232   -201      0    200       N  
ATOM   1840  CD2 HIS A 229     -18.308 -40.973 -24.558  1.00 23.79           C  
ANISOU 1840  CD2 HIS A 229     2942   3123   2976   -125    -87    223       C  
ATOM   1841  CE1 HIS A 229     -17.133 -40.837 -26.407  1.00 22.76           C  
ANISOU 1841  CE1 HIS A 229     2804   2993   2851   -155      2    165       C  
ATOM   1842  NE2 HIS A 229     -17.357 -41.585 -25.340  1.00 21.27           N  
ANISOU 1842  NE2 HIS A 229     2616   2803   2661   -102    -57    179       N  
ATOM   1843  N   THR A 230     -22.573 -36.928 -26.104  1.00 21.41           N  
ANISOU 1843  N   THR A 230     2746   2784   2603   -262   -127    331       N  
ATOM   1844  CA  THR A 230     -23.580 -35.969 -25.679  1.00 20.19           C  
ANISOU 1844  CA  THR A 230     2585   2638   2450   -254   -163    342       C  
ATOM   1845  C   THR A 230     -24.885 -36.224 -26.419  1.00 25.99           C  
ANISOU 1845  C   THR A 230     3345   3367   3161   -240   -221    336       C  
ATOM   1846  O   THR A 230     -24.880 -36.444 -27.633  1.00 21.75           O  
ANISOU 1846  O   THR A 230     2875   2805   2583   -232   -230    330       O  
ATOM   1847  CB  THR A 230     -23.108 -34.525 -25.939  1.00 21.04           C  
ANISOU 1847  CB  THR A 230     2734   2723   2537   -259   -132    345       C  
ATOM   1848  OG1 THR A 230     -21.805 -34.337 -25.357  1.00 22.09           O  
ANISOU 1848  OG1 THR A 230     2825   2869   2701   -284    -75    327       O  
ATOM   1849  CG2 THR A 230     -24.084 -33.512 -25.336  1.00 19.19           C  
ANISOU 1849  CG2 THR A 230     2492   2495   2304   -237   -173    354       C  
ATOM   1850  N   LEU A 231     -25.999 -36.183 -25.680  1.00 24.67           N  
ANISOU 1850  N   LEU A 231     3123   3228   3024   -235   -260    325       N  
ATOM   1851  CA  LEU A 231     -27.331 -36.272 -26.275  1.00 26.49           C  
ANISOU 1851  CA  LEU A 231     3345   3471   3250   -216   -325    292       C  
ATOM   1852  C   LEU A 231     -27.803 -34.926 -26.804  1.00 22.24           C  
ANISOU 1852  C   LEU A 231     2853   2923   2675   -161   -374    288       C  
ATOM   1853  O   LEU A 231     -27.554 -33.881 -26.195  1.00 22.89           O  
ANISOU 1853  O   LEU A 231     2939   2999   2758   -149   -355    307       O  
ATOM   1854  CB  LEU A 231     -28.345 -36.767 -25.241  1.00 23.20           C  
ANISOU 1854  CB  LEU A 231     2837   3090   2888   -242   -330    263       C  
ATOM   1855  CG  LEU A 231     -28.045 -38.160 -24.710  1.00 18.70           C  
ANISOU 1855  CG  LEU A 231     2257   2509   2338   -293   -281    267       C  
ATOM   1856  CD1 LEU A 231     -28.793 -38.380 -23.372  1.00 18.84           C  
ANISOU 1856  CD1 LEU A 231     2214   2546   2397   -328   -249    252       C  
ATOM   1857  CD2 LEU A 231     -28.461 -39.223 -25.761  1.00 16.41           C  
ANISOU 1857  CD2 LEU A 231     1987   2206   2040   -313   -303    233       C  
ATOM   1858  N   TRP A 232     -28.508 -34.968 -27.938  1.00 19.36           N  
ANISOU 1858  N   TRP A 232     2534   2551   2271   -120   -443    258       N  
ATOM   1859  CA  TRP A 232     -29.248 -33.835 -28.484  1.00 22.91           C  
ANISOU 1859  CA  TRP A 232     3039   2990   2675    -40   -519    241       C  
ATOM   1860  C   TRP A 232     -28.412 -32.552 -28.538  1.00 24.98           C  
ANISOU 1860  C   TRP A 232     3411   3195   2885    -21   -474    290       C  
ATOM   1861  O   TRP A 232     -28.615 -31.629 -27.738  1.00 25.54           O  
ANISOU 1861  O   TRP A 232     3458   3271   2976     -3   -472    295       O  
ATOM   1862  CB  TRP A 232     -30.533 -33.623 -27.666  1.00 21.49           C  
ANISOU 1862  CB  TRP A 232     2736   2870   2557    -15   -575    186       C  
ATOM   1863  CG  TRP A 232     -31.587 -32.831 -28.400  1.00 21.35           C  
ANISOU 1863  CG  TRP A 232     2752   2860   2502     91   -692    135       C  
ATOM   1864  CD1 TRP A 232     -31.514 -32.361 -29.680  1.00 24.35           C  
ANISOU 1864  CD1 TRP A 232     3280   3188   2785    169   -754    141       C  
ATOM   1865  CD2 TRP A 232     -32.868 -32.423 -27.895  1.00 23.32           C  
ANISOU 1865  CD2 TRP A 232     2889   3169   2803    145   -764     61       C  
ATOM   1866  NE1 TRP A 232     -32.666 -31.694 -30.003  1.00 28.18           N  
ANISOU 1866  NE1 TRP A 232     3761   3696   3252    282   -877     76       N  
ATOM   1867  CE2 TRP A 232     -33.514 -31.718 -28.924  1.00 27.21           C  
ANISOU 1867  CE2 TRP A 232     3463   3647   3227    269   -886     20       C  
ATOM   1868  CE3 TRP A 232     -33.536 -32.602 -26.674  1.00 23.99           C  
ANISOU 1868  CE3 TRP A 232     2818   3315   2980    102   -733     18       C  
ATOM   1869  CZ2 TRP A 232     -34.797 -31.179 -28.772  1.00 30.20           C  
ANISOU 1869  CZ2 TRP A 232     3752   4083   3639    364   -992    -72       C  
ATOM   1870  CZ3 TRP A 232     -34.811 -32.060 -26.523  1.00 23.54           C  
ANISOU 1870  CZ3 TRP A 232     2668   3316   2962    178   -817    -73       C  
ATOM   1871  CH2 TRP A 232     -35.425 -31.361 -27.563  1.00 29.48           C  
ANISOU 1871  CH2 TRP A 232     3482   4062   3655    312   -951   -122       C  
ATOM   1872  N   THR A 233     -27.507 -32.463 -29.514  1.00 22.03           N  
ANISOU 1872  N   THR A 233     3166   2761   2443    -31   -428    319       N  
ATOM   1873  CA  THR A 233     -26.518 -31.389 -29.594  1.00 24.34           C  
ANISOU 1873  CA  THR A 233     3567   2988   2692    -49   -347    357       C  
ATOM   1874  C   THR A 233     -26.845 -30.320 -30.643  1.00 28.56           C  
ANISOU 1874  C   THR A 233     4290   3444   3117     27   -383    367       C  
ATOM   1875  O   THR A 233     -26.104 -29.337 -30.759  1.00 28.17           O  
ANISOU 1875  O   THR A 233     4358   3322   3021      5   -304    395       O  
ATOM   1876  CB  THR A 233     -25.143 -31.986 -29.914  1.00 27.70           C  
ANISOU 1876  CB  THR A 233     4011   3394   3119   -126   -239    371       C  
ATOM   1877  OG1 THR A 233     -25.237 -32.750 -31.131  1.00 24.71           O  
ANISOU 1877  OG1 THR A 233     3709   2995   2684   -109   -261    362       O  
ATOM   1878  CG2 THR A 233     -24.669 -32.897 -28.772  1.00 19.59           C  
ANISOU 1878  CG2 THR A 233     2825   2432   2188   -180   -207    362       C  
ATOM   1879  N   ASP A 234     -27.901 -30.492 -31.422  1.00 24.94           N  
ANISOU 1879  N   ASP A 234     3876   2990   2609    116   -500    337       N  
ATOM   1880  CA  ASP A 234     -28.224 -29.559 -32.490  1.00 27.86           C  
ANISOU 1880  CA  ASP A 234     4458   3276   2853    212   -553    345       C  
ATOM   1881  C   ASP A 234     -29.215 -28.513 -32.006  1.00 32.23           C  
ANISOU 1881  C   ASP A 234     5010   3833   3403    313   -647    325       C  
ATOM   1882  O   ASP A 234     -30.081 -28.790 -31.173  1.00 29.17           O  
ANISOU 1882  O   ASP A 234     4441   3536   3107    331   -714    280       O  
ATOM   1883  CB  ASP A 234     -28.810 -30.281 -33.705  1.00 28.13           C  
ANISOU 1883  CB  ASP A 234     4559   3310   2819    278   -650    312       C  
ATOM   1884  CG  ASP A 234     -30.167 -30.901 -33.423  1.00 31.09           C  
ANISOU 1884  CG  ASP A 234     4764   3785   3263    337   -793    235       C  
ATOM   1885  OD1 ASP A 234     -30.216 -31.872 -32.643  1.00 29.15           O  
ANISOU 1885  OD1 ASP A 234     4328   3617   3129    256   -764    214       O  
ATOM   1886  OD2 ASP A 234     -31.176 -30.423 -33.981  1.00 28.95           O  
ANISOU 1886  OD2 ASP A 234     4554   3512   2933    467   -932    188       O  
ATOM   1887  N   GLY A 235     -29.090 -27.308 -32.558  1.00 33.75           N  
ANISOU 1887  N   GLY A 235     5420   3919   3483    378   -642    355       N  
ATOM   1888  CA  GLY A 235     -29.969 -26.222 -32.187  1.00 30.34           C  
ANISOU 1888  CA  GLY A 235     5022   3474   3032    493   -732    337       C  
ATOM   1889  C   GLY A 235     -29.767 -25.708 -30.785  1.00 31.46           C  
ANISOU 1889  C   GLY A 235     5035   3649   3272    431   -666    346       C  
ATOM   1890  O   GLY A 235     -30.672 -25.071 -30.235  1.00 33.70           O  
ANISOU 1890  O   GLY A 235     5271   3957   3576    522   -750    313       O  
ATOM   1891  N   VAL A 236     -28.606 -25.973 -30.189  1.00 29.66           N  
ANISOU 1891  N   VAL A 236     4745   3423   3102    289   -523    380       N  
ATOM   1892  CA  VAL A 236     -28.306 -25.595 -28.810  1.00 33.39           C  
ANISOU 1892  CA  VAL A 236     5089   3931   3665    224   -462    384       C  
ATOM   1893  C   VAL A 236     -27.641 -24.226 -28.813  1.00 39.25           C  
ANISOU 1893  C   VAL A 236     6010   4560   4343    208   -378    417       C  
ATOM   1894  O   VAL A 236     -26.688 -23.996 -29.565  1.00 46.77           O  
ANISOU 1894  O   VAL A 236     7118   5423   5229    148   -276    446       O  
ATOM   1895  CB  VAL A 236     -27.387 -26.640 -28.143  1.00 36.60           C  
ANISOU 1895  CB  VAL A 236     5336   4405   4167     94   -371    388       C  
ATOM   1896  CG1 VAL A 236     -26.839 -26.130 -26.831  1.00 43.33           C  
ANISOU 1896  CG1 VAL A 236     6101   5275   5087     29   -301    391       C  
ATOM   1897  CG2 VAL A 236     -28.102 -27.924 -27.928  1.00 31.21           C  
ANISOU 1897  CG2 VAL A 236     4488   3821   3551    100   -440    354       C  
ATOM   1898  N   GLU A 237     -28.142 -23.312 -27.981  1.00 34.06           N  
ANISOU 1898  N   GLU A 237     5336   3900   3706    256   -408    408       N  
ATOM   1899  CA  GLU A 237     -27.478 -22.032 -27.752  1.00 34.04           C  
ANISOU 1899  CA  GLU A 237     5482   3791   3661    221   -314    432       C  
ATOM   1900  C   GLU A 237     -26.533 -22.189 -26.569  1.00 37.72           C  
ANISOU 1900  C   GLU A 237     5790   4309   4232     85   -210    425       C  
ATOM   1901  O   GLU A 237     -26.976 -22.498 -25.458  1.00 30.94           O  
ANISOU 1901  O   GLU A 237     4749   3545   3460     90   -253    402       O  
ATOM   1902  CB  GLU A 237     -28.486 -20.911 -27.483  1.00 37.04           C  
ANISOU 1902  CB  GLU A 237     5945   4130   4000    355   -405    420       C  
ATOM   1903  CG  GLU A 237     -29.158 -20.377 -28.735  1.00 54.90           C  
ANISOU 1903  CG  GLU A 237     8443   6295   6121    503   -496    428       C  
ATOM   1904  CD  GLU A 237     -28.153 -19.840 -29.736  1.00 69.15           C  
ANISOU 1904  CD  GLU A 237    10524   7945   7805    444   -375    477       C  
ATOM   1905  OE1 GLU A 237     -27.247 -19.088 -29.320  1.00 78.42           O  
ANISOU 1905  OE1 GLU A 237    11772   9042   8982    335   -236    496       O  
ATOM   1906  OE2 GLU A 237     -28.259 -20.182 -30.933  1.00 75.93           O  
ANISOU 1906  OE2 GLU A 237    11527   8758   8565    498   -411    489       O  
ATOM   1907  N   GLU A 238     -25.236 -21.977 -26.805  1.00 33.64           N  
ANISOU 1907  N   GLU A 238     5346   3732   3706    -35    -73    435       N  
ATOM   1908  CA  GLU A 238     -24.258 -22.154 -25.735  1.00 32.76           C  
ANISOU 1908  CA  GLU A 238     5077   3678   3694   -154     11    409       C  
ATOM   1909  C   GLU A 238     -24.502 -21.193 -24.577  1.00 29.39           C  
ANISOU 1909  C   GLU A 238     4619   3247   3299   -143      3    395       C  
ATOM   1910  O   GLU A 238     -24.168 -21.515 -23.427  1.00 27.85           O  
ANISOU 1910  O   GLU A 238     4255   3136   3192   -193     10    369       O  
ATOM   1911  CB  GLU A 238     -22.841 -21.996 -26.284  1.00 38.86           C  
ANISOU 1911  CB  GLU A 238     5925   4385   4454   -283    164    397       C  
ATOM   1912  CG  GLU A 238     -22.418 -23.169 -27.153  1.00 52.50           C  
ANISOU 1912  CG  GLU A 238     7623   6146   6179   -311    184    398       C  
ATOM   1913  CD  GLU A 238     -20.972 -23.087 -27.621  1.00 57.82           C  
ANISOU 1913  CD  GLU A 238     8335   6773   6859   -446    348    365       C  
ATOM   1914  OE1 GLU A 238     -20.278 -22.089 -27.311  1.00 54.01           O  
ANISOU 1914  OE1 GLU A 238     7908   6229   6386   -531    453    337       O  
ATOM   1915  OE2 GLU A 238     -20.537 -24.033 -28.310  1.00 62.57           O  
ANISOU 1915  OE2 GLU A 238     8910   7402   7463   -471    376    359       O  
ATOM   1916  N   SER A 239     -25.097 -20.026 -24.850  1.00 23.66           N  
ANISOU 1916  N   SER A 239     4070   2423   2495    -67    -20    410       N  
ATOM   1917  CA  SER A 239     -25.428 -19.107 -23.756  1.00 29.26           C  
ANISOU 1917  CA  SER A 239     4757   3128   3232    -44    -35    394       C  
ATOM   1918  C   SER A 239     -26.585 -19.605 -22.886  1.00 33.10           C  
ANISOU 1918  C   SER A 239     5068   3730   3779     49   -154    377       C  
ATOM   1919  O   SER A 239     -26.872 -18.979 -21.854  1.00 28.06           O  
ANISOU 1919  O   SER A 239     4385   3105   3173     66   -165    359       O  
ATOM   1920  CB  SER A 239     -25.741 -17.712 -24.315  1.00 28.75           C  
ANISOU 1920  CB  SER A 239     4952   2912   3059     22    -24    412       C  
ATOM   1921  OG  SER A 239     -26.856 -17.742 -25.185  1.00 37.82           O  
ANISOU 1921  OG  SER A 239     6206   4036   4127    178   -142    431       O  
ATOM   1922  N   ASP A 240     -27.248 -20.710 -23.260  1.00 27.56           N  
ANISOU 1922  N   ASP A 240     4267   3110   3095     99   -234    376       N  
ATOM   1923  CA  ASP A 240     -28.272 -21.338 -22.422  1.00 29.94           C  
ANISOU 1923  CA  ASP A 240     4385   3525   3466    154   -317    347       C  
ATOM   1924  C   ASP A 240     -27.758 -22.518 -21.603  1.00 27.50           C  
ANISOU 1924  C   ASP A 240     3894   3314   3242     61   -280    340       C  
ATOM   1925  O   ASP A 240     -28.530 -23.092 -20.820  1.00 29.28           O  
ANISOU 1925  O   ASP A 240     3981   3623   3521     84   -322    316       O  
ATOM   1926  CB  ASP A 240     -29.450 -21.831 -23.270  1.00 27.61           C  
ANISOU 1926  CB  ASP A 240     4084   3261   3145    267   -430    330       C  
ATOM   1927  CG  ASP A 240     -30.193 -20.701 -23.951  1.00 36.83           C  
ANISOU 1927  CG  ASP A 240     5426   4344   4226    404   -504    324       C  
ATOM   1928  OD1 ASP A 240     -30.236 -19.593 -23.379  1.00 37.09           O  
ANISOU 1928  OD1 ASP A 240     5527   4324   4244    433   -487    323       O  
ATOM   1929  OD2 ASP A 240     -30.723 -20.926 -25.054  1.00 45.19           O  
ANISOU 1929  OD2 ASP A 240     6562   5386   5224    491   -584    317       O  
ATOM   1930  N   LEU A 241     -26.502 -22.915 -21.770  1.00 21.49           N  
ANISOU 1930  N   LEU A 241     3135   2541   2489    -40   -201    352       N  
ATOM   1931  CA  LEU A 241     -25.993 -24.110 -21.094  1.00 21.08           C  
ANISOU 1931  CA  LEU A 241     2933   2575   2503   -103   -182    343       C  
ATOM   1932  C   LEU A 241     -25.702 -23.800 -19.625  1.00 27.14           C  
ANISOU 1932  C   LEU A 241     3618   3377   3317   -134   -161    323       C  
ATOM   1933  O   LEU A 241     -24.793 -23.019 -19.324  1.00 29.36           O  
ANISOU 1933  O   LEU A 241     3938   3619   3598   -187   -104    309       O  
ATOM   1934  CB  LEU A 241     -24.730 -24.619 -21.785  1.00 18.89           C  
ANISOU 1934  CB  LEU A 241     2677   2279   2222   -182   -113    347       C  
ATOM   1935  CG  LEU A 241     -24.926 -25.011 -23.245  1.00 24.99           C  
ANISOU 1935  CG  LEU A 241     3543   3013   2940   -157   -126    367       C  
ATOM   1936  CD1 LEU A 241     -23.565 -25.288 -23.825  1.00 27.63           C  
ANISOU 1936  CD1 LEU A 241     3905   3321   3273   -246    -32    361       C  
ATOM   1937  CD2 LEU A 241     -25.857 -26.225 -23.359  1.00 25.24           C  
ANISOU 1937  CD2 LEU A 241     3483   3116   2993   -110   -205    367       C  
ATOM   1938  N   ILE A 242     -26.436 -24.454 -18.717  1.00 22.98           N  
ANISOU 1938  N   ILE A 242     2983   2923   2827   -108   -199    314       N  
ATOM   1939  CA  ILE A 242     -26.341 -24.137 -17.288  1.00 22.98           C  
ANISOU 1939  CA  ILE A 242     2927   2951   2853   -120   -186    295       C  
ATOM   1940  C   ILE A 242     -24.908 -24.309 -16.798  1.00 23.05           C  
ANISOU 1940  C   ILE A 242     2910   2968   2879   -191   -142    280       C  
ATOM   1941  O   ILE A 242     -24.307 -23.394 -16.223  1.00 21.62           O  
ANISOU 1941  O   ILE A 242     2751   2763   2701   -219   -116    255       O  
ATOM   1942  CB  ILE A 242     -27.308 -25.015 -16.476  1.00 21.79           C  
ANISOU 1942  CB  ILE A 242     2681   2868   2729    -94   -212    288       C  
ATOM   1943  CG1 ILE A 242     -28.753 -24.845 -16.976  1.00 24.50           C  
ANISOU 1943  CG1 ILE A 242     3016   3220   3072    -24   -259    273       C  
ATOM   1944  CG2 ILE A 242     -27.140 -24.715 -14.951  1.00 21.91           C  
ANISOU 1944  CG2 ILE A 242     2664   2906   2755   -105   -192    271       C  
ATOM   1945  CD1 ILE A 242     -29.290 -23.420 -16.922  1.00 26.47           C  
ANISOU 1945  CD1 ILE A 242     3328   3428   3301     41   -280    258       C  
ATOM   1946  N   ILE A 243     -24.351 -25.500 -16.990  1.00 20.40           N  
ANISOU 1946  N   ILE A 243     2522   2668   2559   -216   -140    284       N  
ATOM   1947  CA  ILE A 243     -22.924 -25.712 -16.759  1.00 21.62           C  
ANISOU 1947  CA  ILE A 243     2643   2836   2735   -269   -110    252       C  
ATOM   1948  C   ILE A 243     -22.209 -25.234 -18.015  1.00 25.50           C  
ANISOU 1948  C   ILE A 243     3198   3274   3218   -316    -56    245       C  
ATOM   1949  O   ILE A 243     -22.401 -25.836 -19.086  1.00 24.25           O  
ANISOU 1949  O   ILE A 243     3070   3103   3041   -309    -55    271       O  
ATOM   1950  CB  ILE A 243     -22.594 -27.177 -16.443  1.00 22.97           C  
ANISOU 1950  CB  ILE A 243     2747   3061   2919   -259   -132    253       C  
ATOM   1951  CG1 ILE A 243     -23.407 -27.654 -15.241  1.00 24.15           C  
ANISOU 1951  CG1 ILE A 243     2872   3244   3061   -220   -164    265       C  
ATOM   1952  CG2 ILE A 243     -21.083 -27.321 -16.182  1.00 21.04           C  
ANISOU 1952  CG2 ILE A 243     2452   2840   2701   -292   -118    198       C  
ATOM   1953  CD1 ILE A 243     -23.234 -29.134 -14.909  1.00 24.03           C  
ANISOU 1953  CD1 ILE A 243     2831   3258   3040   -204   -180    275       C  
ATOM   1954  N   PRO A 244     -21.383 -24.180 -17.936  1.00 23.22           N  
ANISOU 1954  N   PRO A 244     2940   2946   2936   -372     -2    205       N  
ATOM   1955  CA  PRO A 244     -20.790 -23.609 -19.154  1.00 22.48           C  
ANISOU 1955  CA  PRO A 244     2939   2780   2823   -431     76    198       C  
ATOM   1956  C   PRO A 244     -19.955 -24.618 -19.930  1.00 26.05           C  
ANISOU 1956  C   PRO A 244     3347   3258   3294   -467    109    181       C  
ATOM   1957  O   PRO A 244     -19.334 -25.515 -19.357  1.00 24.03           O  
ANISOU 1957  O   PRO A 244     2973   3075   3081   -466     85    147       O  
ATOM   1958  CB  PRO A 244     -19.905 -22.473 -18.619  1.00 24.03           C  
ANISOU 1958  CB  PRO A 244     3142   2944   3043   -507    140    135       C  
ATOM   1959  CG  PRO A 244     -20.464 -22.156 -17.227  1.00 24.29           C  
ANISOU 1959  CG  PRO A 244     3128   3015   3087   -458     74    130       C  
ATOM   1960  CD  PRO A 244     -20.948 -23.480 -16.709  1.00 28.34           C  
ANISOU 1960  CD  PRO A 244     3548   3611   3609   -392     -3    157       C  
ATOM   1961  N   LYS A 245     -19.942 -24.441 -21.260  1.00 23.95           N  
ANISOU 1961  N   LYS A 245     3192   2923   2983   -489    164    204       N  
ATOM   1962  CA  LYS A 245     -19.018 -25.177 -22.121  1.00 24.96           C  
ANISOU 1962  CA  LYS A 245     3298   3060   3124   -539    225    177       C  
ATOM   1963  C   LYS A 245     -17.597 -25.137 -21.581  1.00 25.30           C  
ANISOU 1963  C   LYS A 245     3224   3148   3242   -618    285     82       C  
ATOM   1964  O   LYS A 245     -16.897 -26.156 -21.588  1.00 21.83           O  
ANISOU 1964  O   LYS A 245     2677   2773   2844   -617    279     43       O  
ATOM   1965  CB  LYS A 245     -19.035 -24.594 -23.543  1.00 22.30           C  
ANISOU 1965  CB  LYS A 245     3136   2619   2716   -572    307    202       C  
ATOM   1966  CG  LYS A 245     -18.041 -25.244 -24.480  1.00 26.02           C  
ANISOU 1966  CG  LYS A 245     3599   3090   3198   -634    394    167       C  
ATOM   1967  CD  LYS A 245     -18.086 -24.644 -25.900  1.00 25.42           C  
ANISOU 1967  CD  LYS A 245     3733   2895   3030   -666    486    196       C  
ATOM   1968  CE  LYS A 245     -17.070 -25.319 -26.810  1.00 37.04           C  
ANISOU 1968  CE  LYS A 245     5192   4369   4513   -735    589    153       C  
ATOM   1969  NZ  LYS A 245     -16.905 -24.595 -28.122  1.00 44.53           N  
ANISOU 1969  NZ  LYS A 245     6370   5186   5364   -790    715    170       N  
ATOM   1970  N   SER A 246     -17.145 -23.955 -21.143  1.00 23.03           N  
ANISOU 1970  N   SER A 246     2955   2823   2971   -684    343     33       N  
ATOM   1971  CA  SER A 246     -15.780 -23.762 -20.654  1.00 22.56           C  
ANISOU 1971  CA  SER A 246     2773   2807   2991   -770    403    -84       C  
ATOM   1972  C   SER A 246     -15.523 -24.457 -19.312  1.00 21.97           C  
ANISOU 1972  C   SER A 246     2531   2845   2971   -708    294   -129       C  
ATOM   1973  O   SER A 246     -14.370 -24.455 -18.848  1.00 24.37           O  
ANISOU 1973  O   SER A 246     2708   3206   3347   -755    313   -243       O  
ATOM   1974  CB  SER A 246     -15.486 -22.262 -20.531  1.00 24.26           C  
ANISOU 1974  CB  SER A 246     3069   2942   3206   -864    496   -128       C  
ATOM   1975  OG  SER A 246     -16.399 -21.689 -19.607  1.00 30.02           O  
ANISOU 1975  OG  SER A 246     3834   3663   3910   -800    413    -82       O  
ATOM   1976  N   LEU A 247     -16.555 -25.052 -18.699  1.00 21.03           N  
ANISOU 1976  N   LEU A 247     2417   2755   2819   -604    184    -52       N  
ATOM   1977  CA  LEU A 247     -16.408 -25.854 -17.484  1.00 23.86           C  
ANISOU 1977  CA  LEU A 247     2663   3202   3202   -532     83    -77       C  
ATOM   1978  C   LEU A 247     -16.792 -27.309 -17.734  1.00 27.35           C  
ANISOU 1978  C   LEU A 247     3091   3676   3624   -457     26    -23       C  
ATOM   1979  O   LEU A 247     -17.348 -27.977 -16.851  1.00 23.17           O  
ANISOU 1979  O   LEU A 247     2549   3180   3073   -381    -55     11       O  
ATOM   1980  CB  LEU A 247     -17.253 -25.300 -16.341  1.00 25.80           C  
ANISOU 1980  CB  LEU A 247     2938   3445   3421   -487     21    -44       C  
ATOM   1981  CG  LEU A 247     -16.630 -24.160 -15.544  1.00 45.83           C  
ANISOU 1981  CG  LEU A 247     5444   5980   5989   -539     40   -127       C  
ATOM   1982  CD1 LEU A 247     -17.585 -23.807 -14.452  1.00 51.40           C  
ANISOU 1982  CD1 LEU A 247     6188   6685   6657   -479    -25    -84       C  
ATOM   1983  CD2 LEU A 247     -15.283 -24.548 -14.955  1.00 47.71           C  
ANISOU 1983  CD2 LEU A 247     5540   6298   6288   -549     12   -249       C  
ATOM   1984  N   ALA A 248     -16.520 -27.795 -18.948  1.00 24.11           N  
ANISOU 1984  N   ALA A 248     2701   3247   3213   -483     80    -16       N  
ATOM   1985  CA  ALA A 248     -16.831 -29.163 -19.362  1.00 21.70           C  
ANISOU 1985  CA  ALA A 248     2395   2961   2888   -424     39     29       C  
ATOM   1986  C   ALA A 248     -18.331 -29.448 -19.352  1.00 21.91           C  
ANISOU 1986  C   ALA A 248     2501   2961   2862   -373    -11    128       C  
ATOM   1987  O   ALA A 248     -18.750 -30.603 -19.226  1.00 23.90           O  
ANISOU 1987  O   ALA A 248     2747   3234   3100   -321    -59    161       O  
ATOM   1988  CB  ALA A 248     -16.070 -30.194 -18.513  1.00 21.02           C  
ANISOU 1988  CB  ALA A 248     2205   2948   2832   -361    -28    -26       C  
ATOM   1989  N   GLY A 249     -19.160 -28.421 -19.533  1.00 23.29           N  
ANISOU 1989  N   GLY A 249     2754   3086   3008   -388      4    166       N  
ATOM   1990  CA  GLY A 249     -20.582 -28.641 -19.644  1.00 22.36           C  
ANISOU 1990  CA  GLY A 249     2690   2953   2852   -340    -42    234       C  
ATOM   1991  C   GLY A 249     -20.916 -29.334 -20.961  1.00 21.43           C  
ANISOU 1991  C   GLY A 249     2624   2811   2707   -335    -35    266       C  
ATOM   1992  O   GLY A 249     -20.419 -28.952 -22.022  1.00 23.42           O  
ANISOU 1992  O   GLY A 249     2937   3021   2942   -373     24    258       O  
ATOM   1993  N   PRO A 250     -21.760 -30.367 -20.920  1.00 22.50           N  
ANISOU 1993  N   PRO A 250     2746   2969   2835   -294    -85    297       N  
ATOM   1994  CA  PRO A 250     -22.231 -30.980 -22.177  1.00 22.21           C  
ANISOU 1994  CA  PRO A 250     2761   2909   2768   -285    -90    320       C  
ATOM   1995  C   PRO A 250     -22.987 -29.969 -23.023  1.00 22.53           C  
ANISOU 1995  C   PRO A 250     2897   2899   2764   -271    -96    340       C  
ATOM   1996  O   PRO A 250     -23.822 -29.212 -22.516  1.00 22.74           O  
ANISOU 1996  O   PRO A 250     2932   2923   2787   -241   -129    347       O  
ATOM   1997  CB  PRO A 250     -23.156 -32.111 -21.710  1.00 22.56           C  
ANISOU 1997  CB  PRO A 250     2765   2985   2820   -255   -141    337       C  
ATOM   1998  CG  PRO A 250     -22.667 -32.443 -20.281  1.00 21.68           C  
ANISOU 1998  CG  PRO A 250     2593   2909   2735   -249   -145    324       C  
ATOM   1999  CD  PRO A 250     -22.218 -31.093 -19.720  1.00 22.88           C  
ANISOU 1999  CD  PRO A 250     2739   3057   2896   -262   -129    304       C  
ATOM   2000  N   LEU A 251     -22.695 -29.969 -24.329  1.00 24.16           N  
ANISOU 2000  N   LEU A 251     3189   3060   2929   -283    -65    345       N  
ATOM   2001  CA  LEU A 251     -23.318 -29.029 -25.271  1.00 23.54           C  
ANISOU 2001  CA  LEU A 251     3244   2916   2784   -253    -75    364       C  
ATOM   2002  C   LEU A 251     -24.649 -29.611 -25.749  1.00 22.88           C  
ANISOU 2002  C   LEU A 251     3165   2850   2677   -185   -169    374       C  
ATOM   2003  O   LEU A 251     -24.796 -30.056 -26.890  1.00 25.52           O  
ANISOU 2003  O   LEU A 251     3571   3160   2965   -168   -184    378       O  
ATOM   2004  CB  LEU A 251     -22.391 -28.747 -26.449  1.00 27.07           C  
ANISOU 2004  CB  LEU A 251     3807   3296   3182   -298     11    362       C  
ATOM   2005  CG  LEU A 251     -20.953 -28.327 -26.138  1.00 30.99           C  
ANISOU 2005  CG  LEU A 251     4274   3783   3716   -385    122    324       C  
ATOM   2006  CD1 LEU A 251     -20.238 -27.878 -27.421  1.00 29.25           C  
ANISOU 2006  CD1 LEU A 251     4200   3480   3435   -439    229    318       C  
ATOM   2007  CD2 LEU A 251     -20.947 -27.229 -25.085  1.00 27.35           C  
ANISOU 2007  CD2 LEU A 251     3792   3319   3283   -399    128    312       C  
ATOM   2008  N   SER A 252     -25.643 -29.572 -24.858  1.00 20.55           N  
ANISOU 2008  N   SER A 252     2791   2600   2417   -148   -229    366       N  
ATOM   2009  CA  SER A 252     -26.834 -30.413 -24.949  1.00 23.44           C  
ANISOU 2009  CA  SER A 252     3096   3011   2800   -111   -304    348       C  
ATOM   2010  C   SER A 252     -28.066 -29.638 -24.510  1.00 23.47           C  
ANISOU 2010  C   SER A 252     3074   3031   2810    -47   -369    326       C  
ATOM   2011  O   SER A 252     -28.003 -28.823 -23.588  1.00 23.45           O  
ANISOU 2011  O   SER A 252     3054   3029   2825    -47   -348    329       O  
ATOM   2012  CB  SER A 252     -26.693 -31.655 -24.050  1.00 20.44           C  
ANISOU 2012  CB  SER A 252     2603   2685   2480   -156   -284    341       C  
ATOM   2013  OG  SER A 252     -27.889 -32.443 -24.034  1.00 22.34           O  
ANISOU 2013  OG  SER A 252     2780   2964   2745   -143   -334    312       O  
ATOM   2014  N   HIS A 253     -29.207 -29.931 -25.140  1.00 21.44           N  
ANISOU 2014  N   HIS A 253     2803   2797   2546     10   -451    290       N  
ATOM   2015  CA  HIS A 253     -30.462 -29.455 -24.572  1.00 17.81           C  
ANISOU 2015  CA  HIS A 253     2269   2379   2119     69   -512    244       C  
ATOM   2016  C   HIS A 253     -30.699 -30.017 -23.175  1.00 24.82           C  
ANISOU 2016  C   HIS A 253     3021   3326   3085     10   -465    228       C  
ATOM   2017  O   HIS A 253     -31.473 -29.439 -22.415  1.00 24.94           O  
ANISOU 2017  O   HIS A 253     2976   3370   3131     42   -481    195       O  
ATOM   2018  CB  HIS A 253     -31.644 -29.810 -25.481  1.00 18.03           C  
ANISOU 2018  CB  HIS A 253     2274   2438   2140    139   -616    181       C  
ATOM   2019  CG  HIS A 253     -31.653 -29.047 -26.769  1.00 22.23           C  
ANISOU 2019  CG  HIS A 253     2967   2906   2575    232   -685    190       C  
ATOM   2020  ND1 HIS A 253     -32.176 -27.776 -26.875  1.00 31.17           N  
ANISOU 2020  ND1 HIS A 253     4176   4005   3662    338   -748    177       N  
ATOM   2021  CD2 HIS A 253     -31.186 -29.364 -27.999  1.00 19.68           C  
ANISOU 2021  CD2 HIS A 253     2765   2534   2179    239   -696    211       C  
ATOM   2022  CE1 HIS A 253     -32.052 -27.351 -28.123  1.00 33.29           C  
ANISOU 2022  CE1 HIS A 253     4621   4200   3825    412   -798    193       C  
ATOM   2023  NE2 HIS A 253     -31.449 -28.294 -28.825  1.00 28.16           N  
ANISOU 2023  NE2 HIS A 253     4002   3542   3157    350   -764    214       N  
ATOM   2024  N   HIS A 254     -30.057 -31.137 -22.824  1.00 20.29           N  
ANISOU 2024  N   HIS A 254     2412   2762   2534    -67   -407    248       N  
ATOM   2025  CA  HIS A 254     -30.224 -31.711 -21.491  1.00 24.18           C  
ANISOU 2025  CA  HIS A 254     2819   3290   3078   -119   -355    241       C  
ATOM   2026  C   HIS A 254     -29.582 -30.841 -20.414  1.00 27.92           C  
ANISOU 2026  C   HIS A 254     3309   3753   3549   -122   -314    269       C  
ATOM   2027  O   HIS A 254     -29.924 -30.978 -19.231  1.00 25.37           O  
ANISOU 2027  O   HIS A 254     2932   3455   3254   -143   -280    258       O  
ATOM   2028  CB  HIS A 254     -29.624 -33.117 -21.451  1.00 22.61           C  
ANISOU 2028  CB  HIS A 254     2617   3087   2885   -182   -311    259       C  
ATOM   2029  CG  HIS A 254     -30.387 -34.121 -22.261  1.00 24.20           C  
ANISOU 2029  CG  HIS A 254     2790   3303   3101   -197   -339    218       C  
ATOM   2030  ND1 HIS A 254     -31.218 -35.055 -21.686  1.00 27.53           N  
ANISOU 2030  ND1 HIS A 254     3141   3752   3569   -248   -309    176       N  
ATOM   2031  CD2 HIS A 254     -30.452 -34.330 -23.601  1.00 18.39           C  
ANISOU 2031  CD2 HIS A 254     2094   2556   2338   -172   -391    206       C  
ATOM   2032  CE1 HIS A 254     -31.766 -35.798 -22.635  1.00 27.21           C  
ANISOU 2032  CE1 HIS A 254     3082   3719   3537   -260   -344    132       C  
ATOM   2033  NE2 HIS A 254     -31.312 -35.385 -23.807  1.00 20.33           N  
ANISOU 2033  NE2 HIS A 254     2279   2828   2619   -208   -402    151       N  
ATOM   2034  N   ASN A 255     -28.645 -29.975 -20.802  1.00 19.76           N  
ANISOU 2034  N   ASN A 255     2354   2675   2477   -110   -308    300       N  
ATOM   2035  CA  ASN A 255     -27.942 -29.032 -19.924  1.00 23.17           C  
ANISOU 2035  CA  ASN A 255     2806   3090   2906   -118   -273    315       C  
ATOM   2036  C   ASN A 255     -28.545 -27.636 -20.055  1.00 23.23           C  
ANISOU 2036  C   ASN A 255     2861   3072   2895    -59   -304    303       C  
ATOM   2037  O   ASN A 255     -27.839 -26.634 -20.202  1.00 23.09           O  
ANISOU 2037  O   ASN A 255     2924   3002   2846    -60   -282    319       O  
ATOM   2038  CB  ASN A 255     -26.446 -29.054 -20.269  1.00 23.20           C  
ANISOU 2038  CB  ASN A 255     2859   3063   2893   -160   -230    336       C  
ATOM   2039  CG  ASN A 255     -25.568 -28.162 -19.392  1.00 24.39           C  
ANISOU 2039  CG  ASN A 255     3016   3202   3050   -182   -193    332       C  
ATOM   2040  OD1 ASN A 255     -25.902 -27.814 -18.254  1.00 24.37           O  
ANISOU 2040  OD1 ASN A 255     2977   3220   3061   -172   -196    322       O  
ATOM   2041  ND2 ASN A 255     -24.388 -27.814 -19.933  1.00 19.89           N  
ANISOU 2041  ND2 ASN A 255     2490   2599   2470   -221   -151    329       N  
ATOM   2042  N   THR A 256     -29.875 -27.550 -20.029  1.00 19.89           N  
ANISOU 2042  N   THR A 256     2389   2681   2489     -5   -354    266       N  
ATOM   2043  CA  THR A 256     -30.570 -26.275 -20.111  1.00 21.28           C  
ANISOU 2043  CA  THR A 256     2606   2834   2644     76   -399    245       C  
ATOM   2044  C   THR A 256     -31.727 -26.291 -19.129  1.00 27.02           C  
ANISOU 2044  C   THR A 256     3219   3623   3424    101   -408    192       C  
ATOM   2045  O   THR A 256     -32.188 -27.353 -18.706  1.00 23.88           O  
ANISOU 2045  O   THR A 256     2722   3280   3072     55   -386    166       O  
ATOM   2046  CB  THR A 256     -31.120 -25.980 -21.516  1.00 28.20           C  
ANISOU 2046  CB  THR A 256     3561   3681   3474    159   -478    231       C  
ATOM   2047  OG1 THR A 256     -32.151 -26.925 -21.823  1.00 28.31           O  
ANISOU 2047  OG1 THR A 256     3469   3760   3526    177   -532    177       O  
ATOM   2048  CG2 THR A 256     -30.009 -26.036 -22.578  1.00 26.03           C  
ANISOU 2048  CG2 THR A 256     3414   3338   3139    126   -450    280       C  
ATOM   2049  N   ARG A 257     -32.215 -25.097 -18.790  1.00 25.51           N  
ANISOU 2049  N   ARG A 257     3053   3417   3224    170   -432    170       N  
ATOM   2050  CA  ARG A 257     -33.372 -24.973 -17.908  1.00 21.51           C  
ANISOU 2050  CA  ARG A 257     2435   2970   2769    203   -436    106       C  
ATOM   2051  C   ARG A 257     -34.052 -23.651 -18.204  1.00 25.95           C  
ANISOU 2051  C   ARG A 257     3048   3505   3307    326   -506     71       C  
ATOM   2052  O   ARG A 257     -33.405 -22.600 -18.149  1.00 24.20           O  
ANISOU 2052  O   ARG A 257     2949   3210   3035    347   -496    111       O  
ATOM   2053  CB  ARG A 257     -32.968 -25.049 -16.428  1.00 26.88           C  
ANISOU 2053  CB  ARG A 257     3082   3664   3469    134   -350    121       C  
ATOM   2054  CG  ARG A 257     -34.163 -25.012 -15.464  1.00 31.18           C  
ANISOU 2054  CG  ARG A 257     3515   4268   4065    151   -327     50       C  
ATOM   2055  CD  ARG A 257     -34.652 -26.413 -15.055  1.00 25.31           C  
ANISOU 2055  CD  ARG A 257     2668   3580   3369     70   -269     19       C  
ATOM   2056  NE  ARG A 257     -35.694 -26.342 -14.025  1.00 26.30           N  
ANISOU 2056  NE  ARG A 257     2697   3754   3541     65   -214    -53       N  
ATOM   2057  CZ  ARG A 257     -36.039 -27.344 -13.220  1.00 25.02           C  
ANISOU 2057  CZ  ARG A 257     2479   3621   3408    -24   -119    -77       C  
ATOM   2058  NH1 ARG A 257     -35.415 -28.520 -13.300  1.00 25.08           N  
ANISOU 2058  NH1 ARG A 257     2524   3608   3398   -105    -80    -29       N  
ATOM   2059  NH2 ARG A 257     -37.005 -27.171 -12.330  1.00 24.64           N  
ANISOU 2059  NH2 ARG A 257     2349   3613   3400    -31    -54   -151       N  
ATOM   2060  N   GLU A 258     -35.348 -23.714 -18.507  1.00 24.00           N  
ANISOU 2060  N   GLU A 258     2708   3316   3097    408   -577    -14       N  
ATOM   2061  CA  GLU A 258     -36.114 -22.533 -18.875  1.00 29.70           C  
ANISOU 2061  CA  GLU A 258     3475   4017   3792    557   -668    -63       C  
ATOM   2062  C   GLU A 258     -36.019 -21.439 -17.812  1.00 32.11           C  
ANISOU 2062  C   GLU A 258     3817   4292   4092    578   -624    -56       C  
ATOM   2063  O   GLU A 258     -36.199 -21.691 -16.619  1.00 27.03           O  
ANISOU 2063  O   GLU A 258     3071   3698   3503    514   -548    -77       O  
ATOM   2064  CB  GLU A 258     -37.574 -22.925 -19.094  1.00 36.04           C  
ANISOU 2064  CB  GLU A 258     4114   4917   4662    632   -745   -186       C  
ATOM   2065  CG  GLU A 258     -38.498 -21.731 -19.156  1.00 59.66           C  
ANISOU 2065  CG  GLU A 258     7114   7908   7644    801   -839   -261       C  
ATOM   2066  CD  GLU A 258     -39.063 -21.509 -20.530  1.00 82.48           C  
ANISOU 2066  CD  GLU A 258    10062  10788  10487    951   -993   -310       C  
ATOM   2067  OE1 GLU A 258     -40.262 -21.805 -20.718  1.00 91.64           O  
ANISOU 2067  OE1 GLU A 258    11060  12046  11715   1029  -1076   -441       O  
ATOM   2068  OE2 GLU A 258     -38.312 -21.049 -21.420  1.00 87.98           O  
ANISOU 2068  OE2 GLU A 258    10968  11380  11078    990  -1029   -227       O  
ATOM   2069  N   GLY A 259     -35.741 -20.214 -18.260  1.00 30.87           N  
ANISOU 2069  N   GLY A 259     3828   4042   3862    667   -667    -26       N  
ATOM   2070  CA  GLY A 259     -35.613 -19.074 -17.378  1.00 36.14           C  
ANISOU 2070  CA  GLY A 259     4557   4661   4513    693   -631    -20       C  
ATOM   2071  C   GLY A 259     -34.229 -18.857 -16.801  1.00 36.44           C  
ANISOU 2071  C   GLY A 259     4686   4634   4523    570   -530     60       C  
ATOM   2072  O   GLY A 259     -34.052 -17.929 -15.998  1.00 33.09           O  
ANISOU 2072  O   GLY A 259     4315   4171   4089    577   -495     61       O  
ATOM   2073  N   TYR A 260     -33.248 -19.684 -17.169  1.00 24.14           N  
ANISOU 2073  N   TYR A 260     3142   3071   2960    460   -486    116       N  
ATOM   2074  CA  TYR A 260     -31.873 -19.507 -16.725  1.00 25.53           C  
ANISOU 2074  CA  TYR A 260     3387   3196   3117    349   -402    171       C  
ATOM   2075  C   TYR A 260     -30.947 -19.503 -17.932  1.00 32.43           C  
ANISOU 2075  C   TYR A 260     4393   3994   3936    314   -392    220       C  
ATOM   2076  O   TYR A 260     -31.184 -20.214 -18.911  1.00 28.90           O  
ANISOU 2076  O   TYR A 260     3940   3563   3479    334   -434    225       O  
ATOM   2077  CB  TYR A 260     -31.471 -20.605 -15.735  1.00 22.82           C  
ANISOU 2077  CB  TYR A 260     2913   2930   2828    243   -342    175       C  
ATOM   2078  CG  TYR A 260     -32.315 -20.508 -14.490  1.00 27.46           C  
ANISOU 2078  CG  TYR A 260     3404   3575   3455    267   -327    128       C  
ATOM   2079  CD1 TYR A 260     -31.961 -19.645 -13.454  1.00 23.93           C  
ANISOU 2079  CD1 TYR A 260     2997   3100   2996    256   -288    125       C  
ATOM   2080  CD2 TYR A 260     -33.502 -21.219 -14.378  1.00 27.15           C  
ANISOU 2080  CD2 TYR A 260     3236   3615   3463    297   -344     74       C  
ATOM   2081  CE1 TYR A 260     -32.762 -19.521 -12.317  1.00 24.81           C  
ANISOU 2081  CE1 TYR A 260     3033   3259   3135    280   -265     78       C  
ATOM   2082  CE2 TYR A 260     -34.306 -21.109 -13.248  1.00 24.74           C  
ANISOU 2082  CE2 TYR A 260     2844   3360   3195    310   -309     21       C  
ATOM   2083  CZ  TYR A 260     -33.934 -20.255 -12.223  1.00 27.52           C  
ANISOU 2083  CZ  TYR A 260     3249   3680   3526    306   -269     28       C  
ATOM   2084  OH  TYR A 260     -34.731 -20.142 -11.104  1.00 26.34           O  
ANISOU 2084  OH  TYR A 260     3027   3577   3406    319   -224    -27       O  
ATOM   2085  N   ARG A 261     -29.910 -18.685 -17.876  1.00 26.05           N  
ANISOU 2085  N   ARG A 261     3706   3100   3092    257   -330    248       N  
ATOM   2086  CA  ARG A 261     -28.870 -18.738 -18.889  1.00 30.03           C  
ANISOU 2086  CA  ARG A 261     4324   3533   3553    190   -284    285       C  
ATOM   2087  C   ARG A 261     -27.602 -19.300 -18.260  1.00 26.65           C  
ANISOU 2087  C   ARG A 261     3816   3140   3171     53   -204    288       C  
ATOM   2088  O   ARG A 261     -27.595 -19.713 -17.097  1.00 24.13           O  
ANISOU 2088  O   ARG A 261     3370   2895   2903     25   -199    269       O  
ATOM   2089  CB  ARG A 261     -28.683 -17.363 -19.531  1.00 30.17           C  
ANISOU 2089  CB  ARG A 261     4564   3412   3488    228   -265    300       C  
ATOM   2090  CG  ARG A 261     -29.857 -17.063 -20.450  1.00 34.35           C  
ANISOU 2090  CG  ARG A 261     5188   3908   3955    387   -368    296       C  
ATOM   2091  CD  ARG A 261     -29.625 -15.889 -21.350  1.00 48.45           C  
ANISOU 2091  CD  ARG A 261     7244   5534   5631    434   -351    323       C  
ATOM   2092  NE  ARG A 261     -29.695 -14.638 -20.616  1.00 62.15           N  
ANISOU 2092  NE  ARG A 261     9068   7196   7349    461   -327    310       N  
ATOM   2093  CZ  ARG A 261     -28.728 -13.735 -20.630  1.00 74.58           C  
ANISOU 2093  CZ  ARG A 261    10809   8646   8881    371   -219    327       C  
ATOM   2094  NH1 ARG A 261     -28.844 -12.609 -19.930  1.00 73.40           N  
ANISOU 2094  NH1 ARG A 261    10743   8429   8718    396   -200    310       N  
ATOM   2095  NH2 ARG A 261     -27.639 -13.971 -21.353  1.00 81.08           N  
ANISOU 2095  NH2 ARG A 261    11714   9414   9679    247   -122    354       N  
ATOM   2096  N   THR A 262     -26.532 -19.341 -19.047  1.00 25.07           N  
ANISOU 2096  N   THR A 262     3692   2885   2947    -25   -141    305       N  
ATOM   2097  CA  THR A 262     -25.332 -20.048 -18.618  1.00 24.38           C  
ANISOU 2097  CA  THR A 262     3506   2846   2910   -137    -82    291       C  
ATOM   2098  C   THR A 262     -24.773 -19.450 -17.322  1.00 22.05           C  
ANISOU 2098  C   THR A 262     3164   2562   2651   -188    -49    254       C  
ATOM   2099  O   THR A 262     -24.703 -18.230 -17.159  1.00 22.80           O  
ANISOU 2099  O   THR A 262     3362   2580   2721   -192    -19    241       O  
ATOM   2100  CB  THR A 262     -24.286 -20.012 -19.737  1.00 31.01           C  
ANISOU 2100  CB  THR A 262     4441   3619   3722   -215     -6    297       C  
ATOM   2101  OG1 THR A 262     -23.137 -20.776 -19.336  1.00 25.88           O  
ANISOU 2101  OG1 THR A 262     3669   3032   3132   -308     40    266       O  
ATOM   2102  CG2 THR A 262     -23.876 -18.565 -20.069  1.00 31.21           C  
ANISOU 2102  CG2 THR A 262     4647   3516   3696   -249     68    291       C  
ATOM   2103  N   GLN A 263     -24.394 -20.320 -16.383  1.00 23.63           N  
ANISOU 2103  N   GLN A 263     3223   2854   2902   -219    -61    234       N  
ATOM   2104  CA  GLN A 263     -23.984 -19.869 -15.046  1.00 23.00           C  
ANISOU 2104  CA  GLN A 263     3094   2798   2847   -246    -52    193       C  
ATOM   2105  C   GLN A 263     -22.468 -19.657 -14.999  1.00 22.10           C  
ANISOU 2105  C   GLN A 263     2963   2673   2761   -350      8    141       C  
ATOM   2106  O   GLN A 263     -21.737 -20.327 -14.279  1.00 23.99           O  
ANISOU 2106  O   GLN A 263     3095   2982   3036   -377     -7    103       O  
ATOM   2107  CB  GLN A 263     -24.446 -20.863 -13.987  1.00 23.17           C  
ANISOU 2107  CB  GLN A 263     3001   2913   2891   -209   -100    194       C  
ATOM   2108  CG  GLN A 263     -25.967 -21.051 -13.926  1.00 20.34           C  
ANISOU 2108  CG  GLN A 263     2633   2575   2521   -124   -142    220       C  
ATOM   2109  CD  GLN A 263     -26.685 -19.776 -13.490  1.00 22.69           C  
ANISOU 2109  CD  GLN A 263     2992   2828   2801    -73   -146    205       C  
ATOM   2110  OE1 GLN A 263     -26.437 -19.243 -12.401  1.00 24.08           O  
ANISOU 2110  OE1 GLN A 263     3163   3007   2979    -86   -133    176       O  
ATOM   2111  NE2 GLN A 263     -27.564 -19.278 -14.338  1.00 22.20           N  
ANISOU 2111  NE2 GLN A 263     2996   2724   2714     -3   -172    218       N  
ATOM   2112  N   VAL A 264     -22.000 -18.674 -15.772  1.00 23.19           N  
ANISOU 2112  N   VAL A 264     3217   2716   2880   -406     78    129       N  
ATOM   2113  CA  VAL A 264     -20.557 -18.441 -15.849  1.00 23.08           C  
ANISOU 2113  CA  VAL A 264     3175   2690   2904   -525    156     59       C  
ATOM   2114  C   VAL A 264     -19.984 -17.943 -14.517  1.00 27.57           C  
ANISOU 2114  C   VAL A 264     3670   3293   3511   -562    148    -17       C  
ATOM   2115  O   VAL A 264     -18.807 -18.173 -14.224  1.00 27.60           O  
ANISOU 2115  O   VAL A 264     3574   3344   3569   -636    170    -98       O  
ATOM   2116  CB  VAL A 264     -20.224 -17.472 -16.997  1.00 33.19           C  
ANISOU 2116  CB  VAL A 264     4623   3842   4146   -594    260     60       C  
ATOM   2117  CG1 VAL A 264     -20.326 -18.197 -18.342  1.00 28.83           C  
ANISOU 2117  CG1 VAL A 264     4121   3273   3561   -581    278    110       C  
ATOM   2118  CG2 VAL A 264     -21.153 -16.276 -16.958  1.00 34.49           C  
ANISOU 2118  CG2 VAL A 264     4949   3907   4250   -535    254     95       C  
ATOM   2119  N   LYS A 265     -20.778 -17.241 -13.704  1.00 23.47           N  
ANISOU 2119  N   LYS A 265     3196   2754   2967   -506    112     -4       N  
ATOM   2120  CA  LYS A 265     -20.323 -16.727 -12.413  1.00 24.78           C  
ANISOU 2120  CA  LYS A 265     3309   2948   3158   -531     96    -76       C  
ATOM   2121  C   LYS A 265     -20.956 -17.469 -11.239  1.00 26.29           C  
ANISOU 2121  C   LYS A 265     3416   3230   3342   -440      5    -59       C  
ATOM   2122  O   LYS A 265     -21.163 -16.891 -10.162  1.00 24.29           O  
ANISOU 2122  O   LYS A 265     3171   2981   3079   -419    -18    -88       O  
ATOM   2123  CB  LYS A 265     -20.591 -15.224 -12.304  1.00 24.72           C  
ANISOU 2123  CB  LYS A 265     3440   2832   3122   -552    144    -90       C  
ATOM   2124  CG  LYS A 265     -19.847 -14.405 -13.357  1.00 30.15           C  
ANISOU 2124  CG  LYS A 265     4242   3408   3807   -663    259   -117       C  
ATOM   2125  CD  LYS A 265     -20.204 -12.928 -13.306  1.00 30.80           C  
ANISOU 2125  CD  LYS A 265     4500   3359   3845   -673    310   -120       C  
ATOM   2126  CE  LYS A 265     -19.315 -12.139 -14.266  1.00 39.69           C  
ANISOU 2126  CE  LYS A 265     5755   4360   4964   -809    450   -159       C  
ATOM   2127  NZ  LYS A 265     -19.642 -10.683 -14.281  1.00 36.74           N  
ANISOU 2127  NZ  LYS A 265     5591   3833   4534   -820    510   -159       N  
ATOM   2128  N   GLY A 266     -21.247 -18.752 -11.423  1.00 22.58           N  
ANISOU 2128  N   GLY A 266     2880   2826   2873   -392    -37    -14       N  
ATOM   2129  CA  GLY A 266     -21.595 -19.619 -10.317  1.00 18.79           C  
ANISOU 2129  CA  GLY A 266     2332   2425   2382   -328   -102     -7       C  
ATOM   2130  C   GLY A 266     -20.416 -19.770  -9.361  1.00 24.14           C  
ANISOU 2130  C   GLY A 266     2935   3156   3080   -354   -135    -92       C  
ATOM   2131  O   GLY A 266     -19.298 -19.317  -9.636  1.00 26.12           O  
ANISOU 2131  O   GLY A 266     3153   3398   3371   -432   -106   -167       O  
ATOM   2132  N   PRO A 267     -20.655 -20.410  -8.173  1.00 24.69           N  
ANISOU 2132  N   PRO A 267     2981   3281   3118   -288   -197    -92       N  
ATOM   2133  CA  PRO A 267     -19.582 -20.557  -7.167  1.00 26.75           C  
ANISOU 2133  CA  PRO A 267     3185   3595   3383   -284   -255   -180       C  
ATOM   2134  C   PRO A 267     -18.611 -21.688  -7.504  1.00 32.97           C  
ANISOU 2134  C   PRO A 267     3890   4442   4197   -277   -293   -212       C  
ATOM   2135  O   PRO A 267     -18.443 -22.653  -6.751  1.00 25.17           O  
ANISOU 2135  O   PRO A 267     2889   3502   3173   -203   -364   -216       O  
ATOM   2136  CB  PRO A 267     -20.380 -20.822  -5.881  1.00 24.49           C  
ANISOU 2136  CB  PRO A 267     2949   3326   3030   -204   -296   -151       C  
ATOM   2137  CG  PRO A 267     -21.608 -21.598  -6.374  1.00 19.38           C  
ANISOU 2137  CG  PRO A 267     2335   2669   2362   -168   -266    -50       C  
ATOM   2138  CD  PRO A 267     -21.944 -20.962  -7.711  1.00 20.88           C  
ANISOU 2138  CD  PRO A 267     2535   2808   2592   -216   -209    -20       C  
ATOM   2139  N   TRP A 268     -17.938 -21.569  -8.653  1.00 25.68           N  
ANISOU 2139  N   TRP A 268     2922   3506   3330   -350   -242   -239       N  
ATOM   2140  CA  TRP A 268     -17.101 -22.654  -9.160  1.00 22.95           C  
ANISOU 2140  CA  TRP A 268     2494   3212   3015   -341   -265   -267       C  
ATOM   2141  C   TRP A 268     -15.764 -22.793  -8.433  1.00 27.79           C  
ANISOU 2141  C   TRP A 268     3001   3897   3662   -330   -335   -402       C  
ATOM   2142  O   TRP A 268     -14.995 -23.702  -8.767  1.00 26.78           O  
ANISOU 2142  O   TRP A 268     2794   3820   3562   -305   -367   -443       O  
ATOM   2143  CB  TRP A 268     -16.839 -22.461 -10.656  1.00 22.98           C  
ANISOU 2143  CB  TRP A 268     2493   3176   3064   -426   -174   -258       C  
ATOM   2144  CG  TRP A 268     -18.085 -22.254 -11.488  1.00 23.98           C  
ANISOU 2144  CG  TRP A 268     2725   3232   3154   -425   -121   -144       C  
ATOM   2145  CD1 TRP A 268     -18.407 -21.148 -12.214  1.00 25.93           C  
ANISOU 2145  CD1 TRP A 268     3056   3397   3398   -484    -45   -125       C  
ATOM   2146  CD2 TRP A 268     -19.162 -23.178 -11.670  1.00 19.62           C  
ANISOU 2146  CD2 TRP A 268     2210   2684   2562   -354   -148    -46       C  
ATOM   2147  NE1 TRP A 268     -19.612 -21.326 -12.846  1.00 23.84           N  
ANISOU 2147  NE1 TRP A 268     2870   3094   3093   -438    -41    -26       N  
ATOM   2148  CE2 TRP A 268     -20.101 -22.561 -12.525  1.00 21.43           C  
ANISOU 2148  CE2 TRP A 268     2524   2846   2772   -367   -100     18       C  
ATOM   2149  CE3 TRP A 268     -19.423 -24.466 -11.204  1.00 27.08           C  
ANISOU 2149  CE3 TRP A 268     3133   3676   3481   -283   -205    -13       C  
ATOM   2150  CZ2 TRP A 268     -21.278 -23.190 -12.922  1.00 25.84           C  
ANISOU 2150  CZ2 TRP A 268     3115   3400   3302   -313   -115     97       C  
ATOM   2151  CZ3 TRP A 268     -20.597 -25.087 -11.599  1.00 29.35           C  
ANISOU 2151  CZ3 TRP A 268     3464   3947   3739   -249   -199     73       C  
ATOM   2152  CH2 TRP A 268     -21.507 -24.448 -12.446  1.00 28.32           C  
ANISOU 2152  CH2 TRP A 268     3388   3766   3605   -265   -159    119       C  
ATOM   2153  N   HIS A 269     -15.465 -21.919  -7.468  1.00 24.42           N  
ANISOU 2153  N   HIS A 269     2567   3478   3235   -341   -366   -480       N  
ATOM   2154  CA  HIS A 269     -14.339 -22.126  -6.564  1.00 22.83           C  
ANISOU 2154  CA  HIS A 269     2268   3356   3051   -299   -467   -616       C  
ATOM   2155  C   HIS A 269     -14.602 -23.248  -5.561  1.00 27.24           C  
ANISOU 2155  C   HIS A 269     2873   3954   3524   -151   -583   -578       C  
ATOM   2156  O   HIS A 269     -13.664 -23.677  -4.879  1.00 25.61           O  
ANISOU 2156  O   HIS A 269     2598   3815   3316    -79   -692   -685       O  
ATOM   2157  CB  HIS A 269     -14.044 -20.844  -5.799  1.00 28.11           C  
ANISOU 2157  CB  HIS A 269     2930   4015   3735   -353   -470   -712       C  
ATOM   2158  CG  HIS A 269     -15.140 -20.464  -4.854  1.00 30.52           C  
ANISOU 2158  CG  HIS A 269     3363   4279   3954   -297   -490   -632       C  
ATOM   2159  ND1 HIS A 269     -16.396 -20.108  -5.290  1.00 30.77           N  
ANISOU 2159  ND1 HIS A 269     3503   4234   3953   -314   -408   -504       N  
ATOM   2160  CD2 HIS A 269     -15.181 -20.412  -3.501  1.00 32.15           C  
ANISOU 2160  CD2 HIS A 269     3607   4511   4096   -217   -582   -669       C  
ATOM   2161  CE1 HIS A 269     -17.162 -19.837  -4.247  1.00 32.58           C  
ANISOU 2161  CE1 HIS A 269     3818   4448   4113   -255   -438   -470       C  
ATOM   2162  NE2 HIS A 269     -16.447 -20.009  -3.150  1.00 30.23           N  
ANISOU 2162  NE2 HIS A 269     3489   4206   3789   -200   -538   -563       N  
ATOM   2163  N   SER A 270     -15.848 -23.708  -5.449  1.00 26.49           N  
ANISOU 2163  N   SER A 270     2897   3812   3354   -105   -561   -439       N  
ATOM   2164  CA  SER A 270     -16.209 -24.761  -4.505  1.00 31.12           C  
ANISOU 2164  CA  SER A 270     3567   4410   3846     19   -640   -392       C  
ATOM   2165  C   SER A 270     -15.468 -26.052  -4.836  1.00 28.90           C  
ANISOU 2165  C   SER A 270     3240   4171   3568     89   -702   -413       C  
ATOM   2166  O   SER A 270     -15.261 -26.385  -6.005  1.00 28.68           O  
ANISOU 2166  O   SER A 270     3151   4145   3602     40   -649   -399       O  
ATOM   2167  CB  SER A 270     -17.724 -25.012  -4.545  1.00 28.31           C  
ANISOU 2167  CB  SER A 270     3330   3995   3433     22   -568   -250       C  
ATOM   2168  OG  SER A 270     -18.462 -23.830  -4.254  1.00 28.85           O  
ANISOU 2168  OG  SER A 270     3438   4024   3497    -26   -514   -234       O  
ATOM   2169  N   GLU A 271     -15.056 -26.775  -3.790  1.00 26.68           N  
ANISOU 2169  N   GLU A 271     3007   3919   3211    215   -818   -451       N  
ATOM   2170  CA  GLU A 271     -14.399 -28.066  -3.979  1.00 31.83           C  
ANISOU 2170  CA  GLU A 271     3644   4601   3848    312   -892   -470       C  
ATOM   2171  C   GLU A 271     -15.369 -29.125  -4.481  1.00 29.62           C  
ANISOU 2171  C   GLU A 271     3475   4262   3520    323   -827   -327       C  
ATOM   2172  O   GLU A 271     -14.959 -30.076  -5.157  1.00 36.32           O  
ANISOU 2172  O   GLU A 271     4294   5120   4386    357   -840   -324       O  
ATOM   2173  CB  GLU A 271     -13.754 -28.501  -2.656  1.00 42.08           C  
ANISOU 2173  CB  GLU A 271     4998   5933   5056    465  -1046   -550       C  
ATOM   2174  CG  GLU A 271     -12.739 -27.488  -2.142  1.00 53.84           C  
ANISOU 2174  CG  GLU A 271     6360   7493   6602    456  -1126   -718       C  
ATOM   2175  CD  GLU A 271     -12.375 -27.670  -0.677  1.00 67.58           C  
ANISOU 2175  CD  GLU A 271     8190   9255   8231    607  -1281   -787       C  
ATOM   2176  OE1 GLU A 271     -13.286 -27.639   0.178  1.00 62.93           O  
ANISOU 2176  OE1 GLU A 271     7780   8605   7528    641  -1265   -695       O  
ATOM   2177  OE2 GLU A 271     -11.172 -27.844  -0.378  1.00 70.83           O  
ANISOU 2177  OE2 GLU A 271     8497   9748   8669    698  -1419   -943       O  
ATOM   2178  N   GLU A 272     -16.653 -28.954  -4.200  1.00 28.14           N  
ANISOU 2178  N   GLU A 272     3401   4014   3278    289   -750   -220       N  
ATOM   2179  CA  GLU A 272     -17.680 -29.905  -4.584  1.00 28.86           C  
ANISOU 2179  CA  GLU A 272     3590   4048   3326    285   -679    -99       C  
ATOM   2180  C   GLU A 272     -19.005 -29.168  -4.499  1.00 28.99           C  
ANISOU 2180  C   GLU A 272     3653   4023   3338    206   -578    -27       C  
ATOM   2181  O   GLU A 272     -19.177 -28.318  -3.620  1.00 26.56           O  
ANISOU 2181  O   GLU A 272     3374   3715   3001    209   -588    -54       O  
ATOM   2182  CB  GLU A 272     -17.630 -31.121  -3.643  1.00 35.14           C  
ANISOU 2182  CB  GLU A 272     4536   4813   4001    410   -745    -76       C  
ATOM   2183  CG  GLU A 272     -18.892 -31.941  -3.542  1.00 44.65           C  
ANISOU 2183  CG  GLU A 272     5889   5942   5136    394   -653     41       C  
ATOM   2184  CD  GLU A 272     -18.684 -33.209  -2.719  1.00 52.28           C  
ANISOU 2184  CD  GLU A 272     7031   6859   5973    518   -710     61       C  
ATOM   2185  OE1 GLU A 272     -17.602 -33.359  -2.102  1.00 56.76           O  
ANISOU 2185  OE1 GLU A 272     7613   7457   6496    638   -841    -17       O  
ATOM   2186  OE2 GLU A 272     -19.593 -34.065  -2.701  1.00 38.52           O  
ANISOU 2186  OE2 GLU A 272     5419   5044   4172    498   -624    147       O  
ATOM   2187  N   LEU A 273     -19.923 -29.450  -5.421  1.00 24.69           N  
ANISOU 2187  N   LEU A 273     3107   3449   2826    142   -490     50       N  
ATOM   2188  CA  LEU A 273     -21.204 -28.776  -5.317  1.00 30.81           C  
ANISOU 2188  CA  LEU A 273     3912   4194   3600     86   -407    100       C  
ATOM   2189  C   LEU A 273     -22.296 -29.623  -5.943  1.00 29.94           C  
ANISOU 2189  C   LEU A 273     3834   4052   3491     54   -331    176       C  
ATOM   2190  O   LEU A 273     -22.048 -30.484  -6.793  1.00 27.09           O  
ANISOU 2190  O   LEU A 273     3452   3689   3152     50   -333    195       O  
ATOM   2191  CB  LEU A 273     -21.165 -27.361  -5.924  1.00 35.50           C  
ANISOU 2191  CB  LEU A 273     4418   4800   4272     18   -382     68       C  
ATOM   2192  CG  LEU A 273     -20.798 -27.050  -7.360  1.00 42.31           C  
ANISOU 2192  CG  LEU A 273     5192   5667   5217    -44   -357     60       C  
ATOM   2193  CD1 LEU A 273     -21.990 -27.287  -8.274  1.00 56.20           C  
ANISOU 2193  CD1 LEU A 273     6964   7397   6992    -79   -291    134       C  
ATOM   2194  CD2 LEU A 273     -20.341 -25.613  -7.458  1.00 32.51           C  
ANISOU 2194  CD2 LEU A 273     3907   4425   4020    -95   -348      1       C  
ATOM   2195  N   GLU A 274     -23.516 -29.372  -5.476  1.00 30.55           N  
ANISOU 2195  N   GLU A 274     3957   4105   3546     29   -261    209       N  
ATOM   2196  CA  GLU A 274     -24.727 -29.962  -6.027  1.00 26.03           C  
ANISOU 2196  CA  GLU A 274     3389   3512   2991    -18   -180    257       C  
ATOM   2197  C   GLU A 274     -25.567 -28.842  -6.624  1.00 26.30           C  
ANISOU 2197  C   GLU A 274     3343   3558   3091    -62   -143    250       C  
ATOM   2198  O   GLU A 274     -25.799 -27.823  -5.965  1.00 25.62           O  
ANISOU 2198  O   GLU A 274     3262   3475   2998    -55   -137    226       O  
ATOM   2199  CB  GLU A 274     -25.518 -30.705  -4.936  1.00 29.76           C  
ANISOU 2199  CB  GLU A 274     3981   3944   3382    -10   -115    282       C  
ATOM   2200  CG  GLU A 274     -26.826 -31.327  -5.417  1.00 39.58           C  
ANISOU 2200  CG  GLU A 274     5214   5170   4654    -76    -16    307       C  
ATOM   2201  CD  GLU A 274     -27.772 -31.673  -4.271  1.00 57.15           C  
ANISOU 2201  CD  GLU A 274     7543   7356   6813    -96     84    312       C  
ATOM   2202  OE1 GLU A 274     -27.427 -31.405  -3.096  1.00 60.91           O  
ANISOU 2202  OE1 GLU A 274     8120   7815   7208    -50     72    306       O  
ATOM   2203  OE2 GLU A 274     -28.866 -32.211  -4.548  1.00 64.38           O  
ANISOU 2203  OE2 GLU A 274     8444   8261   7758   -163    180    314       O  
ATOM   2204  N   ILE A 275     -26.007 -29.012  -7.867  1.00 27.18           N  
ANISOU 2204  N   ILE A 275     3392   3674   3260    -97   -126    266       N  
ATOM   2205  CA  ILE A 275     -26.971 -28.094  -8.467  1.00 26.02           C  
ANISOU 2205  CA  ILE A 275     3189   3534   3164   -116   -102    257       C  
ATOM   2206  C   ILE A 275     -28.358 -28.655  -8.194  1.00 28.42           C  
ANISOU 2206  C   ILE A 275     3490   3839   3470   -137    -32    259       C  
ATOM   2207  O   ILE A 275     -28.643 -29.814  -8.521  1.00 28.14           O  
ANISOU 2207  O   ILE A 275     3461   3797   3435   -164     -4    275       O  
ATOM   2208  CB  ILE A 275     -26.717 -27.911  -9.972  1.00 26.17           C  
ANISOU 2208  CB  ILE A 275     3158   3554   3233   -131   -129    264       C  
ATOM   2209  CG1 ILE A 275     -25.308 -27.365 -10.179  1.00 28.38           C  
ANISOU 2209  CG1 ILE A 275     3437   3830   3516   -131   -171    246       C  
ATOM   2210  CG2 ILE A 275     -27.774 -26.970 -10.585  1.00 25.54           C  
ANISOU 2210  CG2 ILE A 275     3044   3472   3188   -124   -121    252       C  
ATOM   2211  CD1 ILE A 275     -24.970 -27.060 -11.634  1.00 32.37           C  
ANISOU 2211  CD1 ILE A 275     3919   4322   4057   -154   -177    251       C  
ATOM   2212  N   ARG A 276     -29.203 -27.855  -7.543  1.00 24.11           N  
ANISOU 2212  N   ARG A 276     2934   3300   2928   -130      4    232       N  
ATOM   2213  CA  ARG A 276     -30.514 -28.310  -7.095  1.00 29.01           C  
ANISOU 2213  CA  ARG A 276     3539   3928   3556   -158     89    210       C  
ATOM   2214  C   ARG A 276     -31.521 -27.202  -7.354  1.00 31.31           C  
ANISOU 2214  C   ARG A 276     3750   4246   3902   -137     93    165       C  
ATOM   2215  O   ARG A 276     -31.265 -26.038  -7.027  1.00 32.07           O  
ANISOU 2215  O   ARG A 276     3860   4336   3988    -98     63    154       O  
ATOM   2216  CB  ARG A 276     -30.498 -28.674  -5.596  1.00 29.58           C  
ANISOU 2216  CB  ARG A 276     3713   3974   3551   -163    152    214       C  
ATOM   2217  CG  ARG A 276     -31.819 -29.199  -5.063  1.00 35.05           C  
ANISOU 2217  CG  ARG A 276     4402   4666   4249   -214    273    183       C  
ATOM   2218  CD  ARG A 276     -31.824 -29.287  -3.528  1.00 41.85           C  
ANISOU 2218  CD  ARG A 276     5391   5491   5018   -213    345    185       C  
ATOM   2219  NE  ARG A 276     -30.753 -30.130  -2.999  1.00 40.10           N  
ANISOU 2219  NE  ARG A 276     5314   5222   4701   -189    314    234       N  
ATOM   2220  CZ  ARG A 276     -30.551 -30.344  -1.702  1.00 44.60           C  
ANISOU 2220  CZ  ARG A 276     6035   5746   5163   -169    354    244       C  
ATOM   2221  NH1 ARG A 276     -29.556 -31.121  -1.295  1.00 41.60           N  
ANISOU 2221  NH1 ARG A 276     5792   5323   4690   -123    303    282       N  
ATOM   2222  NH2 ARG A 276     -31.348 -29.778  -0.810  1.00 36.77           N  
ANISOU 2222  NH2 ARG A 276     5068   4753   4151   -184    442    211       N  
ATOM   2223  N   PHE A 277     -32.661 -27.557  -7.936  1.00 28.31           N  
ANISOU 2223  N   PHE A 277     3285   3893   3578   -157    125    127       N  
ATOM   2224  CA  PHE A 277     -33.724 -26.583  -8.178  1.00 22.87           C  
ANISOU 2224  CA  PHE A 277     2509   3237   2943   -115    118     66       C  
ATOM   2225  C   PHE A 277     -34.638 -26.622  -6.966  1.00 25.72           C  
ANISOU 2225  C   PHE A 277     2858   3614   3302   -141    224     15       C  
ATOM   2226  O   PHE A 277     -35.514 -27.484  -6.850  1.00 23.97           O  
ANISOU 2226  O   PHE A 277     2584   3413   3112   -199    308    -28       O  
ATOM   2227  CB  PHE A 277     -34.424 -26.869  -9.502  1.00 28.01           C  
ANISOU 2227  CB  PHE A 277     3064   3920   3658   -107     76     31       C  
ATOM   2228  CG  PHE A 277     -33.544 -26.573 -10.663  1.00 25.20           C  
ANISOU 2228  CG  PHE A 277     2745   3540   3291    -73    -20     79       C  
ATOM   2229  CD1 PHE A 277     -33.457 -25.284 -11.155  1.00 23.78           C  
ANISOU 2229  CD1 PHE A 277     2584   3344   3108      0    -87     75       C  
ATOM   2230  CD2 PHE A 277     -32.707 -27.552 -11.185  1.00 23.66           C  
ANISOU 2230  CD2 PHE A 277     2587   3326   3076   -115    -31    129       C  
ATOM   2231  CE1 PHE A 277     -32.586 -24.983 -12.186  1.00 23.19           C  
ANISOU 2231  CE1 PHE A 277     2569   3231   3012     18   -150    119       C  
ATOM   2232  CE2 PHE A 277     -31.835 -27.260 -12.215  1.00 21.49           C  
ANISOU 2232  CE2 PHE A 277     2351   3026   2788    -93    -99    167       C  
ATOM   2233  CZ  PHE A 277     -31.770 -25.975 -12.713  1.00 21.86           C  
ANISOU 2233  CZ  PHE A 277     2422   3053   2831    -33   -152    162       C  
ATOM   2234  N   GLU A 278     -34.381 -25.703  -6.031  1.00 25.67           N  
ANISOU 2234  N   GLU A 278     2908   3590   3254   -105    231     16       N  
ATOM   2235  CA  GLU A 278     -35.017 -25.697  -4.721  1.00 26.10           C  
ANISOU 2235  CA  GLU A 278     2989   3647   3283   -128    340    -21       C  
ATOM   2236  C   GLU A 278     -34.565 -24.452  -3.966  1.00 22.28           C  
ANISOU 2236  C   GLU A 278     2568   3143   2755    -70    309    -18       C  
ATOM   2237  O   GLU A 278     -33.396 -24.057  -4.066  1.00 24.29           O  
ANISOU 2237  O   GLU A 278     2892   3368   2971    -46    229     31       O  
ATOM   2238  CB  GLU A 278     -34.654 -26.968  -3.940  1.00 28.12           C  
ANISOU 2238  CB  GLU A 278     3352   3865   3469   -198    422     18       C  
ATOM   2239  CG  GLU A 278     -35.236 -27.054  -2.544  1.00 32.45           C  
ANISOU 2239  CG  GLU A 278     3969   4396   3965   -230    553    -13       C  
ATOM   2240  CD  GLU A 278     -34.771 -28.310  -1.812  1.00 47.84           C  
ANISOU 2240  CD  GLU A 278     6074   6285   5819   -284    625     37       C  
ATOM   2241  OE1 GLU A 278     -35.266 -29.414  -2.120  1.00 53.09           O  
ANISOU 2241  OE1 GLU A 278     6728   6940   6505   -359    704     29       O  
ATOM   2242  OE2 GLU A 278     -33.886 -28.195  -0.944  1.00 45.62           O  
ANISOU 2242  OE2 GLU A 278     5935   5962   5437   -246    597     81       O  
ATOM   2243  N   GLU A 279     -35.479 -23.824  -3.230  1.00 21.19           N  
ANISOU 2243  N   GLU A 279     2400   3021   2628    -52    377    -81       N  
ATOM   2244  CA  GLU A 279     -35.122 -22.660  -2.425  1.00 24.78           C  
ANISOU 2244  CA  GLU A 279     2925   3453   3038      0    358    -85       C  
ATOM   2245  C   GLU A 279     -33.998 -22.995  -1.448  1.00 29.24           C  
ANISOU 2245  C   GLU A 279     3636   3974   3500    -21    359    -30       C  
ATOM   2246  O   GLU A 279     -33.962 -24.082  -0.867  1.00 24.64           O  
ANISOU 2246  O   GLU A 279     3120   3377   2866    -71    428     -9       O  
ATOM   2247  CB  GLU A 279     -36.340 -22.154  -1.643  1.00 25.63           C  
ANISOU 2247  CB  GLU A 279     2984   3586   3166     16    455   -167       C  
ATOM   2248  CG  GLU A 279     -37.430 -21.509  -2.490  1.00 40.49           C  
ANISOU 2248  CG  GLU A 279     4719   5517   5148     77    426   -245       C  
ATOM   2249  CD  GLU A 279     -38.332 -22.526  -3.191  1.00 56.19           C  
ANISOU 2249  CD  GLU A 279     6576   7559   7215     28    469   -295       C  
ATOM   2250  OE1 GLU A 279     -38.160 -23.756  -2.987  1.00 46.22           O  
ANISOU 2250  OE1 GLU A 279     5345   6286   5929    -65    540   -265       O  
ATOM   2251  OE2 GLU A 279     -39.217 -22.084  -3.955  1.00 62.90           O  
ANISOU 2251  OE2 GLU A 279     7293   8457   8147     90    424   -372       O  
ATOM   2252  N   CYS A 280     -33.076 -22.053  -1.273  1.00 28.42           N  
ANISOU 2252  N   CYS A 280     3589   3845   3364     21    277    -15       N  
ATOM   2253  CA  CYS A 280     -32.139 -22.149  -0.168  1.00 28.10           C  
ANISOU 2253  CA  CYS A 280     3677   3774   3227     21    267      5       C  
ATOM   2254  C   CYS A 280     -32.913 -22.122   1.153  1.00 31.00           C  
ANISOU 2254  C   CYS A 280     4110   4133   3535     19    378    -29       C  
ATOM   2255  O   CYS A 280     -33.955 -21.464   1.256  1.00 32.38           O  
ANISOU 2255  O   CYS A 280     4222   4326   3754     34    438    -83       O  
ATOM   2256  CB  CYS A 280     -31.127 -21.002  -0.222  1.00 27.68           C  
ANISOU 2256  CB  CYS A 280     3650   3701   3166     56    168      0       C  
ATOM   2257  SG  CYS A 280     -29.941 -21.114  -1.607  1.00 28.21           S  
ANISOU 2257  SG  CYS A 280     3671   3766   3281     40     62     36       S  
ATOM   2258  N   PRO A 281     -32.420 -22.821   2.180  1.00 27.32           N  
ANISOU 2258  N   PRO A 281     3781   3636   2963      9    406     -6       N  
ATOM   2259  CA  PRO A 281     -33.174 -22.935   3.441  1.00 28.74           C  
ANISOU 2259  CA  PRO A 281     4055   3796   3070     -2    534    -34       C  
ATOM   2260  C   PRO A 281     -33.493 -21.576   4.047  1.00 30.03           C  
ANISOU 2260  C   PRO A 281     4216   3962   3231     42    540    -88       C  
ATOM   2261  O   PRO A 281     -32.617 -20.720   4.190  1.00 32.66           O  
ANISOU 2261  O   PRO A 281     4583   4283   3541     86    436    -89       O  
ATOM   2262  CB  PRO A 281     -32.233 -23.742   4.348  1.00 33.51           C  
ANISOU 2262  CB  PRO A 281     4844   4352   3536     10    512      9       C  
ATOM   2263  CG  PRO A 281     -31.373 -24.510   3.418  1.00 32.02           C  
ANISOU 2263  CG  PRO A 281     4624   4169   3374      7    415     57       C  
ATOM   2264  CD  PRO A 281     -31.187 -23.625   2.191  1.00 27.06           C  
ANISOU 2264  CD  PRO A 281     3831   3582   2867     16    324     44       C  
ATOM   2265  N   GLY A 282     -34.767 -21.387   4.399  1.00 29.59           N  
ANISOU 2265  N   GLY A 282     4114   3922   3206     26    670   -143       N  
ATOM   2266  CA  GLY A 282     -35.212 -20.150   5.009  1.00 30.77           C  
ANISOU 2266  CA  GLY A 282     4263   4073   3354     73    693   -202       C  
ATOM   2267  C   GLY A 282     -35.350 -18.970   4.072  1.00 35.78           C  
ANISOU 2267  C   GLY A 282     4773   4731   4090    129    602   -232       C  
ATOM   2268  O   GLY A 282     -35.475 -17.836   4.551  1.00 29.74           O  
ANISOU 2268  O   GLY A 282     4033   3953   3314    180    594   -273       O  
ATOM   2269  N   THR A 283     -35.332 -19.196   2.751  1.00 29.49           N  
ANISOU 2269  N   THR A 283     3865   3960   3382    125    535   -211       N  
ATOM   2270  CA  THR A 283     -35.437 -18.123   1.769  1.00 31.66           C  
ANISOU 2270  CA  THR A 283     4056   4239   3735    186    445   -231       C  
ATOM   2271  C   THR A 283     -36.630 -18.360   0.849  1.00 32.88           C  
ANISOU 2271  C   THR A 283     4054   4445   3992    199    473   -278       C  
ATOM   2272  O   THR A 283     -37.105 -19.489   0.688  1.00 30.62           O  
ANISOU 2272  O   THR A 283     3709   4192   3731    139    540   -281       O  
ATOM   2273  CB  THR A 283     -34.162 -17.988   0.903  1.00 26.16           C  
ANISOU 2273  CB  THR A 283     3387   3514   3038    183    317   -170       C  
ATOM   2274  OG1 THR A 283     -34.054 -19.107   0.004  1.00 28.71           O  
ANISOU 2274  OG1 THR A 283     3651   3861   3397    139    302   -129       O  
ATOM   2275  CG2 THR A 283     -32.895 -17.914   1.780  1.00 26.65           C  
ANISOU 2275  CG2 THR A 283     3577   3540   3009    166    276   -144       C  
ATOM   2276  N   LYS A 284     -37.100 -17.269   0.234  1.00 28.27           N  
ANISOU 2276  N   LYS A 284     3412   3864   3464    284    414   -321       N  
ATOM   2277  CA  LYS A 284     -38.122 -17.317  -0.807  1.00 31.05           C  
ANISOU 2277  CA  LYS A 284     3618   4267   3913    330    392   -376       C  
ATOM   2278  C   LYS A 284     -37.703 -16.424  -1.965  1.00 29.86           C  
ANISOU 2278  C   LYS A 284     3488   4077   3780    410    257   -349       C  
ATOM   2279  O   LYS A 284     -37.115 -15.359  -1.753  1.00 30.39           O  
ANISOU 2279  O   LYS A 284     3660   4082   3804    451    212   -332       O  
ATOM   2280  CB  LYS A 284     -39.498 -16.866  -0.276  1.00 36.40           C  
ANISOU 2280  CB  LYS A 284     4197   4993   4642    384    475   -492       C  
ATOM   2281  CG  LYS A 284     -40.095 -17.812   0.770  1.00 56.65           C  
ANISOU 2281  CG  LYS A 284     6734   7593   7196    290    642   -534       C  
ATOM   2282  CD  LYS A 284     -41.451 -17.338   1.286  1.00 73.91           C  
ANISOU 2282  CD  LYS A 284     8806   9834   9444    336    740   -667       C  
ATOM   2283  CE  LYS A 284     -42.022 -18.321   2.311  1.00 85.84           C  
ANISOU 2283  CE  LYS A 284    10308  11368  10940    220    936   -711       C  
ATOM   2284  NZ  LYS A 284     -43.239 -17.797   3.005  1.00 89.65           N  
ANISOU 2284  NZ  LYS A 284    10691  11899  11472    253   1057   -849       N  
ATOM   2285  N   VAL A 285     -38.031 -16.852  -3.186  1.00 29.40           N  
ANISOU 2285  N   VAL A 285     3344   4048   3779    428    197   -351       N  
ATOM   2286  CA  VAL A 285     -37.696 -16.133  -4.406  1.00 26.79           C  
ANISOU 2286  CA  VAL A 285     3055   3671   3451    504     76   -323       C  
ATOM   2287  C   VAL A 285     -38.989 -15.680  -5.072  1.00 37.13           C  
ANISOU 2287  C   VAL A 285     4257   5023   4826    627     29   -417       C  
ATOM   2288  O   VAL A 285     -39.905 -16.486  -5.268  1.00 31.09           O  
ANISOU 2288  O   VAL A 285     3343   4341   4129    617     58   -483       O  
ATOM   2289  CB  VAL A 285     -36.868 -17.006  -5.369  1.00 28.60           C  
ANISOU 2289  CB  VAL A 285     3300   3892   3676    437     29   -246       C  
ATOM   2290  CG1 VAL A 285     -36.448 -16.196  -6.608  1.00 24.30           C  
ANISOU 2290  CG1 VAL A 285     2834   3283   3117    507    -77   -213       C  
ATOM   2291  CG2 VAL A 285     -35.664 -17.598  -4.658  1.00 25.75           C  
ANISOU 2291  CG2 VAL A 285     3018   3507   3259    329     70   -175       C  
ATOM   2292  N   TYR A 286     -39.054 -14.397  -5.421  1.00 33.93           N  
ANISOU 2292  N   TYR A 286     3933   4559   4401    746    -47   -430       N  
ATOM   2293  CA  TYR A 286     -40.192 -13.802  -6.110  1.00 33.85           C  
ANISOU 2293  CA  TYR A 286     3850   4574   4436    902   -124   -522       C  
ATOM   2294  C   TYR A 286     -39.787 -13.438  -7.534  1.00 39.61           C  
ANISOU 2294  C   TYR A 286     4680   5237   5133    974   -250   -470       C  
ATOM   2295  O   TYR A 286     -38.770 -12.770  -7.735  1.00 33.83           O  
ANISOU 2295  O   TYR A 286     4125   4398   4331    959   -271   -388       O  
ATOM   2296  CB  TYR A 286     -40.676 -12.550  -5.385  1.00 30.42           C  
ANISOU 2296  CB  TYR A 286     3461   4108   3989   1011   -115   -586       C  
ATOM   2297  CG  TYR A 286     -41.129 -12.819  -3.968  1.00 42.34           C  
ANISOU 2297  CG  TYR A 286     4889   5677   5521    948     19   -644       C  
ATOM   2298  CD1 TYR A 286     -40.205 -12.975  -2.941  1.00 38.27           C  
ANISOU 2298  CD1 TYR A 286     4474   5123   4944    828    104   -575       C  
ATOM   2299  CD2 TYR A 286     -42.476 -12.923  -3.660  1.00 51.99           C  
ANISOU 2299  CD2 TYR A 286     5937   6995   6823   1011     63   -779       C  
ATOM   2300  CE1 TYR A 286     -40.611 -13.229  -1.645  1.00 41.87           C  
ANISOU 2300  CE1 TYR A 286     4888   5621   5401    775    230   -624       C  
ATOM   2301  CE2 TYR A 286     -42.895 -13.172  -2.369  1.00 57.53           C  
ANISOU 2301  CE2 TYR A 286     6579   7742   7537    943    208   -836       C  
ATOM   2302  CZ  TYR A 286     -41.959 -13.327  -1.366  1.00 55.65           C  
ANISOU 2302  CZ  TYR A 286     6473   7452   7221    826    292   -751       C  
ATOM   2303  OH  TYR A 286     -42.376 -13.574  -0.082  1.00 60.67           O  
ANISOU 2303  OH  TYR A 286     7081   8121   7850    764    440   -803       O  
ATOM   2304  N   VAL A 287     -40.581 -13.858  -8.513  1.00 35.40           N  
ANISOU 2304  N   VAL A 287     4041   4762   4647   1050   -328   -526       N  
ATOM   2305  CA  VAL A 287     -40.351 -13.445  -9.895  1.00 29.13           C  
ANISOU 2305  CA  VAL A 287     3362   3899   3807   1147   -454   -488       C  
ATOM   2306  C   VAL A 287     -41.019 -12.091 -10.097  1.00 31.40           C  
ANISOU 2306  C   VAL A 287     3731   4133   4068   1346   -542   -551       C  
ATOM   2307  O   VAL A 287     -42.242 -11.964  -9.961  1.00 37.39           O  
ANISOU 2307  O   VAL A 287     4343   4974   4890   1467   -578   -678       O  
ATOM   2308  CB  VAL A 287     -40.889 -14.485 -10.887  1.00 35.59           C  
ANISOU 2308  CB  VAL A 287     4048   4800   4676   1154   -517   -526       C  
ATOM   2309  CG1 VAL A 287     -40.572 -14.063 -12.326  1.00 35.37           C  
ANISOU 2309  CG1 VAL A 287     4174   4687   4578   1255   -645   -477       C  
ATOM   2310  CG2 VAL A 287     -40.308 -15.871 -10.582  1.00 30.25           C  
ANISOU 2310  CG2 VAL A 287     3294   4172   4027    960   -420   -471       C  
ATOM   2311  N   GLU A 288     -40.217 -11.066 -10.377  1.00 36.26           N  
ANISOU 2311  N   GLU A 288     4580   4606   4592   1380   -568   -473       N  
ATOM   2312  CA  GLU A 288     -40.755  -9.717 -10.521  1.00 34.97           C  
ANISOU 2312  CA  GLU A 288     4540   4363   4384   1572   -644   -522       C  
ATOM   2313  C   GLU A 288     -39.753  -8.865 -11.283  1.00 38.16           C  
ANISOU 2313  C   GLU A 288     5231   4592   4674   1582   -675   -418       C  
ATOM   2314  O   GLU A 288     -38.543  -8.963 -11.051  1.00 33.73           O  
ANISOU 2314  O   GLU A 288     4765   3969   4081   1415   -589   -326       O  
ATOM   2315  CB  GLU A 288     -41.067  -9.092  -9.151  1.00 33.28           C  
ANISOU 2315  CB  GLU A 288     4291   4161   4193   1579   -564   -578       C  
ATOM   2316  CG  GLU A 288     -39.929  -9.221  -8.134  1.00 35.55           C  
ANISOU 2316  CG  GLU A 288     4637   4413   4457   1384   -435   -496       C  
ATOM   2317  CD  GLU A 288     -40.374  -8.926  -6.698  1.00 43.31           C  
ANISOU 2317  CD  GLU A 288     5543   5441   5471   1376   -346   -564       C  
ATOM   2318  OE1 GLU A 288     -41.591  -9.034  -6.409  1.00 41.09           O  
ANISOU 2318  OE1 GLU A 288     5095   5258   5257   1472   -349   -679       O  
ATOM   2319  OE2 GLU A 288     -39.504  -8.586  -5.858  1.00 41.17           O  
ANISOU 2319  OE2 GLU A 288     5376   5111   5158   1273   -270   -513       O  
ATOM   2320  N   GLU A 289     -40.271  -8.027 -12.187  1.00 42.57           N  
ANISOU 2320  N   GLU A 289     5934   5070   5172   1781   -794   -445       N  
ATOM   2321  CA  GLU A 289     -39.425  -7.251 -13.087  1.00 49.73           C  
ANISOU 2321  CA  GLU A 289     7143   5795   5958   1798   -818   -351       C  
ATOM   2322  C   GLU A 289     -38.670  -6.130 -12.384  1.00 44.93           C  
ANISOU 2322  C   GLU A 289     6733   5047   5292   1744   -731   -308       C  
ATOM   2323  O   GLU A 289     -37.705  -5.606 -12.951  1.00 41.56           O  
ANISOU 2323  O   GLU A 289     6548   4466   4775   1682   -697   -224       O  
ATOM   2324  CB  GLU A 289     -40.265  -6.668 -14.225  1.00 61.16           C  
ANISOU 2324  CB  GLU A 289     8716   7184   7337   2049   -978   -396       C  
ATOM   2325  CG  GLU A 289     -40.596  -7.678 -15.310  1.00 77.42           C  
ANISOU 2325  CG  GLU A 289    10677   9326   9412   2079  -1071   -407       C  
ATOM   2326  CD  GLU A 289     -41.432  -7.079 -16.426  1.00 96.63           C  
ANISOU 2326  CD  GLU A 289    13249  11702  11765   2350  -1251   -462       C  
ATOM   2327  OE1 GLU A 289     -41.309  -5.860 -16.683  1.00102.63           O  
ANISOU 2327  OE1 GLU A 289    14292  12291  12410   2479  -1284   -434       O  
ATOM   2328  OE2 GLU A 289     -42.221  -7.826 -17.042  1.00102.84           O  
ANISOU 2328  OE2 GLU A 289    13869  12607  12597   2440  -1363   -540       O  
ATOM   2329  N   THR A 290     -39.078  -5.749 -11.174  1.00 38.03           N  
ANISOU 2329  N   THR A 290     5768   4217   4464   1758   -685   -370       N  
ATOM   2330  CA  THR A 290     -38.341  -4.733 -10.419  1.00 42.40           C  
ANISOU 2330  CA  THR A 290     6496   4644   4968   1692   -599   -339       C  
ATOM   2331  C   THR A 290     -37.033  -5.264  -9.840  1.00 42.00           C  
ANISOU 2331  C   THR A 290     6422   4602   4935   1438   -477   -269       C  
ATOM   2332  O   THR A 290     -36.271  -4.497  -9.238  1.00 41.54           O  
ANISOU 2332  O   THR A 290     6498   4443   4840   1355   -404   -249       O  
ATOM   2333  CB  THR A 290     -39.215  -4.181  -9.293  1.00 48.05           C  
ANISOU 2333  CB  THR A 290     7122   5411   5726   1794   -590   -436       C  
ATOM   2334  OG1 THR A 290     -39.746  -5.272  -8.533  1.00 47.70           O  
ANISOU 2334  OG1 THR A 290     6783   5554   5786   1728   -550   -492       O  
ATOM   2335  CG2 THR A 290     -40.371  -3.348  -9.865  1.00 44.41           C  
ANISOU 2335  CG2 THR A 290     6736   4907   5231   2071   -719   -514       C  
ATOM   2336  N   CYS A 291     -36.758  -6.550 -10.019  1.00 34.75           N  
ANISOU 2336  N   CYS A 291     5337   3797   4071   1320   -460   -241       N  
ATOM   2337  CA  CYS A 291     -35.558  -7.160  -9.483  1.00 34.27           C  
ANISOU 2337  CA  CYS A 291     5235   3758   4029   1104   -364   -187       C  
ATOM   2338  C   CYS A 291     -34.323  -6.663 -10.227  1.00 41.77           C  
ANISOU 2338  C   CYS A 291     6399   4561   4910   1007   -329   -116       C  
ATOM   2339  O   CYS A 291     -34.392  -6.203 -11.372  1.00 37.59           O  
ANISOU 2339  O   CYS A 291     6039   3927   4316   1090   -376    -88       O  
ATOM   2340  CB  CYS A 291     -35.649  -8.680  -9.603  1.00 35.38           C  
ANISOU 2340  CB  CYS A 291     5162   4045   4235   1026   -364   -177       C  
ATOM   2341  SG  CYS A 291     -34.450  -9.557  -8.609  1.00 33.72           S  
ANISOU 2341  SG  CYS A 291     4861   3896   4057    805   -264   -139       S  
ATOM   2342  N   GLY A 292     -33.177  -6.779  -9.566  1.00 35.14           N  
ANISOU 2342  N   GLY A 292     5554   3715   4083    830   -243    -95       N  
ATOM   2343  CA  GLY A 292     -31.912  -6.544 -10.234  1.00 34.80           C  
ANISOU 2343  CA  GLY A 292     5659   3562   4000    700   -188    -46       C  
ATOM   2344  C   GLY A 292     -31.677  -7.555 -11.338  1.00 37.41           C  
ANISOU 2344  C   GLY A 292     5942   3935   4338    664   -210      3       C  
ATOM   2345  O   GLY A 292     -32.351  -8.578 -11.452  1.00 37.87           O  
ANISOU 2345  O   GLY A 292     5829   4119   4441    710   -262     -1       O  
ATOM   2346  N   THR A 293     -30.693  -7.260 -12.179  1.00 38.02           N  
ANISOU 2346  N   THR A 293     6178   3899   4369    571   -157     43       N  
ATOM   2347  CA  THR A 293     -30.396  -8.155 -13.280  1.00 37.34           C  
ANISOU 2347  CA  THR A 293     6069   3837   4279    534   -168     88       C  
ATOM   2348  C   THR A 293     -29.394  -9.230 -12.846  1.00 32.89           C  
ANISOU 2348  C   THR A 293     5330   3380   3786    362   -114     92       C  
ATOM   2349  O   THR A 293     -28.919  -9.259 -11.707  1.00 35.30           O  
ANISOU 2349  O   THR A 293     5542   3737   4135    279    -77     58       O  
ATOM   2350  CB  THR A 293     -29.887  -7.359 -14.477  1.00 53.53           C  
ANISOU 2350  CB  THR A 293     8392   5709   6237    526   -127    126       C  
ATOM   2351  OG1 THR A 293     -29.952  -8.176 -15.654  1.00 58.31           O  
ANISOU 2351  OG1 THR A 293     8996   6338   6822    547   -163    167       O  
ATOM   2352  CG2 THR A 293     -28.462  -6.918 -14.234  1.00 41.81           C  
ANISOU 2352  CG2 THR A 293     6985   4143   4758    327      3    119       C  
ATOM   2353  N   ARG A 294     -29.099 -10.143 -13.769  1.00 32.61           N  
ANISOU 2353  N   ARG A 294     5256   3380   3756    324   -119    128       N  
ATOM   2354  CA  ARG A 294     -28.101 -11.186 -13.550  1.00 32.81           C  
ANISOU 2354  CA  ARG A 294     5135   3493   3838    178    -75    131       C  
ATOM   2355  C   ARG A 294     -26.794 -10.593 -13.040  1.00 32.93           C  
ANISOU 2355  C   ARG A 294     5196   3450   3865     28     18     98       C  
ATOM   2356  O   ARG A 294     -26.350  -9.541 -13.507  1.00 32.92           O  
ANISOU 2356  O   ARG A 294     5385   3308   3816    -10     80     95       O  
ATOM   2357  CB  ARG A 294     -27.833 -11.930 -14.864  1.00 30.74           C  
ANISOU 2357  CB  ARG A 294     4896   3225   3558    158    -77    174       C  
ATOM   2358  CG  ARG A 294     -28.448 -13.285 -14.970  1.00 38.27           C  
ANISOU 2358  CG  ARG A 294     5672   4314   4554    200   -143    186       C  
ATOM   2359  CD  ARG A 294     -28.452 -13.768 -16.417  1.00 34.34           C  
ANISOU 2359  CD  ARG A 294     5245   3786   4018    221   -162    225       C  
ATOM   2360  NE  ARG A 294     -27.118 -14.067 -16.944  1.00 36.60           N  
ANISOU 2360  NE  ARG A 294     5563   4038   4304     78    -76    240       N  
ATOM   2361  CZ  ARG A 294     -26.523 -15.260 -16.906  1.00 36.30           C  
ANISOU 2361  CZ  ARG A 294     5377   4095   4319     -3    -62    242       C  
ATOM   2362  NH1 ARG A 294     -25.314 -15.407 -17.448  1.00 36.11           N  
ANISOU 2362  NH1 ARG A 294     5389   4035   4298   -122     21    241       N  
ATOM   2363  NH2 ARG A 294     -27.117 -16.310 -16.328  1.00 23.41           N  
ANISOU 2363  NH2 ARG A 294     3568   2589   2739     33   -121    237       N  
ATOM   2364  N   GLY A 295     -26.168 -11.290 -12.094  1.00 30.07           N  
ANISOU 2364  N   GLY A 295     4666   3195   3565    -57     26     67       N  
ATOM   2365  CA  GLY A 295     -24.833 -10.959 -11.652  1.00 29.54           C  
ANISOU 2365  CA  GLY A 295     4594   3105   3525   -204     98     14       C  
ATOM   2366  C   GLY A 295     -24.115 -12.155 -11.044  1.00 27.99           C  
ANISOU 2366  C   GLY A 295     4203   3044   3389   -271     80    -11       C  
ATOM   2367  O   GLY A 295     -24.575 -13.297 -11.138  1.00 25.54           O  
ANISOU 2367  O   GLY A 295     3784   2827   3093   -220     29     25       O  
ATOM   2368  N   PRO A 296     -22.971 -11.909 -10.403  1.00 30.35           N  
ANISOU 2368  N   PRO A 296     4458   3351   3722   -382    117    -83       N  
ATOM   2369  CA  PRO A 296     -22.257 -12.990  -9.707  1.00 29.17           C  
ANISOU 2369  CA  PRO A 296     4134   3328   3621   -420     80   -121       C  
ATOM   2370  C   PRO A 296     -23.180 -13.723  -8.743  1.00 25.47           C  
ANISOU 2370  C   PRO A 296     3583   2953   3140   -315      3    -92       C  
ATOM   2371  O   PRO A 296     -24.013 -13.109  -8.070  1.00 24.94           O  
ANISOU 2371  O   PRO A 296     3564   2866   3046   -248    -11    -90       O  
ATOM   2372  CB  PRO A 296     -21.143 -12.255  -8.950  1.00 29.72           C  
ANISOU 2372  CB  PRO A 296     4189   3382   3720   -524    113   -224       C  
ATOM   2373  CG  PRO A 296     -20.999 -10.943  -9.641  1.00 37.18           C  
ANISOU 2373  CG  PRO A 296     5304   4180   4645   -589    204   -237       C  
ATOM   2374  CD  PRO A 296     -22.347 -10.591 -10.185  1.00 33.72           C  
ANISOU 2374  CD  PRO A 296     4997   3671   4143   -466    187   -146       C  
ATOM   2375  N   SER A 297     -23.025 -15.044  -8.680  1.00 25.38           N  
ANISOU 2375  N   SER A 297     3457   3038   3147   -304    -35    -74       N  
ATOM   2376  CA  SER A 297     -23.809 -15.840  -7.744  1.00 22.45           C  
ANISOU 2376  CA  SER A 297     3024   2746   2760   -225    -86    -51       C  
ATOM   2377  C   SER A 297     -23.528 -15.408  -6.307  1.00 24.53           C  
ANISOU 2377  C   SER A 297     3284   3030   3007   -225   -106   -111       C  
ATOM   2378  O   SER A 297     -22.379 -15.170  -5.923  1.00 26.17           O  
ANISOU 2378  O   SER A 297     3466   3246   3232   -290   -112   -182       O  
ATOM   2379  CB  SER A 297     -23.499 -17.330  -7.917  1.00 26.22           C  
ANISOU 2379  CB  SER A 297     3408   3304   3252   -226   -115    -27       C  
ATOM   2380  OG  SER A 297     -24.098 -18.097  -6.880  1.00 35.87           O  
ANISOU 2380  OG  SER A 297     4595   4588   4448   -167   -146    -13       O  
ATOM   2381  N   LEU A 298     -24.594 -15.281  -5.522  1.00 25.65           N  
ANISOU 2381  N   LEU A 298     3448   3182   3116   -150   -113    -94       N  
ATOM   2382  CA  LEU A 298     -24.527 -14.831  -4.140  1.00 22.48           C  
ANISOU 2382  CA  LEU A 298     3067   2792   2684   -135   -128   -145       C  
ATOM   2383  C   LEU A 298     -24.932 -15.971  -3.217  1.00 24.28           C  
ANISOU 2383  C   LEU A 298     3254   3095   2876    -84   -153   -125       C  
ATOM   2384  O   LEU A 298     -25.763 -16.806  -3.578  1.00 23.75           O  
ANISOU 2384  O   LEU A 298     3158   3056   2811    -50   -139    -70       O  
ATOM   2385  CB  LEU A 298     -25.458 -13.635  -3.903  1.00 23.66           C  
ANISOU 2385  CB  LEU A 298     3301   2876   2814    -88    -99   -149       C  
ATOM   2386  CG  LEU A 298     -25.208 -12.427  -4.808  1.00 30.08           C  
ANISOU 2386  CG  LEU A 298     4204   3586   3641   -125    -65   -160       C  
ATOM   2387  CD1 LEU A 298     -26.263 -11.347  -4.600  1.00 28.26           C  
ANISOU 2387  CD1 LEU A 298     4067   3289   3383    -48    -48   -161       C  
ATOM   2388  CD2 LEU A 298     -23.835 -11.906  -4.505  1.00 31.23           C  
ANISOU 2388  CD2 LEU A 298     4355   3708   3802   -227    -57   -237       C  
ATOM   2389  N   ARG A 299     -24.363 -15.990  -2.014  1.00 22.78           N  
ANISOU 2389  N   ARG A 299     3076   2932   2648    -81   -187   -176       N  
ATOM   2390  CA  ARG A 299     -24.716 -17.008  -1.031  1.00 24.59           C  
ANISOU 2390  CA  ARG A 299     3311   3212   2819    -29   -201   -158       C  
ATOM   2391  C   ARG A 299     -25.919 -16.545  -0.223  1.00 23.06           C  
ANISOU 2391  C   ARG A 299     3175   3001   2584     20   -153   -151       C  
ATOM   2392  O   ARG A 299     -26.095 -15.349   0.019  1.00 26.07           O  
ANISOU 2392  O   ARG A 299     3599   3340   2968     23   -138   -188       O  
ATOM   2393  CB  ARG A 299     -23.539 -17.304  -0.088  1.00 26.34           C  
ANISOU 2393  CB  ARG A 299     3539   3469   3001    -27   -275   -221       C  
ATOM   2394  CG  ARG A 299     -23.542 -18.733   0.453  1.00 22.54           C  
ANISOU 2394  CG  ARG A 299     3073   3031   2459     24   -303   -188       C  
ATOM   2395  CD  ARG A 299     -22.289 -19.063   1.260  1.00 28.56           C  
ANISOU 2395  CD  ARG A 299     3844   3831   3179     52   -403   -260       C  
ATOM   2396  NE  ARG A 299     -22.243 -18.281   2.497  1.00 27.37           N  
ANISOU 2396  NE  ARG A 299     3766   3668   2964     80   -428   -321       N  
ATOM   2397  CZ  ARG A 299     -21.149 -18.073   3.215  1.00 22.68           C  
ANISOU 2397  CZ  ARG A 299     3171   3101   2343    100   -526   -417       C  
ATOM   2398  NH1 ARG A 299     -19.994 -18.596   2.819  1.00 22.91           N  
ANISOU 2398  NH1 ARG A 299     3116   3177   2411     97   -606   -470       N  
ATOM   2399  NH2 ARG A 299     -21.208 -17.335   4.330  1.00 23.45           N  
ANISOU 2399  NH2 ARG A 299     3348   3185   2378    127   -547   -472       N  
ATOM   2400  N   SER A 300     -26.749 -17.504   0.203  1.00 26.26           N  
ANISOU 2400  N   SER A 300     3587   3436   2954     54   -116   -112       N  
ATOM   2401  CA  SER A 300     -27.979 -17.145   0.909  1.00 24.02           C  
ANISOU 2401  CA  SER A 300     3341   3144   2643     94    -49   -116       C  
ATOM   2402  C   SER A 300     -27.722 -16.658   2.329  1.00 25.04           C  
ANISOU 2402  C   SER A 300     3559   3262   2693    117    -56   -165       C  
ATOM   2403  O   SER A 300     -28.635 -16.095   2.940  1.00 27.53           O  
ANISOU 2403  O   SER A 300     3911   3563   2987    148      3   -183       O  
ATOM   2404  CB  SER A 300     -28.950 -18.331   0.958  1.00 21.51           C  
ANISOU 2404  CB  SER A 300     3002   2857   2314    101     17    -75       C  
ATOM   2405  OG  SER A 300     -28.447 -19.358   1.816  1.00 23.87           O  
ANISOU 2405  OG  SER A 300     3367   3168   2534    103      8    -63       O  
ATOM   2406  N   THR A 301     -26.519 -16.882   2.868  1.00 27.18           N  
ANISOU 2406  N   THR A 301     3863   3545   2920    111   -132   -196       N  
ATOM   2407  CA  THR A 301     -26.134 -16.449   4.208  1.00 27.90           C  
ANISOU 2407  CA  THR A 301     4045   3628   2927    141   -163   -253       C  
ATOM   2408  C   THR A 301     -24.957 -15.490   4.124  1.00 29.33           C  
ANISOU 2408  C   THR A 301     4206   3798   3140    108   -242   -328       C  
ATOM   2409  O   THR A 301     -24.082 -15.645   3.261  1.00 26.30           O  
ANISOU 2409  O   THR A 301     3744   3428   2819     65   -288   -339       O  
ATOM   2410  CB  THR A 301     -25.713 -17.622   5.088  1.00 29.85           C  
ANISOU 2410  CB  THR A 301     4367   3900   3075    181   -201   -244       C  
ATOM   2411  OG1 THR A 301     -24.829 -18.473   4.338  1.00 28.88           O  
ANISOU 2411  OG1 THR A 301     4178   3807   2988    168   -269   -228       O  
ATOM   2412  CG2 THR A 301     -26.939 -18.411   5.590  1.00 27.83           C  
ANISOU 2412  CG2 THR A 301     4181   3635   2759    203    -92   -189       C  
ATOM   2413  N   THR A 302     -24.925 -14.518   5.044  1.00 26.72           N  
ANISOU 2413  N   THR A 302     3945   3442   2767    123   -250   -391       N  
ATOM   2414  CA  THR A 302     -23.764 -13.647   5.172  1.00 28.12           C  
ANISOU 2414  CA  THR A 302     4109   3610   2967     82   -323   -485       C  
ATOM   2415  C   THR A 302     -22.564 -14.452   5.663  1.00 32.14           C  
ANISOU 2415  C   THR A 302     4600   4175   3436    101   -434   -538       C  
ATOM   2416  O   THR A 302     -22.682 -15.612   6.067  1.00 27.76           O  
ANISOU 2416  O   THR A 302     4083   3652   2813    160   -455   -494       O  
ATOM   2417  CB  THR A 302     -24.024 -12.496   6.148  1.00 26.72           C  
ANISOU 2417  CB  THR A 302     4022   3391   2742     98   -310   -547       C  
ATOM   2418  OG1 THR A 302     -24.097 -13.005   7.488  1.00 27.63           O  
ANISOU 2418  OG1 THR A 302     4230   3529   2738    167   -340   -563       O  
ATOM   2419  CG2 THR A 302     -25.310 -11.746   5.792  1.00 27.09           C  
ANISOU 2419  CG2 THR A 302     4095   3384   2815    110   -207   -502       C  
ATOM   2420  N   ALA A 303     -21.391 -13.813   5.636  1.00 29.22           N  
ANISOU 2420  N   ALA A 303     4177   3815   3110     52   -507   -644       N  
ATOM   2421  CA  ALA A 303     -20.187 -14.491   6.098  1.00 31.39           C  
ANISOU 2421  CA  ALA A 303     4413   4156   3359     84   -633   -723       C  
ATOM   2422  C   ALA A 303     -20.307 -14.943   7.546  1.00 30.72           C  
ANISOU 2422  C   ALA A 303     4455   4085   3131    191   -698   -739       C  
ATOM   2423  O   ALA A 303     -19.597 -15.867   7.958  1.00 28.31           O  
ANISOU 2423  O   ALA A 303     4156   3830   2770    262   -804   -769       O  
ATOM   2424  CB  ALA A 303     -18.967 -13.576   5.942  1.00 35.85           C  
ANISOU 2424  CB  ALA A 303     4887   4732   4003      4   -690   -866       C  
ATOM   2425  N   SER A 304     -21.196 -14.323   8.319  1.00 28.77           N  
ANISOU 2425  N   SER A 304     4323   3793   2816    214   -636   -721       N  
ATOM   2426  CA  SER A 304     -21.404 -14.668   9.717  1.00 30.31           C  
ANISOU 2426  CA  SER A 304     4670   3986   2859    311   -675   -732       C  
ATOM   2427  C   SER A 304     -22.599 -15.593   9.921  1.00 32.11           C  
ANISOU 2427  C   SER A 304     5001   4191   3009    357   -571   -609       C  
ATOM   2428  O   SER A 304     -22.946 -15.899  11.071  1.00 34.37           O  
ANISOU 2428  O   SER A 304     5444   4458   3156    430   -566   -604       O  
ATOM   2429  CB  SER A 304     -21.570 -13.394  10.548  1.00 30.46           C  
ANISOU 2429  CB  SER A 304     4763   3969   2844    304   -666   -808       C  
ATOM   2430  OG  SER A 304     -20.400 -12.581  10.462  1.00 32.09           O  
ANISOU 2430  OG  SER A 304     4880   4194   3117    250   -762   -941       O  
ATOM   2431  N   GLY A 305     -23.229 -16.044   8.837  1.00 32.00           N  
ANISOU 2431  N   GLY A 305     4906   4173   3078    312   -481   -519       N  
ATOM   2432  CA  GLY A 305     -24.278 -17.040   8.905  1.00 30.87           C  
ANISOU 2432  CA  GLY A 305     4832   4015   2881    336   -379   -418       C  
ATOM   2433  C   GLY A 305     -25.698 -16.508   8.942  1.00 29.14           C  
ANISOU 2433  C   GLY A 305     4634   3761   2678    313   -231   -378       C  
ATOM   2434  O   GLY A 305     -26.628 -17.303   9.103  1.00 31.25           O  
ANISOU 2434  O   GLY A 305     4954   4016   2903    321   -129   -315       O  
ATOM   2435  N   ARG A 306     -25.904 -15.198   8.826  1.00 27.77           N  
ANISOU 2435  N   ARG A 306     4424   3567   2562    286   -211   -423       N  
ATOM   2436  CA  ARG A 306     -27.260 -14.665   8.871  1.00 31.39           C  
ANISOU 2436  CA  ARG A 306     4893   3997   3038    285    -81   -401       C  
ATOM   2437  C   ARG A 306     -27.965 -14.921   7.539  1.00 24.65           C  
ANISOU 2437  C   ARG A 306     3914   3154   2300    248    -18   -340       C  
ATOM   2438  O   ARG A 306     -27.394 -14.684   6.471  1.00 26.40           O  
ANISOU 2438  O   ARG A 306     4041   3379   2610    211    -71   -337       O  
ATOM   2439  CB  ARG A 306     -27.244 -13.171   9.191  1.00 29.46           C  
ANISOU 2439  CB  ARG A 306     4670   3717   2809    284    -88   -471       C  
ATOM   2440  CG  ARG A 306     -28.633 -12.552   9.261  1.00 30.54           C  
ANISOU 2440  CG  ARG A 306     4813   3826   2965    303     37   -463       C  
ATOM   2441  CD  ARG A 306     -28.618 -11.070   9.696  1.00 30.11           C  
ANISOU 2441  CD  ARG A 306     4809   3723   2908    315     30   -536       C  
ATOM   2442  NE  ARG A 306     -28.013 -10.200   8.685  1.00 29.62           N  
ANISOU 2442  NE  ARG A 306     4679   3631   2943    270    -25   -557       N  
ATOM   2443  CZ  ARG A 306     -28.645  -9.739   7.608  1.00 37.09           C  
ANISOU 2443  CZ  ARG A 306     5560   4551   3981    267     18   -527       C  
ATOM   2444  NH1 ARG A 306     -28.000  -8.961   6.750  1.00 34.70           N  
ANISOU 2444  NH1 ARG A 306     5237   4204   3745    222    -23   -545       N  
ATOM   2445  NH2 ARG A 306     -29.917 -10.053   7.381  1.00 31.35           N  
ANISOU 2445  NH2 ARG A 306     4796   3841   3275    311    104   -488       N  
ATOM   2446  N   VAL A 307     -29.210 -15.392   7.608  1.00 29.56           N  
ANISOU 2446  N   VAL A 307     4535   3778   2917    257     99   -303       N  
ATOM   2447  CA  VAL A 307     -29.970 -15.745   6.410  1.00 28.58           C  
ANISOU 2447  CA  VAL A 307     4289   3673   2896    232    151   -259       C  
ATOM   2448  C   VAL A 307     -30.594 -14.492   5.808  1.00 34.03           C  
ANISOU 2448  C   VAL A 307     4917   4343   3669    247    170   -288       C  
ATOM   2449  O   VAL A 307     -31.238 -13.706   6.515  1.00 28.79           O  
ANISOU 2449  O   VAL A 307     4300   3660   2980    282    224   -332       O  
ATOM   2450  CB  VAL A 307     -31.058 -16.785   6.731  1.00 34.54           C  
ANISOU 2450  CB  VAL A 307     5057   4446   3623    226    273   -230       C  
ATOM   2451  CG1 VAL A 307     -31.857 -17.100   5.459  1.00 32.95           C  
ANISOU 2451  CG1 VAL A 307     4711   4272   3538    202    312   -205       C  
ATOM   2452  CG2 VAL A 307     -30.451 -18.059   7.319  1.00 28.41           C  
ANISOU 2452  CG2 VAL A 307     4382   3666   2746    220    259   -193       C  
ATOM   2453  N   ILE A 308     -30.423 -14.319   4.496  1.00 27.66           N  
ANISOU 2453  N   ILE A 308     4021   3535   2954    229    127   -265       N  
ATOM   2454  CA  ILE A 308     -31.116 -13.287   3.725  1.00 28.50           C  
ANISOU 2454  CA  ILE A 308     4083   3613   3131    261    140   -282       C  
ATOM   2455  C   ILE A 308     -32.436 -13.889   3.259  1.00 31.48           C  
ANISOU 2455  C   ILE A 308     4370   4033   3559    286    212   -269       C  
ATOM   2456  O   ILE A 308     -32.442 -14.806   2.436  1.00 28.99           O  
ANISOU 2456  O   ILE A 308     3984   3748   3284    258    202   -227       O  
ATOM   2457  CB  ILE A 308     -30.273 -12.819   2.533  1.00 32.68           C  
ANISOU 2457  CB  ILE A 308     4591   4109   3718    231     66   -265       C  
ATOM   2458  CG1 ILE A 308     -28.859 -12.443   2.989  1.00 31.99           C  
ANISOU 2458  CG1 ILE A 308     4562   3997   3594    182      1   -297       C  
ATOM   2459  CG2 ILE A 308     -30.961 -11.654   1.799  1.00 28.05           C  
ANISOU 2459  CG2 ILE A 308     4009   3470   3179    282     73   -282       C  
ATOM   2460  CD1 ILE A 308     -28.846 -11.377   4.056  1.00 40.86           C  
ANISOU 2460  CD1 ILE A 308     5776   5080   4667    205      9   -361       C  
ATOM   2461  N   GLU A 309     -33.559 -13.382   3.774  1.00 25.14           N  
ANISOU 2461  N   GLU A 309     3559   3233   2759    338    286   -318       N  
ATOM   2462  CA  GLU A 309     -34.799 -14.145   3.622  1.00 29.51           C  
ANISOU 2462  CA  GLU A 309     4012   3842   3357    345    372   -332       C  
ATOM   2463  C   GLU A 309     -35.436 -14.010   2.238  1.00 30.51           C  
ANISOU 2463  C   GLU A 309     4023   3988   3582    385    334   -336       C  
ATOM   2464  O   GLU A 309     -35.987 -14.984   1.717  1.00 34.06           O  
ANISOU 2464  O   GLU A 309     4375   4489   4079    360    364   -329       O  
ATOM   2465  CB  GLU A 309     -35.799 -13.736   4.697  1.00 26.98           C  
ANISOU 2465  CB  GLU A 309     3708   3531   3012    382    478   -402       C  
ATOM   2466  CG  GLU A 309     -35.401 -14.255   6.076  1.00 29.21           C  
ANISOU 2466  CG  GLU A 309     4113   3804   3182    339    541   -395       C  
ATOM   2467  CD  GLU A 309     -36.393 -13.884   7.162  1.00 38.19           C  
ANISOU 2467  CD  GLU A 309     5279   4946   4287    367    666   -466       C  
ATOM   2468  OE1 GLU A 309     -37.336 -14.664   7.395  1.00 42.38           O  
ANISOU 2468  OE1 GLU A 309     5753   5515   4833    336    792   -492       O  
ATOM   2469  OE2 GLU A 309     -36.215 -12.823   7.787  1.00 45.61           O  
ANISOU 2469  OE2 GLU A 309     6299   5847   5184    413    648   -502       O  
ATOM   2470  N   GLU A 310     -35.411 -12.826   1.638  1.00 29.06           N  
ANISOU 2470  N   GLU A 310     3860   3758   3424    451    268   -352       N  
ATOM   2471  CA  GLU A 310     -36.224 -12.556   0.457  1.00 28.33           C  
ANISOU 2471  CA  GLU A 310     3681   3677   3407    525    229   -372       C  
ATOM   2472  C   GLU A 310     -35.340 -12.259  -0.744  1.00 27.70           C  
ANISOU 2472  C   GLU A 310     3651   3541   3333    518    131   -314       C  
ATOM   2473  O   GLU A 310     -34.468 -11.383  -0.688  1.00 27.37           O  
ANISOU 2473  O   GLU A 310     3723   3423   3253    508     96   -299       O  
ATOM   2474  CB  GLU A 310     -37.197 -11.401   0.706  1.00 36.41           C  
ANISOU 2474  CB  GLU A 310     4703   4684   4447    640    241   -452       C  
ATOM   2475  CG  GLU A 310     -38.264 -11.737   1.727  1.00 36.39           C  
ANISOU 2475  CG  GLU A 310     4621   4748   4456    648    355   -527       C  
ATOM   2476  CD  GLU A 310     -39.433 -10.772   1.699  1.00 49.88           C  
ANISOU 2476  CD  GLU A 310     6275   6465   6211    781    360   -625       C  
ATOM   2477  OE1 GLU A 310     -39.510  -9.947   0.764  1.00 50.75           O  
ANISOU 2477  OE1 GLU A 310     6409   6530   6342    880    262   -629       O  
ATOM   2478  OE2 GLU A 310     -40.278 -10.841   2.616  1.00 63.51           O  
ANISOU 2478  OE2 GLU A 310     7945   8240   7948    791    466   -703       O  
ATOM   2479  N   TRP A 311     -35.585 -12.992  -1.826  1.00 31.09           N  
ANISOU 2479  N   TRP A 311     3997   4005   3809    517     99   -290       N  
ATOM   2480  CA  TRP A 311     -34.823 -12.925  -3.063  1.00 29.71           C  
ANISOU 2480  CA  TRP A 311     3866   3784   3638    502     23   -233       C  
ATOM   2481  C   TRP A 311     -35.790 -12.688  -4.207  1.00 29.95           C  
ANISOU 2481  C   TRP A 311     3846   3821   3714    607    -32   -260       C  
ATOM   2482  O   TRP A 311     -37.004 -12.850  -4.063  1.00 27.53           O  
ANISOU 2482  O   TRP A 311     3430   3579   3452    675    -13   -327       O  
ATOM   2483  CB  TRP A 311     -34.023 -14.218  -3.290  1.00 27.10           C  
ANISOU 2483  CB  TRP A 311     3499   3490   3307    397     26   -175       C  
ATOM   2484  CG  TRP A 311     -32.979 -14.384  -2.237  1.00 29.85           C  
ANISOU 2484  CG  TRP A 311     3910   3828   3603    320     50   -158       C  
ATOM   2485  CD1 TRP A 311     -33.179 -14.676  -0.919  1.00 31.24           C  
ANISOU 2485  CD1 TRP A 311     4094   4034   3742    304    111   -183       C  
ATOM   2486  CD2 TRP A 311     -31.569 -14.230  -2.409  1.00 28.71           C  
ANISOU 2486  CD2 TRP A 311     3834   3640   3434    255     10   -127       C  
ATOM   2487  NE1 TRP A 311     -31.975 -14.720  -0.254  1.00 28.34           N  
ANISOU 2487  NE1 TRP A 311     3802   3646   3321    248     92   -167       N  
ATOM   2488  CE2 TRP A 311     -30.969 -14.445  -1.146  1.00 26.97           C  
ANISOU 2488  CE2 TRP A 311     3650   3433   3163    215     29   -141       C  
ATOM   2489  CE3 TRP A 311     -30.752 -13.946  -3.512  1.00 25.96           C  
ANISOU 2489  CE3 TRP A 311     3521   3244   3100    225    -35    -98       C  
ATOM   2490  CZ2 TRP A 311     -29.586 -14.383  -0.953  1.00 25.59           C  
ANISOU 2490  CZ2 TRP A 311     3521   3239   2964    155    -11   -140       C  
ATOM   2491  CZ3 TRP A 311     -29.373 -13.885  -3.323  1.00 27.77           C  
ANISOU 2491  CZ3 TRP A 311     3791   3450   3311    147    -51    -96       C  
ATOM   2492  CH2 TRP A 311     -28.806 -14.096  -2.047  1.00 29.24           C  
ANISOU 2492  CH2 TRP A 311     3988   3663   3459    116    -48   -124       C  
ATOM   2493  N   CYS A 312     -35.247 -12.308  -5.358  1.00 26.58           N  
ANISOU 2493  N   CYS A 312     3500   3326   3272    623    -98   -216       N  
ATOM   2494  CA  CYS A 312     -36.086 -12.105  -6.525  1.00 27.91           C  
ANISOU 2494  CA  CYS A 312     3648   3492   3465    737   -170   -238       C  
ATOM   2495  C   CYS A 312     -35.290 -12.470  -7.767  1.00 25.79           C  
ANISOU 2495  C   CYS A 312     3439   3182   3178    693   -216   -168       C  
ATOM   2496  O   CYS A 312     -34.072 -12.660  -7.722  1.00 26.74           O  
ANISOU 2496  O   CYS A 312     3621   3266   3273    580   -189   -112       O  
ATOM   2497  CB  CYS A 312     -36.603 -10.658  -6.618  1.00 31.54           C  
ANISOU 2497  CB  CYS A 312     4215   3872   3897    877   -212   -280       C  
ATOM   2498  SG  CYS A 312     -35.290  -9.378  -6.714  1.00 35.22           S  
ANISOU 2498  SG  CYS A 312     4925   4173   4283    834   -207   -225       S  
ATOM   2499  N   CYS A 313     -36.006 -12.557  -8.883  1.00 27.49           N  
ANISOU 2499  N   CYS A 313     3632   3406   3407    789   -289   -183       N  
ATOM   2500  CA  CYS A 313     -35.403 -12.656 -10.205  1.00 24.35           C  
ANISOU 2500  CA  CYS A 313     3329   2947   2975    780   -339   -124       C  
ATOM   2501  C   CYS A 313     -36.357 -12.001 -11.190  1.00 29.02           C  
ANISOU 2501  C   CYS A 313     3975   3503   3547    956   -439   -163       C  
ATOM   2502  O   CYS A 313     -37.566 -11.920 -10.942  1.00 29.04           O  
ANISOU 2502  O   CYS A 313     3867   3575   3592   1071   -476   -247       O  
ATOM   2503  CB  CYS A 313     -35.128 -14.106 -10.606  1.00 28.18           C  
ANISOU 2503  CB  CYS A 313     3701   3512   3496    683   -329    -92       C  
ATOM   2504  SG  CYS A 313     -36.605 -15.104 -10.902  1.00 31.12           S  
ANISOU 2504  SG  CYS A 313     3868   4013   3942    753   -370   -170       S  
ATOM   2505  N   ARG A 314     -35.809 -11.520 -12.307  1.00 27.97           N  
ANISOU 2505  N   ARG A 314     4020   3261   3345    982   -480   -109       N  
ATOM   2506  CA  ARG A 314     -36.650 -10.766 -13.230  1.00 29.47           C  
ANISOU 2506  CA  ARG A 314     4315   3393   3490   1173   -587   -143       C  
ATOM   2507  C   ARG A 314     -37.609 -11.678 -13.985  1.00 29.71           C  
ANISOU 2507  C   ARG A 314     4193   3532   3564   1256   -678   -194       C  
ATOM   2508  O   ARG A 314     -38.784 -11.334 -14.162  1.00 35.24           O  
ANISOU 2508  O   ARG A 314     4839   4270   4281   1430   -771   -283       O  
ATOM   2509  CB  ARG A 314     -35.786  -9.967 -14.207  1.00 32.59           C  
ANISOU 2509  CB  ARG A 314     4983   3619   3779   1175   -591    -69       C  
ATOM   2510  CG  ARG A 314     -35.173  -8.715 -13.581  1.00 30.12           C  
ANISOU 2510  CG  ARG A 314     4850   3177   3417   1147   -523    -53       C  
ATOM   2511  CD  ARG A 314     -34.461  -7.855 -14.643  1.00 33.73           C  
ANISOU 2511  CD  ARG A 314     5605   3447   3762   1155   -513      8       C  
ATOM   2512  NE  ARG A 314     -34.024  -6.586 -14.059  1.00 35.78           N  
ANISOU 2512  NE  ARG A 314     6045   3573   3976   1138   -449      8       N  
ATOM   2513  CZ  ARG A 314     -33.394  -5.631 -14.731  1.00 37.87           C  
ANISOU 2513  CZ  ARG A 314     6597   3650   4141   1128   -408     51       C  
ATOM   2514  NH1 ARG A 314     -33.115  -5.797 -16.016  1.00 33.52           N  
ANISOU 2514  NH1 ARG A 314     6194   3022   3519   1136   -423    101       N  
ATOM   2515  NH2 ARG A 314     -33.044  -4.512 -14.116  1.00 37.01           N  
ANISOU 2515  NH2 ARG A 314     6640   3423   3999   1102   -344     39       N  
ATOM   2516  N   GLU A 315     -37.133 -12.838 -14.433  1.00 34.09           N  
ANISOU 2516  N   GLU A 315     4671   4140   4143   1138   -657   -153       N  
ATOM   2517  CA  GLU A 315     -37.955 -13.716 -15.262  1.00 35.65           C  
ANISOU 2517  CA  GLU A 315     4740   4428   4376   1204   -744   -203       C  
ATOM   2518  C   GLU A 315     -37.473 -15.164 -15.220  1.00 31.33           C  
ANISOU 2518  C   GLU A 315     4056   3964   3883   1037   -681   -170       C  
ATOM   2519  O   GLU A 315     -37.656 -15.917 -16.182  1.00 32.39           O  
ANISOU 2519  O   GLU A 315     4154   4132   4020   1048   -740   -174       O  
ATOM   2520  CB  GLU A 315     -37.974 -13.205 -16.706  1.00 44.21           C  
ANISOU 2520  CB  GLU A 315     6020   5413   5365   1335   -854   -179       C  
ATOM   2521  CG  GLU A 315     -36.596 -12.933 -17.285  1.00 48.20           C  
ANISOU 2521  CG  GLU A 315     6752   5781   5780   1230   -791    -64       C  
ATOM   2522  CD  GLU A 315     -36.655 -12.050 -18.522  1.00 64.67           C  
ANISOU 2522  CD  GLU A 315     9102   7726   7743   1378   -878    -40       C  
ATOM   2523  OE1 GLU A 315     -37.500 -12.312 -19.403  1.00 59.41           O  
ANISOU 2523  OE1 GLU A 315     8418   7097   7060   1524  -1007    -90       O  
ATOM   2524  OE2 GLU A 315     -35.873 -11.078 -18.598  1.00 80.81           O  
ANISOU 2524  OE2 GLU A 315    11382   9619   9705   1351   -817     20       O  
ATOM   2525  N   CYS A 316     -36.849 -15.566 -14.119  1.00 30.15           N  
ANISOU 2525  N   CYS A 316     3843   3843   3767    890   -569   -139       N  
ATOM   2526  CA  CYS A 316     -36.473 -16.961 -13.965  1.00 28.12           C  
ANISOU 2526  CA  CYS A 316     3466   3663   3558    749   -511   -115       C  
ATOM   2527  C   CYS A 316     -37.712 -17.800 -13.608  1.00 32.38           C  
ANISOU 2527  C   CYS A 316     3789   4329   4184    765   -513   -212       C  
ATOM   2528  O   CYS A 316     -38.807 -17.274 -13.391  1.00 32.52           O  
ANISOU 2528  O   CYS A 316     3732   4388   4236    879   -552   -305       O  
ATOM   2529  CB  CYS A 316     -35.353 -17.086 -12.922  1.00 28.89           C  
ANISOU 2529  CB  CYS A 316     3592   3739   3647    608   -406    -55       C  
ATOM   2530  SG  CYS A 316     -35.847 -16.984 -11.181  1.00 34.02           S  
ANISOU 2530  SG  CYS A 316     4140   4448   4338    582   -323   -109       S  
ATOM   2531  N   THR A 317     -37.550 -19.124 -13.589  1.00 30.82           N  
ANISOU 2531  N   THR A 317     3492   4192   4026    649   -465   -199       N  
ATOM   2532  CA  THR A 317     -38.649 -20.027 -13.275  1.00 28.40           C  
ANISOU 2532  CA  THR A 317     2989   3997   3805    629   -440   -295       C  
ATOM   2533  C   THR A 317     -38.435 -20.670 -11.911  1.00 33.94           C  
ANISOU 2533  C   THR A 317     3635   4729   4531    497   -304   -283       C  
ATOM   2534  O   THR A 317     -37.301 -20.844 -11.456  1.00 30.77           O  
ANISOU 2534  O   THR A 317     3331   4277   4082    409   -250   -192       O  
ATOM   2535  CB  THR A 317     -38.818 -21.141 -14.328  1.00 34.73           C  
ANISOU 2535  CB  THR A 317     3725   4839   4631    599   -485   -307       C  
ATOM   2536  OG1 THR A 317     -37.624 -21.924 -14.421  1.00 28.63           O  
ANISOU 2536  OG1 THR A 317     3029   4027   3823    474   -432   -202       O  
ATOM   2537  CG2 THR A 317     -39.165 -20.576 -15.694  1.00 30.80           C  
ANISOU 2537  CG2 THR A 317     3288   4317   4100    745   -631   -332       C  
ATOM   2538  N   MET A 318     -39.541 -21.023 -11.264  1.00 31.25           N  
ANISOU 2538  N   MET A 318     3141   4471   4263    488   -247   -387       N  
ATOM   2539  CA  MET A 318     -39.504 -21.773 -10.007  1.00 29.41           C  
ANISOU 2539  CA  MET A 318     2868   4261   4044    361   -103   -385       C  
ATOM   2540  C   MET A 318     -39.645 -23.280 -10.277  1.00 32.17           C  
ANISOU 2540  C   MET A 318     3139   4652   4432    247    -51   -394       C  
ATOM   2541  O   MET A 318     -40.273 -23.665 -11.251  1.00 31.00           O  
ANISOU 2541  O   MET A 318     2896   4550   4334    277   -116   -457       O  
ATOM   2542  CB  MET A 318     -40.618 -21.292  -9.084  1.00 26.83           C  
ANISOU 2542  CB  MET A 318     2436   3990   3770    399    -39   -498       C  
ATOM   2543  CG  MET A 318     -40.522 -19.801  -8.768  1.00 31.45           C  
ANISOU 2543  CG  MET A 318     3107   4528   4315    516    -86   -495       C  
ATOM   2544  SD  MET A 318     -39.079 -19.422  -7.741  1.00 34.20           S  
ANISOU 2544  SD  MET A 318     3646   4784   4565    442    -25   -368       S  
ATOM   2545  CE  MET A 318     -38.017 -18.578  -8.912  1.00 33.98           C  
ANISOU 2545  CE  MET A 318     3776   4662   4474    509   -153   -277       C  
ATOM   2546  N   PRO A 319     -39.057 -24.141  -9.423  1.00 31.39           N  
ANISOU 2546  N   PRO A 319     3094   4530   4302    123     61   -336       N  
ATOM   2547  CA  PRO A 319     -38.194 -23.830  -8.273  1.00 33.27           C  
ANISOU 2547  CA  PRO A 319     3460   4714   4468     90    123   -261       C  
ATOM   2548  C   PRO A 319     -36.822 -23.272  -8.694  1.00 31.18           C  
ANISOU 2548  C   PRO A 319     3333   4380   4134    119     38   -156       C  
ATOM   2549  O   PRO A 319     -36.348 -23.547  -9.810  1.00 27.74           O  
ANISOU 2549  O   PRO A 319     2916   3929   3695    126    -35   -117       O  
ATOM   2550  CB  PRO A 319     -38.049 -25.185  -7.555  1.00 28.91           C  
ANISOU 2550  CB  PRO A 319     2928   4158   3900    -39    245   -239       C  
ATOM   2551  CG  PRO A 319     -38.354 -26.218  -8.608  1.00 35.09           C  
ANISOU 2551  CG  PRO A 319     3634   4969   4732    -82    222   -260       C  
ATOM   2552  CD  PRO A 319     -39.359 -25.583  -9.524  1.00 33.54           C  
ANISOU 2552  CD  PRO A 319     3302   4832   4611     11    134   -359       C  
ATOM   2553  N   PRO A 320     -36.199 -22.491  -7.811  1.00 31.40           N  
ANISOU 2553  N   PRO A 320     3454   4367   4110    131     55   -123       N  
ATOM   2554  CA  PRO A 320     -35.028 -21.705  -8.212  1.00 27.61           C  
ANISOU 2554  CA  PRO A 320     3085   3823   3580    160    -18    -56       C  
ATOM   2555  C   PRO A 320     -33.751 -22.525  -8.307  1.00 26.85           C  
ANISOU 2555  C   PRO A 320     3055   3701   3445     86    -19     20       C  
ATOM   2556  O   PRO A 320     -33.532 -23.482  -7.559  1.00 25.75           O  
ANISOU 2556  O   PRO A 320     2925   3572   3285     22     42     37       O  
ATOM   2557  CB  PRO A 320     -34.913 -20.656  -7.099  1.00 25.93           C  
ANISOU 2557  CB  PRO A 320     2934   3585   3335    189     11    -69       C  
ATOM   2558  CG  PRO A 320     -35.500 -21.347  -5.877  1.00 29.20           C  
ANISOU 2558  CG  PRO A 320     3310   4036   3747    137    118   -103       C  
ATOM   2559  CD  PRO A 320     -36.617 -22.211  -6.422  1.00 32.30           C  
ANISOU 2559  CD  PRO A 320     3574   4489   4209    120    148   -161       C  
ATOM   2560  N   LEU A 321     -32.893 -22.116  -9.243  1.00 22.39           N  
ANISOU 2560  N   LEU A 321     2546   3096   2866     99    -85     62       N  
ATOM   2561  CA  LEU A 321     -31.580 -22.732  -9.392  1.00 17.89           C  
ANISOU 2561  CA  LEU A 321     2026   2504   2266     39    -92    118       C  
ATOM   2562  C   LEU A 321     -30.708 -22.376  -8.194  1.00 25.21           C  
ANISOU 2562  C   LEU A 321     3015   3412   3151     17    -70    125       C  
ATOM   2563  O   LEU A 321     -30.521 -21.195  -7.883  1.00 25.19           O  
ANISOU 2563  O   LEU A 321     3057   3378   3136     45    -82    109       O  
ATOM   2564  CB  LEU A 321     -30.906 -22.246 -10.685  1.00 21.91           C  
ANISOU 2564  CB  LEU A 321     2581   2970   2772     52   -148    145       C  
ATOM   2565  CG  LEU A 321     -29.686 -23.015 -11.233  1.00 28.41           C  
ANISOU 2565  CG  LEU A 321     3427   3783   3585     -6   -155    187       C  
ATOM   2566  CD1 LEU A 321     -29.384 -22.572 -12.678  1.00 25.32           C  
ANISOU 2566  CD1 LEU A 321     3083   3349   3190      8   -192    204       C  
ATOM   2567  CD2 LEU A 321     -28.447 -22.855 -10.384  1.00 28.88           C  
ANISOU 2567  CD2 LEU A 321     3524   3830   3619    -46   -143    191       C  
ATOM   2568  N   SER A 322     -30.157 -23.391  -7.536  1.00 22.26           N  
ANISOU 2568  N   SER A 322     2655   3052   2750    -25    -47    145       N  
ATOM   2569  CA  SER A 322     -29.266 -23.168  -6.407  1.00 23.83           C  
ANISOU 2569  CA  SER A 322     2916   3238   2899    -32    -47    143       C  
ATOM   2570  C   SER A 322     -28.090 -24.128  -6.494  1.00 24.15           C  
ANISOU 2570  C   SER A 322     2976   3282   2918    -59    -77    169       C  
ATOM   2571  O   SER A 322     -28.144 -25.152  -7.182  1.00 26.25           O  
ANISOU 2571  O   SER A 322     3218   3558   3199    -77    -75    194       O  
ATOM   2572  CB  SER A 322     -29.988 -23.337  -5.055  1.00 22.11           C  
ANISOU 2572  CB  SER A 322     2725   3031   2644    -25     15    123       C  
ATOM   2573  OG  SER A 322     -30.259 -24.703  -4.771  1.00 25.05           O  
ANISOU 2573  OG  SER A 322     3108   3414   2995    -56     63    142       O  
ATOM   2574  N   PHE A 323     -27.010 -23.761  -5.801  1.00 21.30           N  
ANISOU 2574  N   PHE A 323     2656   2914   2525    -55   -112    151       N  
ATOM   2575  CA  PHE A 323     -25.819 -24.588  -5.654  1.00 19.19           C  
ANISOU 2575  CA  PHE A 323     2402   2658   2232    -57   -155    153       C  
ATOM   2576  C   PHE A 323     -25.593 -24.855  -4.171  1.00 23.53           C  
ANISOU 2576  C   PHE A 323     3027   3209   2706    -23   -164    137       C  
ATOM   2577  O   PHE A 323     -25.571 -23.911  -3.369  1.00 24.34           O  
ANISOU 2577  O   PHE A 323     3157   3305   2786     -9   -169    102       O  
ATOM   2578  CB  PHE A 323     -24.559 -23.909  -6.218  1.00 21.50           C  
ANISOU 2578  CB  PHE A 323     2663   2948   2558    -78   -203    118       C  
ATOM   2579  CG  PHE A 323     -24.719 -23.270  -7.592  1.00 24.73           C  
ANISOU 2579  CG  PHE A 323     3040   3334   3022   -110   -186    129       C  
ATOM   2580  CD1 PHE A 323     -25.264 -21.998  -7.716  1.00 23.56           C  
ANISOU 2580  CD1 PHE A 323     2915   3151   2885   -109   -166    118       C  
ATOM   2581  CD2 PHE A 323     -24.232 -23.905  -8.737  1.00 25.23           C  
ANISOU 2581  CD2 PHE A 323     3072   3401   3115   -135   -192    147       C  
ATOM   2582  CE1 PHE A 323     -25.370 -21.375  -8.966  1.00 26.60           C  
ANISOU 2582  CE1 PHE A 323     3310   3497   3298   -124   -154    130       C  
ATOM   2583  CE2 PHE A 323     -24.332 -23.291  -9.986  1.00 28.75           C  
ANISOU 2583  CE2 PHE A 323     3520   3813   3591   -159   -173    157       C  
ATOM   2584  CZ  PHE A 323     -24.904 -22.026 -10.097  1.00 26.00           C  
ANISOU 2584  CZ  PHE A 323     3214   3422   3243   -151   -156    151       C  
ATOM   2585  N   ARG A 324     -25.407 -26.132  -3.810  1.00 23.24           N  
ANISOU 2585  N   ARG A 324     3040   3171   2618     -4   -167    160       N  
ATOM   2586  CA  ARG A 324     -25.153 -26.551  -2.435  1.00 25.79           C  
ANISOU 2586  CA  ARG A 324     3473   3482   2845     44   -181    152       C  
ATOM   2587  C   ARG A 324     -23.679 -26.913  -2.307  1.00 26.25           C  
ANISOU 2587  C   ARG A 324     3536   3558   2879     92   -287    118       C  
ATOM   2588  O   ARG A 324     -23.196 -27.806  -3.011  1.00 24.69           O  
ANISOU 2588  O   ARG A 324     3314   3366   2699     97   -312    134       O  
ATOM   2589  CB  ARG A 324     -26.035 -27.742  -2.043  1.00 25.14           C  
ANISOU 2589  CB  ARG A 324     3479   3368   2705     39   -102    197       C  
ATOM   2590  CG  ARG A 324     -27.512 -27.574  -2.464  1.00 27.95           C  
ANISOU 2590  CG  ARG A 324     3780   3724   3116    -20      4    210       C  
ATOM   2591  CD  ARG A 324     -28.096 -26.336  -1.805  1.00 33.11           C  
ANISOU 2591  CD  ARG A 324     4426   4382   3771    -14     35    175       C  
ATOM   2592  NE  ARG A 324     -29.430 -25.978  -2.296  1.00 29.52           N  
ANISOU 2592  NE  ARG A 324     3889   3942   3385    -50    112    163       N  
ATOM   2593  CZ  ARG A 324     -30.530 -26.042  -1.559  1.00 31.63           C  
ANISOU 2593  CZ  ARG A 324     4183   4203   3634    -68    215    144       C  
ATOM   2594  NH1 ARG A 324     -30.464 -26.469  -0.297  1.00 29.84           N  
ANISOU 2594  NH1 ARG A 324     4089   3943   3306    -60    265    149       N  
ATOM   2595  NH2 ARG A 324     -31.693 -25.670  -2.076  1.00 31.85           N  
ANISOU 2595  NH2 ARG A 324     4106   4257   3738    -89    269    111       N  
ATOM   2596  N   ALA A 325     -22.972 -26.226  -1.406  1.00 23.77           N  
ANISOU 2596  N   ALA A 325     3249   3257   2527    132   -352     60       N  
ATOM   2597  CA  ALA A 325     -21.541 -26.398  -1.188  1.00 21.43           C  
ANISOU 2597  CA  ALA A 325     2931   2992   2218    186   -467     -6       C  
ATOM   2598  C   ALA A 325     -21.280 -26.486   0.311  1.00 26.07           C  
ANISOU 2598  C   ALA A 325     3647   3571   2688    272   -527    -38       C  
ATOM   2599  O   ALA A 325     -22.194 -26.332   1.128  1.00 26.76           O  
ANISOU 2599  O   ALA A 325     3840   3622   2707    274   -462     -6       O  
ATOM   2600  CB  ALA A 325     -20.753 -25.250  -1.833  1.00 26.28           C  
ANISOU 2600  CB  ALA A 325     3414   3640   2930    133   -498    -78       C  
ATOM   2601  N   LYS A 326     -20.022 -26.735   0.694  1.00 24.97           N  
ANISOU 2601  N   LYS A 326     3500   3466   2521    349   -653   -113       N  
ATOM   2602  CA  LYS A 326     -19.751 -26.948   2.116  1.00 23.89           C  
ANISOU 2602  CA  LYS A 326     3510   3315   2250    455   -730   -145       C  
ATOM   2603  C   LYS A 326     -20.014 -25.690   2.934  1.00 27.57           C  
ANISOU 2603  C   LYS A 326     3996   3782   2699    435   -721   -189       C  
ATOM   2604  O   LYS A 326     -20.340 -25.785   4.124  1.00 25.27           O  
ANISOU 2604  O   LYS A 326     3865   3456   2282    498   -727   -182       O  
ATOM   2605  CB  LYS A 326     -18.311 -27.430   2.331  1.00 33.11           C  
ANISOU 2605  CB  LYS A 326     4650   4532   3399    562   -893   -238       C  
ATOM   2606  CG  LYS A 326     -17.252 -26.360   2.097  1.00 39.04           C  
ANISOU 2606  CG  LYS A 326     5223   5357   4254    529   -973   -369       C  
ATOM   2607  CD  LYS A 326     -15.859 -26.869   2.441  1.00 42.65           C  
ANISOU 2607  CD  LYS A 326     5638   5875   4692    650  -1144   -488       C  
ATOM   2608  CE  LYS A 326     -14.824 -25.760   2.312  1.00 48.09           C  
ANISOU 2608  CE  LYS A 326     6140   6641   5491    601  -1211   -644       C  
ATOM   2609  NZ  LYS A 326     -13.465 -26.233   2.683  1.00 50.42           N  
ANISOU 2609  NZ  LYS A 326     6367   7013   5780    727  -1389   -789       N  
ATOM   2610  N   ASP A 327     -19.906 -24.510   2.325  1.00 25.15           N  
ANISOU 2610  N   ASP A 327     3549   3501   2505    347   -697   -232       N  
ATOM   2611  CA  ASP A 327     -20.122 -23.285   3.082  1.00 30.11           C  
ANISOU 2611  CA  ASP A 327     4201   4122   3118    328   -689   -280       C  
ATOM   2612  C   ASP A 327     -21.567 -22.808   3.040  1.00 35.83           C  
ANISOU 2612  C   ASP A 327     4970   4798   3844    270   -549   -202       C  
ATOM   2613  O   ASP A 327     -21.876 -21.762   3.620  1.00 29.48           O  
ANISOU 2613  O   ASP A 327     4191   3980   3028    255   -528   -235       O  
ATOM   2614  CB  ASP A 327     -19.193 -22.171   2.587  1.00 22.76           C  
ANISOU 2614  CB  ASP A 327     3121   3230   2297    265   -735   -384       C  
ATOM   2615  CG  ASP A 327     -19.493 -21.729   1.168  1.00 30.00           C  
ANISOU 2615  CG  ASP A 327     3926   4135   3336    156   -641   -346       C  
ATOM   2616  OD1 ASP A 327     -19.962 -22.550   0.358  1.00 27.35           O  
ANISOU 2616  OD1 ASP A 327     3582   3790   3021    145   -590   -263       O  
ATOM   2617  OD2 ASP A 327     -19.239 -20.546   0.857  1.00 30.84           O  
ANISOU 2617  OD2 ASP A 327     3969   4236   3513     82   -620   -403       O  
ATOM   2618  N   GLY A 328     -22.456 -23.533   2.368  1.00 29.31           N  
ANISOU 2618  N   GLY A 328     4148   3951   3038    239   -457   -112       N  
ATOM   2619  CA  GLY A 328     -23.853 -23.151   2.400  1.00 24.95           C  
ANISOU 2619  CA  GLY A 328     3622   3365   2491    197   -332    -61       C  
ATOM   2620  C   GLY A 328     -24.525 -23.231   1.043  1.00 28.56           C  
ANISOU 2620  C   GLY A 328     3974   3825   3053    131   -261    -11       C  
ATOM   2621  O   GLY A 328     -24.108 -24.005   0.176  1.00 29.36           O  
ANISOU 2621  O   GLY A 328     4023   3940   3193    120   -285     12       O  
ATOM   2622  N   CYS A 329     -25.559 -22.421   0.850  1.00 24.55           N  
ANISOU 2622  N   CYS A 329     3439   3303   2586     98   -182     -2       N  
ATOM   2623  CA  CYS A 329     -26.434 -22.498  -0.313  1.00 24.23           C  
ANISOU 2623  CA  CYS A 329     3316   3263   2628     56   -119     38       C  
ATOM   2624  C   CYS A 329     -26.287 -21.222  -1.126  1.00 23.77           C  
ANISOU 2624  C   CYS A 329     3186   3198   2647     31   -137     11       C  
ATOM   2625  O   CYS A 329     -26.420 -20.121  -0.578  1.00 26.22           O  
ANISOU 2625  O   CYS A 329     3524   3491   2948     40   -132    -27       O  
ATOM   2626  CB  CYS A 329     -27.896 -22.677   0.125  1.00 26.22           C  
ANISOU 2626  CB  CYS A 329     3596   3505   2861     52    -11     56       C  
ATOM   2627  SG  CYS A 329     -29.073 -22.937  -1.258  1.00 33.18           S  
ANISOU 2627  SG  CYS A 329     4362   4402   3845     15     50     82       S  
ATOM   2628  N   TRP A 330     -26.037 -21.374  -2.427  1.00 21.74           N  
ANISOU 2628  N   TRP A 330     2859   2944   2457      0   -151     32       N  
ATOM   2629  CA  TRP A 330     -25.820 -20.263  -3.345  1.00 24.62           C  
ANISOU 2629  CA  TRP A 330     3188   3283   2882    -27   -159     14       C  
ATOM   2630  C   TRP A 330     -26.920 -20.232  -4.400  1.00 28.64           C  
ANISOU 2630  C   TRP A 330     3664   3782   3436    -23   -119     52       C  
ATOM   2631  O   TRP A 330     -27.468 -21.273  -4.765  1.00 27.48           O  
ANISOU 2631  O   TRP A 330     3485   3659   3297    -22   -100     87       O  
ATOM   2632  CB  TRP A 330     -24.490 -20.399  -4.054  1.00 23.40           C  
ANISOU 2632  CB  TRP A 330     2994   3135   2761    -67   -205     -5       C  
ATOM   2633  CG  TRP A 330     -23.267 -20.397  -3.185  1.00 21.81           C  
ANISOU 2633  CG  TRP A 330     2796   2957   2532    -65   -266    -69       C  
ATOM   2634  CD1 TRP A 330     -22.843 -21.388  -2.343  1.00 25.07           C  
ANISOU 2634  CD1 TRP A 330     3232   3404   2889    -20   -314    -77       C  
ATOM   2635  CD2 TRP A 330     -22.277 -19.371  -3.141  1.00 20.80           C  
ANISOU 2635  CD2 TRP A 330     2651   2818   2434   -107   -291   -147       C  
ATOM   2636  NE1 TRP A 330     -21.655 -21.017  -1.746  1.00 21.67           N  
ANISOU 2636  NE1 TRP A 330     2787   2996   2452    -16   -386   -162       N  
ATOM   2637  CE2 TRP A 330     -21.281 -19.788  -2.237  1.00 23.24           C  
ANISOU 2637  CE2 TRP A 330     2948   3170   2711    -81   -367   -211       C  
ATOM   2638  CE3 TRP A 330     -22.129 -18.136  -3.800  1.00 24.28           C  
ANISOU 2638  CE3 TRP A 330     3095   3207   2921   -167   -253   -174       C  
ATOM   2639  CZ2 TRP A 330     -20.153 -19.010  -1.959  1.00 24.36           C  
ANISOU 2639  CZ2 TRP A 330     3052   3323   2882   -119   -410   -317       C  
ATOM   2640  CZ3 TRP A 330     -21.021 -17.362  -3.518  1.00 27.07           C  
ANISOU 2640  CZ3 TRP A 330     3429   3556   3299   -219   -275   -269       C  
ATOM   2641  CH2 TRP A 330     -20.042 -17.802  -2.601  1.00 29.61           C  
ANISOU 2641  CH2 TRP A 330     3708   3938   3603   -199   -354   -347       C  
ATOM   2642  N   TYR A 331     -27.226 -19.046  -4.919  1.00 26.75           N  
ANISOU 2642  N   TYR A 331     3438   3502   3222    -16   -112     39       N  
ATOM   2643  CA  TYR A 331     -28.307 -18.907  -5.890  1.00 25.18           C  
ANISOU 2643  CA  TYR A 331     3217   3294   3057     16    -97     60       C  
ATOM   2644  C   TYR A 331     -27.777 -18.687  -7.307  1.00 29.03           C  
ANISOU 2644  C   TYR A 331     3712   3745   3571     -8   -118     81       C  
ATOM   2645  O   TYR A 331     -26.685 -18.145  -7.504  1.00 24.34           O  
ANISOU 2645  O   TYR A 331     3155   3116   2979    -54   -124     65       O  
ATOM   2646  CB  TYR A 331     -29.228 -17.755  -5.493  1.00 21.88           C  
ANISOU 2646  CB  TYR A 331     2831   2848   2635     71    -79     30       C  
ATOM   2647  CG  TYR A 331     -30.411 -18.206  -4.678  1.00 27.72           C  
ANISOU 2647  CG  TYR A 331     3530   3633   3369    106    -35     14       C  
ATOM   2648  CD1 TYR A 331     -31.232 -19.233  -5.132  1.00 25.13           C  
ANISOU 2648  CD1 TYR A 331     3127   3350   3071    107    -15     26       C  
ATOM   2649  CD2 TYR A 331     -30.707 -17.615  -3.453  1.00 24.74           C  
ANISOU 2649  CD2 TYR A 331     3190   3250   2958    128     -3    -23       C  
ATOM   2650  CE1 TYR A 331     -32.333 -19.649  -4.404  1.00 23.85           C  
ANISOU 2650  CE1 TYR A 331     2921   3226   2913    119     49     -5       C  
ATOM   2651  CE2 TYR A 331     -31.812 -18.033  -2.703  1.00 22.72           C  
ANISOU 2651  CE2 TYR A 331     2901   3034   2699    149     61    -47       C  
ATOM   2652  CZ  TYR A 331     -32.619 -19.051  -3.187  1.00 25.54           C  
ANISOU 2652  CZ  TYR A 331     3176   3435   3093    139     92    -41       C  
ATOM   2653  OH  TYR A 331     -33.715 -19.479  -2.472  1.00 23.30           O  
ANISOU 2653  OH  TYR A 331     2851   3188   2815    139    178    -79       O  
ATOM   2654  N   GLY A 332     -28.572 -19.104  -8.302  1.00 22.68           N  
ANISOU 2654  N   GLY A 332     2879   2950   2790     21   -124    106       N  
ATOM   2655  CA  GLY A 332     -28.224 -18.825  -9.685  1.00 24.80           C  
ANISOU 2655  CA  GLY A 332     3184   3171   3065     12   -141    127       C  
ATOM   2656  C   GLY A 332     -28.032 -17.342  -9.942  1.00 25.57           C  
ANISOU 2656  C   GLY A 332     3386   3185   3145     26   -135    111       C  
ATOM   2657  O   GLY A 332     -28.519 -16.486  -9.198  1.00 23.95           O  
ANISOU 2657  O   GLY A 332     3213   2959   2928     67   -130     84       O  
ATOM   2658  N   MET A 333     -27.302 -17.038 -11.029  1.00 23.07           N  
ANISOU 2658  N   MET A 333     3137   2808   2822    -13   -126    127       N  
ATOM   2659  CA  MET A 333     -26.951 -15.648 -11.322  1.00 25.56           C  
ANISOU 2659  CA  MET A 333     3582   3019   3111    -23   -100    113       C  
ATOM   2660  C   MET A 333     -28.177 -14.749 -11.406  1.00 26.77           C  
ANISOU 2660  C   MET A 333     3808   3126   3236     90   -127    111       C  
ATOM   2661  O   MET A 333     -28.102 -13.564 -11.057  1.00 26.04           O  
ANISOU 2661  O   MET A 333     3817   2957   3120    100   -107     88       O  
ATOM   2662  CB  MET A 333     -26.159 -15.558 -12.625  1.00 22.51           C  
ANISOU 2662  CB  MET A 333     3277   2566   2711    -80    -68    134       C  
ATOM   2663  CG  MET A 333     -24.788 -16.194 -12.556  1.00 25.63           C  
ANISOU 2663  CG  MET A 333     3602   2997   3140   -194    -32    112       C  
ATOM   2664  SD  MET A 333     -23.961 -16.183 -14.160  1.00 24.96           S  
ANISOU 2664  SD  MET A 333     3606   2838   3041   -266     27    130       S  
ATOM   2665  CE  MET A 333     -23.795 -14.433 -14.536  1.00 27.10           C  
ANISOU 2665  CE  MET A 333     4085   2949   3262   -293     97    115       C  
ATOM   2666  N   GLU A 334     -29.309 -15.294 -11.862  1.00 22.64           N  
ANISOU 2666  N   GLU A 334     3233   2648   2720    179   -175    123       N  
ATOM   2667  CA  GLU A 334     -30.519 -14.503 -12.067  1.00 24.61           C  
ANISOU 2667  CA  GLU A 334     3535   2865   2949    309   -219    103       C  
ATOM   2668  C   GLU A 334     -31.151 -14.024 -10.766  1.00 28.96           C  
ANISOU 2668  C   GLU A 334     4041   3448   3515    352   -210     58       C  
ATOM   2669  O   GLU A 334     -31.963 -13.097 -10.798  1.00 26.42           O  
ANISOU 2669  O   GLU A 334     3783   3082   3174    460   -239     30       O  
ATOM   2670  CB  GLU A 334     -31.560 -15.325 -12.839  1.00 24.83           C  
ANISOU 2670  CB  GLU A 334     3481   2958   2996    388   -280    102       C  
ATOM   2671  CG  GLU A 334     -31.265 -15.529 -14.335  1.00 23.58           C  
ANISOU 2671  CG  GLU A 334     3409   2748   2802    395   -309    140       C  
ATOM   2672  CD  GLU A 334     -30.170 -16.559 -14.620  1.00 24.09           C  
ANISOU 2672  CD  GLU A 334     3428   2841   2883    268   -266    177       C  
ATOM   2673  OE1 GLU A 334     -29.651 -17.212 -13.673  1.00 23.96           O  
ANISOU 2673  OE1 GLU A 334     3309   2888   2905    186   -227    172       O  
ATOM   2674  OE2 GLU A 334     -29.830 -16.709 -15.816  1.00 26.48           O  
ANISOU 2674  OE2 GLU A 334     3812   3097   3153    262   -273    207       O  
ATOM   2675  N   ILE A 335     -30.814 -14.641  -9.637  1.00 26.41           N  
ANISOU 2675  N   ILE A 335     3623   3194   3217    281   -173     47       N  
ATOM   2676  CA  ILE A 335     -31.549 -14.477  -8.381  1.00 26.31           C  
ANISOU 2676  CA  ILE A 335     3554   3228   3215    320   -155      3       C  
ATOM   2677  C   ILE A 335     -30.741 -13.557  -7.461  1.00 26.40           C  
ANISOU 2677  C   ILE A 335     3649   3184   3198    274   -123    -15       C  
ATOM   2678  O   ILE A 335     -29.591 -13.859  -7.114  1.00 27.43           O  
ANISOU 2678  O   ILE A 335     3779   3318   3324    177   -104     -7       O  
ATOM   2679  CB  ILE A 335     -31.837 -15.850  -7.741  1.00 23.19           C  
ANISOU 2679  CB  ILE A 335     3024   2937   2849    279   -130      2       C  
ATOM   2680  CG1 ILE A 335     -32.692 -16.678  -8.710  1.00 27.15           C  
ANISOU 2680  CG1 ILE A 335     3442   3487   3385    317   -161      4       C  
ATOM   2681  CG2 ILE A 335     -32.506 -15.732  -6.353  1.00 28.89           C  
ANISOU 2681  CG2 ILE A 335     3707   3699   3570    300    -86    -44       C  
ATOM   2682  CD1 ILE A 335     -32.720 -18.190  -8.427  1.00 25.74           C  
ANISOU 2682  CD1 ILE A 335     3160   3388   3231    248   -129     16       C  
ATOM   2683  N   ARG A 336     -31.333 -12.419  -7.096  1.00 26.33           N  
ANISOU 2683  N   ARG A 336     3710   3124   3171    351   -124    -50       N  
ATOM   2684  CA  ARG A 336     -30.696 -11.367  -6.318  1.00 25.41           C  
ANISOU 2684  CA  ARG A 336     3691   2939   3025    318    -96    -77       C  
ATOM   2685  C   ARG A 336     -31.500 -11.111  -5.047  1.00 27.77           C  
ANISOU 2685  C   ARG A 336     3953   3277   3320    375    -77   -125       C  
ATOM   2686  O   ARG A 336     -32.691 -11.439  -4.976  1.00 27.74           O  
ANISOU 2686  O   ARG A 336     3867   3332   3339    458    -81   -145       O  
ATOM   2687  CB  ARG A 336     -30.594 -10.059  -7.125  1.00 24.47           C  
ANISOU 2687  CB  ARG A 336     3739   2687   2872    358   -103    -75       C  
ATOM   2688  CG  ARG A 336     -30.297 -10.207  -8.623  1.00 22.37           C  
ANISOU 2688  CG  ARG A 336     3538   2367   2594    350   -120    -28       C  
ATOM   2689  CD  ARG A 336     -29.061 -11.050  -8.926  1.00 28.42           C  
ANISOU 2689  CD  ARG A 336     4254   3162   3381    211    -92     -2       C  
ATOM   2690  NE  ARG A 336     -27.814 -10.500  -8.380  1.00 26.95           N  
ANISOU 2690  NE  ARG A 336     4118   2928   3192     93    -42    -33       N  
ATOM   2691  CZ  ARG A 336     -26.676 -11.192  -8.331  1.00 28.73           C  
ANISOU 2691  CZ  ARG A 336     4271   3199   3447    -23    -22    -40       C  
ATOM   2692  NH1 ARG A 336     -26.652 -12.436  -8.784  1.00 23.06           N  
ANISOU 2692  NH1 ARG A 336     3447   2562   2752    -31    -44     -6       N  
ATOM   2693  NH2 ARG A 336     -25.563 -10.650  -7.845  1.00 26.79           N  
ANISOU 2693  NH2 ARG A 336     4051   2918   3208   -127     16    -93       N  
ATOM   2694  N   PRO A 337     -30.888 -10.523  -4.021  1.00 26.52           N  
ANISOU 2694  N   PRO A 337     3850   3091   3136    330    -51   -155       N  
ATOM   2695  CA  PRO A 337     -31.670 -10.160  -2.835  1.00 28.30           C  
ANISOU 2695  CA  PRO A 337     4065   3341   3347    389    -25   -203       C  
ATOM   2696  C   PRO A 337     -32.765  -9.167  -3.205  1.00 31.06           C  
ANISOU 2696  C   PRO A 337     4465   3639   3697    519    -38   -233       C  
ATOM   2697  O   PRO A 337     -32.577  -8.286  -4.049  1.00 28.69           O  
ANISOU 2697  O   PRO A 337     4282   3238   3380    551    -64   -221       O  
ATOM   2698  CB  PRO A 337     -30.630  -9.549  -1.883  1.00 27.93           C  
ANISOU 2698  CB  PRO A 337     4096   3252   3264    316    -10   -234       C  
ATOM   2699  CG  PRO A 337     -29.452  -9.215  -2.728  1.00 30.83           C  
ANISOU 2699  CG  PRO A 337     4529   3549   3637    231    -24   -217       C  
ATOM   2700  CD  PRO A 337     -29.466 -10.156  -3.895  1.00 26.47           C  
ANISOU 2700  CD  PRO A 337     3911   3033   3115    221    -42   -162       C  
ATOM   2701  N   ARG A 338     -33.933  -9.348  -2.587  1.00 29.46           N  
ANISOU 2701  N   ARG A 338     4177   3503   3512    598    -16   -276       N  
ATOM   2702  CA  ARG A 338     -35.090  -8.514  -2.889  1.00 32.09           C  
ANISOU 2702  CA  ARG A 338     4527   3810   3857    745    -39   -324       C  
ATOM   2703  C   ARG A 338     -34.944  -7.113  -2.295  1.00 38.64           C  
ANISOU 2703  C   ARG A 338     5502   4538   4641    788    -29   -360       C  
ATOM   2704  O   ARG A 338     -35.302  -6.122  -2.943  1.00 37.58           O  
ANISOU 2704  O   ARG A 338     5474   4315   4491    894    -69   -372       O  
ATOM   2705  CB  ARG A 338     -36.355  -9.193  -2.368  1.00 33.92           C  
ANISOU 2705  CB  ARG A 338     4597   4156   4134    801     -4   -382       C  
ATOM   2706  CG  ARG A 338     -37.626  -8.698  -3.015  1.00 37.96           C  
ANISOU 2706  CG  ARG A 338     5062   4678   4683    963    -52   -445       C  
ATOM   2707  CD  ARG A 338     -38.837  -9.297  -2.346  1.00 38.82           C  
ANISOU 2707  CD  ARG A 338     4995   4906   4850    997      7   -529       C  
ATOM   2708  NE  ARG A 338     -40.037  -9.184  -3.166  1.00 42.77           N  
ANISOU 2708  NE  ARG A 338     5392   5452   5409   1142    -57   -604       N  
ATOM   2709  CZ  ARG A 338     -41.269  -9.358  -2.699  1.00 45.87           C  
ANISOU 2709  CZ  ARG A 338     5624   5939   5864   1208    -14   -715       C  
ATOM   2710  NH1 ARG A 338     -41.457  -9.642  -1.415  1.00 38.12           N  
ANISOU 2710  NH1 ARG A 338     4593   5005   4886   1134    109   -751       N  
ATOM   2711  NH2 ARG A 338     -42.311  -9.245  -3.511  1.00 43.44           N  
ANISOU 2711  NH2 ARG A 338     5210   5681   5616   1351    -92   -799       N  
ATOM   2712  N   LYS A 339     -34.408  -7.010  -1.079  1.00 32.08           N  
ANISOU 2712  N   LYS A 339     4695   3712   3782    714     21   -378       N  
ATOM   2713  CA  LYS A 339     -34.265  -5.747  -0.352  1.00 42.24           C  
ANISOU 2713  CA  LYS A 339     6113   4909   5026    742     38   -422       C  
ATOM   2714  C   LYS A 339     -32.847  -5.476   0.119  1.00 48.09           C  
ANISOU 2714  C   LYS A 339     6946   5595   5730    609     48   -412       C  
ATOM   2715  O   LYS A 339     -32.382  -4.339   0.020  1.00 49.43           O  
ANISOU 2715  O   LYS A 339     7261   5648   5873    603     47   -429       O  
ATOM   2716  CB  LYS A 339     -35.199  -5.707   0.871  1.00 45.45           C  
ANISOU 2716  CB  LYS A 339     6462   5379   5430    805     91   -488       C  
ATOM   2717  CG  LYS A 339     -36.681  -5.753   0.551  1.00 54.19           C  
ANISOU 2717  CG  LYS A 339     7464   6541   6583    946     89   -537       C  
ATOM   2718  CD  LYS A 339     -37.270  -7.133   0.837  1.00 55.94           C  
ANISOU 2718  CD  LYS A 339     7504   6900   6849    906    138   -546       C  
ATOM   2719  CE  LYS A 339     -38.716  -7.007   1.272  1.00 64.19           C  
ANISOU 2719  CE  LYS A 339     8441   8011   7937   1019    185   -642       C  
ATOM   2720  NZ  LYS A 339     -39.483  -6.115   0.351  1.00 65.53           N  
ANISOU 2720  NZ  LYS A 339     8622   8140   8136   1185    106   -687       N  
ATOM   2721  N   GLU A 340     -32.149  -6.484   0.633  1.00 35.61           N  
ANISOU 2721  N   GLU A 340     5288   4094   4150    505     57   -394       N  
ATOM   2722  CA  GLU A 340     -30.836  -6.243   1.204  1.00 36.82           C  
ANISOU 2722  CA  GLU A 340     5502   4213   4273    393     53   -413       C  
ATOM   2723  C   GLU A 340     -29.845  -5.827   0.119  1.00 42.17           C  
ANISOU 2723  C   GLU A 340     6248   4806   4968    315     34   -391       C  
ATOM   2724  O   GLU A 340     -29.895  -6.343  -1.004  1.00 39.12           O  
ANISOU 2724  O   GLU A 340     5824   4429   4612    315     19   -339       O  
ATOM   2725  CB  GLU A 340     -30.332  -7.493   1.909  1.00 31.32           C  
ANISOU 2725  CB  GLU A 340     4714   3621   3566    326     49   -402       C  
ATOM   2726  CG  GLU A 340     -31.290  -7.985   2.980  1.00 47.21           C  
ANISOU 2726  CG  GLU A 340     6684   5704   5549    385     92   -421       C  
ATOM   2727  CD  GLU A 340     -30.587  -8.269   4.289  1.00 52.67           C  
ANISOU 2727  CD  GLU A 340     7412   6425   6177    337     90   -452       C  
ATOM   2728  OE1 GLU A 340     -31.233  -8.826   5.210  1.00 43.48           O  
ANISOU 2728  OE1 GLU A 340     6236   5314   4972    368    138   -461       O  
ATOM   2729  OE2 GLU A 340     -29.386  -7.928   4.390  1.00 49.41           O  
ANISOU 2729  OE2 GLU A 340     7044   5980   5752    267     43   -477       O  
ATOM   2730  N   PRO A 341     -28.931  -4.909   0.423  1.00 41.10           N  
ANISOU 2730  N   PRO A 341     6215   4586   4814    240     44   -438       N  
ATOM   2731  CA  PRO A 341     -27.903  -4.544  -0.560  1.00 40.73           C  
ANISOU 2731  CA  PRO A 341     6232   4457   4788    138     53   -431       C  
ATOM   2732  C   PRO A 341     -26.956  -5.710  -0.805  1.00 43.31           C  
ANISOU 2732  C   PRO A 341     6433   4874   5149     38     32   -415       C  
ATOM   2733  O   PRO A 341     -26.583  -6.435   0.122  1.00 39.09           O  
ANISOU 2733  O   PRO A 341     5808   4434   4608     12      4   -441       O  
ATOM   2734  CB  PRO A 341     -27.187  -3.351   0.090  1.00 42.53           C  
ANISOU 2734  CB  PRO A 341     6578   4588   4993     68     79   -511       C  
ATOM   2735  CG  PRO A 341     -27.492  -3.458   1.570  1.00 46.84           C  
ANISOU 2735  CG  PRO A 341     7084   5205   5507    110     62   -558       C  
ATOM   2736  CD  PRO A 341     -28.821  -4.149   1.687  1.00 38.18           C  
ANISOU 2736  CD  PRO A 341     5911   4190   4405    240     56   -509       C  
ATOM   2737  N   GLU A 342     -26.580  -5.898  -2.078  1.00 36.25           N  
ANISOU 2737  N   GLU A 342     5547   3944   4281     -8     44   -373       N  
ATOM   2738  CA  GLU A 342     -25.700  -7.012  -2.422  1.00 33.16           C  
ANISOU 2738  CA  GLU A 342     5036   3636   3928    -94     27   -361       C  
ATOM   2739  C   GLU A 342     -24.327  -6.871  -1.777  1.00 34.40           C  
ANISOU 2739  C   GLU A 342     5162   3807   4102   -218     24   -449       C  
ATOM   2740  O   GLU A 342     -23.650  -7.881  -1.538  1.00 38.21           O  
ANISOU 2740  O   GLU A 342     5522   4390   4606   -257    -15   -463       O  
ATOM   2741  CB  GLU A 342     -25.561  -7.134  -3.946  1.00 36.49           C  
ANISOU 2741  CB  GLU A 342     5492   4005   4369   -120     51   -306       C  
ATOM   2742  CG  GLU A 342     -26.880  -7.492  -4.630  1.00 35.15           C  
ANISOU 2742  CG  GLU A 342     5321   3847   4186     12     28   -232       C  
ATOM   2743  CD  GLU A 342     -26.726  -7.819  -6.097  1.00 39.97           C  
ANISOU 2743  CD  GLU A 342     5960   4422   4804     -6     37   -177       C  
ATOM   2744  OE1 GLU A 342     -25.572  -7.915  -6.569  1.00 33.74           O  
ANISOU 2744  OE1 GLU A 342     5174   3610   4036   -129     74   -191       O  
ATOM   2745  OE2 GLU A 342     -27.765  -7.980  -6.778  1.00 41.26           O  
ANISOU 2745  OE2 GLU A 342     6138   4583   4954    106      8   -129       O  
ATOM   2746  N   SER A 343     -23.902  -5.636  -1.488  1.00 34.82           N  
ANISOU 2746  N   SER A 343     5323   3761   4147   -275     60   -518       N  
ATOM   2747  CA  SER A 343     -22.588  -5.401  -0.890  1.00 37.18           C  
ANISOU 2747  CA  SER A 343     5581   4074   4473   -401     55   -629       C  
ATOM   2748  C   SER A 343     -22.442  -6.065   0.475  1.00 40.75           C  
ANISOU 2748  C   SER A 343     5934   4646   4902   -360    -25   -674       C  
ATOM   2749  O   SER A 343     -21.315  -6.265   0.939  1.00 41.53           O  
ANISOU 2749  O   SER A 343     5954   4798   5026   -440    -64   -768       O  
ATOM   2750  CB  SER A 343     -22.325  -3.892  -0.771  1.00 38.45           C  
ANISOU 2750  CB  SER A 343     5892   4093   4624   -467    116   -700       C  
ATOM   2751  OG  SER A 343     -23.276  -3.278   0.086  1.00 44.76           O  
ANISOU 2751  OG  SER A 343     6778   4862   5368   -360    103   -696       O  
ATOM   2752  N   ASN A 344     -23.549  -6.417   1.125  1.00 36.16           N  
ANISOU 2752  N   ASN A 344     5362   4107   4270   -236    -49   -620       N  
ATOM   2753  CA  ASN A 344     -23.489  -7.137   2.388  1.00 39.41           C  
ANISOU 2753  CA  ASN A 344     5715   4620   4638   -190   -112   -649       C  
ATOM   2754  C   ASN A 344     -23.324  -8.640   2.223  1.00 38.92           C  
ANISOU 2754  C   ASN A 344     5539   4666   4583   -169   -157   -598       C  
ATOM   2755  O   ASN A 344     -23.147  -9.332   3.233  1.00 37.54           O  
ANISOU 2755  O   ASN A 344     5338   4567   4360   -129   -213   -621       O  
ATOM   2756  CB  ASN A 344     -24.756  -6.874   3.200  1.00 40.43           C  
ANISOU 2756  CB  ASN A 344     5915   4741   4707    -78    -93   -620       C  
ATOM   2757  CG  ASN A 344     -24.801  -5.472   3.780  1.00 43.28           C  
ANISOU 2757  CG  ASN A 344     6393   5009   5043    -85    -69   -691       C  
ATOM   2758  OD1 ASN A 344     -23.947  -4.624   3.489  1.00 44.44           O  
ANISOU 2758  OD1 ASN A 344     6582   5082   5220   -182    -56   -758       O  
ATOM   2759  ND2 ASN A 344     -25.799  -5.225   4.614  1.00 52.53           N  
ANISOU 2759  ND2 ASN A 344     7621   6179   6160     11    -51   -685       N  
ATOM   2760  N   LEU A 345     -23.406  -9.165   1.000  1.00 28.54           N  
ANISOU 2760  N   LEU A 345     4177   3352   3314   -186   -133   -530       N  
ATOM   2761  CA  LEU A 345     -23.485 -10.603   0.790  1.00 30.43           C  
ANISOU 2761  CA  LEU A 345     4326   3682   3555   -153   -164   -470       C  
ATOM   2762  C   LEU A 345     -22.155 -11.166   0.298  1.00 31.69           C  
ANISOU 2762  C   LEU A 345     4393   3883   3763   -234   -202   -513       C  
ATOM   2763  O   LEU A 345     -21.265 -10.437  -0.148  1.00 33.63           O  
ANISOU 2763  O   LEU A 345     4636   4085   4056   -329   -182   -582       O  
ATOM   2764  CB  LEU A 345     -24.602 -10.942  -0.206  1.00 27.59           C  
ANISOU 2764  CB  LEU A 345     3965   3307   3211   -103   -120   -370       C  
ATOM   2765  CG  LEU A 345     -26.014 -10.452   0.141  1.00 43.29           C  
ANISOU 2765  CG  LEU A 345     6014   5267   5169    -11    -83   -341       C  
ATOM   2766  CD1 LEU A 345     -27.051 -11.320  -0.555  1.00 38.80           C  
ANISOU 2766  CD1 LEU A 345     5390   4738   4616     48    -66   -264       C  
ATOM   2767  CD2 LEU A 345     -26.233 -10.461   1.640  1.00 51.20           C  
ANISOU 2767  CD2 LEU A 345     7043   6303   6109     30    -93   -381       C  
ATOM   2768  N   VAL A 346     -22.029 -12.485   0.407  1.00 26.05           N  
ANISOU 2768  N   VAL A 346     3608   3253   3035   -196   -248   -480       N  
ATOM   2769  CA  VAL A 346     -20.871 -13.208  -0.115  1.00 25.18           C  
ANISOU 2769  CA  VAL A 346     3399   3196   2973   -248   -289   -516       C  
ATOM   2770  C   VAL A 346     -21.120 -13.500  -1.590  1.00 28.49           C  
ANISOU 2770  C   VAL A 346     3794   3588   3443   -280   -231   -440       C  
ATOM   2771  O   VAL A 346     -22.175 -14.033  -1.950  1.00 29.99           O  
ANISOU 2771  O   VAL A 346     4003   3779   3614   -220   -208   -344       O  
ATOM   2772  CB  VAL A 346     -20.650 -14.506   0.678  1.00 23.87           C  
ANISOU 2772  CB  VAL A 346     3196   3119   2756   -173   -370   -512       C  
ATOM   2773  CG1 VAL A 346     -19.476 -15.315   0.108  1.00 26.74           C  
ANISOU 2773  CG1 VAL A 346     3449   3541   3171   -206   -421   -556       C  
ATOM   2774  CG2 VAL A 346     -20.428 -14.172   2.191  1.00 24.21           C  
ANISOU 2774  CG2 VAL A 346     3293   3180   2727   -126   -436   -590       C  
ATOM   2775  N   ARG A 347     -20.162 -13.154  -2.453  1.00 24.15           N  
ANISOU 2775  N   ARG A 347     3204   3014   2957   -378   -202   -491       N  
ATOM   2776  CA  ARG A 347     -20.362 -13.332  -3.891  1.00 25.61           C  
ANISOU 2776  CA  ARG A 347     3395   3159   3177   -411   -140   -422       C  
ATOM   2777  C   ARG A 347     -19.263 -14.190  -4.505  1.00 25.21           C  
ANISOU 2777  C   ARG A 347     3233   3168   3179   -466   -154   -459       C  
ATOM   2778  O   ARG A 347     -18.134 -14.240  -4.005  1.00 28.53           O  
ANISOU 2778  O   ARG A 347     3569   3640   3632   -509   -195   -570       O  
ATOM   2779  CB  ARG A 347     -20.430 -11.984  -4.633  1.00 32.77           C  
ANISOU 2779  CB  ARG A 347     4407   3945   4098   -481    -53   -431       C  
ATOM   2780  CG  ARG A 347     -19.135 -11.201  -4.749  1.00 41.66           C  
ANISOU 2780  CG  ARG A 347     5518   5033   5276   -617     -9   -550       C  
ATOM   2781  CD  ARG A 347     -19.385  -9.966  -5.623  1.00 47.58           C  
ANISOU 2781  CD  ARG A 347     6422   5636   6020   -679     97   -531       C  
ATOM   2782  NE  ARG A 347     -18.161  -9.319  -6.087  1.00 59.63           N  
ANISOU 2782  NE  ARG A 347     7946   7108   7602   -839    181   -637       N  
ATOM   2783  CZ  ARG A 347     -17.538  -9.595  -7.237  1.00 69.62           C  
ANISOU 2783  CZ  ARG A 347     9193   8353   8906   -926    255   -639       C  
ATOM   2784  NH1 ARG A 347     -17.999 -10.533  -8.068  1.00 46.97           N  
ANISOU 2784  NH1 ARG A 347     6309   5516   6023   -862    241   -537       N  
ATOM   2785  NH2 ARG A 347     -16.433  -8.931  -7.558  1.00 73.98           N  
ANISOU 2785  NH2 ARG A 347     9743   8853   9514  -1088    352   -753       N  
ATOM   2786  N   SER A 348     -19.604 -14.857  -5.606  1.00 25.39           N  
ANISOU 2786  N   SER A 348     3249   3185   3212   -457   -125   -377       N  
ATOM   2787  CA  SER A 348     -18.601 -15.590  -6.368  1.00 24.51           C  
ANISOU 2787  CA  SER A 348     3043   3117   3153   -513   -119   -410       C  
ATOM   2788  C   SER A 348     -17.611 -14.631  -7.017  1.00 29.36           C  
ANISOU 2788  C   SER A 348     3659   3671   3824   -648    -36   -500       C  
ATOM   2789  O   SER A 348     -18.000 -13.611  -7.592  1.00 25.67           O  
ANISOU 2789  O   SER A 348     3313   3097   3345   -694     46   -473       O  
ATOM   2790  CB  SER A 348     -19.256 -16.446  -7.457  1.00 24.83           C  
ANISOU 2790  CB  SER A 348     3095   3154   3185   -477    -99   -302       C  
ATOM   2791  OG  SER A 348     -18.248 -17.109  -8.217  1.00 25.03           O  
ANISOU 2791  OG  SER A 348     3034   3215   3260   -533    -85   -340       O  
ATOM   2792  N   MET A 349     -16.325 -14.980  -6.956  1.00 27.98           N  
ANISOU 2792  N   MET A 349     3357   3564   3711   -711    -51   -614       N  
ATOM   2793  CA  MET A 349     -15.283 -14.185  -7.591  1.00 29.60           C  
ANISOU 2793  CA  MET A 349     3539   3721   3985   -863     48   -723       C  
ATOM   2794  C   MET A 349     -14.752 -14.829  -8.867  1.00 35.98           C  
ANISOU 2794  C   MET A 349     4298   4536   4836   -920    115   -714       C  
ATOM   2795  O   MET A 349     -13.754 -14.360  -9.413  1.00 37.36           O  
ANISOU 2795  O   MET A 349     4431   4687   5077  -1056    211   -821       O  
ATOM   2796  CB  MET A 349     -14.127 -13.941  -6.617  1.00 28.83           C  
ANISOU 2796  CB  MET A 349     3312   3698   3944   -913     -5   -899       C  
ATOM   2797  CG  MET A 349     -14.545 -13.268  -5.312  1.00 37.34           C  
ANISOU 2797  CG  MET A 349     4444   4768   4975   -862    -72   -923       C  
ATOM   2798  SD  MET A 349     -15.226 -11.622  -5.607  1.00 41.86           S  
ANISOU 2798  SD  MET A 349     5213   5173   5518   -943     52   -886       S  
ATOM   2799  CE  MET A 349     -13.782 -10.756  -6.235  1.00 47.57           C  
ANISOU 2799  CE  MET A 349     5882   5849   6344  -1159    182  -1059       C  
ATOM   2800  N   VAL A 350     -15.387 -15.884  -9.364  1.00 28.15           N  
ANISOU 2800  N   VAL A 350     3312   3574   3811   -828     80   -599       N  
ATOM   2801  CA  VAL A 350     -14.869 -16.574 -10.535  1.00 29.72           C  
ANISOU 2801  CA  VAL A 350     3463   3784   4045   -873    136   -595       C  
ATOM   2802  C   VAL A 350     -15.819 -16.360 -11.702  1.00 32.23           C  
ANISOU 2802  C   VAL A 350     3941   3998   4309   -867    212   -463       C  
ATOM   2803  O   VAL A 350     -17.041 -16.223 -11.540  1.00 29.87           O  
ANISOU 2803  O   VAL A 350     3744   3661   3945   -776    173   -358       O  
ATOM   2804  CB  VAL A 350     -14.620 -18.079 -10.283  1.00 40.45           C  
ANISOU 2804  CB  VAL A 350     4694   5263   5414   -776     32   -591       C  
ATOM   2805  CG1 VAL A 350     -13.412 -18.270  -9.371  1.00 45.60           C  
ANISOU 2805  CG1 VAL A 350     5184   6015   6126   -784    -41   -752       C  
ATOM   2806  CG2 VAL A 350     -15.826 -18.732  -9.681  1.00 34.90           C  
ANISOU 2806  CG2 VAL A 350     4048   4577   4635   -639    -60   -470       C  
ATOM   2807  N   THR A 351     -15.233 -16.308 -12.893  1.00 29.91           N  
ANISOU 2807  N   THR A 351     3669   3656   4039   -963    321   -481       N  
ATOM   2808  CA  THR A 351     -15.974 -16.199 -14.145  1.00 33.56           C  
ANISOU 2808  CA  THR A 351     4291   4019   4440   -953    388   -368       C  
ATOM   2809  C   THR A 351     -15.454 -17.300 -15.053  1.00 36.30           C  
ANISOU 2809  C   THR A 351     4562   4417   4814   -966    409   -366       C  
ATOM   2810  O   THR A 351     -14.275 -17.295 -15.422  1.00 41.29           O  
ANISOU 2810  O   THR A 351     5114   5064   5510  -1079    494   -473       O  
ATOM   2811  CB  THR A 351     -15.796 -14.825 -14.792  1.00 36.14           C  
ANISOU 2811  CB  THR A 351     4790   4196   4745  -1068    529   -388       C  
ATOM   2812  OG1 THR A 351     -16.186 -13.796 -13.871  1.00 42.78           O  
ANISOU 2812  OG1 THR A 351     5696   4991   5567  -1057    507   -405       O  
ATOM   2813  CG2 THR A 351     -16.652 -14.724 -16.051  1.00 45.88           C  
ANISOU 2813  CG2 THR A 351     6219   5322   5892  -1024    572   -266       C  
ATOM   2814  N   ALA A 352     -16.313 -18.261 -15.378  1.00 36.07           N  
ANISOU 2814  N   ALA A 352     4545   4419   4742   -855    336   -259       N  
ATOM   2815  CA  ALA A 352     -15.908 -19.364 -16.229  1.00 35.25           C  
ANISOU 2815  CA  ALA A 352     4380   4359   4655   -855    349   -250       C  
ATOM   2816  C   ALA A 352     -15.906 -18.900 -17.679  1.00 46.85           C  
ANISOU 2816  C   ALA A 352     6003   5714   6083   -925    474   -214       C  
ATOM   2817  O   ALA A 352     -15.244 -19.493 -18.530  1.00 45.39           O  
ANISOU 2817  O   ALA A 352     5784   5542   5920   -974    536   -240       O  
ATOM   2818  CB  ALA A 352     -16.825 -20.551 -16.050  1.00 36.74           C  
ANISOU 2818  CB  ALA A 352     4536   4611   4810   -724    234   -158       C  
ATOM   2819  OXT ALA A 352     -16.568 -17.918 -18.023  1.00 46.52           O  
ANISOU 2819  OXT ALA A 352     6137   5559   5977   -926    514   -160       O  
TER    2820      ALA A 352                                                      
ATOM   2821  N   ASN B  -1     -32.348 -43.060 -13.421  1.00 70.38           N  
ATOM   2822  CA  ASN B  -1     -31.014 -42.612 -13.019  1.00 66.73           C  
ATOM   2823  C   ASN B  -1     -30.557 -43.275 -11.710  1.00 64.26           C  
ATOM   2824  O   ASN B  -1     -29.355 -43.281 -11.407  1.00 43.64           O  
ATOM   2825  CB  ASN B  -1     -30.974 -41.079 -12.877  1.00 56.35           C  
ATOM   2826  CG  ASN B  -1     -30.942 -40.351 -14.234  1.00 53.34           C  
ATOM   2827  OD1 ASN B  -1     -30.611 -40.944 -15.259  1.00 57.07           O  
ATOM   2828  ND2 ASN B  -1     -31.283 -39.063 -14.232  1.00 45.76           N  
ATOM   2829  N   ALA B   0     -31.521 -43.849 -10.964  1.00 83.47           N  
ANISOU 2829  N   ALA B   0    10503  11461   9751    528    124   -330       N  
ATOM   2830  CA  ALA B   0     -31.322 -44.350  -9.604  1.00 65.96           C  
ANISOU 2830  CA  ALA B   0     8264   9410   7389    377    161   -299       C  
ATOM   2831  C   ALA B   0     -31.646 -45.837  -9.473  1.00 56.30           C  
ANISOU 2831  C   ALA B   0     6930   8339   6123    151    212   -137       C  
ATOM   2832  O   ALA B   0     -31.985 -46.314  -8.384  1.00 45.94           O  
ANISOU 2832  O   ALA B   0     5564   7254   4637     21    270   -117       O  
ATOM   2833  CB  ALA B   0     -32.157 -43.546  -8.609  1.00 59.30           C  
ANISOU 2833  CB  ALA B   0     7357   8814   6361    513    216   -502       C  
ATOM   2834  N   ASP B   1     -31.564 -46.578 -10.573  1.00 48.56           N  
ANISOU 2834  N   ASP B   1     5934   7232   5283     91    188    -20       N  
ATOM   2835  CA  ASP B   1     -31.596 -48.029 -10.499  1.00 36.65           C  
ANISOU 2835  CA  ASP B   1     4389   5771   3766   -138    194    151       C  
ATOM   2836  C   ASP B   1     -30.359 -48.545  -9.777  1.00 36.72           C  
ANISOU 2836  C   ASP B   1     4537   5635   3779   -270    119    277       C  
ATOM   2837  O   ASP B   1     -29.303 -47.914  -9.796  1.00 31.54           O  
ANISOU 2837  O   ASP B   1     3989   4788   3207   -191     54    251       O  
ATOM   2838  CB  ASP B   1     -31.656 -48.622 -11.896  1.00 34.09           C  
ANISOU 2838  CB  ASP B   1     4048   5302   3601   -142    162    221       C  
ATOM   2839  CG  ASP B   1     -32.992 -48.374 -12.569  1.00 47.33           C  
ANISOU 2839  CG  ASP B   1     5567   7157   5260    -44    212    117       C  
ATOM   2840  OD1 ASP B   1     -33.926 -47.841 -11.907  1.00 40.06           O  
ANISOU 2840  OD1 ASP B   1     4518   6500   4203     21    283    -11       O  
ATOM   2841  OD2 ASP B   1     -33.105 -48.729 -13.759  1.00 42.41           O  
ANISOU 2841  OD2 ASP B   1     4938   6425   4752    -25    176    151       O  
ATOM   2842  N   VAL B   2     -30.488 -49.699  -9.124  1.00 34.73           N  
ANISOU 2842  N   VAL B   2     4287   5474   3433   -479    117    415       N  
ATOM   2843  CA  VAL B   2     -29.348 -50.349  -8.484  1.00 35.23           C  
ANISOU 2843  CA  VAL B   2     4493   5389   3504   -593      9    548       C  
ATOM   2844  C   VAL B   2     -29.046 -51.643  -9.227  1.00 35.80           C  
ANISOU 2844  C   VAL B   2     4606   5288   3708   -702    -67    702       C  
ATOM   2845  O   VAL B   2     -29.961 -52.390  -9.600  1.00 33.48           O  
ANISOU 2845  O   VAL B   2     4247   5082   3392   -813    -25    756       O  
ATOM   2846  CB  VAL B   2     -29.580 -50.604  -6.981  1.00 44.34           C  
ANISOU 2846  CB  VAL B   2     5686   6748   4414   -740     29    595       C  
ATOM   2847  CG1 VAL B   2     -29.749 -49.293  -6.250  1.00 51.04           C  
ANISOU 2847  CG1 VAL B   2     6512   7747   5134   -603     89    412       C  
ATOM   2848  CG2 VAL B   2     -30.789 -51.477  -6.759  1.00 59.43           C  
ANISOU 2848  CG2 VAL B   2     7510   8892   6180   -936    120    674       C  
ATOM   2849  N   GLY B   3     -27.758 -51.905  -9.446  1.00 34.62           N  
ANISOU 2849  N   GLY B   3     4556   4897   3700   -667   -186    756       N  
ATOM   2850  CA  GLY B   3     -27.373 -53.089 -10.191  1.00 37.80           C  
ANISOU 2850  CA  GLY B   3     5006   5114   4241   -722   -274    868       C  
ATOM   2851  C   GLY B   3     -25.945 -53.499  -9.915  1.00 36.98           C  
ANISOU 2851  C   GLY B   3     5005   4811   4234   -697   -424    927       C  
ATOM   2852  O   GLY B   3     -25.191 -52.804  -9.231  1.00 29.97           O  
ANISOU 2852  O   GLY B   3     4140   3924   3322   -643   -463    880       O  
ATOM   2853  N   CYS B   4     -25.602 -54.673 -10.449  1.00 30.67           N  
ANISOU 2853  N   CYS B   4     4265   3842   3546   -732   -525   1018       N  
ATOM   2854  CA  CYS B   4     -24.251 -55.220 -10.450  1.00 31.07           C  
ANISOU 2854  CA  CYS B   4     4385   3691   3729   -664   -685   1051       C  
ATOM   2855  C   CYS B   4     -23.977 -55.800 -11.828  1.00 33.02           C  
ANISOU 2855  C   CYS B   4     4605   3777   4163   -579   -702   1019       C  
ATOM   2856  O   CYS B   4     -24.877 -56.344 -12.470  1.00 32.34           O  
ANISOU 2856  O   CYS B   4     4522   3692   4072   -642   -659   1045       O  
ATOM   2857  CB  CYS B   4     -24.053 -56.341  -9.429  1.00 29.32           C  
ANISOU 2857  CB  CYS B   4     4320   3403   3417   -788   -850   1208       C  
ATOM   2858  SG  CYS B   4     -24.489 -55.960  -7.726  1.00 36.86           S  
ANISOU 2858  SG  CYS B   4     5349   4566   4089   -935   -838   1278       S  
ATOM   2859  N   SER B   5     -22.722 -55.737 -12.260  1.00 28.10           N  
ANISOU 2859  N   SER B   5     3950   3028   3697   -443   -770    955       N  
ATOM   2860  CA  SER B   5     -22.409 -56.200 -13.604  1.00 27.65           C  
ANISOU 2860  CA  SER B   5     3856   2849   3799   -345   -763    896       C  
ATOM   2861  C   SER B   5     -20.953 -56.633 -13.686  1.00 33.64           C  
ANISOU 2861  C   SER B   5     4596   3477   4707   -218   -897    854       C  
ATOM   2862  O   SER B   5     -20.119 -56.260 -12.851  1.00 30.12           O  
ANISOU 2862  O   SER B   5     4128   3054   4262   -193   -973    846       O  
ATOM   2863  CB  SER B   5     -22.694 -55.111 -14.643  1.00 27.29           C  
ANISOU 2863  CB  SER B   5     3706   2881   3782   -280   -589    784       C  
ATOM   2864  OG  SER B   5     -21.901 -53.952 -14.402  1.00 30.94           O  
ANISOU 2864  OG  SER B   5     4102   3388   4265   -226   -546    710       O  
ATOM   2865  N   VAL B   6     -20.668 -57.454 -14.695  1.00 27.67           N  
ANISOU 2865  N   VAL B   6     3841   2596   4075   -131   -936    811       N  
ATOM   2866  CA  VAL B   6     -19.304 -57.680 -15.160  1.00 31.47           C  
ANISOU 2866  CA  VAL B   6     4235   3003   4718     34  -1006    707       C  
ATOM   2867  C   VAL B   6     -18.993 -56.614 -16.205  1.00 36.51           C  
ANISOU 2867  C   VAL B   6     4723   3742   5407     86   -814    580       C  
ATOM   2868  O   VAL B   6     -19.652 -56.542 -17.251  1.00 34.34           O  
ANISOU 2868  O   VAL B   6     4452   3477   5119     83   -695    549       O  
ATOM   2869  CB  VAL B   6     -19.125 -59.086 -15.743  1.00 28.45           C  
ANISOU 2869  CB  VAL B   6     3936   2438   4435    125  -1145    696       C  
ATOM   2870  CG1 VAL B   6     -17.645 -59.337 -16.050  1.00 31.69           C  
ANISOU 2870  CG1 VAL B   6     4227   2806   5009    326  -1234    563       C  
ATOM   2871  CG2 VAL B   6     -19.684 -60.148 -14.797  1.00 32.94           C  
ANISOU 2871  CG2 VAL B   6     4714   2876   4925     20  -1331    856       C  
ATOM   2872  N   ASP B   7     -17.995 -55.783 -15.917  1.00 34.06           N  
ANISOU 2872  N   ASP B   7     4292   3506   5144    117   -794    514       N  
ATOM   2873  CA  ASP B   7     -17.607 -54.672 -16.783  1.00 31.47           C  
ANISOU 2873  CA  ASP B   7     3842   3268   4846    121   -616    416       C  
ATOM   2874  C   ASP B   7     -16.352 -55.107 -17.532  1.00 32.25           C  
ANISOU 2874  C   ASP B   7     3797   3364   5093    245   -629    295       C  
ATOM   2875  O   ASP B   7     -15.237 -54.999 -17.015  1.00 28.58           O  
ANISOU 2875  O   ASP B   7     3210   2939   4710    285   -708    239       O  
ATOM   2876  CB  ASP B   7     -17.372 -53.410 -15.957  1.00 32.24           C  
ANISOU 2876  CB  ASP B   7     3907   3451   4890     37   -583    418       C  
ATOM   2877  CG  ASP B   7     -17.410 -52.142 -16.791  1.00 37.29           C  
ANISOU 2877  CG  ASP B   7     4507   4148   5514    -10   -400    362       C  
ATOM   2878  OD1 ASP B   7     -16.728 -52.087 -17.839  1.00 32.35           O  
ANISOU 2878  OD1 ASP B   7     3786   3539   4967     23   -312    286       O  
ATOM   2879  OD2 ASP B   7     -18.121 -51.195 -16.385  1.00 37.80           O  
ANISOU 2879  OD2 ASP B   7     4648   4240   5476    -79   -347    392       O  
ATOM   2880  N   PHE B   8     -16.537 -55.610 -18.754  1.00 28.73           N  
ANISOU 2880  N   PHE B   8     3351   2888   4675    311   -553    237       N  
ATOM   2881  CA  PHE B   8     -15.406 -56.164 -19.490  1.00 32.17           C  
ANISOU 2881  CA  PHE B   8     3644   3342   5237    453   -560     96       C  
ATOM   2882  C   PHE B   8     -14.373 -55.093 -19.849  1.00 27.79           C  
ANISOU 2882  C   PHE B   8     2892   2945   4721    414   -415      0       C  
ATOM   2883  O   PHE B   8     -13.164 -55.348 -19.777  1.00 30.77           O  
ANISOU 2883  O   PHE B   8     3087   3390   5214    506   -468   -111       O  
ATOM   2884  CB  PHE B   8     -15.914 -56.891 -20.739  1.00 35.12           C  
ANISOU 2884  CB  PHE B   8     4083   3658   5601    525   -502     43       C  
ATOM   2885  CG  PHE B   8     -16.707 -58.139 -20.427  1.00 33.09           C  
ANISOU 2885  CG  PHE B   8     4007   3227   5338    558   -677    116       C  
ATOM   2886  CD1 PHE B   8     -16.081 -59.263 -19.899  1.00 33.02           C  
ANISOU 2886  CD1 PHE B   8     4022   3094   5432    690   -895     90       C  
ATOM   2887  CD2 PHE B   8     -18.076 -58.186 -20.647  1.00 34.32           C  
ANISOU 2887  CD2 PHE B   8     4313   3339   5387    450   -639    210       C  
ATOM   2888  CE1 PHE B   8     -16.809 -60.414 -19.608  1.00 38.56           C  
ANISOU 2888  CE1 PHE B   8     4930   3602   6120    687  -1069    175       C  
ATOM   2889  CE2 PHE B   8     -18.812 -59.342 -20.352  1.00 32.78           C  
ANISOU 2889  CE2 PHE B   8     4285   2988   5184    431   -798    285       C  
ATOM   2890  CZ  PHE B   8     -18.176 -60.452 -19.837  1.00 30.82           C  
ANISOU 2890  CZ  PHE B   8     4093   2587   5028    537  -1012    276       C  
ATOM   2891  N   SER B   9     -14.813 -53.884 -20.227  1.00 29.74           N  
ANISOU 2891  N   SER B   9     3171   3253   4874    274   -243     38       N  
ATOM   2892  CA  SER B   9     -13.817 -52.900 -20.649  1.00 30.64           C  
ANISOU 2892  CA  SER B   9     3122   3501   5018    196   -103    -40       C  
ATOM   2893  C   SER B   9     -13.060 -52.296 -19.461  1.00 32.15           C  
ANISOU 2893  C   SER B   9     3217   3739   5261    126   -196    -38       C  
ATOM   2894  O   SER B   9     -11.902 -51.893 -19.617  1.00 32.94           O  
ANISOU 2894  O   SER B   9     3114   3962   5439     87   -146   -134       O  
ATOM   2895  CB  SER B   9     -14.465 -51.807 -21.507  1.00 28.55           C  
ANISOU 2895  CB  SER B   9     2962   3251   4632     68     87      6       C  
ATOM   2896  OG  SER B   9     -15.392 -51.032 -20.770  1.00 34.78           O  
ANISOU 2896  OG  SER B   9     3908   3973   5334    -19     56    114       O  
ATOM   2897  N   LYS B  10     -13.667 -52.244 -18.273  1.00 30.96           N  
ANISOU 2897  N   LYS B  10     3194   3512   5060     99   -331     60       N  
ATOM   2898  CA  LYS B  10     -12.986 -51.741 -17.083  1.00 28.25           C  
ANISOU 2898  CA  LYS B  10     2781   3207   4747     42   -446     56       C  
ATOM   2899  C   LYS B  10     -12.385 -52.852 -16.220  1.00 32.25           C  
ANISOU 2899  C   LYS B  10     3228   3689   5337    178   -678     39       C  
ATOM   2900  O   LYS B  10     -11.808 -52.550 -15.170  1.00 32.95           O  
ANISOU 2900  O   LYS B  10     3265   3811   5443    147   -809     35       O  
ATOM   2901  CB  LYS B  10     -13.939 -50.874 -16.248  1.00 29.55           C  
ANISOU 2901  CB  LYS B  10     3125   3325   4778    -69   -451    154       C  
ATOM   2902  CG  LYS B  10     -14.356 -49.563 -16.939  1.00 28.42           C  
ANISOU 2902  CG  LYS B  10     3050   3185   4564   -192   -268    158       C  
ATOM   2903  CD  LYS B  10     -14.941 -48.548 -15.960  1.00 29.28           C  
ANISOU 2903  CD  LYS B  10     3294   3261   4569   -277   -303    201       C  
ATOM   2904  CE  LYS B  10     -15.233 -47.204 -16.626  1.00 33.04           C  
ANISOU 2904  CE  LYS B  10     3861   3701   4989   -381   -161    196       C  
ATOM   2905  NZ  LYS B  10     -15.480 -46.114 -15.621  1.00 32.56           N  
ANISOU 2905  NZ  LYS B  10     3912   3602   4856   -453   -219    192       N  
ATOM   2906  N   LYS B  11     -12.481 -54.118 -16.657  1.00 25.70           N  
ANISOU 2906  N   LYS B  11     2420   2787   4558    333   -750     23       N  
ATOM   2907  CA  LYS B  11     -11.810 -55.261 -16.022  1.00 27.42           C  
ANISOU 2907  CA  LYS B  11     2597   2949   4872    499   -993     -7       C  
ATOM   2908  C   LYS B  11     -12.184 -55.393 -14.544  1.00 34.77           C  
ANISOU 2908  C   LYS B  11     3690   3803   5718    455  -1192    124       C  
ATOM   2909  O   LYS B  11     -11.329 -55.575 -13.672  1.00 35.84           O  
ANISOU 2909  O   LYS B  11     3750   3958   5909    517  -1385     97       O  
ATOM   2910  CB  LYS B  11     -10.290 -55.165 -16.192  1.00 36.56           C  
ANISOU 2910  CB  LYS B  11     3456   4252   6182    586  -1020   -177       C  
ATOM   2911  CG  LYS B  11      -9.853 -54.551 -17.517  1.00 48.45           C  
ANISOU 2911  CG  LYS B  11     4778   5909   7722    534   -760   -297       C  
ATOM   2912  CD  LYS B  11      -9.190 -55.557 -18.417  1.00 55.19           C  
ANISOU 2912  CD  LYS B  11     5476   6805   8689    746   -764   -456       C  
ATOM   2913  CE  LYS B  11      -8.774 -54.914 -19.728  1.00 61.65           C  
ANISOU 2913  CE  LYS B  11     6118   7806   9500    665   -480   -569       C  
ATOM   2914  NZ  LYS B  11      -9.973 -54.499 -20.508  1.00 58.99           N  
ANISOU 2914  NZ  LYS B  11     6008   7390   9015    542   -297   -460       N  
ATOM   2915  N   GLU B  12     -13.482 -55.309 -14.263  1.00 35.59           N  
ANISOU 2915  N   GLU B  12     4012   3838   5674    346  -1147    261       N  
ATOM   2916  CA  GLU B  12     -13.953 -55.338 -12.887  1.00 38.12           C  
ANISOU 2916  CA  GLU B  12     4493   4123   5867    271  -1290    388       C  
ATOM   2917  C   GLU B  12     -15.376 -55.871 -12.858  1.00 32.75           C  
ANISOU 2917  C   GLU B  12     4030   3359   5055    197  -1259    523       C  
ATOM   2918  O   GLU B  12     -16.124 -55.755 -13.832  1.00 29.53           O  
ANISOU 2918  O   GLU B  12     3638   2951   4633    169  -1092    514       O  
ATOM   2919  CB  GLU B  12     -13.909 -53.940 -12.236  1.00 30.92           C  
ANISOU 2919  CB  GLU B  12     3548   3327   4875    136  -1213    377       C  
ATOM   2920  CG  GLU B  12     -14.872 -52.946 -12.886  1.00 28.87           C  
ANISOU 2920  CG  GLU B  12     3334   3106   4529     26   -976    383       C  
ATOM   2921  CD  GLU B  12     -14.671 -51.502 -12.424  1.00 35.83           C  
ANISOU 2921  CD  GLU B  12     4187   4067   5361    -84   -910    338       C  
ATOM   2922  OE1 GLU B  12     -13.919 -51.258 -11.454  1.00 29.29           O  
ANISOU 2922  OE1 GLU B  12     3315   3276   4538   -101  -1047    312       O  
ATOM   2923  OE2 GLU B  12     -15.283 -50.609 -13.044  1.00 32.20           O  
ANISOU 2923  OE2 GLU B  12     3763   3617   4853   -147   -737    325       O  
ATOM   2924  N   THR B  13     -15.734 -56.475 -11.732  1.00 31.75           N  
ANISOU 2924  N   THR B  13     4071   3172   4823    155  -1428    650       N  
ATOM   2925  CA  THR B  13     -17.117 -56.805 -11.410  1.00 40.33           C  
ANISOU 2925  CA  THR B  13     5347   4232   5743     21  -1389    790       C  
ATOM   2926  C   THR B  13     -17.519 -55.961 -10.209  1.00 41.11           C  
ANISOU 2926  C   THR B  13     5502   4454   5663   -107  -1369    847       C  
ATOM   2927  O   THR B  13     -16.817 -55.962  -9.191  1.00 39.27           O  
ANISOU 2927  O   THR B  13     5294   4230   5399    -94  -1533    866       O  
ATOM   2928  CB  THR B  13     -17.269 -58.293 -11.098  1.00 43.57           C  
ANISOU 2928  CB  THR B  13     5939   4468   6148     40  -1597    906       C  
ATOM   2929  OG1 THR B  13     -16.768 -59.057 -12.197  1.00 43.24           O  
ANISOU 2929  OG1 THR B  13     5843   4303   6282    198  -1636    815       O  
ATOM   2930  CG2 THR B  13     -18.730 -58.644 -10.870  1.00 41.22           C  
ANISOU 2930  CG2 THR B  13     5812   4170   5681   -144  -1531   1049       C  
ATOM   2931  N   ARG B  14     -18.620 -55.226 -10.333  1.00 29.07           N  
ANISOU 2931  N   ARG B  14     3992   3033   4019   -211  -1180    856       N  
ATOM   2932  CA  ARG B  14     -18.955 -54.227  -9.323  1.00 36.35           C  
ANISOU 2932  CA  ARG B  14     4940   4093   4778   -298  -1133    855       C  
ATOM   2933  C   ARG B  14     -20.451 -53.943  -9.344  1.00 35.60           C  
ANISOU 2933  C   ARG B  14     4895   4104   4526   -400   -968    893       C  
ATOM   2934  O   ARG B  14     -21.185 -54.387 -10.231  1.00 31.65           O  
ANISOU 2934  O   ARG B  14     4390   3577   4059   -410   -885    912       O  
ATOM   2935  CB  ARG B  14     -18.150 -52.930  -9.522  1.00 28.27           C  
ANISOU 2935  CB  ARG B  14     3782   3122   3837   -251  -1068    714       C  
ATOM   2936  CG  ARG B  14     -18.132 -52.389 -10.950  1.00 30.09           C  
ANISOU 2936  CG  ARG B  14     3901   3334   4197   -204   -900    621       C  
ATOM   2937  CD  ARG B  14     -19.362 -51.533 -11.301  1.00 28.96           C  
ANISOU 2937  CD  ARG B  14     3795   3260   3947   -249   -720    605       C  
ATOM   2938  NE  ARG B  14     -19.696 -50.503 -10.312  1.00 31.78           N  
ANISOU 2938  NE  ARG B  14     4201   3711   4162   -297   -701    572       N  
ATOM   2939  CZ  ARG B  14     -19.336 -49.223 -10.384  1.00 33.93           C  
ANISOU 2939  CZ  ARG B  14     4447   3989   4455   -293   -647    471       C  
ATOM   2940  NH1 ARG B  14     -18.603 -48.777 -11.396  1.00 29.59           N  
ANISOU 2940  NH1 ARG B  14     3818   3371   4053   -272   -593    410       N  
ATOM   2941  NH2 ARG B  14     -19.714 -48.379  -9.435  1.00 33.67           N  
ANISOU 2941  NH2 ARG B  14     4482   4029   4282   -319   -648    426       N  
ATOM   2942  N   CYS B  15     -20.887 -53.192  -8.336  1.00 28.90           N  
ANISOU 2942  N   CYS B  15     4085   3394   3501   -468   -931    886       N  
ATOM   2943  CA  CYS B  15     -22.271 -52.790  -8.151  1.00 30.12           C  
ANISOU 2943  CA  CYS B  15     4253   3704   3485   -546   -777    888       C  
ATOM   2944  C   CYS B  15     -22.314 -51.277  -7.973  1.00 36.91           C  
ANISOU 2944  C   CYS B  15     5062   4660   4304   -491   -678    745       C  
ATOM   2945  O   CYS B  15     -21.276 -50.623  -7.832  1.00 32.00           O  
ANISOU 2945  O   CYS B  15     4416   3980   3761   -438   -742    670       O  
ATOM   2946  CB  CYS B  15     -22.894 -53.482  -6.932  1.00 28.39           C  
ANISOU 2946  CB  CYS B  15     4158   3587   3043   -694   -830   1018       C  
ATOM   2947  SG  CYS B  15     -22.755 -55.293  -6.897  1.00 38.11           S  
ANISOU 2947  SG  CYS B  15     5532   4649   4299   -786  -1006   1214       S  
ATOM   2948  N   GLY B  16     -23.525 -50.731  -7.960  1.00 29.03           N  
ANISOU 2948  N   GLY B  16     4043   3807   3180   -504   -535    698       N  
ATOM   2949  CA  GLY B  16     -23.724 -49.307  -7.777  1.00 30.45           C  
ANISOU 2949  CA  GLY B  16     4204   4059   3307   -428   -456    550       C  
ATOM   2950  C   GLY B  16     -25.092 -48.901  -8.296  1.00 36.64           C  
ANISOU 2950  C   GLY B  16     4928   4965   4027   -386   -305    488       C  
ATOM   2951  O   GLY B  16     -25.911 -49.744  -8.658  1.00 37.48           O  
ANISOU 2951  O   GLY B  16     4995   5134   4111   -447   -258    564       O  
ATOM   2952  N   THR B  17     -25.330 -47.591  -8.297  1.00 29.42           N  
ANISOU 2952  N   THR B  17     4012   4079   3085   -279   -249    341       N  
ATOM   2953  CA  THR B  17     -26.511 -47.028  -8.939  1.00 30.63           C  
ANISOU 2953  CA  THR B  17     4105   4321   3214   -181   -137    251       C  
ATOM   2954  C   THR B  17     -26.119 -46.455 -10.300  1.00 30.24           C  
ANISOU 2954  C   THR B  17     4066   4076   3349    -83   -133    216       C  
ATOM   2955  O   THR B  17     -24.943 -46.203 -10.582  1.00 29.29           O  
ANISOU 2955  O   THR B  17     3993   3785   3351    -95   -193    227       O  
ATOM   2956  CB  THR B  17     -27.173 -45.940  -8.078  1.00 32.05           C  
ANISOU 2956  CB  THR B  17     4295   4657   3227    -90    -90     92       C  
ATOM   2957  OG1 THR B  17     -26.368 -44.752  -8.085  1.00 34.51           O  
ANISOU 2957  OG1 THR B  17     4703   4803   3607      0   -151    -14       O  
ATOM   2958  CG2 THR B  17     -27.369 -46.417  -6.622  1.00 33.14           C  
ANISOU 2958  CG2 THR B  17     4445   5001   3146   -205    -90    123       C  
ATOM   2959  N   GLY B  18     -27.116 -46.262 -11.155  1.00 24.25           N  
ANISOU 2959  N   GLY B  18     3256   3360   2597      2    -63    175       N  
ATOM   2960  CA  GLY B  18     -26.832 -45.700 -12.470  1.00 20.90           C  
ANISOU 2960  CA  GLY B  18     2872   2758   2311     88    -61    154       C  
ATOM   2961  C   GLY B  18     -27.977 -45.973 -13.431  1.00 31.21           C  
ANISOU 2961  C   GLY B  18     4107   4135   3617    154    -10    150       C  
ATOM   2962  O   GLY B  18     -29.120 -46.172 -13.014  1.00 26.23           O  
ANISOU 2962  O   GLY B  18     3381   3710   2875    170     32    110       O  
ATOM   2963  N   VAL B  19     -27.633 -45.960 -14.721  1.00 26.90           N  
ANISOU 2963  N   VAL B  19     3600   3435   3188    183    -14    183       N  
ATOM   2964  CA  VAL B  19     -28.576 -46.163 -15.817  1.00 26.78           C  
ANISOU 2964  CA  VAL B  19     3540   3453   3182    253      9    178       C  
ATOM   2965  C   VAL B  19     -28.136 -47.403 -16.587  1.00 28.56           C  
ANISOU 2965  C   VAL B  19     3743   3613   3496    149      4    285       C  
ATOM   2966  O   VAL B  19     -26.990 -47.483 -17.040  1.00 28.75           O  
ANISOU 2966  O   VAL B  19     3826   3485   3614    114     -6    326       O  
ATOM   2967  CB  VAL B  19     -28.642 -44.936 -16.746  1.00 24.99           C  
ANISOU 2967  CB  VAL B  19     3426   3090   2981    400     -7    112       C  
ATOM   2968  CG1 VAL B  19     -29.701 -45.131 -17.849  1.00 23.00           C  
ANISOU 2968  CG1 VAL B  19     3130   2891   2720    492     -9     99       C  
ATOM   2969  CG2 VAL B  19     -28.914 -43.655 -15.949  1.00 28.33           C  
ANISOU 2969  CG2 VAL B  19     3913   3522   3331    521    -31    -11       C  
ATOM   2970  N   PHE B  20     -29.035 -48.373 -16.726  1.00 24.71           N  
ANISOU 2970  N   PHE B  20     3163   3248   2979     98     11    318       N  
ATOM   2971  CA  PHE B  20     -28.690 -49.664 -17.315  1.00 27.03           C  
ANISOU 2971  CA  PHE B  20     3452   3469   3349     -2    -16    406       C  
ATOM   2972  C   PHE B  20     -29.560 -49.920 -18.541  1.00 26.96           C  
ANISOU 2972  C   PHE B  20     3411   3481   3349     45    -14    385       C  
ATOM   2973  O   PHE B  20     -30.791 -49.986 -18.434  1.00 28.64           O  
ANISOU 2973  O   PHE B  20     3527   3865   3491     48     -6    348       O  
ATOM   2974  CB  PHE B  20     -28.850 -50.763 -16.266  1.00 30.31           C  
ANISOU 2974  CB  PHE B  20     3828   3973   3716   -157    -42    486       C  
ATOM   2975  CG  PHE B  20     -28.159 -50.430 -14.964  1.00 38.26           C  
ANISOU 2975  CG  PHE B  20     4870   4992   4674   -192    -58    499       C  
ATOM   2976  CD1 PHE B  20     -26.828 -50.013 -14.958  1.00 44.81           C  
ANISOU 2976  CD1 PHE B  20     5767   5669   5590   -155    -91    494       C  
ATOM   2977  CD2 PHE B  20     -28.849 -50.447 -13.769  1.00 39.29           C  
ANISOU 2977  CD2 PHE B  20     4957   5310   4660   -265    -34    501       C  
ATOM   2978  CE1 PHE B  20     -26.189 -49.677 -13.766  1.00 38.16           C  
ANISOU 2978  CE1 PHE B  20     4956   4842   4701   -187   -127    494       C  
ATOM   2979  CE2 PHE B  20     -28.215 -50.120 -12.574  1.00 38.86           C  
ANISOU 2979  CE2 PHE B  20     4954   5273   4539   -294    -59    505       C  
ATOM   2980  CZ  PHE B  20     -26.889 -49.739 -12.573  1.00 32.89           C  
ANISOU 2980  CZ  PHE B  20     4271   4345   3879   -251   -117    501       C  
ATOM   2981  N   ILE B  21     -28.918 -50.085 -19.691  1.00 21.37           N  
ANISOU 2981  N   ILE B  21     2774   2625   2721     77    -22    398       N  
ATOM   2982  CA  ILE B  21     -29.593 -50.215 -20.978  1.00 24.50           C  
ANISOU 2982  CA  ILE B  21     3174   3020   3115    137    -33    370       C  
ATOM   2983  C   ILE B  21     -29.424 -51.655 -21.429  1.00 29.71           C  
ANISOU 2983  C   ILE B  21     3829   3627   3831     37    -71    418       C  
ATOM   2984  O   ILE B  21     -28.317 -52.062 -21.809  1.00 27.15           O  
ANISOU 2984  O   ILE B  21     3567   3168   3581     30    -72    437       O  
ATOM   2985  CB  ILE B  21     -29.009 -49.259 -22.026  1.00 25.36           C  
ANISOU 2985  CB  ILE B  21     3399   3000   3235    244    -11    345       C  
ATOM   2986  CG1 ILE B  21     -29.143 -47.794 -21.572  1.00 31.90           C  
ANISOU 2986  CG1 ILE B  21     4279   3827   4014    343     -3    298       C  
ATOM   2987  CG2 ILE B  21     -29.650 -49.511 -23.410  1.00 24.38           C  
ANISOU 2987  CG2 ILE B  21     3304   2873   3088    301    -38    325       C  
ATOM   2988  CD1 ILE B  21     -30.517 -47.382 -21.279  1.00 38.45           C  
ANISOU 2988  CD1 ILE B  21     5031   4810   4768    441    -33    228       C  
ATOM   2989  N   TYR B  22     -30.505 -52.430 -21.407  1.00 23.24           N  
ANISOU 2989  N   TYR B  22     2934   2917   2980    -39   -108    424       N  
ATOM   2990  CA  TYR B  22     -30.423 -53.832 -21.785  1.00 22.47           C  
ANISOU 2990  CA  TYR B  22     2862   2740   2936   -147   -169    465       C  
ATOM   2991  C   TYR B  22     -30.707 -54.060 -23.270  1.00 23.91           C  
ANISOU 2991  C   TYR B  22     3083   2873   3131    -82   -198    412       C  
ATOM   2992  O   TYR B  22     -31.575 -53.420 -23.866  1.00 26.27           O  
ANISOU 2992  O   TYR B  22     3342   3268   3372     -3   -197    357       O  
ATOM   2993  CB  TYR B  22     -31.389 -54.675 -20.957  1.00 21.37           C  
ANISOU 2993  CB  TYR B  22     2641   2727   2750   -322   -202    515       C  
ATOM   2994  CG  TYR B  22     -30.949 -54.819 -19.523  1.00 21.34           C  
ANISOU 2994  CG  TYR B  22     2646   2742   2719   -421   -194    592       C  
ATOM   2995  CD1 TYR B  22     -30.035 -55.794 -19.158  1.00 24.35           C  
ANISOU 2995  CD1 TYR B  22     3132   2956   3163   -499   -266    672       C  
ATOM   2996  CD2 TYR B  22     -31.437 -53.963 -18.538  1.00 26.52           C  
ANISOU 2996  CD2 TYR B  22     3217   3582   3279   -416   -127    572       C  
ATOM   2997  CE1 TYR B  22     -29.626 -55.934 -17.833  1.00 27.12           C  
ANISOU 2997  CE1 TYR B  22     3512   3319   3471   -587   -283    752       C  
ATOM   2998  CE2 TYR B  22     -31.037 -54.092 -17.212  1.00 24.20           C  
ANISOU 2998  CE2 TYR B  22     2947   3318   2931   -511   -123    640       C  
ATOM   2999  CZ  TYR B  22     -30.133 -55.073 -16.868  1.00 34.66           C  
ANISOU 2999  CZ  TYR B  22     4387   4471   4311   -602   -205    739       C  
ATOM   3000  OH  TYR B  22     -29.735 -55.195 -15.554  1.00 27.07           O  
ANISOU 3000  OH  TYR B  22     3470   3536   3279   -691   -224    814       O  
ATOM   3001  N   ASN B  23     -29.984 -55.014 -23.843  1.00 23.03           N  
ANISOU 3001  N   ASN B  23     3052   2611   3087   -104   -238    417       N  
ATOM   3002  CA  ASN B  23     -30.221 -55.511 -25.193  1.00 25.72           C  
ANISOU 3002  CA  ASN B  23     3445   2898   3427    -66   -279    359       C  
ATOM   3003  C   ASN B  23     -31.332 -56.554 -25.118  1.00 28.78           C  
ANISOU 3003  C   ASN B  23     3789   3337   3809   -210   -372    370       C  
ATOM   3004  O   ASN B  23     -31.087 -57.747 -24.933  1.00 25.94           O  
ANISOU 3004  O   ASN B  23     3489   2860   3507   -316   -448    401       O  
ATOM   3005  CB  ASN B  23     -28.938 -56.101 -25.762  1.00 25.29           C  
ANISOU 3005  CB  ASN B  23     3487   2679   3445    -15   -279    332       C  
ATOM   3006  CG  ASN B  23     -29.081 -56.540 -27.207  1.00 30.82           C  
ANISOU 3006  CG  ASN B  23     4258   3332   4120     43   -308    251       C  
ATOM   3007  OD1 ASN B  23     -30.182 -56.609 -27.745  1.00 24.81           O  
ANISOU 3007  OD1 ASN B  23     3483   2643   3301     22   -360    225       O  
ATOM   3008  ND2 ASN B  23     -27.956 -56.852 -27.837  1.00 27.16           N  
ANISOU 3008  ND2 ASN B  23     3859   2766   3693    121   -277    195       N  
ATOM   3009  N   ASP B  24     -32.574 -56.111 -25.252  1.00 27.25           N  
ANISOU 3009  N   ASP B  24     3491   3317   3547   -219   -380    340       N  
ATOM   3010  CA  ASP B  24     -33.678 -57.058 -25.322  1.00 30.21           C  
ANISOU 3010  CA  ASP B  24     3798   3768   3914   -381   -466    336       C  
ATOM   3011  C   ASP B  24     -34.044 -57.402 -26.757  1.00 28.93           C  
ANISOU 3011  C   ASP B  24     3687   3563   3741   -328   -545    252       C  
ATOM   3012  O   ASP B  24     -34.947 -58.217 -26.980  1.00 31.52           O  
ANISOU 3012  O   ASP B  24     3967   3941   4068   -469   -636    234       O  
ATOM   3013  CB  ASP B  24     -34.885 -56.514 -24.561  1.00 34.27           C  
ANISOU 3013  CB  ASP B  24     4118   4544   4359   -441   -434    332       C  
ATOM   3014  CG  ASP B  24     -34.646 -56.505 -23.035  1.00 36.97           C  
ANISOU 3014  CG  ASP B  24     4420   4944   4685   -555   -368    419       C  
ATOM   3015  OD1 ASP B  24     -34.268 -57.560 -22.479  1.00 37.97           O  
ANISOU 3015  OD1 ASP B  24     4626   4956   4844   -728   -410    508       O  
ATOM   3016  OD2 ASP B  24     -34.797 -55.443 -22.410  1.00 43.53           O  
ANISOU 3016  OD2 ASP B  24     5164   5913   5461   -461   -290    395       O  
ATOM   3017  N   VAL B  25     -33.348 -56.809 -27.727  1.00 22.29           N  
ANISOU 3017  N   VAL B  25     2951   2637   2881   -147   -513    203       N  
ATOM   3018  CA  VAL B  25     -33.606 -57.106 -29.130  1.00 25.34           C  
ANISOU 3018  CA  VAL B  25     3414   2985   3227    -86   -585    120       C  
ATOM   3019  C   VAL B  25     -33.017 -58.462 -29.504  1.00 27.29           C  
ANISOU 3019  C   VAL B  25     3783   3047   3539   -160   -652     95       C  
ATOM   3020  O   VAL B  25     -33.677 -59.290 -30.136  1.00 27.01           O  
ANISOU 3020  O   VAL B  25     3772   2993   3497   -236   -766     39       O  
ATOM   3021  CB  VAL B  25     -33.049 -55.974 -30.018  1.00 22.41           C  
ANISOU 3021  CB  VAL B  25     3138   2596   2780    110   -516     89       C  
ATOM   3022  CG1 VAL B  25     -33.041 -56.396 -31.490  1.00 23.84           C  
ANISOU 3022  CG1 VAL B  25     3443   2718   2897    169   -578      6       C  
ATOM   3023  CG2 VAL B  25     -33.876 -54.724 -29.830  1.00 25.35           C  
ANISOU 3023  CG2 VAL B  25     3423   3123   3086    202   -510     92       C  
ATOM   3024  N   GLU B  26     -31.770 -58.710 -29.117  1.00 23.19           N  
ANISOU 3024  N   GLU B  26     3340   2384   3086   -127   -599    122       N  
ATOM   3025  CA  GLU B  26     -31.083 -59.946 -29.454  1.00 24.94           C  
ANISOU 3025  CA  GLU B  26     3686   2414   3378   -141   -674     75       C  
ATOM   3026  C   GLU B  26     -31.256 -61.040 -28.413  1.00 28.60           C  
ANISOU 3026  C   GLU B  26     4165   2776   3926   -322   -775    151       C  
ATOM   3027  O   GLU B  26     -30.798 -62.162 -28.641  1.00 31.09           O  
ANISOU 3027  O   GLU B  26     4608   2896   4308   -334   -878    111       O  
ATOM   3028  CB  GLU B  26     -29.596 -59.661 -29.668  1.00 27.95           C  
ANISOU 3028  CB  GLU B  26     4124   2709   3787     15   -576     40       C  
ATOM   3029  CG  GLU B  26     -29.400 -58.744 -30.866  1.00 32.64           C  
ANISOU 3029  CG  GLU B  26     4749   3382   4271    153   -481    -29       C  
ATOM   3030  CD  GLU B  26     -27.958 -58.549 -31.224  1.00 35.23           C  
ANISOU 3030  CD  GLU B  26     5113   3660   4611    271   -368    -81       C  
ATOM   3031  OE1 GLU B  26     -27.259 -57.814 -30.499  1.00 34.94           O  
ANISOU 3031  OE1 GLU B  26     5013   3653   4608    283   -273    -19       O  
ATOM   3032  OE2 GLU B  26     -27.531 -59.136 -32.234  1.00 41.32           O  
ANISOU 3032  OE2 GLU B  26     5967   4379   5353    348   -375   -196       O  
ATOM   3033  N   ALA B  27     -31.922 -60.750 -27.302  1.00 31.06           N  
ANISOU 3033  N   ALA B  27     4365   3212   4223   -461   -755    255       N  
ATOM   3034  CA  ALA B  27     -32.127 -61.745 -26.261  1.00 26.20           C  
ANISOU 3034  CA  ALA B  27     3786   2514   3655   -671   -844    356       C  
ATOM   3035  C   ALA B  27     -33.124 -62.792 -26.725  1.00 33.82           C  
ANISOU 3035  C   ALA B  27     4792   3438   4622   -857   -982    333       C  
ATOM   3036  O   ALA B  27     -34.150 -62.467 -27.328  1.00 34.42           O  
ANISOU 3036  O   ALA B  27     4759   3681   4638   -889   -984    277       O  
ATOM   3037  CB  ALA B  27     -32.625 -61.065 -24.986  1.00 29.23           C  
ANISOU 3037  CB  ALA B  27     4029   3093   3986   -779   -759    462       C  
ATOM   3038  N   TRP B  28     -32.830 -64.068 -26.453  1.00 32.36           N  
ANISOU 3038  N   TRP B  28     4773   3016   4507   -980  -1120    373       N  
ATOM   3039  CA  TRP B  28     -33.796 -65.075 -26.878  1.00 31.53           C  
ANISOU 3039  CA  TRP B  28     4724   2850   4405  -1193  -1265    354       C  
ATOM   3040  C   TRP B  28     -35.007 -65.135 -25.959  1.00 37.88           C  
ANISOU 3040  C   TRP B  28     5390   3852   5153  -1502  -1255    472       C  
ATOM   3041  O   TRP B  28     -36.035 -65.692 -26.356  1.00 36.38           O  
ANISOU 3041  O   TRP B  28     5166   3709   4948  -1704  -1345    446       O  
ATOM   3042  CB  TRP B  28     -33.149 -66.463 -27.003  1.00 32.96           C  
ANISOU 3042  CB  TRP B  28     5167   2676   4679  -1225  -1447    343       C  
ATOM   3043  CG  TRP B  28     -32.495 -67.026 -25.786  1.00 37.26           C  
ANISOU 3043  CG  TRP B  28     5841   3043   5273  -1307  -1506    486       C  
ATOM   3044  CD1 TRP B  28     -31.166 -66.979 -25.483  1.00 37.08           C  
ANISOU 3044  CD1 TRP B  28     5901   2874   5314  -1087  -1501    480       C  
ATOM   3045  CD2 TRP B  28     -33.123 -67.765 -24.725  1.00 38.26           C  
ANISOU 3045  CD2 TRP B  28     6023   3148   5368  -1614  -1578    652       C  
ATOM   3046  NE1 TRP B  28     -30.926 -67.629 -24.297  1.00 39.00           N  
ANISOU 3046  NE1 TRP B  28     6238   3026   5553  -1200  -1570    623       N  
ATOM   3047  CE2 TRP B  28     -32.110 -68.123 -23.812  1.00 39.48           C  
ANISOU 3047  CE2 TRP B  28     6285   3181   5534  -1503  -1597    730       C  
ATOM   3048  CE3 TRP B  28     -34.440 -68.159 -24.460  1.00 40.55           C  
ANISOU 3048  CE3 TRP B  28     6235   3592   5580  -1918  -1585    722       C  
ATOM   3049  CZ2 TRP B  28     -32.373 -68.839 -22.646  1.00 40.81           C  
ANISOU 3049  CZ2 TRP B  28     6521   3356   5628  -1692  -1638    881       C  
ATOM   3050  CZ3 TRP B  28     -34.700 -68.873 -23.304  1.00 43.37           C  
ANISOU 3050  CZ3 TRP B  28     6653   3960   5865  -2108  -1598    875       C  
ATOM   3051  CH2 TRP B  28     -33.670 -69.207 -22.411  1.00 45.33           C  
ANISOU 3051  CH2 TRP B  28     7044   4063   6115  -1996  -1633    956       C  
ATOM   3052  N   ARG B  29     -34.915 -64.563 -24.756  1.00 39.68           N  
ANISOU 3052  N   ARG B  29     5522   4215   5338  -1550  -1143    589       N  
ATOM   3053  CA  ARG B  29     -36.038 -64.540 -23.819  1.00 48.05           C  
ANISOU 3053  CA  ARG B  29     6423   5518   6316  -1839  -1095    690       C  
ATOM   3054  C   ARG B  29     -36.977 -63.383 -24.160  1.00 45.02           C  
ANISOU 3054  C   ARG B  29     5757   5489   5861  -1753   -976    593       C  
ATOM   3055  O   ARG B  29     -36.540 -62.232 -24.236  1.00 41.25           O  
ANISOU 3055  O   ARG B  29     5205   5104   5364  -1493   -865    541       O  
ATOM   3056  CB  ARG B  29     -35.528 -64.395 -22.384  1.00 41.82           C  
ANISOU 3056  CB  ARG B  29     5664   4740   5486  -1908  -1026    839       C  
ATOM   3057  CG  ARG B  29     -34.756 -65.596 -21.843  1.00 45.18           C  
ANISOU 3057  CG  ARG B  29     6374   4826   5966  -2026  -1177    962       C  
ATOM   3058  CD  ARG B  29     -34.039 -65.234 -20.531  1.00 47.22           C  
ANISOU 3058  CD  ARG B  29     6665   5106   6172  -1994  -1110   1083       C  
ATOM   3059  NE  ARG B  29     -33.338 -66.365 -19.922  1.00 55.26           N  
ANISOU 3059  NE  ARG B  29     7915   5888   7192  -1979  -1236   1152       N  
ATOM   3060  CZ  ARG B  29     -32.072 -66.696 -20.174  1.00 54.73           C  
ANISOU 3060  CZ  ARG B  29     8004   5563   7227  -1738  -1334   1103       C  
ATOM   3061  NH1 ARG B  29     -31.352 -65.993 -21.047  1.00 40.00           N  
ANISOU 3061  NH1 ARG B  29     6100   3634   5465  -1496  -1304    990       N  
ATOM   3062  NH2 ARG B  29     -31.526 -67.744 -19.564  1.00 55.00           N  
ANISOU 3062  NH2 ARG B  29     8226   5417   7257  -1737  -1467   1160       N  
ATOM   3063  N   ASP B  30     -38.259 -63.685 -24.360  1.00 47.25           N  
ANISOU 3063  N   ASP B  30     5883   5963   6106  -1971  -1014    565       N  
ATOM   3064  CA  ASP B  30     -39.291 -62.671 -24.554  1.00 49.52           C  
ANISOU 3064  CA  ASP B  30     5872   6616   6326  -1900   -927    466       C  
ATOM   3065  C   ASP B  30     -39.823 -62.234 -23.192  1.00 50.82           C  
ANISOU 3065  C   ASP B  30     5840   7069   6400  -2052   -787    545       C  
ATOM   3066  O   ASP B  30     -40.390 -63.052 -22.459  1.00 65.91           O  
ANISOU 3066  O   ASP B  30     7723   9050   8272  -2402   -797    647       O  
ATOM   3067  CB  ASP B  30     -40.429 -63.222 -25.415  1.00 62.19           C  
ANISOU 3067  CB  ASP B  30     7367   8325   7936  -2061  -1046    376       C  
ATOM   3068  CG  ASP B  30     -39.968 -63.635 -26.806  1.00 75.13           C  
ANISOU 3068  CG  ASP B  30     9205   9702   9637  -1904  -1187    276       C  
ATOM   3069  OD1 ASP B  30     -39.067 -62.966 -27.359  1.00 82.30           O  
ANISOU 3069  OD1 ASP B  30    10220  10496  10554  -1587  -1147    224       O  
ATOM   3070  OD2 ASP B  30     -40.497 -64.632 -27.345  1.00 74.52           O  
ANISOU 3070  OD2 ASP B  30     9184   9540   9589  -2112  -1335    245       O  
ATOM   3071  N   ARG B  31     -39.646 -60.955 -22.844  1.00 36.09           N  
ANISOU 3071  N   ARG B  31     3853   5372   4488  -1804   -656    498       N  
ATOM   3072  CA  ARG B  31     -40.058 -60.500 -21.523  1.00 41.34           C  
ANISOU 3072  CA  ARG B  31     4346   6309   5051  -1913   -516    549       C  
ATOM   3073  C   ARG B  31     -41.101 -59.385 -21.495  1.00 35.46           C  
ANISOU 3073  C   ARG B  31     3277   5961   4237  -1777   -424    406       C  
ATOM   3074  O   ARG B  31     -41.741 -59.217 -20.453  1.00 41.42           O  
ANISOU 3074  O   ARG B  31     3837   7011   4890  -1929   -310    421       O  
ATOM   3075  CB  ARG B  31     -38.838 -60.055 -20.696  1.00 44.57           C  
ANISOU 3075  CB  ARG B  31     4921   6562   5450  -1777   -445    632       C  
ATOM   3076  CG  ARG B  31     -38.146 -58.801 -21.157  1.00 32.01           C  
ANISOU 3076  CG  ARG B  31     3352   4920   3889  -1399   -400    535       C  
ATOM   3077  CD  ARG B  31     -37.022 -58.418 -20.171  1.00 34.57           C  
ANISOU 3077  CD  ARG B  31     3808   5130   4199  -1325   -333    617       C  
ATOM   3078  NE  ARG B  31     -37.560 -58.231 -18.829  1.00 41.84           N  
ANISOU 3078  NE  ARG B  31     4595   6309   4994  -1484   -229    665       N  
ATOM   3079  CZ  ARG B  31     -37.354 -59.052 -17.801  1.00 45.13           C  
ANISOU 3079  CZ  ARG B  31     5110   6686   5351  -1741   -231    814       C  
ATOM   3080  NH1 ARG B  31     -36.585 -60.125 -17.936  1.00 44.11           N  
ANISOU 3080  NH1 ARG B  31     5224   6238   5299  -1846   -355    929       N  
ATOM   3081  NH2 ARG B  31     -37.918 -58.795 -16.628  1.00 36.50           N  
ANISOU 3081  NH2 ARG B  31     3883   5874   4110  -1884   -116    843       N  
ATOM   3082  N   TYR B  32     -41.298 -58.621 -22.572  1.00 33.85           N  
ANISOU 3082  N   TYR B  32     3611   4790   4460     52  -1059   2249       N  
ATOM   3083  CA  TYR B  32     -42.273 -57.532 -22.567  1.00 29.99           C  
ANISOU 3083  CA  TYR B  32     3240   4412   3745    -55  -1026   2099       C  
ATOM   3084  C   TYR B  32     -43.506 -57.912 -23.376  1.00 44.57           C  
ANISOU 3084  C   TYR B  32     5182   6077   5677    -11   -865   1952       C  
ATOM   3085  O   TYR B  32     -43.392 -58.504 -24.454  1.00 44.94           O  
ANISOU 3085  O   TYR B  32     5192   5930   5952    118   -788   1901       O  
ATOM   3086  CB  TYR B  32     -41.668 -56.227 -23.117  1.00 28.79           C  
ANISOU 3086  CB  TYR B  32     3048   4347   3544    -72  -1029   1916       C  
ATOM   3087  CG  TYR B  32     -40.506 -55.752 -22.264  1.00 35.01           C  
ANISOU 3087  CG  TYR B  32     3752   5315   4236   -153  -1172   2003       C  
ATOM   3088  CD1 TYR B  32     -40.690 -55.465 -20.917  1.00 38.68           C  
ANISOU 3088  CD1 TYR B  32     4289   5954   4453   -315  -1242   2040       C  
ATOM   3089  CD2 TYR B  32     -39.222 -55.642 -22.786  1.00 32.03           C  
ANISOU 3089  CD2 TYR B  32     3228   4919   4025    -75  -1208   2020       C  
ATOM   3090  CE1 TYR B  32     -39.634 -55.067 -20.115  1.00 40.60           C  
ANISOU 3090  CE1 TYR B  32     4468   6346   4614   -402  -1361   2092       C  
ATOM   3091  CE2 TYR B  32     -38.154 -55.245 -21.988  1.00 35.78           C  
ANISOU 3091  CE2 TYR B  32     3625   5542   4426   -162  -1326   2084       C  
ATOM   3092  CZ  TYR B  32     -38.365 -54.957 -20.655  1.00 37.97           C  
ANISOU 3092  CZ  TYR B  32     3982   5988   4455   -328  -1410   2120       C  
ATOM   3093  OH  TYR B  32     -37.313 -54.566 -19.842  1.00 40.81           O  
ANISOU 3093  OH  TYR B  32     4271   6497   4738   -426  -1536   2185       O  
ATOM   3094  N   LYS B  33     -44.684 -57.559 -22.855  1.00 41.89           N  
ANISOU 3094  N   LYS B  33     4962   5806   5150   -127   -808   1870       N  
ATOM   3095  CA  LYS B  33     -45.930 -57.630 -23.613  1.00 37.85           C  
ANISOU 3095  CA  LYS B  33     4528   5161   4690   -113   -663   1696       C  
ATOM   3096  C   LYS B  33     -46.661 -56.294 -23.546  1.00 34.74           C  
ANISOU 3096  C   LYS B  33     4207   4885   4106   -209   -600   1482       C  
ATOM   3097  O   LYS B  33     -46.859 -55.746 -22.454  1.00 30.93           O  
ANISOU 3097  O   LYS B  33     3773   4574   3405   -331   -628   1501       O  
ATOM   3098  CB  LYS B  33     -46.828 -58.756 -23.084  1.00 37.98           C  
ANISOU 3098  CB  LYS B  33     4596   5098   4736   -145   -631   1835       C  
ATOM   3099  CG  LYS B  33     -46.363 -60.152 -23.483  1.00 49.34           C  
ANISOU 3099  CG  LYS B  33     5977   6332   6438    -27   -647   1998       C  
ATOM   3100  CD  LYS B  33     -47.507 -61.159 -23.448  1.00 62.51           C  
ANISOU 3100  CD  LYS B  33     7709   7852   8188    -54   -568   2043       C  
ATOM   3101  CE  LYS B  33     -47.754 -61.681 -22.052  1.00 77.98           C  
ANISOU 3101  CE  LYS B  33     9697   9911  10020   -157   -627   2291       C  
ATOM   3102  NZ  LYS B  33     -48.676 -62.861 -22.039  1.00 86.63           N  
ANISOU 3102  NZ  LYS B  33    10835  10827  11253   -174   -558   2384       N  
ATOM   3103  N   TYR B  34     -47.041 -55.767 -24.713  1.00 30.64           N  
ANISOU 3103  N   TYR B  34     3696   4274   3671   -154   -513   1282       N  
ATOM   3104  CA  TYR B  34     -47.935 -54.615 -24.781  1.00 30.69           C  
ANISOU 3104  CA  TYR B  34     3763   4341   3555   -222   -434   1089       C  
ATOM   3105  C   TYR B  34     -49.364 -55.023 -24.430  1.00 34.27           C  
ANISOU 3105  C   TYR B  34     4278   4767   3977   -278   -346   1079       C  
ATOM   3106  O   TYR B  34     -49.859 -56.053 -24.897  1.00 33.65           O  
ANISOU 3106  O   TYR B  34     4195   4550   4039   -234   -315   1128       O  
ATOM   3107  CB  TYR B  34     -47.935 -54.004 -26.187  1.00 34.15           C  
ANISOU 3107  CB  TYR B  34     4184   4686   4106   -145   -381    916       C  
ATOM   3108  CG  TYR B  34     -46.751 -53.129 -26.540  1.00 30.70           C  
ANISOU 3108  CG  TYR B  34     3695   4304   3665   -122   -432    872       C  
ATOM   3109  CD1 TYR B  34     -45.610 -53.095 -25.742  1.00 34.17           C  
ANISOU 3109  CD1 TYR B  34     4083   4855   4046   -153   -539    994       C  
ATOM   3110  CD2 TYR B  34     -46.784 -52.330 -27.676  1.00 30.99           C  
ANISOU 3110  CD2 TYR B  34     3729   4290   3758    -81   -381    721       C  
ATOM   3111  CE1 TYR B  34     -44.536 -52.280 -26.075  1.00 42.25           C  
ANISOU 3111  CE1 TYR B  34     5044   5930   5080   -146   -585    954       C  
ATOM   3112  CE2 TYR B  34     -45.725 -51.513 -28.014  1.00 34.10           C  
ANISOU 3112  CE2 TYR B  34     4072   4730   4155    -71   -417    687       C  
ATOM   3113  CZ  TYR B  34     -44.606 -51.488 -27.214  1.00 38.27           C  
ANISOU 3113  CZ  TYR B  34     4541   5362   4638   -106   -515    797       C  
ATOM   3114  OH  TYR B  34     -43.550 -50.670 -27.564  1.00 37.30           O  
ANISOU 3114  OH  TYR B  34     4354   5286   4534   -108   -551    766       O  
ATOM   3115  N   HIS B  35     -50.037 -54.194 -23.625  1.00 30.51           N  
ANISOU 3115  N   HIS B  35     3853   4416   3323   -380   -295   1003       N  
ATOM   3116  CA  HIS B  35     -51.460 -54.360 -23.286  1.00 30.18           C  
ANISOU 3116  CA  HIS B  35     3851   4368   3249   -438   -185    969       C  
ATOM   3117  C   HIS B  35     -52.130 -52.996 -23.340  1.00 32.71           C  
ANISOU 3117  C   HIS B  35     4192   4742   3494   -472    -93    767       C  
ATOM   3118  O   HIS B  35     -51.503 -51.989 -22.982  1.00 32.14           O  
ANISOU 3118  O   HIS B  35     4139   4767   3307   -508   -117    692       O  
ATOM   3119  CB  HIS B  35     -51.669 -54.964 -21.886  1.00 27.96           C  
ANISOU 3119  CB  HIS B  35     3611   4200   2811   -543   -189   1133       C  
ATOM   3120  CG  HIS B  35     -51.045 -56.314 -21.710  1.00 38.47           C  
ANISOU 3120  CG  HIS B  35     4918   5468   4231   -511   -283   1367       C  
ATOM   3121  ND1 HIS B  35     -51.449 -57.420 -22.428  1.00 49.46           N  
ANISOU 3121  ND1 HIS B  35     6285   6673   5833   -444   -260   1425       N  
ATOM   3122  CD2 HIS B  35     -50.053 -56.740 -20.892  1.00 40.85           C  
ANISOU 3122  CD2 HIS B  35     5210   5859   4452   -537   -402   1563       C  
ATOM   3123  CE1 HIS B  35     -50.734 -58.469 -22.060  1.00 49.31           C  
ANISOU 3123  CE1 HIS B  35     6245   6610   5879   -419   -346   1644       C  
ATOM   3124  NE2 HIS B  35     -49.879 -58.084 -21.129  1.00 45.79           N  
ANISOU 3124  NE2 HIS B  35     5800   6335   5261   -470   -440   1745       N  
ATOM   3125  N   PRO B  36     -53.394 -52.929 -23.767  1.00 34.84           N  
ANISOU 3125  N   PRO B  36     4451   4945   3842   -465     12    679       N  
ATOM   3126  CA  PRO B  36     -54.140 -51.671 -23.646  1.00 29.34           C  
ANISOU 3126  CA  PRO B  36     3762   4292   3093   -493    117    509       C  
ATOM   3127  C   PRO B  36     -54.307 -51.297 -22.186  1.00 31.97           C  
ANISOU 3127  C   PRO B  36     4155   4781   3209   -609    181    505       C  
ATOM   3128  O   PRO B  36     -54.612 -52.143 -21.335  1.00 31.17           O  
ANISOU 3128  O   PRO B  36     4080   4741   3023   -678    199    633       O  
ATOM   3129  CB  PRO B  36     -55.497 -51.988 -24.288  1.00 30.84           C  
ANISOU 3129  CB  PRO B  36     3903   4386   3430   -466    200    473       C  
ATOM   3130  CG  PRO B  36     -55.290 -53.246 -25.057  1.00 42.07           C  
ANISOU 3130  CG  PRO B  36     5303   5693   4988   -417    123    580       C  
ATOM   3131  CD  PRO B  36     -54.224 -54.005 -24.337  1.00 35.27           C  
ANISOU 3131  CD  PRO B  36     4477   4876   4049   -437     39    736       C  
ATOM   3132  N   ASP B  37     -54.113 -50.010 -21.900  1.00 32.22           N  
ANISOU 3132  N   ASP B  37     4219   4874   3149   -640    221    353       N  
ATOM   3133  CA  ASP B  37     -54.421 -49.497 -20.567  1.00 38.64           C  
ANISOU 3133  CA  ASP B  37     5104   5831   3745   -761    317    293       C  
ATOM   3134  C   ASP B  37     -55.853 -49.858 -20.174  1.00 32.66           C  
ANISOU 3134  C   ASP B  37     4332   5077   3001   -790    477    289       C  
ATOM   3135  O   ASP B  37     -56.127 -50.215 -19.024  1.00 31.05           O  
ANISOU 3135  O   ASP B  37     4184   5001   2614   -898    539    349       O  
ATOM   3136  CB  ASP B  37     -54.189 -47.982 -20.552  1.00 45.60           C  
ANISOU 3136  CB  ASP B  37     6017   6723   4588   -776    366     86       C  
ATOM   3137  CG  ASP B  37     -54.358 -47.365 -19.185  1.00 69.70           C  
ANISOU 3137  CG  ASP B  37     9164   9924   7396   -913    468    -16       C  
ATOM   3138  OD1 ASP B  37     -53.765 -47.877 -18.210  1.00 79.61           O  
ANISOU 3138  OD1 ASP B  37    10481  11330   8436  -1022    394     94       O  
ATOM   3139  OD2 ASP B  37     -55.079 -46.349 -19.095  1.00 79.85           O  
ANISOU 3139  OD2 ASP B  37    10460  11173   8706   -915    625   -206       O  
ATOM   3140  N   SER B  38     -56.770 -49.828 -21.139  1.00 34.66           N  
ANISOU 3140  N   SER B  38     4502   5199   3468   -703    538    238       N  
ATOM   3141  CA  SER B  38     -58.163 -50.185 -20.909  1.00 38.80           C  
ANISOU 3141  CA  SER B  38     4977   5713   4050   -724    683    243       C  
ATOM   3142  C   SER B  38     -58.781 -50.744 -22.186  1.00 33.11           C  
ANISOU 3142  C   SER B  38     4156   4844   3580   -633    643    282       C  
ATOM   3143  O   SER B  38     -59.002 -49.987 -23.140  1.00 30.93           O  
ANISOU 3143  O   SER B  38     3824   4482   3448   -551    640    177       O  
ATOM   3144  CB  SER B  38     -58.963 -48.968 -20.440  1.00 40.56           C  
ANISOU 3144  CB  SER B  38     5196   5970   4246   -742    869     54       C  
ATOM   3145  OG  SER B  38     -60.350 -49.259 -20.466  1.00 39.99           O  
ANISOU 3145  OG  SER B  38     5033   5867   4293   -736   1010     57       O  
ATOM   3146  N   PRO B  39     -59.065 -52.051 -22.249  1.00 33.37           N  
ANISOU 3146  N   PRO B  39     4169   4843   3669   -655    606    433       N  
ATOM   3147  CA  PRO B  39     -59.723 -52.592 -23.453  1.00 33.32           C  
ANISOU 3147  CA  PRO B  39     4073   4699   3887   -595    567    449       C  
ATOM   3148  C   PRO B  39     -61.060 -51.934 -23.747  1.00 26.96           C  
ANISOU 3148  C   PRO B  39     3166   3873   3205   -578    689    345       C  
ATOM   3149  O   PRO B  39     -61.389 -51.709 -24.918  1.00 28.79           O  
ANISOU 3149  O   PRO B  39     3326   4012   3602   -509    634    299       O  
ATOM   3150  CB  PRO B  39     -59.880 -54.086 -23.124  1.00 39.10           C  
ANISOU 3150  CB  PRO B  39     4816   5407   4635   -656    541    624       C  
ATOM   3151  CG  PRO B  39     -58.806 -54.365 -22.095  1.00 37.99           C  
ANISOU 3151  CG  PRO B  39     4772   5364   4298   -705    492    731       C  
ATOM   3152  CD  PRO B  39     -58.691 -53.106 -21.288  1.00 38.11           C  
ANISOU 3152  CD  PRO B  39     4830   5517   4133   -741    576    607       C  
ATOM   3153  N   ARG B  40     -61.842 -51.608 -22.714  1.00 30.22           N  
ANISOU 3153  N   ARG B  40     3563   4376   3542   -642    856    313       N  
ATOM   3154  CA  ARG B  40     -63.120 -50.950 -22.962  1.00 32.13           C  
ANISOU 3154  CA  ARG B  40     3681   4593   3933   -612    986    221       C  
ATOM   3155  C   ARG B  40     -62.930 -49.538 -23.504  1.00 36.71           C  
ANISOU 3155  C   ARG B  40     4243   5131   4575   -518    992     70       C  
ATOM   3156  O   ARG B  40     -63.772 -49.050 -24.265  1.00 30.69           O  
ANISOU 3156  O   ARG B  40     3358   4298   4006   -452   1015     26       O  
ATOM   3157  CB  ARG B  40     -63.955 -50.931 -21.681  1.00 33.06           C  
ANISOU 3157  CB  ARG B  40     3787   4821   3954   -699   1193    213       C  
ATOM   3158  CG  ARG B  40     -64.208 -52.330 -21.137  1.00 37.66           C  
ANISOU 3158  CG  ARG B  40     4383   5440   4485   -802   1194    387       C  
ATOM   3159  CD  ARG B  40     -65.361 -52.406 -20.134  1.00 38.09           C  
ANISOU 3159  CD  ARG B  40     4379   5589   4505   -889   1418    395       C  
ATOM   3160  NE  ARG B  40     -65.864 -53.780 -20.074  1.00 52.78           N  
ANISOU 3160  NE  ARG B  40     6200   7428   6427   -970   1397    574       N  
ATOM   3161  CZ  ARG B  40     -66.876 -54.258 -20.801  1.00 49.24           C  
ANISOU 3161  CZ  ARG B  40     5603   6892   6213   -967   1396    610       C  
ATOM   3162  NH1 ARG B  40     -67.541 -53.474 -21.651  1.00 43.13           N  
ANISOU 3162  NH1 ARG B  40     4694   6058   5634   -880   1408    497       N  
ATOM   3163  NH2 ARG B  40     -67.235 -55.531 -20.669  1.00 49.03           N  
ANISOU 3163  NH2 ARG B  40     5559   6836   6234  -1060   1377    772       N  
ATOM   3164  N   ARG B  41     -61.845 -48.861 -23.118  1.00 32.04           N  
ANISOU 3164  N   ARG B  41     3763   4578   3832   -519    965      3       N  
ATOM   3165  CA  ARG B  41     -61.581 -47.548 -23.693  1.00 30.50           C  
ANISOU 3165  CA  ARG B  41     3557   4319   3713   -437    961   -128       C  
ATOM   3166  C   ARG B  41     -61.055 -47.679 -25.117  1.00 27.28           C  
ANISOU 3166  C   ARG B  41     3124   3813   3428   -358    780    -80       C  
ATOM   3167  O   ARG B  41     -61.412 -46.882 -25.993  1.00 27.74           O  
ANISOU 3167  O   ARG B  41     3109   3790   3641   -279    769   -132       O  
ATOM   3168  CB  ARG B  41     -60.599 -46.777 -22.818  1.00 35.75           C  
ANISOU 3168  CB  ARG B  41     4349   5055   4180   -485    989   -224       C  
ATOM   3169  CG  ARG B  41     -60.451 -45.320 -23.188  1.00 48.06           C  
ANISOU 3169  CG  ARG B  41     5901   6535   5823   -420   1029   -376       C  
ATOM   3170  CD  ARG B  41     -59.683 -44.569 -22.106  1.00 62.20           C  
ANISOU 3170  CD  ARG B  41     7821   8406   7407   -503   1091   -499       C  
ATOM   3171  NE  ARG B  41     -60.401 -44.571 -20.835  1.00 69.95           N  
ANISOU 3171  NE  ARG B  41     8834   9487   8256   -588   1286   -568       N  
ATOM   3172  CZ  ARG B  41     -61.339 -43.683 -20.516  1.00 79.02           C  
ANISOU 3172  CZ  ARG B  41     9936  10592   9496   -561   1494   -719       C  
ATOM   3173  NH1 ARG B  41     -61.668 -42.729 -21.380  1.00 74.32           N  
ANISOU 3173  NH1 ARG B  41     9255   9842   9140   -446   1515   -794       N  
ATOM   3174  NH2 ARG B  41     -61.950 -43.748 -19.339  1.00 80.28           N  
ANISOU 3174  NH2 ARG B  41    10131  10857   9514   -648   1689   -787       N  
ATOM   3175  N   LEU B  42     -60.220 -48.688 -25.371  1.00 29.17           N  
ANISOU 3175  N   LEU B  42     3421   4057   3604   -379    643     25       N  
ATOM   3176  CA  LEU B  42     -59.750 -48.920 -26.731  1.00 28.89           C  
ANISOU 3176  CA  LEU B  42     3369   3937   3672   -313    496     59       C  
ATOM   3177  C   LEU B  42     -60.907 -49.281 -27.654  1.00 30.73           C  
ANISOU 3177  C   LEU B  42     3490   4103   4082   -288    481     86       C  
ATOM   3178  O   LEU B  42     -60.945 -48.845 -28.811  1.00 25.41           O  
ANISOU 3178  O   LEU B  42     2775   3369   3511   -227    404     66       O  
ATOM   3179  CB  LEU B  42     -58.686 -50.019 -26.747  1.00 26.53           C  
ANISOU 3179  CB  LEU B  42     3144   3644   3293   -334    382    160       C  
ATOM   3180  CG  LEU B  42     -58.075 -50.308 -28.131  1.00 25.38           C  
ANISOU 3180  CG  LEU B  42     2997   3414   3234   -271    253    176       C  
ATOM   3181  CD1 LEU B  42     -57.551 -49.023 -28.818  1.00 26.21           C  
ANISOU 3181  CD1 LEU B  42     3102   3500   3357   -210    227     90       C  
ATOM   3182  CD2 LEU B  42     -56.962 -51.350 -28.001  1.00 22.49           C  
ANISOU 3182  CD2 LEU B  42     2693   3043   2808   -279    171    269       C  
ATOM   3183  N   ALA B  43     -61.863 -50.075 -27.160  1.00 25.02           N  
ANISOU 3183  N   ALA B  43     2714   3400   3391   -346    548    141       N  
ATOM   3184  CA  ALA B  43     -63.028 -50.413 -27.974  1.00 28.47           C  
ANISOU 3184  CA  ALA B  43     3027   3787   4003   -343    527    168       C  
ATOM   3185  C   ALA B  43     -63.818 -49.161 -28.344  1.00 29.46           C  
ANISOU 3185  C   ALA B  43     3040   3895   4259   -276    584     97       C  
ATOM   3186  O   ALA B  43     -64.292 -49.030 -29.478  1.00 30.97           O  
ANISOU 3186  O   ALA B  43     3146   4038   4584   -239    491    113       O  
ATOM   3187  CB  ALA B  43     -63.915 -51.422 -27.232  1.00 26.29           C  
ANISOU 3187  CB  ALA B  43     2704   3540   3745   -432    608    243       C  
ATOM   3188  N   ALA B  44     -63.956 -48.221 -27.401  1.00 25.52           N  
ANISOU 3188  N   ALA B  44     2542   3433   3724   -262    736     18       N  
ATOM   3189  CA  ALA B  44     -64.678 -46.986 -27.690  1.00 25.50           C  
ANISOU 3189  CA  ALA B  44     2427   3385   3876   -183    809    -49       C  
ATOM   3190  C   ALA B  44     -63.921 -46.120 -28.694  1.00 32.73           C  
ANISOU 3190  C   ALA B  44     3376   4233   4824   -105    692    -75       C  
ATOM   3191  O   ALA B  44     -64.540 -45.504 -29.570  1.00 28.36           O  
ANISOU 3191  O   ALA B  44     2711   3622   4443    -37    652    -57       O  
ATOM   3192  CB  ALA B  44     -64.948 -46.209 -26.396  1.00 30.60           C  
ANISOU 3192  CB  ALA B  44     3084   4070   4472   -191   1026   -155       C  
ATOM   3193  N   ALA B  45     -62.586 -46.054 -28.578  1.00 28.41           N  
ANISOU 3193  N   ALA B  45     2974   3699   4121   -118    633   -100       N  
ATOM   3194  CA  ALA B  45     -61.777 -45.339 -29.564  1.00 29.21           C  
ANISOU 3194  CA  ALA B  45     3111   3743   4243    -59    522   -109       C  
ATOM   3195  C   ALA B  45     -61.943 -45.928 -30.960  1.00 28.69           C  
ANISOU 3195  C   ALA B  45     3000   3650   4250    -42    364    -22       C  
ATOM   3196  O   ALA B  45     -62.020 -45.192 -31.949  1.00 27.61           O  
ANISOU 3196  O   ALA B  45     2819   3465   4206     15    296     -5       O  
ATOM   3197  CB  ALA B  45     -60.302 -45.376 -29.161  1.00 24.60           C  
ANISOU 3197  CB  ALA B  45     2672   3195   3481    -92    482   -135       C  
ATOM   3198  N   VAL B  46     -61.964 -47.257 -31.060  1.00 30.26           N  
ANISOU 3198  N   VAL B  46     3220   3877   4401   -100    304     35       N  
ATOM   3199  CA  VAL B  46     -62.114 -47.912 -32.356  1.00 26.64           C  
ANISOU 3199  CA  VAL B  46     2739   3395   3988   -106    162     90       C  
ATOM   3200  C   VAL B  46     -63.489 -47.630 -32.945  1.00 30.58           C  
ANISOU 3200  C   VAL B  46     3083   3883   4655    -94    142    125       C  
ATOM   3201  O   VAL B  46     -63.618 -47.344 -34.144  1.00 25.99           O  
ANISOU 3201  O   VAL B  46     2465   3286   4124    -71     24    159       O  
ATOM   3202  CB  VAL B  46     -61.859 -49.421 -32.201  1.00 26.58           C  
ANISOU 3202  CB  VAL B  46     2793   3393   3913   -177    125    126       C  
ATOM   3203  CG1 VAL B  46     -62.389 -50.189 -33.405  1.00 25.91           C  
ANISOU 3203  CG1 VAL B  46     2670   3281   3895   -211      6    158       C  
ATOM   3204  CG2 VAL B  46     -60.375 -49.681 -31.970  1.00 24.42           C  
ANISOU 3204  CG2 VAL B  46     2651   3122   3504   -169    102    117       C  
ATOM   3205  N   LYS B  47     -64.537 -47.718 -32.116  1.00 25.87           N  
ANISOU 3205  N   LYS B  47     2383   3304   4143   -114    255    129       N  
ATOM   3206  CA  LYS B  47     -65.884 -47.396 -32.571  1.00 27.43           C  
ANISOU 3206  CA  LYS B  47     2398   3495   4529    -96    246    174       C  
ATOM   3207  C   LYS B  47     -65.964 -45.969 -33.090  1.00 31.16           C  
ANISOU 3207  C   LYS B  47     2807   3924   5110      5    238    173       C  
ATOM   3208  O   LYS B  47     -66.561 -45.709 -34.142  1.00 27.96           O  
ANISOU 3208  O   LYS B  47     2294   3509   4820     27    119    246       O  
ATOM   3209  CB  LYS B  47     -66.883 -47.601 -31.435  1.00 27.50           C  
ANISOU 3209  CB  LYS B  47     2303   3533   4614   -126    413    169       C  
ATOM   3210  CG  LYS B  47     -68.304 -47.114 -31.730  1.00 28.22           C  
ANISOU 3210  CG  LYS B  47     2167   3617   4937    -91    438    216       C  
ATOM   3211  CD  LYS B  47     -69.177 -47.230 -30.479  1.00 28.02           C  
ANISOU 3211  CD  LYS B  47     2045   3625   4976   -115    650    194       C  
ATOM   3212  CE  LYS B  47     -70.656 -46.988 -30.777  1.00 37.68           C  
ANISOU 3212  CE  LYS B  47     3010   4850   6458    -90    673    259       C  
ATOM   3213  NZ  LYS B  47     -70.995 -45.543 -30.774  1.00 47.38           N  
ANISOU 3213  NZ  LYS B  47     4130   6020   7854     43    766    229       N  
ATOM   3214  N   GLN B  48     -65.389 -45.022 -32.353  1.00 29.35           N  
ANISOU 3214  N   GLN B  48     2641   3663   4847     58    360     96       N  
ATOM   3215  CA  GLN B  48     -65.423 -43.636 -32.810  1.00 28.72           C  
ANISOU 3215  CA  GLN B  48     2509   3511   4893    155    364     96       C  
ATOM   3216  C   GLN B  48     -64.587 -43.448 -34.071  1.00 28.67           C  
ANISOU 3216  C   GLN B  48     2578   3490   4824    166    188    150       C  
ATOM   3217  O   GLN B  48     -65.006 -42.740 -34.997  1.00 32.17           O  
ANISOU 3217  O   GLN B  48     2931   3897   5396    221    104    230       O  
ATOM   3218  CB  GLN B  48     -64.940 -42.695 -31.710  1.00 28.59           C  
ANISOU 3218  CB  GLN B  48     2563   3451   4849    189    540    -23       C  
ATOM   3219  CG  GLN B  48     -65.042 -41.222 -32.104  1.00 39.16           C  
ANISOU 3219  CG  GLN B  48     3843   4677   6357    291    567    -29       C  
ATOM   3220  CD  GLN B  48     -64.786 -40.262 -30.947  1.00 43.24           C  
ANISOU 3220  CD  GLN B  48     4417   5133   6881    315    769   -176       C  
ATOM   3221  OE1 GLN B  48     -64.871 -40.638 -29.778  1.00 36.61           O  
ANISOU 3221  OE1 GLN B  48     3621   4350   5940    260    912   -270       O  
ATOM   3222  NE2 GLN B  48     -64.481 -39.011 -31.276  1.00 37.86           N  
ANISOU 3222  NE2 GLN B  48     3741   4333   6313    386    783   -197       N  
ATOM   3223  N   ALA B  49     -63.406 -44.070 -34.124  1.00 24.68           N  
ANISOU 3223  N   ALA B  49     2232   3019   4127    115    136    120       N  
ATOM   3224  CA  ALA B  49     -62.567 -43.990 -35.317  1.00 27.52           C  
ANISOU 3224  CA  ALA B  49     2668   3378   4411    117     -7    163       C  
ATOM   3225  C   ALA B  49     -63.343 -44.430 -36.549  1.00 29.76           C  
ANISOU 3225  C   ALA B  49     2868   3692   4748     94   -157    258       C  
ATOM   3226  O   ALA B  49     -63.365 -43.736 -37.578  1.00 29.96           O  
ANISOU 3226  O   ALA B  49     2865   3707   4813    126   -256    331       O  
ATOM   3227  CB  ALA B  49     -61.319 -44.860 -35.132  1.00 25.76           C  
ANISOU 3227  CB  ALA B  49     2598   3191   3998     65    -25    119       C  
ATOM   3228  N   TRP B  50     -64.012 -45.578 -36.444  1.00 28.65           N  
ANISOU 3228  N   TRP B  50     2687   3594   4606     26   -181    264       N  
ATOM   3229  CA  TRP B  50     -64.791 -46.092 -37.564  1.00 28.61           C  
ANISOU 3229  CA  TRP B  50     2604   3628   4637    -25   -335    338       C  
ATOM   3230  C   TRP B  50     -65.867 -45.105 -37.985  1.00 32.11           C  
ANISOU 3230  C   TRP B  50     2867   4062   5272     33   -377    434       C  
ATOM   3231  O   TRP B  50     -66.088 -44.900 -39.183  1.00 29.36           O  
ANISOU 3231  O   TRP B  50     2483   3746   4926     19   -535    522       O  
ATOM   3232  CB  TRP B  50     -65.404 -47.442 -37.191  1.00 27.93           C  
ANISOU 3232  CB  TRP B  50     2492   3569   4551   -118   -332    321       C  
ATOM   3233  CG  TRP B  50     -66.294 -48.011 -38.256  1.00 27.09           C  
ANISOU 3233  CG  TRP B  50     2299   3507   4489   -197   -494    382       C  
ATOM   3234  CD1 TRP B  50     -67.648 -47.899 -38.335  1.00 30.94           C  
ANISOU 3234  CD1 TRP B  50     2588   4020   5147   -214   -531    457       C  
ATOM   3235  CD2 TRP B  50     -65.884 -48.777 -39.395  1.00 26.26           C  
ANISOU 3235  CD2 TRP B  50     2297   3431   4248   -280   -640    367       C  
ATOM   3236  NE1 TRP B  50     -68.114 -48.560 -39.449  1.00 34.64           N  
ANISOU 3236  NE1 TRP B  50     3032   4542   5588   -316   -714    495       N  
ATOM   3237  CE2 TRP B  50     -67.048 -49.113 -40.113  1.00 35.09           C  
ANISOU 3237  CE2 TRP B  50     3285   4601   5448   -362   -777    429       C  
ATOM   3238  CE3 TRP B  50     -64.644 -49.226 -39.867  1.00 31.44           C  
ANISOU 3238  CE3 TRP B  50     3139   4077   4728   -298   -659    299       C  
ATOM   3239  CZ2 TRP B  50     -67.013 -49.865 -41.292  1.00 40.26           C  
ANISOU 3239  CZ2 TRP B  50     4011   5301   5986   -474   -937    411       C  
ATOM   3240  CZ3 TRP B  50     -64.612 -49.983 -41.030  1.00 43.37           C  
ANISOU 3240  CZ3 TRP B  50     4718   5623   6139   -393   -793    276       C  
ATOM   3241  CH2 TRP B  50     -65.794 -50.293 -41.731  1.00 38.28           C  
ANISOU 3241  CH2 TRP B  50     3961   5033   5552   -488   -933    325       C  
ATOM   3242  N   GLU B  51     -66.539 -44.469 -37.015  1.00 31.99           N  
ANISOU 3242  N   GLU B  51     2733   4002   5417     98   -231    424       N  
ATOM   3243  CA  GLU B  51     -67.587 -43.508 -37.354  1.00 37.52           C  
ANISOU 3243  CA  GLU B  51     3237   4673   6346    174   -253    523       C  
ATOM   3244  C   GLU B  51     -67.020 -42.276 -38.054  1.00 36.39           C  
ANISOU 3244  C   GLU B  51     3127   4471   6228    256   -307    582       C  
ATOM   3245  O   GLU B  51     -67.744 -41.590 -38.784  1.00 35.82           O  
ANISOU 3245  O   GLU B  51     2909   4384   6318    307   -402    714       O  
ATOM   3246  CB  GLU B  51     -68.352 -43.102 -36.093  1.00 36.19           C  
ANISOU 3246  CB  GLU B  51     2944   4457   6350    234    -44    473       C  
ATOM   3247  CG  GLU B  51     -69.159 -44.247 -35.455  1.00 38.77           C  
ANISOU 3247  CG  GLU B  51     3193   4847   6692    149     12    454       C  
ATOM   3248  CD  GLU B  51     -69.589 -43.951 -34.014  1.00 44.07           C  
ANISOU 3248  CD  GLU B  51     3806   5488   7449    189    265    368       C  
ATOM   3249  OE1 GLU B  51     -69.097 -42.958 -33.425  1.00 45.96           O  
ANISOU 3249  OE1 GLU B  51     4107   5658   7698    268    402    289       O  
ATOM   3250  OE2 GLU B  51     -70.407 -44.726 -33.468  1.00 44.09           O  
ANISOU 3250  OE2 GLU B  51     3711   5540   7503    127    334    374       O  
ATOM   3251  N   GLU B  52     -65.743 -41.980 -37.834  1.00 29.13           N  
ANISOU 3251  N   GLU B  52     2386   3518   5164    265   -252    502       N  
ATOM   3252  CA  GLU B  52     -65.041 -40.877 -38.473  1.00 35.49           C  
ANISOU 3252  CA  GLU B  52     3247   4264   5975    322   -294    554       C  
ATOM   3253  C   GLU B  52     -64.383 -41.276 -39.795  1.00 34.13           C  
ANISOU 3253  C   GLU B  52     3175   4168   5623    257   -475    623       C  
ATOM   3254  O   GLU B  52     -63.648 -40.470 -40.374  1.00 32.89           O  
ANISOU 3254  O   GLU B  52     3086   3977   5433    285   -508    672       O  
ATOM   3255  CB  GLU B  52     -63.977 -40.323 -37.522  1.00 33.86           C  
ANISOU 3255  CB  GLU B  52     3172   3987   5708    348   -137    426       C  
ATOM   3256  CG  GLU B  52     -64.545 -39.718 -36.245  1.00 46.39           C  
ANISOU 3256  CG  GLU B  52     4683   5491   7452    409     61    336       C  
ATOM   3257  CD  GLU B  52     -63.456 -39.299 -35.263  1.00 54.63           C  
ANISOU 3257  CD  GLU B  52     5877   6490   8390    398    198    191       C  
ATOM   3258  OE1 GLU B  52     -62.265 -39.633 -35.492  1.00 50.51           O  
ANISOU 3258  OE1 GLU B  52     5502   6012   7678    343    137    168       O  
ATOM   3259  OE2 GLU B  52     -63.797 -38.637 -34.257  1.00 60.81           O  
ANISOU 3259  OE2 GLU B  52     6626   7198   9280    440    371     95       O  
ATOM   3260  N   GLY B  53     -64.609 -42.498 -40.272  1.00 29.79           N  
ANISOU 3260  N   GLY B  53     2646   3716   4956    162   -578    620       N  
ATOM   3261  CA  GLY B  53     -64.058 -42.926 -41.543  1.00 32.14           C  
ANISOU 3261  CA  GLY B  53     3046   4094   5073     90   -731    662       C  
ATOM   3262  C   GLY B  53     -62.663 -43.494 -41.475  1.00 29.03           C  
ANISOU 3262  C   GLY B  53     2846   3711   4474     52   -680    552       C  
ATOM   3263  O   GLY B  53     -62.027 -43.673 -42.522  1.00 27.75           O  
ANISOU 3263  O   GLY B  53     2783   3605   4158      5   -770    572       O  
ATOM   3264  N   ILE B  54     -62.159 -43.774 -40.282  1.00 25.97           N  
ANISOU 3264  N   ILE B  54     2510   3280   4076     70   -537    441       N  
ATOM   3265  CA  ILE B  54     -60.885 -44.462 -40.120  1.00 24.90           C  
ANISOU 3265  CA  ILE B  54     2530   3157   3772     37   -494    350       C  
ATOM   3266  C   ILE B  54     -61.206 -45.951 -40.131  1.00 33.14           C  
ANISOU 3266  C   ILE B  54     3597   4239   4754    -42   -527    302       C  
ATOM   3267  O   ILE B  54     -61.850 -46.456 -39.209  1.00 28.49           O  
ANISOU 3267  O   ILE B  54     2950   3635   4239    -54   -465    275       O  
ATOM   3268  CB  ILE B  54     -60.184 -44.041 -38.822  1.00 27.99           C  
ANISOU 3268  CB  ILE B  54     2962   3496   4179     81   -348    275       C  
ATOM   3269  CG1 ILE B  54     -59.934 -42.526 -38.815  1.00 27.69           C  
ANISOU 3269  CG1 ILE B  54     2901   3393   4226    147   -311    309       C  
ATOM   3270  CG2 ILE B  54     -58.897 -44.857 -38.617  1.00 27.24           C  
ANISOU 3270  CG2 ILE B  54     2998   3422   3931     49   -320    205       C  
ATOM   3271  CD1 ILE B  54     -59.314 -42.001 -37.510  1.00 30.67           C  
ANISOU 3271  CD1 ILE B  54     3320   3719   4615    171   -170    216       C  
ATOM   3272  N   CYS B  55     -60.798 -46.658 -41.183  1.00 22.85           N  
ANISOU 3272  N   CYS B  55     2380   2980   3320   -103   -615    287       N  
ATOM   3273  CA  CYS B  55     -61.237 -48.035 -41.332  1.00 25.76           C  
ANISOU 3273  CA  CYS B  55     2768   3363   3656   -189   -656    237       C  
ATOM   3274  C   CYS B  55     -60.214 -49.052 -40.842  1.00 27.62           C  
ANISOU 3274  C   CYS B  55     3124   3558   3811   -199   -573    144       C  
ATOM   3275  O   CYS B  55     -60.405 -50.249 -41.057  1.00 28.48           O  
ANISOU 3275  O   CYS B  55     3274   3654   3896   -270   -598     93       O  
ATOM   3276  CB  CYS B  55     -61.603 -48.325 -42.789  1.00 34.88           C  
ANISOU 3276  CB  CYS B  55     3944   4588   4722   -271   -805    259       C  
ATOM   3277  SG  CYS B  55     -60.399 -47.745 -44.007  1.00 40.61           S  
ANISOU 3277  SG  CYS B  55     4799   5363   5269   -263   -837    268       S  
ATOM   3278  N   GLY B  56     -59.143 -48.624 -40.184  1.00 27.56           N  
ANISOU 3278  N   GLY B  56     3168   3526   3778   -133   -479    125       N  
ATOM   3279  CA  GLY B  56     -58.192 -49.605 -39.705  1.00 20.89           C  
ANISOU 3279  CA  GLY B  56     2413   2645   2881   -135   -415     65       C  
ATOM   3280  C   GLY B  56     -56.932 -48.956 -39.175  1.00 20.50           C  
ANISOU 3280  C   GLY B  56     2404   2591   2794    -70   -343     62       C  
ATOM   3281  O   GLY B  56     -56.867 -47.742 -38.977  1.00 25.15           O  
ANISOU 3281  O   GLY B  56     2957   3192   3408    -32   -327     93       O  
ATOM   3282  N   ILE B  57     -55.932 -49.807 -38.965  1.00 22.33           N  
ANISOU 3282  N   ILE B  57     2705   2798   2983    -63   -302     26       N  
ATOM   3283  CA  ILE B  57     -54.722 -49.469 -38.234  1.00 22.78           C  
ANISOU 3283  CA  ILE B  57     2783   2856   3018    -16   -242     32       C  
ATOM   3284  C   ILE B  57     -53.524 -49.933 -39.043  1.00 24.11           C  
ANISOU 3284  C   ILE B  57     3015   3017   3128      3   -230      2       C  
ATOM   3285  O   ILE B  57     -53.553 -51.005 -39.660  1.00 23.48           O  
ANISOU 3285  O   ILE B  57     2980   2903   3038    -18   -235    -41       O  
ATOM   3286  CB  ILE B  57     -54.678 -50.145 -36.834  1.00 27.30           C  
ANISOU 3286  CB  ILE B  57     3346   3407   3620    -19   -196     48       C  
ATOM   3287  CG1 ILE B  57     -55.794 -49.663 -35.905  1.00 27.82           C  
ANISOU 3287  CG1 ILE B  57     3350   3489   3732    -40   -171     67       C  
ATOM   3288  CG2 ILE B  57     -53.327 -49.933 -36.157  1.00 26.00           C  
ANISOU 3288  CG2 ILE B  57     3200   3260   3420     16   -162     64       C  
ATOM   3289  CD1 ILE B  57     -55.674 -48.235 -35.455  1.00 25.26           C  
ANISOU 3289  CD1 ILE B  57     2998   3193   3407    -14   -139     62       C  
ATOM   3290  N  ASER B  58     -52.469 -49.132 -39.036  0.50 21.78           N  
ANISOU 3290  N  ASER B  58     2720   2750   2804     38   -203     17       N  
ATOM   3291  N  BSER B  58     -52.468 -49.124 -39.039  0.50 21.61           N  
ANISOU 3291  N  BSER B  58     2699   2729   2783     38   -203     17       N  
ATOM   3292  CA ASER B  58     -51.135 -49.600 -39.385  0.50 26.02           C  
ANISOU 3292  CA ASER B  58     3289   3282   3315     69   -161     -1       C  
ATOM   3293  CA BSER B  58     -51.123 -49.569 -39.388  0.50 26.26           C  
ANISOU 3293  CA BSER B  58     3319   3314   3345     70   -161      0       C  
ATOM   3294  C  ASER B  58     -50.303 -49.508 -38.112  0.50 24.66           C  
ANISOU 3294  C  ASER B  58     3080   3116   3175     96   -135     39       C  
ATOM   3295  C  BSER B  58     -50.296 -49.502 -38.109  0.50 24.76           C  
ANISOU 3295  C  BSER B  58     3092   3128   3188     96   -135     39       C  
ATOM   3296  O  ASER B  58     -50.081 -48.409 -37.591  0.50 26.11           O  
ANISOU 3296  O  ASER B  58     3235   3335   3351     91   -138     61       O  
ATOM   3297  O  BSER B  58     -50.050 -48.408 -37.587  0.50 26.34           O  
ANISOU 3297  O  BSER B  58     3264   3364   3380     91   -138     61       O  
ATOM   3298  CB ASER B  58     -50.551 -48.776 -40.528  0.50 27.62           C  
ANISOU 3298  CB ASER B  58     3510   3529   3455     71   -154     -2       C  
ATOM   3299  CB BSER B  58     -50.522 -48.696 -40.488  0.50 27.11           C  
ANISOU 3299  CB BSER B  58     3443   3467   3392     72   -154      1       C  
ATOM   3300  OG ASER B  58     -51.361 -48.941 -41.680  0.50 21.33           O  
ANISOU 3300  OG ASER B  58     2755   2747   2602     30   -195    -28       O  
ATOM   3301  OG BSER B  58     -49.209 -49.116 -40.800  0.50 31.89           O  
ANISOU 3301  OG BSER B  58     4060   4073   3986    106    -92    -17       O  
ATOM   3302  N   SER B  59     -49.906 -50.666 -37.578  1.00 26.82           N  
ANISOU 3302  N   SER B  59     3355   3348   3487    117   -118     51       N  
ATOM   3303  CA  SER B  59     -49.140 -50.691 -36.333  1.00 24.99           C  
ANISOU 3303  CA  SER B  59     3084   3139   3273    131   -118    113       C  
ATOM   3304  C   SER B  59     -47.815 -49.967 -36.531  1.00 24.95           C  
ANISOU 3304  C   SER B  59     3044   3180   3256    155   -106    127       C  
ATOM   3305  O   SER B  59     -47.231 -49.998 -37.618  1.00 23.32           O  
ANISOU 3305  O   SER B  59     2844   2966   3050    182    -70     98       O  
ATOM   3306  CB  SER B  59     -48.881 -52.137 -35.880  1.00 28.00           C  
ANISOU 3306  CB  SER B  59     3465   3454   3717    158   -109    153       C  
ATOM   3307  OG  SER B  59     -50.073 -52.807 -35.488  1.00 27.01           O  
ANISOU 3307  OG  SER B  59     3364   3286   3612    119   -119    157       O  
ATOM   3308  N  AVAL B  60     -47.346 -49.287 -35.479  0.50 25.74           N  
ANISOU 3308  N  AVAL B  60     3107   3336   3337    131   -131    168       N  
ATOM   3309  N  BVAL B  60     -47.341 -49.287 -35.486  0.50 25.70           N  
ANISOU 3309  N  BVAL B  60     3102   3331   3333    132   -131    168       N  
ATOM   3310  CA AVAL B  60     -46.013 -48.692 -35.549  0.50 25.91           C  
ANISOU 3310  CA AVAL B  60     3077   3404   3364    139   -130    192       C  
ATOM   3311  CA BVAL B  60     -46.010 -48.704 -35.621  0.50 25.60           C  
ANISOU 3311  CA BVAL B  60     3040   3363   3326    142   -127    190       C  
ATOM   3312  C  AVAL B  60     -44.946 -49.764 -35.418  0.50 29.73           C  
ANISOU 3312  C  AVAL B  60     3507   3874   3913    195   -123    252       C  
ATOM   3313  C  BVAL B  60     -44.930 -49.750 -35.406  0.50 29.83           C  
ANISOU 3313  C  BVAL B  60     3519   3889   3926    195   -123    253       C  
ATOM   3314  O  AVAL B  60     -43.892 -49.694 -36.062  0.50 28.71           O  
ANISOU 3314  O  AVAL B  60     3328   3756   3824    231    -88    260       O  
ATOM   3315  O  BVAL B  60     -43.843 -49.647 -35.987  0.50 28.06           O  
ANISOU 3315  O  BVAL B  60     3241   3678   3741    229    -92    264       O  
ATOM   3316  CB AVAL B  60     -45.821 -47.619 -34.461  0.50 26.76           C  
ANISOU 3316  CB AVAL B  60     3165   3575   3427     76   -168    203       C  
ATOM   3317  CB BVAL B  60     -45.796 -47.526 -34.657  0.50 28.04           C  
ANISOU 3317  CB BVAL B  60     3328   3734   3591     79   -163    197       C  
ATOM   3318  CG1AVAL B  60     -44.492 -46.889 -34.667  0.50 15.11           C  
ANISOU 3318  CG1AVAL B  60     1629   2145   1966     64   -173    223       C  
ATOM   3319  CG1BVAL B  60     -46.757 -46.439 -34.943  0.50 27.53           C  
ANISOU 3319  CG1BVAL B  60     3304   3651   3504     46   -149    138       C  
ATOM   3320  CG2AVAL B  60     -46.939 -46.667 -34.473  0.50 20.83           C  
ANISOU 3320  CG2AVAL B  60     2459   2809   2647     38   -157    143       C  
ATOM   3321  CG2BVAL B  60     -45.934 -47.983 -33.236  0.50 29.38           C  
ANISOU 3321  CG2BVAL B  60     3494   3940   3728     46   -204    240       C  
ATOM   3322  N   SER B  61     -45.189 -50.755 -34.566  1.00 24.73           N  
ANISOU 3322  N   SER B  61     2873   3215   3306    206   -150    308       N  
ATOM   3323  CA  SER B  61     -44.142 -51.647 -34.111  1.00 28.86           C  
ANISOU 3323  CA  SER B  61     3325   3729   3912    258   -166    404       C  
ATOM   3324  C   SER B  61     -44.660 -53.073 -34.040  1.00 27.85           C  
ANISOU 3324  C   SER B  61     3226   3495   3859    301   -148    434       C  
ATOM   3325  O   SER B  61     -45.867 -53.321 -33.969  1.00 27.74           O  
ANISOU 3325  O   SER B  61     3283   3444   3812    263   -145    397       O  
ATOM   3326  CB  SER B  61     -43.634 -51.222 -32.727  1.00 26.39           C  
ANISOU 3326  CB  SER B  61     2961   3518   3549    203   -253    497       C  
ATOM   3327  OG  SER B  61     -44.660 -51.441 -31.761  1.00 25.16           O  
ANISOU 3327  OG  SER B  61     2865   3375   3321    148   -284    517       O  
ATOM   3328  N   ARG B  62     -43.711 -54.008 -34.026  1.00 25.52           N  
ANISOU 3328  N   ARG B  62     2865   3145   3687    379   -135    510       N  
ATOM   3329  CA  ARG B  62     -44.058 -55.418 -33.931  1.00 27.57           C  
ANISOU 3329  CA  ARG B  62     3148   3274   4054    426   -112    551       C  
ATOM   3330  C   ARG B  62     -44.857 -55.700 -32.661  1.00 34.57           C  
ANISOU 3330  C   ARG B  62     4063   4184   4886    361   -184    647       C  
ATOM   3331  O   ARG B  62     -45.828 -56.467 -32.686  1.00 27.40           O  
ANISOU 3331  O   ARG B  62     3220   3183   4007    343   -162    631       O  
ATOM   3332  CB  ARG B  62     -42.783 -56.254 -33.983  1.00 28.33           C  
ANISOU 3332  CB  ARG B  62     3142   3303   4320    533    -87    641       C  
ATOM   3333  CG  ARG B  62     -42.992 -57.755 -34.051  1.00 42.79           C  
ANISOU 3333  CG  ARG B  62     4994   4954   6310    600    -41    675       C  
ATOM   3334  CD  ARG B  62     -41.672 -58.486 -33.800  1.00 50.83           C  
ANISOU 3334  CD  ARG B  62     5880   5912   7522    716    -33    811       C  
ATOM   3335  NE  ARG B  62     -41.159 -58.175 -32.468  1.00 56.47           N  
ANISOU 3335  NE  ARG B  62     6503   6755   8198    686   -169   1004       N  
ATOM   3336  CZ  ARG B  62     -41.277 -58.965 -31.405  1.00 51.13           C  
ANISOU 3336  CZ  ARG B  62     5808   6047   7574    686   -249   1183       C  
ATOM   3337  NH1 ARG B  62     -41.871 -60.148 -31.509  1.00 56.56           N  
ANISOU 3337  NH1 ARG B  62     6554   6552   8384    723   -199   1198       N  
ATOM   3338  NH2 ARG B  62     -40.787 -58.571 -30.238  1.00 39.90           N  
ANISOU 3338  NH2 ARG B  62     4312   4776   6074    636   -384   1351       N  
ATOM   3339  N   MET B  63     -44.498 -55.048 -31.549  1.00 28.26           N  
ANISOU 3339  N   MET B  63     3224   3518   3996    307   -267    739       N  
ATOM   3340  CA  MET B  63     -45.193 -55.327 -30.294  1.00 30.11           C  
ANISOU 3340  CA  MET B  63     3491   3796   4152    235   -322    835       C  
ATOM   3341  C   MET B  63     -46.602 -54.749 -30.271  1.00 30.38           C  
ANISOU 3341  C   MET B  63     3614   3855   4074    153   -288    725       C  
ATOM   3342  O   MET B  63     -47.474 -55.306 -29.599  1.00 31.64           O  
ANISOU 3342  O   MET B  63     3813   3998   4210    107   -286    777       O  
ATOM   3343  CB  MET B  63     -44.364 -54.816 -29.128  1.00 33.90           C  
ANISOU 3343  CB  MET B  63     3913   4427   4542    186   -422    954       C  
ATOM   3344  CG  MET B  63     -43.058 -55.588 -29.049  1.00 46.83           C  
ANISOU 3344  CG  MET B  63     5435   6033   6325    274   -470   1106       C  
ATOM   3345  SD  MET B  63     -42.343 -55.652 -27.420  1.00 51.31           S  
ANISOU 3345  SD  MET B  63     5935   6758   6802    206   -626   1329       S  
ATOM   3346  CE  MET B  63     -43.792 -56.023 -26.449  1.00 49.59           C  
ANISOU 3346  CE  MET B  63     5844   6557   6439    105   -621   1362       C  
ATOM   3347  N   GLU B  64     -46.858 -53.666 -31.018  1.00 23.26           N  
ANISOU 3347  N   GLU B  64     2732   2985   3121    138   -254    587       N  
ATOM   3348  CA  GLU B  64     -48.226 -53.168 -31.125  1.00 27.00           C  
ANISOU 3348  CA  GLU B  64     3266   3462   3533     81   -218    493       C  
ATOM   3349  C   GLU B  64     -49.115 -54.164 -31.865  1.00 27.59           C  
ANISOU 3349  C   GLU B  64     3376   3413   3695     99   -178    460       C  
ATOM   3350  O   GLU B  64     -50.249 -54.426 -31.450  1.00 27.33           O  
ANISOU 3350  O   GLU B  64     3369   3369   3646     46   -164    463       O  
ATOM   3351  CB  GLU B  64     -48.267 -51.812 -31.833  1.00 23.22           C  
ANISOU 3351  CB  GLU B  64     2790   3024   3008     71   -200    379       C  
ATOM   3352  CG  GLU B  64     -49.702 -51.291 -31.969  1.00 26.35           C  
ANISOU 3352  CG  GLU B  64     3224   3414   3374     28   -165    300       C  
ATOM   3353  CD  GLU B  64     -49.803 -49.978 -32.716  1.00 32.73           C  
ANISOU 3353  CD  GLU B  64     4030   4240   4164     28   -152    213       C  
ATOM   3354  OE1 GLU B  64     -48.778 -49.284 -32.880  1.00 29.84           O  
ANISOU 3354  OE1 GLU B  64     3645   3910   3784     37   -165    209       O  
ATOM   3355  OE2 GLU B  64     -50.921 -49.633 -33.127  1.00 26.59           O  
ANISOU 3355  OE2 GLU B  64     3264   3440   3401     15   -131    162       O  
ATOM   3356  N   ASN B  65     -48.623 -54.727 -32.965  1.00 27.45           N  
ANISOU 3356  N   ASN B  65     3357   3303   3768    164   -152    419       N  
ATOM   3357  CA  ASN B  65     -49.413 -55.722 -33.681  1.00 29.91           C  
ANISOU 3357  CA  ASN B  65     3715   3492   4158    163   -119    368       C  
ATOM   3358  C   ASN B  65     -49.709 -56.940 -32.802  1.00 28.45           C  
ANISOU 3358  C   ASN B  65     3534   3228   4048    149   -126    479       C  
ATOM   3359  O   ASN B  65     -50.831 -57.458 -32.811  1.00 27.78           O  
ANISOU 3359  O   ASN B  65     3482   3086   3986     93   -114    461       O  
ATOM   3360  CB  ASN B  65     -48.687 -56.135 -34.954  1.00 25.29           C  
ANISOU 3360  CB  ASN B  65     3141   2825   3643    229    -73    289       C  
ATOM   3361  CG  ASN B  65     -49.326 -57.334 -35.626  1.00 32.97           C  
ANISOU 3361  CG  ASN B  65     4170   3652   4704    220    -37    226       C  
ATOM   3362  OD1 ASN B  65     -48.949 -58.473 -35.363  1.00 31.54           O  
ANISOU 3362  OD1 ASN B  65     3987   3349   4647    261    -13    282       O  
ATOM   3363  ND2 ASN B  65     -50.307 -57.080 -36.499  1.00 25.90           N  
ANISOU 3363  ND2 ASN B  65     3325   2763   3753    159    -39    113       N  
ATOM   3364  N   ILE B  66     -48.720 -57.404 -32.027  1.00 28.52           N  
ANISOU 3364  N   ILE B  66     3500   3234   4102    194   -152    613       N  
ATOM   3365  CA  ILE B  66     -48.960 -58.503 -31.091  1.00 29.47           C  
ANISOU 3365  CA  ILE B  66     3621   3286   4288    178   -169    759       C  
ATOM   3366  C   ILE B  66     -50.045 -58.121 -30.088  1.00 31.77           C  
ANISOU 3366  C   ILE B  66     3937   3678   4456     72   -182    798       C  
ATOM   3367  O   ILE B  66     -50.923 -58.932 -29.765  1.00 31.51           O  
ANISOU 3367  O   ILE B  66     3930   3573   4468     22   -163    847       O  
ATOM   3368  CB  ILE B  66     -47.646 -58.923 -30.395  1.00 28.80           C  
ANISOU 3368  CB  ILE B  66     3468   3208   4266    245   -217    926       C  
ATOM   3369  CG1 ILE B  66     -46.663 -59.469 -31.435  1.00 29.91           C  
ANISOU 3369  CG1 ILE B  66     3573   3219   4573    362   -169    880       C  
ATOM   3370  CG2 ILE B  66     -47.909 -59.989 -29.321  1.00 28.21           C  
ANISOU 3370  CG2 ILE B  66     3397   3078   4246    219   -249   1116       C  
ATOM   3371  CD1 ILE B  66     -45.262 -59.772 -30.896  1.00 42.11           C  
ANISOU 3371  CD1 ILE B  66     5013   4774   6214    448   -216   1045       C  
ATOM   3372  N  AMET B  67     -50.021 -56.878 -29.600  0.50 27.41           N  
ANISOU 3372  N  AMET B  67     3375   3287   3754     32   -201    767       N  
ATOM   3373  N  BMET B  67     -50.016 -56.878 -29.596  0.50 27.35           N  
ANISOU 3373  N  BMET B  67     3367   3279   3745     32   -201    768       N  
ATOM   3374  CA AMET B  67     -51.062 -56.430 -28.680  0.50 28.43           C  
ANISOU 3374  CA AMET B  67     3527   3512   3764    -64   -183    775       C  
ATOM   3375  CA BMET B  67     -51.057 -56.414 -28.680  0.50 28.49           C  
ANISOU 3375  CA BMET B  67     3535   3521   3770    -64   -183    774       C  
ATOM   3376  C  AMET B  67     -52.445 -56.495 -29.322  0.50 25.98           C  
ANISOU 3376  C  AMET B  67     3235   3140   3497   -101   -128    673       C  
ATOM   3377  C  BMET B  67     -52.440 -56.492 -29.322  0.50 26.03           C  
ANISOU 3377  C  BMET B  67     3241   3147   3503   -101   -128    673       C  
ATOM   3378  O  AMET B  67     -53.393 -57.016 -28.723  0.50 26.73           O  
ANISOU 3378  O  AMET B  67     3337   3224   3594   -167    -97    727       O  
ATOM   3379  O  BMET B  67     -53.382 -57.023 -28.723  0.50 26.74           O  
ANISOU 3379  O  BMET B  67     3338   3224   3596   -167    -98    728       O  
ATOM   3380  CB AMET B  67     -50.773 -55.009 -28.208  0.50 29.51           C  
ANISOU 3380  CB AMET B  67     3659   3803   3752    -96   -194    717       C  
ATOM   3381  CB BMET B  67     -50.757 -54.984 -28.229  0.50 29.32           C  
ANISOU 3381  CB BMET B  67     3633   3779   3727    -95   -194    714       C  
ATOM   3382  CG AMET B  67     -51.749 -54.534 -27.151  0.50 27.23           C  
ANISOU 3382  CG AMET B  67     3395   3616   3335   -192   -150    713       C  
ATOM   3383  CG BMET B  67     -51.721 -54.445 -27.169  0.50 26.77           C  
ANISOU 3383  CG BMET B  67     3337   3563   3272   -191   -150    705       C  
ATOM   3384  SD AMET B  67     -51.666 -52.762 -26.914  0.50 24.30           S  
ANISOU 3384  SD AMET B  67     3032   3369   2832   -226   -128    575       S  
ATOM   3385  SD BMET B  67     -53.201 -53.667 -27.840  0.50 40.53           S  
ANISOU 3385  SD BMET B  67     5076   5282   5042   -210    -65    545       S  
ATOM   3386  CE AMET B  67     -52.383 -52.205 -28.459  0.50 33.93           C  
ANISOU 3386  CE AMET B  67     4231   4489   4171   -167    -87    428       C  
ATOM   3387  CE BMET B  67     -52.526 -52.129 -28.456  0.50 34.26           C  
ANISOU 3387  CE BMET B  67     4273   4533   4212   -171    -79    418       C  
ATOM   3388  N   TRP B  68     -52.586 -55.947 -30.536  1.00 25.59           N  
ANISOU 3388  N   TRP B  68     3184   3061   3478    -68   -119    536       N  
ATOM   3389  CA  TRP B  68     -53.880 -55.997 -31.218  1.00 27.97           C  
ANISOU 3389  CA  TRP B  68     3487   3318   3824   -110    -93    452       C  
ATOM   3390  C   TRP B  68     -54.362 -57.434 -31.387  1.00 28.73           C  
ANISOU 3390  C   TRP B  68     3602   3279   4037   -137    -86    494       C  
ATOM   3391  O   TRP B  68     -55.549 -57.729 -31.193  1.00 29.61           O  
ANISOU 3391  O   TRP B  68     3699   3375   4175   -210    -65    498       O  
ATOM   3392  CB  TRP B  68     -53.805 -55.317 -32.592  1.00 20.26           C  
ANISOU 3392  CB  TRP B  68     2512   2332   2853    -73   -107    326       C  
ATOM   3393  CG  TRP B  68     -53.768 -53.821 -32.580  1.00 24.24           C  
ANISOU 3393  CG  TRP B  68     2994   2942   3274    -65   -106    275       C  
ATOM   3394  CD1 TRP B  68     -52.669 -53.029 -32.775  1.00 27.21           C  
ANISOU 3394  CD1 TRP B  68     3371   3364   3605    -20   -119    257       C  
ATOM   3395  CD2 TRP B  68     -54.874 -52.935 -32.397  1.00 23.98           C  
ANISOU 3395  CD2 TRP B  68     2928   2962   3221   -103    -82    235       C  
ATOM   3396  NE1 TRP B  68     -53.022 -51.709 -32.716  1.00 25.40           N  
ANISOU 3396  NE1 TRP B  68     3124   3202   3327    -33   -108    207       N  
ATOM   3397  CE2 TRP B  68     -54.370 -51.618 -32.486  1.00 26.10           C  
ANISOU 3397  CE2 TRP B  68     3189   3291   3436    -74    -82    191       C  
ATOM   3398  CE3 TRP B  68     -56.243 -53.125 -32.154  1.00 26.53           C  
ANISOU 3398  CE3 TRP B  68     3214   3282   3585   -157    -54    237       C  
ATOM   3399  CZ2 TRP B  68     -55.181 -50.493 -32.332  1.00 22.73           C  
ANISOU 3399  CZ2 TRP B  68     2728   2903   3007    -87    -49    146       C  
ATOM   3400  CZ3 TRP B  68     -57.060 -51.999 -32.019  1.00 23.93           C  
ANISOU 3400  CZ3 TRP B  68     2833   3006   3253   -164    -20    194       C  
ATOM   3401  CH2 TRP B  68     -56.522 -50.702 -32.110  1.00 23.52           C  
ANISOU 3401  CH2 TRP B  68     2783   2996   3158   -123    -16    148       C  
ATOM   3402  N   LYS B  69     -53.455 -58.346 -31.737  1.00 29.15           N  
ANISOU 3402  N   LYS B  69     3677   3220   4178    -80    -96    525       N  
ATOM   3403  CA  LYS B  69     -53.855 -59.736 -31.924  1.00 31.60           C  
ANISOU 3403  CA  LYS B  69     4015   3368   4625   -106    -81    554       C  
ATOM   3404  C   LYS B  69     -54.365 -60.353 -30.627  1.00 30.87           C  
ANISOU 3404  C   LYS B  69     3912   3274   4541   -170    -72    712       C  
ATOM   3405  O   LYS B  69     -55.354 -61.099 -30.633  1.00 29.92           O  
ANISOU 3405  O   LYS B  69     3799   3069   4499   -246    -51    723       O  
ATOM   3406  CB  LYS B  69     -52.687 -60.552 -32.482  1.00 32.22           C  
ANISOU 3406  CB  LYS B  69     4114   3310   4818    -15    -73    555       C  
ATOM   3407  CG  LYS B  69     -53.091 -61.960 -32.928  1.00 45.97           C  
ANISOU 3407  CG  LYS B  69     5899   4843   6725    -41    -43    537       C  
ATOM   3408  CD  LYS B  69     -54.292 -61.863 -33.856  1.00 55.73           C  
ANISOU 3408  CD  LYS B  69     7163   6068   7943   -133    -45    384       C  
ATOM   3409  CE  LYS B  69     -54.659 -63.182 -34.503  1.00 63.94           C  
ANISOU 3409  CE  LYS B  69     8261   6898   9137   -178    -19    317       C  
ATOM   3410  NZ  LYS B  69     -55.712 -62.948 -35.539  1.00 66.19           N  
ANISOU 3410  NZ  LYS B  69     8568   7208   9375   -278    -47    156       N  
ATOM   3411  N   SER B  70     -53.711 -60.057 -29.501  1.00 29.11           N  
ANISOU 3411  N   SER B  70     3674   3155   4232   -155    -89    843       N  
ATOM   3412  CA  SER B  70     -54.116 -60.674 -28.242  1.00 33.86           C  
ANISOU 3412  CA  SER B  70     4276   3774   4814   -224    -80   1015       C  
ATOM   3413  C   SER B  70     -55.394 -60.068 -27.671  1.00 37.61           C  
ANISOU 3413  C   SER B  70     4737   4368   5184   -326    -30    988       C  
ATOM   3414  O   SER B  70     -56.063 -60.721 -26.868  1.00 35.92           O  
ANISOU 3414  O   SER B  70     4526   4145   4978   -406      4   1106       O  
ATOM   3415  CB  SER B  70     -52.994 -60.573 -27.204  1.00 37.55           C  
ANISOU 3415  CB  SER B  70     4734   4335   5197   -192   -131   1174       C  
ATOM   3416  OG  SER B  70     -52.786 -59.223 -26.822  1.00 49.03           O  
ANISOU 3416  OG  SER B  70     6178   5979   6470   -207   -141   1109       O  
ATOM   3417  N   VAL B  71     -55.765 -58.852 -28.069  1.00 26.94           N  
ANISOU 3417  N   VAL B  71     3365   3119   3751   -324    -13    843       N  
ATOM   3418  CA  VAL B  71     -56.961 -58.203 -27.534  1.00 27.66           C  
ANISOU 3418  CA  VAL B  71     3424   3315   3769   -402     54    809       C  
ATOM   3419  C   VAL B  71     -58.117 -58.196 -28.537  1.00 28.00           C  
ANISOU 3419  C   VAL B  71     3424   3295   3921   -429     70    697       C  
ATOM   3420  O   VAL B  71     -59.222 -57.740 -28.206  1.00 31.99           O  
ANISOU 3420  O   VAL B  71     3875   3869   4412   -487    131    673       O  
ATOM   3421  CB  VAL B  71     -56.630 -56.775 -27.044  1.00 30.07           C  
ANISOU 3421  CB  VAL B  71     3728   3780   3918   -386     72    744       C  
ATOM   3422  CG1 VAL B  71     -56.572 -55.784 -28.207  1.00 26.05           C  
ANISOU 3422  CG1 VAL B  71     3197   3262   3439   -323     51    588       C  
ATOM   3423  CG2 VAL B  71     -57.587 -56.324 -25.938  1.00 42.82           C  
ANISOU 3423  CG2 VAL B  71     5326   5513   5430   -471    169    758       C  
ATOM   3424  N   GLU B  72     -57.899 -58.728 -29.740  1.00 30.48           N  
ANISOU 3424  N   GLU B  72     3756   3483   4343   -396     18    631       N  
ATOM   3425  CA  GLU B  72     -58.914 -58.729 -30.794  1.00 23.93           C  
ANISOU 3425  CA  GLU B  72     2888   2607   3596   -436      2    525       C  
ATOM   3426  C   GLU B  72     -60.241 -59.321 -30.325  1.00 28.54           C  
ANISOU 3426  C   GLU B  72     3418   3174   4254   -546     45    580       C  
ATOM   3427  O   GLU B  72     -61.301 -58.703 -30.485  1.00 29.02           O  
ANISOU 3427  O   GLU B  72     3397   3303   4327   -585     63    531       O  
ATOM   3428  CB  GLU B  72     -58.376 -59.527 -31.982  1.00 32.16           C  
ANISOU 3428  CB  GLU B  72     3987   3507   4726   -409    -50    456       C  
ATOM   3429  CG  GLU B  72     -59.329 -59.702 -33.143  1.00 35.93           C  
ANISOU 3429  CG  GLU B  72     4444   3937   5269   -475    -90    345       C  
ATOM   3430  CD  GLU B  72     -58.783 -60.710 -34.132  1.00 46.96           C  
ANISOU 3430  CD  GLU B  72     5922   5177   6743   -470   -116    270       C  
ATOM   3431  OE1 GLU B  72     -58.432 -61.823 -33.685  1.00 55.03           O  
ANISOU 3431  OE1 GLU B  72     6984   6065   7859   -475    -87    341       O  
ATOM   3432  OE2 GLU B  72     -58.671 -60.387 -35.336  1.00 40.63           O  
ANISOU 3432  OE2 GLU B  72     5148   4384   5907   -460   -159    144       O  
ATOM   3433  N   GLY B  73     -60.205 -60.542 -29.776  1.00 26.27           N  
ANISOU 3433  N   GLY B  73     3161   2785   4034   -595     62    693       N  
ATOM   3434  CA  GLY B  73     -61.437 -61.180 -29.337  1.00 30.67           C  
ANISOU 3434  CA  GLY B  73     3664   3317   4674   -713    109    758       C  
ATOM   3435  C   GLY B  73     -62.152 -60.384 -28.258  1.00 31.64           C  
ANISOU 3435  C   GLY B  73     3717   3605   4700   -751    200    807       C  
ATOM   3436  O   GLY B  73     -63.377 -60.231 -28.292  1.00 29.51           O  
ANISOU 3436  O   GLY B  73     3352   3370   4490   -823    243    786       O  
ATOM   3437  N   GLU B  74     -61.393 -59.846 -27.303  1.00 31.34           N  
ANISOU 3437  N   GLU B  74     3722   3673   4513   -706    234    864       N  
ATOM   3438  CA  GLU B  74     -61.988 -59.051 -26.234  1.00 32.42           C  
ANISOU 3438  CA  GLU B  74     3815   3970   4532   -745    342    884       C  
ATOM   3439  C   GLU B  74     -62.633 -57.773 -26.763  1.00 27.92           C  
ANISOU 3439  C   GLU B  74     3163   3476   3969   -707    370    735       C  
ATOM   3440  O   GLU B  74     -63.740 -57.413 -26.342  1.00 28.97           O  
ANISOU 3440  O   GLU B  74     3206   3678   4125   -758    470    726       O  
ATOM   3441  CB  GLU B  74     -60.941 -58.705 -25.180  1.00 31.46           C  
ANISOU 3441  CB  GLU B  74     3773   3954   4227   -719    353    955       C  
ATOM   3442  CG  GLU B  74     -61.583 -58.064 -23.951  1.00 38.71           C  
ANISOU 3442  CG  GLU B  74     4670   5036   5001   -787    486    972       C  
ATOM   3443  CD  GLU B  74     -60.604 -57.850 -22.811  1.00 45.40           C  
ANISOU 3443  CD  GLU B  74     5608   6006   5636   -800    485   1054       C  
ATOM   3444  OE1 GLU B  74     -59.384 -58.072 -23.008  1.00 37.85           O  
ANISOU 3444  OE1 GLU B  74     4710   5013   4660   -740    370   1100       O  
ATOM   3445  OE2 GLU B  74     -61.069 -57.455 -21.720  1.00 50.48           O  
ANISOU 3445  OE2 GLU B  74     6259   6790   6130   -875    602   1071       O  
ATOM   3446  N   LEU B  75     -61.946 -57.054 -27.659  1.00 25.16           N  
ANISOU 3446  N   LEU B  75     2836   3114   3609   -615    291    631       N  
ATOM   3447  CA  LEU B  75     -62.549 -55.865 -28.260  1.00 27.07           C  
ANISOU 3447  CA  LEU B  75     2997   3405   3884   -573    303    514       C  
ATOM   3448  C   LEU B  75     -63.842 -56.210 -28.976  1.00 29.44           C  
ANISOU 3448  C   LEU B  75     3185   3660   4341   -628    287    500       C  
ATOM   3449  O   LEU B  75     -64.831 -55.471 -28.889  1.00 29.86           O  
ANISOU 3449  O   LEU B  75     3122   3773   4449   -632    351    469       O  
ATOM   3450  CB  LEU B  75     -61.586 -55.209 -29.251  1.00 26.64           C  
ANISOU 3450  CB  LEU B  75     2991   3328   3805   -479    207    430       C  
ATOM   3451  CG  LEU B  75     -60.280 -54.642 -28.694  1.00 25.82           C  
ANISOU 3451  CG  LEU B  75     2972   3278   3561   -423    207    428       C  
ATOM   3452  CD1 LEU B  75     -59.497 -54.011 -29.841  1.00 26.23           C  
ANISOU 3452  CD1 LEU B  75     3047   3300   3618   -343    122    347       C  
ATOM   3453  CD2 LEU B  75     -60.570 -53.641 -27.597  1.00 24.06           C  
ANISOU 3453  CD2 LEU B  75     2731   3168   3241   -436    317    402       C  
ATOM   3454  N   ASN B  76     -63.845 -57.315 -29.717  1.00 28.21           N  
ANISOU 3454  N   ASN B  76     3054   3392   4271   -674    201    519       N  
ATOM   3455  CA  ASN B  76     -65.036 -57.666 -30.483  1.00 30.76           C  
ANISOU 3455  CA  ASN B  76     3271   3679   4737   -749    158    498       C  
ATOM   3456  C   ASN B  76     -66.190 -58.038 -29.565  1.00 31.65           C  
ANISOU 3456  C   ASN B  76     3280   3827   4920   -845    267    581       C  
ATOM   3457  O   ASN B  76     -67.347 -57.698 -29.848  1.00 34.69           O  
ANISOU 3457  O   ASN B  76     3517   4251   5412   -882    277    565       O  
ATOM   3458  CB  ASN B  76     -64.698 -58.784 -31.475  1.00 28.77           C  
ANISOU 3458  CB  ASN B  76     3094   3291   4547   -791     47    472       C  
ATOM   3459  CG  ASN B  76     -63.900 -58.257 -32.661  1.00 32.63           C  
ANISOU 3459  CG  ASN B  76     3646   3770   4981   -710    -51    367       C  
ATOM   3460  OD1 ASN B  76     -64.006 -57.077 -33.003  1.00 27.85           O  
ANISOU 3460  OD1 ASN B  76     2990   3253   4339   -649    -67    323       O  
ATOM   3461  ND2 ASN B  76     -63.088 -59.116 -33.278  1.00 27.37           N  
ANISOU 3461  ND2 ASN B  76     3091   2989   4317   -708   -105    332       N  
ATOM   3462  N   ALA B  77     -65.892 -58.729 -28.454  1.00 27.56           N  
ANISOU 3462  N   ALA B  77     2826   3303   4345   -889    348    684       N  
ATOM   3463  CA  ALA B  77     -66.925 -59.063 -27.478  1.00 31.84           C  
ANISOU 3463  CA  ALA B  77     3278   3894   4927   -988    476    775       C  
ATOM   3464  C   ALA B  77     -67.501 -57.810 -26.817  1.00 30.40           C  
ANISOU 3464  C   ALA B  77     3000   3857   4693   -949    610    733       C  
ATOM   3465  O   ALA B  77     -68.714 -57.729 -26.570  1.00 30.46           O  
ANISOU 3465  O   ALA B  77     2859   3910   4804  -1009    704    752       O  
ATOM   3466  CB  ALA B  77     -66.353 -60.017 -26.421  1.00 31.48           C  
ANISOU 3466  CB  ALA B  77     3339   3820   4801  -1042    527    916       C  
ATOM   3467  N   ILE B  78     -66.644 -56.833 -26.514  1.00 27.11           N  
ANISOU 3467  N   ILE B  78     2661   3507   4133   -851    631    671       N  
ATOM   3468  CA  ILE B  78     -67.110 -55.562 -25.959  1.00 28.73           C  
ANISOU 3468  CA  ILE B  78     2792   3823   4301   -804    766    598       C  
ATOM   3469  C   ILE B  78     -67.998 -54.837 -26.963  1.00 32.42           C  
ANISOU 3469  C   ILE B  78     3102   4274   4944   -755    729    524       C  
ATOM   3470  O   ILE B  78     -69.060 -54.312 -26.609  1.00 30.85           O  
ANISOU 3470  O   ILE B  78     2755   4130   4838   -760    856    511       O  
ATOM   3471  CB  ILE B  78     -65.911 -54.686 -25.551  1.00 30.85           C  
ANISOU 3471  CB  ILE B  78     3189   4143   4388   -723    770    534       C  
ATOM   3472  CG1 ILE B  78     -65.125 -55.322 -24.395  1.00 31.96           C  
ANISOU 3472  CG1 ILE B  78     3463   4336   4344   -783    807    630       C  
ATOM   3473  CG2 ILE B  78     -66.366 -53.255 -25.203  1.00 32.84           C  
ANISOU 3473  CG2 ILE B  78     3372   4471   4637   -663    902    421       C  
ATOM   3474  CD1 ILE B  78     -63.670 -54.817 -24.308  1.00 25.43           C  
ANISOU 3474  CD1 ILE B  78     2770   3532   3361   -717    728    594       C  
ATOM   3475  N   LEU B  79     -67.575 -54.791 -28.231  1.00 33.77           N  
ANISOU 3475  N   LEU B  79     3295   4373   5162   -707    557    483       N  
ATOM   3476  CA  LEU B  79     -68.380 -54.135 -29.260  1.00 28.39           C  
ANISOU 3476  CA  LEU B  79     2466   3686   4634   -669    488    442       C  
ATOM   3477  C   LEU B  79     -69.749 -54.794 -29.386  1.00 35.35           C  
ANISOU 3477  C   LEU B  79     3177   4567   5688   -770    498    503       C  
ATOM   3478  O   LEU B  79     -70.781 -54.111 -29.397  1.00 37.10           O  
ANISOU 3478  O   LEU B  79     3216   4835   6047   -748    560    503       O  
ATOM   3479  CB  LEU B  79     -67.630 -54.154 -30.595  1.00 29.41           C  
ANISOU 3479  CB  LEU B  79     2676   3755   4744   -629    298    401       C  
ATOM   3480  CG  LEU B  79     -66.419 -53.217 -30.645  1.00 32.40           C  
ANISOU 3480  CG  LEU B  79     3174   4143   4993   -520    288    338       C  
ATOM   3481  CD1 LEU B  79     -65.513 -53.505 -31.839  1.00 26.76           C  
ANISOU 3481  CD1 LEU B  79     2565   3372   4231   -499    127    309       C  
ATOM   3482  CD2 LEU B  79     -66.857 -51.735 -30.647  1.00 29.24           C  
ANISOU 3482  CD2 LEU B  79     2671   3785   4655   -429    350    292       C  
ATOM   3483  N   GLU B  80     -69.781 -56.130 -29.449  1.00 31.85           N  
ANISOU 3483  N   GLU B  80     2779   4062   5260   -884    444    563       N  
ATOM   3484  CA  GLU B  80     -71.053 -56.836 -29.558  1.00 35.44           C  
ANISOU 3484  CA  GLU B  80     3071   4509   5884  -1005    446    624       C  
ATOM   3485  C   GLU B  80     -71.906 -56.637 -28.312  1.00 38.52           C  
ANISOU 3485  C   GLU B  80     3340   4983   6314  -1037    662    679       C  
ATOM   3486  O   GLU B  80     -73.132 -56.503 -28.405  1.00 39.58           O  
ANISOU 3486  O   GLU B  80     3262   5155   6622  -1079    703    708       O  
ATOM   3487  CB  GLU B  80     -70.813 -58.328 -29.803  1.00 40.76           C  
ANISOU 3487  CB  GLU B  80     3844   5072   6569  -1127    359    669       C  
ATOM   3488  CG  GLU B  80     -72.104 -59.122 -30.028  1.00 40.73           C  
ANISOU 3488  CG  GLU B  80     3676   5046   6752  -1279    337    725       C  
ATOM   3489  CD  GLU B  80     -71.847 -60.581 -30.392  1.00 50.39           C  
ANISOU 3489  CD  GLU B  80     5011   6127   8009  -1405    243    747       C  
ATOM   3490  OE1 GLU B  80     -71.633 -61.404 -29.481  1.00 52.54           O  
ANISOU 3490  OE1 GLU B  80     5357   6346   8258  -1465    341    836       O  
ATOM   3491  OE2 GLU B  80     -71.848 -60.905 -31.598  1.00 49.42           O  
ANISOU 3491  OE2 GLU B  80     4905   5939   7932  -1448     74    675       O  
ATOM   3492  N   GLU B  81     -71.279 -56.634 -27.136  1.00 39.33           N  
ANISOU 3492  N   GLU B  81     3566   5124   6253  -1025    804    699       N  
ATOM   3493  CA  GLU B  81     -72.019 -56.414 -25.896  1.00 40.65           C  
ANISOU 3493  CA  GLU B  81     3643   5388   6414  -1063   1034    738       C  
ATOM   3494  C   GLU B  81     -72.770 -55.090 -25.925  1.00 39.17           C  
ANISOU 3494  C   GLU B  81     3283   5267   6332   -966   1140    658       C  
ATOM   3495  O   GLU B  81     -73.824 -54.955 -25.293  1.00 44.68           O  
ANISOU 3495  O   GLU B  81     3816   6030   7131  -1003   1318    685       O  
ATOM   3496  CB  GLU B  81     -71.042 -56.459 -24.724  1.00 40.79           C  
ANISOU 3496  CB  GLU B  81     3853   5457   6189  -1061   1138    757       C  
ATOM   3497  CG  GLU B  81     -71.648 -56.372 -23.355  1.00 52.37           C  
ANISOU 3497  CG  GLU B  81     5277   7039   7584  -1125   1384    798       C  
ATOM   3498  CD  GLU B  81     -70.577 -56.319 -22.282  1.00 61.29           C  
ANISOU 3498  CD  GLU B  81     6612   8239   8436  -1129   1449    813       C  
ATOM   3499  OE1 GLU B  81     -70.895 -56.630 -21.119  1.00 71.79           O  
ANISOU 3499  OE1 GLU B  81     7959   9664   9655  -1223   1622    887       O  
ATOM   3500  OE2 GLU B  81     -69.414 -55.969 -22.605  1.00 57.48           O  
ANISOU 3500  OE2 GLU B  81     6271   7728   7843  -1048   1323    758       O  
ATOM   3501  N   ASN B  82     -72.249 -54.113 -26.664  1.00 36.70           N  
ANISOU 3501  N   ASN B  82     2998   4931   6014   -839   1042    569       N  
ATOM   3502  CA  ASN B  82     -72.840 -52.790 -26.784  1.00 41.01           C  
ANISOU 3502  CA  ASN B  82     3392   5507   6685   -725   1126    499       C  
ATOM   3503  C   ASN B  82     -73.632 -52.609 -28.074  1.00 45.16           C  
ANISOU 3503  C   ASN B  82     3726   5997   7437   -703    962    529       C  
ATOM   3504  O   ASN B  82     -74.022 -51.482 -28.392  1.00 43.93           O  
ANISOU 3504  O   ASN B  82     3441   5842   7407   -590    986    493       O  
ATOM   3505  CB  ASN B  82     -71.749 -51.722 -26.679  1.00 37.63           C  
ANISOU 3505  CB  ASN B  82     3117   5071   6109   -605   1136    394       C  
ATOM   3506  CG  ASN B  82     -71.280 -51.526 -25.255  1.00 46.73           C  
ANISOU 3506  CG  ASN B  82     4399   6293   7062   -623   1340    347       C  
ATOM   3507  OD1 ASN B  82     -71.868 -50.753 -24.502  1.00 46.37           O  
ANISOU 3507  OD1 ASN B  82     4270   6295   7051   -589   1553    282       O  
ATOM   3508  ND2 ASN B  82     -70.230 -52.244 -24.869  1.00 41.31           N  
ANISOU 3508  ND2 ASN B  82     3915   5616   6166   -681   1279    381       N  
ATOM   3509  N   GLY B  83     -73.886 -53.687 -28.814  1.00 40.94           N  
ANISOU 3509  N   GLY B  83     3168   5427   6960   -814    793    596       N  
ATOM   3510  CA  GLY B  83     -74.679 -53.592 -30.024  1.00 41.12           C  
ANISOU 3510  CA  GLY B  83     3009   5440   7173   -825    616    632       C  
ATOM   3511  C   GLY B  83     -73.999 -52.901 -31.186  1.00 44.29           C  
ANISOU 3511  C   GLY B  83     3485   5812   7532   -731    424    588       C  
ATOM   3512  O   GLY B  83     -74.686 -52.422 -32.089  1.00 49.39           O  
ANISOU 3512  O   GLY B  83     3960   6474   8332   -706    300    626       O  
ATOM   3513  N   VAL B  84     -72.670 -52.834 -31.199  1.00 38.46           N  
ANISOU 3513  N   VAL B  84     2986   5038   6591   -682    391    526       N  
ATOM   3514  CA  VAL B  84     -71.937 -52.151 -32.263  1.00 33.36           C  
ANISOU 3514  CA  VAL B  84     2422   4368   5887   -596    231    488       C  
ATOM   3515  C   VAL B  84     -71.606 -53.155 -33.363  1.00 40.58           C  
ANISOU 3515  C   VAL B  84     3429   5246   6742   -696     18    491       C  
ATOM   3516  O   VAL B  84     -70.873 -54.122 -33.133  1.00 35.18           O  
ANISOU 3516  O   VAL B  84     2914   4514   5937   -758     17    468       O  
ATOM   3517  CB  VAL B  84     -70.662 -51.484 -31.727  1.00 33.61           C  
ANISOU 3517  CB  VAL B  84     2644   4382   5743   -496    315    414       C  
ATOM   3518  CG1 VAL B  84     -69.950 -50.733 -32.843  1.00 33.58           C  
ANISOU 3518  CG1 VAL B  84     2708   4355   5695   -414    162    388       C  
ATOM   3519  CG2 VAL B  84     -70.998 -50.543 -30.572  1.00 36.86           C  
ANISOU 3519  CG2 VAL B  84     2985   4824   6195   -420    543    380       C  
ATOM   3520  N   GLN B  85     -72.136 -52.918 -34.567  1.00 42.11           N  
ANISOU 3520  N   GLN B  85     3517   5462   7022   -712   -161    519       N  
ATOM   3521  CA  GLN B  85     -71.854 -53.765 -35.728  1.00 41.07           C  
ANISOU 3521  CA  GLN B  85     3483   5308   6815   -816   -365    496       C  
ATOM   3522  C   GLN B  85     -70.473 -53.412 -36.281  1.00 37.92           C  
ANISOU 3522  C   GLN B  85     3298   4881   6228   -737   -421    428       C  
ATOM   3523  O   GLN B  85     -70.315 -52.653 -37.240  1.00 37.58           O  
ANISOU 3523  O   GLN B  85     3249   4871   6158   -687   -541    435       O  
ATOM   3524  CB  GLN B  85     -72.938 -53.607 -36.785  1.00 47.73           C  
ANISOU 3524  CB  GLN B  85     4133   6211   7790   -881   -547    558       C  
ATOM   3525  CG  GLN B  85     -74.300 -54.100 -36.335  1.00 61.33           C  
ANISOU 3525  CG  GLN B  85     5627   7964   9713   -982   -509    629       C  
ATOM   3526  CD  GLN B  85     -74.249 -55.510 -35.777  1.00 65.22           C  
ANISOU 3526  CD  GLN B  85     6211   8391  10177  -1124   -449    601       C  
ATOM   3527  OE1 GLN B  85     -73.783 -56.438 -36.441  1.00 74.37           O  
ANISOU 3527  OE1 GLN B  85     7522   9495  11240  -1228   -571    543       O  
ATOM   3528  NE2 GLN B  85     -74.723 -55.678 -34.549  1.00 58.85           N  
ANISOU 3528  NE2 GLN B  85     5318   7586   9458  -1129   -250    643       N  
ATOM   3529  N   LEU B  86     -69.446 -53.983 -35.655  1.00 30.69           N  
ANISOU 3529  N   LEU B  86     2567   3908   5187   -729   -331    377       N  
ATOM   3530  CA  LEU B  86     -68.072 -53.679 -36.024  1.00 28.23           C  
ANISOU 3530  CA  LEU B  86     2443   3571   4714   -651   -356    318       C  
ATOM   3531  C   LEU B  86     -67.193 -54.827 -35.549  1.00 32.06           C  
ANISOU 3531  C   LEU B  86     3096   3979   5108   -693   -306    282       C  
ATOM   3532  O   LEU B  86     -67.365 -55.322 -34.433  1.00 32.22           O  
ANISOU 3532  O   LEU B  86     3106   3980   5157   -720   -186    319       O  
ATOM   3533  CB  LEU B  86     -67.606 -52.352 -35.412  1.00 26.24           C  
ANISOU 3533  CB  LEU B  86     2187   3346   4436   -512   -248    317       C  
ATOM   3534  CG  LEU B  86     -66.236 -51.831 -35.872  1.00 26.96           C  
ANISOU 3534  CG  LEU B  86     2439   3423   4382   -432   -281    268       C  
ATOM   3535  CD1 LEU B  86     -66.281 -51.499 -37.354  1.00 29.89           C  
ANISOU 3535  CD1 LEU B  86     2804   3819   4734   -440   -449    274       C  
ATOM   3536  CD2 LEU B  86     -65.813 -50.616 -35.055  1.00 30.77           C  
ANISOU 3536  CD2 LEU B  86     2921   3916   4852   -321   -157    258       C  
ATOM   3537  N   THR B  87     -66.281 -55.265 -36.413  1.00 30.41           N  
ANISOU 3537  N   THR B  87     3034   3724   4798   -699   -393    220       N  
ATOM   3538  CA  THR B  87     -65.413 -56.403 -36.132  1.00 28.59           C  
ANISOU 3538  CA  THR B  87     2953   3396   4515   -727   -356    190       C  
ATOM   3539  C   THR B  87     -63.973 -55.962 -36.342  1.00 32.19           C  
ANISOU 3539  C   THR B  87     3544   3844   4842   -620   -344    146       C  
ATOM   3540  O   THR B  87     -63.606 -55.551 -37.448  1.00 30.54           O  
ANISOU 3540  O   THR B  87     3377   3658   4567   -599   -430     93       O  
ATOM   3541  CB  THR B  87     -65.740 -57.596 -37.040  1.00 29.86           C  
ANISOU 3541  CB  THR B  87     3155   3480   4711   -855   -457    136       C  
ATOM   3542  OG1 THR B  87     -67.126 -57.957 -36.910  1.00 32.45           O  
ANISOU 3542  OG1 THR B  87     3335   3824   5171   -971   -484    182       O  
ATOM   3543  CG2 THR B  87     -64.832 -58.805 -36.713  1.00 25.71           C  
ANISOU 3543  CG2 THR B  87     2778   2818   4173   -868   -401    110       C  
ATOM   3544  N   VAL B  88     -63.164 -56.028 -35.282  1.00 27.44           N  
ANISOU 3544  N   VAL B  88     3004   3223   4200   -561   -242    179       N  
ATOM   3545  CA  VAL B  88     -61.727 -55.822 -35.421  1.00 26.43           C  
ANISOU 3545  CA  VAL B  88     2993   3079   3971   -474   -234    147       C  
ATOM   3546  C   VAL B  88     -61.120 -57.070 -36.043  1.00 25.36           C  
ANISOU 3546  C   VAL B  88     2965   2830   3842   -507   -266    100       C  
ATOM   3547  O   VAL B  88     -61.367 -58.191 -35.582  1.00 28.25           O  
ANISOU 3547  O   VAL B  88     3346   3107   4282   -569   -239    132       O  
ATOM   3548  CB  VAL B  88     -61.083 -55.518 -34.058  1.00 31.87           C  
ANISOU 3548  CB  VAL B  88     3701   3797   4611   -417   -134    206       C  
ATOM   3549  CG1 VAL B  88     -59.584 -55.318 -34.221  1.00 29.05           C  
ANISOU 3549  CG1 VAL B  88     3440   3429   4168   -334   -140    185       C  
ATOM   3550  CG2 VAL B  88     -61.714 -54.281 -33.427  1.00 29.08           C  
ANISOU 3550  CG2 VAL B  88     3253   3539   4256   -389    -77    221       C  
ATOM   3551  N   VAL B  89     -60.334 -56.890 -37.099  1.00 29.06           N  
ANISOU 3551  N   VAL B  89     3508   3293   4241   -469   -310     23       N  
ATOM   3552  CA  VAL B  89     -59.724 -58.007 -37.817  1.00 29.84           C  
ANISOU 3552  CA  VAL B  89     3713   3276   4348   -492   -318    -54       C  
ATOM   3553  C   VAL B  89     -58.226 -57.729 -37.889  1.00 29.38           C  
ANISOU 3553  C   VAL B  89     3727   3212   4223   -380   -272    -70       C  
ATOM   3554  O   VAL B  89     -57.798 -56.806 -38.597  1.00 29.86           O  
ANISOU 3554  O   VAL B  89     3799   3354   4194   -337   -295   -107       O  
ATOM   3555  CB  VAL B  89     -60.328 -58.187 -39.220  1.00 31.94           C  
ANISOU 3555  CB  VAL B  89     4002   3549   4584   -583   -411   -157       C  
ATOM   3556  CG1 VAL B  89     -59.675 -59.354 -39.937  1.00 24.28           C  
ANISOU 3556  CG1 VAL B  89     3159   2447   3621   -612   -392   -269       C  
ATOM   3557  CG2 VAL B  89     -61.844 -58.414 -39.126  1.00 32.59           C  
ANISOU 3557  CG2 VAL B  89     3981   3651   4750   -703   -473   -127       C  
ATOM   3558  N   VAL B  90     -57.428 -58.513 -37.159  1.00 26.10           N  
ANISOU 3558  N   VAL B  90     3350   2704   3862   -335   -209    -24       N  
ATOM   3559  CA  VAL B  90     -55.988 -58.276 -37.042  1.00 27.74           C  
ANISOU 3559  CA  VAL B  90     3593   2913   4035   -227   -167    -11       C  
ATOM   3560  C   VAL B  90     -55.236 -59.267 -37.924  1.00 31.93           C  
ANISOU 3560  C   VAL B  90     4207   3313   4612   -206   -134   -103       C  
ATOM   3561  O   VAL B  90     -55.366 -60.486 -37.762  1.00 33.26           O  
ANISOU 3561  O   VAL B  90     4409   3334   4894   -235   -108   -103       O  
ATOM   3562  CB  VAL B  90     -55.512 -58.375 -35.579  1.00 30.87           C  
ANISOU 3562  CB  VAL B  90     3956   3314   4457   -182   -129    125       C  
ATOM   3563  CG1 VAL B  90     -54.017 -58.015 -35.483  1.00 21.61           C  
ANISOU 3563  CG1 VAL B  90     2794   2165   3252    -78   -107    148       C  
ATOM   3564  CG2 VAL B  90     -56.323 -57.462 -34.686  1.00 26.15           C  
ANISOU 3564  CG2 VAL B  90     3290   2839   3808   -215   -133    187       C  
ATOM   3565  N   GLY B  91     -54.424 -58.747 -38.843  1.00 29.78           N  
ANISOU 3565  N   GLY B  91     3970   3085   4262   -154   -120   -182       N  
ATOM   3566  CA  GLY B  91     -53.592 -59.563 -39.692  1.00 28.22           C  
ANISOU 3566  CA  GLY B  91     3849   2774   4098   -121    -57   -286       C  
ATOM   3567  C   GLY B  91     -52.123 -59.473 -39.319  1.00 32.09           C  
ANISOU 3567  C   GLY B  91     4315   3251   4624      7     12   -231       C  
ATOM   3568  O   GLY B  91     -51.741 -58.889 -38.304  1.00 31.32           O  
ANISOU 3568  O   GLY B  91     4149   3227   4524     56     -5   -104       O  
ATOM   3569  N   SER B  92     -51.297 -60.084 -40.163  1.00 32.03           N  
ANISOU 3569  N   SER B  92     4364   3151   4655     54     93   -335       N  
ATOM   3570  CA  SER B  92     -49.855 -60.074 -39.952  1.00 37.50           C  
ANISOU 3570  CA  SER B  92     5014   3825   5410    180    168   -288       C  
ATOM   3571  C   SER B  92     -49.260 -58.715 -40.312  1.00 35.31           C  
ANISOU 3571  C   SER B  92     4700   3721   4996    208    161   -282       C  
ATOM   3572  O   SER B  92     -49.820 -57.953 -41.107  1.00 35.32           O  
ANISOU 3572  O   SER B  92     4738   3825   4856    140    124   -351       O  
ATOM   3573  CB  SER B  92     -49.181 -61.154 -40.798  1.00 39.01           C  
ANISOU 3573  CB  SER B  92     5267   3851   5704    228    287   -417       C  
ATOM   3574  OG  SER B  92     -49.697 -62.434 -40.498  1.00 49.90           O  
ANISOU 3574  OG  SER B  92     6686   5039   7235    199    301   -426       O  
ATOM   3575  N   VAL B  93     -48.102 -58.418 -39.722  1.00 35.95           N  
ANISOU 3575  N   VAL B  93     4700   3831   5128    303    188   -185       N  
ATOM   3576  CA  VAL B  93     -47.348 -57.232 -40.112  1.00 37.48           C  
ANISOU 3576  CA  VAL B  93     4855   4163   5221    329    200   -183       C  
ATOM   3577  C   VAL B  93     -46.555 -57.534 -41.368  1.00 35.36           C  
ANISOU 3577  C   VAL B  93     4627   3858   4949    369    319   -309       C  
ATOM   3578  O   VAL B  93     -46.010 -58.630 -41.538  1.00 39.69           O  
ANISOU 3578  O   VAL B  93     5183   4265   5631    434    412   -355       O  
ATOM   3579  CB  VAL B  93     -46.408 -56.750 -38.993  1.00 49.28           C  
ANISOU 3579  CB  VAL B  93     6239   5719   6767    393    172    -33       C  
ATOM   3580  CG1 VAL B  93     -47.189 -56.084 -37.923  1.00 50.71           C  
ANISOU 3580  CG1 VAL B  93     6399   5983   6884    331     70     57       C  
ATOM   3581  CG2 VAL B  93     -45.592 -57.895 -38.435  1.00 58.18           C  
ANISOU 3581  CG2 VAL B  93     7313   6720   8074    484    215     41       C  
ATOM   3582  N   LYS B  94     -46.498 -56.552 -42.251  1.00 40.73           N  
ANISOU 3582  N   LYS B  94     5333   4662   5480    330    325   -362       N  
ATOM   3583  CA  LYS B  94     -45.600 -56.550 -43.389  1.00 50.14           C  
ANISOU 3583  CA  LYS B  94     6551   5869   6631    362    451   -462       C  
ATOM   3584  C   LYS B  94     -44.558 -55.458 -43.176  1.00 50.82           C  
ANISOU 3584  C   LYS B  94     6536   6073   6703    408    464   -364       C  
ATOM   3585  O   LYS B  94     -44.863 -54.392 -42.626  1.00 42.04           O  
ANISOU 3585  O   LYS B  94     5385   5059   5529    369    362   -270       O  
ATOM   3586  CB  LYS B  94     -46.374 -56.319 -44.690  1.00 52.01           C  
ANISOU 3586  CB  LYS B  94     6911   6168   6683    257    447   -592       C  
ATOM   3587  CG  LYS B  94     -45.483 -56.168 -45.909  1.00 67.88           C  
ANISOU 3587  CG  LYS B  94     8961   8229   8600    269    585   -692       C  
ATOM   3588  CD  LYS B  94     -46.180 -56.593 -47.188  1.00 70.41           C  
ANISOU 3588  CD  LYS B  94     9434   8559   8761    164    609   -862       C  
ATOM   3589  CE  LYS B  94     -45.193 -56.609 -48.342  1.00 75.28           C  
ANISOU 3589  CE  LYS B  94    10099   9219   9285    179    785   -978       C  
ATOM   3590  NZ  LYS B  94     -45.864 -56.780 -49.665  1.00 78.84           N  
ANISOU 3590  NZ  LYS B  94    10712   9732   9509     46    792  -1136       N  
ATOM   3591  N   ASN B  95     -43.326 -55.740 -43.580  1.00 44.40           N  
ANISOU 3591  N   ASN B  95     5671   5236   5963    489    597   -391       N  
ATOM   3592  CA  ASN B  95     -42.242 -54.778 -43.466  1.00 38.14           C  
ANISOU 3592  CA  ASN B  95     4768   4551   5173    523    621   -303       C  
ATOM   3593  C   ASN B  95     -41.982 -54.112 -44.820  1.00 32.91           C  
ANISOU 3593  C   ASN B  95     4164   3987   4354    475    713   -387       C  
ATOM   3594  O   ASN B  95     -42.090 -54.763 -45.859  1.00 34.81           O  
ANISOU 3594  O   ASN B  95     4504   4189   4534    463    822   -530       O  
ATOM   3595  CB  ASN B  95     -40.973 -55.465 -42.945  1.00 37.58           C  
ANISOU 3595  CB  ASN B  95     4563   4405   5310    646    704   -242       C  
ATOM   3596  CG  ASN B  95     -41.048 -55.782 -41.452  1.00 42.43           C  
ANISOU 3596  CG  ASN B  95     5095   4976   6052    679    580    -95       C  
ATOM   3597  OD1 ASN B  95     -41.682 -55.056 -40.688  1.00 39.34           O  
ANISOU 3597  OD1 ASN B  95     4709   4660   5577    609    445    -19       O  
ATOM   3598  ND2 ASN B  95     -40.373 -56.854 -41.031  1.00 44.48           N  
ANISOU 3598  ND2 ASN B  95     5274   5113   6513    785    634    -48       N  
ATOM   3599  N   PRO B  96     -41.651 -52.810 -44.816  1.00 28.91           N  
ANISOU 3599  N   PRO B  96     3605   3607   3772    437    674   -300       N  
ATOM   3600  CA  PRO B  96     -41.636 -51.888 -43.672  1.00 31.52           C  
ANISOU 3600  CA  PRO B  96     3846   3989   4140    422    544   -161       C  
ATOM   3601  C   PRO B  96     -43.030 -51.567 -43.167  1.00 30.90           C  
ANISOU 3601  C   PRO B  96     3838   3911   3993    354    400   -143       C  
ATOM   3602  O   PRO B  96     -43.986 -51.645 -43.932  1.00 25.95           O  
ANISOU 3602  O   PRO B  96     3317   3286   3256    297    383   -215       O  
ATOM   3603  CB  PRO B  96     -40.980 -50.621 -44.237  1.00 28.44           C  
ANISOU 3603  CB  PRO B  96     3418   3715   3671    380    577   -116       C  
ATOM   3604  CG  PRO B  96     -40.225 -51.087 -45.457  1.00 31.24           C  
ANISOU 3604  CG  PRO B  96     3792   4079   3997    409    756   -206       C  
ATOM   3605  CD  PRO B  96     -41.070 -52.191 -46.024  1.00 33.67           C  
ANISOU 3605  CD  PRO B  96     4232   4306   4254    405    786   -342       C  
ATOM   3606  N   MET B  97     -43.139 -51.204 -41.890  1.00 25.63           N  
ANISOU 3606  N   MET B  97     3104   3248   3386    353    301    -49       N  
ATOM   3607  CA  MET B  97     -44.424 -50.855 -41.280  1.00 26.49           C  
ANISOU 3607  CA  MET B  97     3260   3358   3449    296    187    -31       C  
ATOM   3608  C   MET B  97     -44.741 -49.390 -41.572  1.00 28.78           C  
ANISOU 3608  C   MET B  97     3559   3727   3648    233    143     -2       C  
ATOM   3609  O   MET B  97     -44.534 -48.490 -40.753  1.00 22.62           O  
ANISOU 3609  O   MET B  97     2725   2980   2889    214     94     60       O  
ATOM   3610  CB  MET B  97     -44.386 -51.155 -39.786  1.00 25.64           C  
ANISOU 3610  CB  MET B  97     3089   3226   3427    315    122     47       C  
ATOM   3611  CG  MET B  97     -44.047 -52.619 -39.533  1.00 25.94           C  
ANISOU 3611  CG  MET B  97     3111   3166   3578    384    163     48       C  
ATOM   3612  SD  MET B  97     -43.968 -53.029 -37.768  1.00 31.61           S  
ANISOU 3612  SD  MET B  97     3759   3874   4378    397     73    179       S  
ATOM   3613  CE  MET B  97     -45.692 -53.009 -37.352  1.00 35.82           C  
ANISOU 3613  CE  MET B  97     4382   4393   4836    319      8    153       C  
ATOM   3614  N   TRP B  98     -45.290 -49.167 -42.769  1.00 27.22           N  
ANISOU 3614  N   TRP B  98     3440   3555   3349    194    156    -49       N  
ATOM   3615  CA  TRP B  98     -45.475 -47.829 -43.310  1.00 27.27           C  
ANISOU 3615  CA  TRP B  98     3456   3625   3279    142    127     -2       C  
ATOM   3616  C   TRP B  98     -46.463 -47.008 -42.485  1.00 24.69           C  
ANISOU 3616  C   TRP B  98     3115   3287   2980    114     27     47       C  
ATOM   3617  O   TRP B  98     -47.461 -47.524 -41.974  1.00 27.63           O  
ANISOU 3617  O   TRP B  98     3503   3622   3374    111    -24     26       O  
ATOM   3618  CB  TRP B  98     -45.992 -47.906 -44.749  1.00 25.19           C  
ANISOU 3618  CB  TRP B  98     3285   3401   2884     97    140    -45       C  
ATOM   3619  CG  TRP B  98     -45.163 -48.687 -45.728  1.00 25.81           C  
ANISOU 3619  CG  TRP B  98     3403   3496   2906    111    263   -125       C  
ATOM   3620  CD1 TRP B  98     -45.521 -49.857 -46.350  1.00 29.30           C  
ANISOU 3620  CD1 TRP B  98     3928   3905   3300    104    303   -239       C  
ATOM   3621  CD2 TRP B  98     -43.859 -48.349 -46.230  1.00 27.59           C  
ANISOU 3621  CD2 TRP B  98     3591   3772   3122    129    380   -110       C  
ATOM   3622  NE1 TRP B  98     -44.517 -50.268 -47.194  1.00 32.33           N  
ANISOU 3622  NE1 TRP B  98     4333   4309   3641    123    449   -309       N  
ATOM   3623  CE2 TRP B  98     -43.489 -49.362 -47.147  1.00 30.88           C  
ANISOU 3623  CE2 TRP B  98     4069   4184   3481    142    502   -225       C  
ATOM   3624  CE3 TRP B  98     -42.962 -47.303 -45.983  1.00 28.13           C  
ANISOU 3624  CE3 TRP B  98     3573   3882   3232    128    401    -18       C  
ATOM   3625  CZ2 TRP B  98     -42.265 -49.351 -47.827  1.00 31.08           C  
ANISOU 3625  CZ2 TRP B  98     4066   4254   3490    164    658   -246       C  
ATOM   3626  CZ3 TRP B  98     -41.745 -47.290 -46.665  1.00 35.07           C  
ANISOU 3626  CZ3 TRP B  98     4415   4810   4098    141    540    -24       C  
ATOM   3627  CH2 TRP B  98     -41.408 -48.311 -47.568  1.00 34.02           C  
ANISOU 3627  CH2 TRP B  98     4338   4679   3909    164    674   -136       C  
ATOM   3628  N   ARG B  99     -46.189 -45.705 -42.395  1.00 25.57           N  
ANISOU 3628  N   ARG B  99     3195   3422   3098     89     13    107       N  
ATOM   3629  CA  ARG B  99     -47.072 -44.775 -41.694  1.00 29.79           C  
ANISOU 3629  CA  ARG B  99     3715   3929   3674     68    -54    140       C  
ATOM   3630  C   ARG B  99     -48.456 -44.728 -42.321  1.00 29.20           C  
ANISOU 3630  C   ARG B  99     3681   3847   3565     50   -113    147       C  
ATOM   3631  O   ARG B  99     -48.609 -44.814 -43.540  1.00 32.53           O  
ANISOU 3631  O   ARG B  99     4150   4309   3901     28   -119    157       O  
ATOM   3632  CB  ARG B  99     -46.522 -43.350 -41.737  1.00 32.15           C  
ANISOU 3632  CB  ARG B  99     3986   4231   3999     38    -47    198       C  
ATOM   3633  CG  ARG B  99     -45.126 -43.182 -41.273  1.00 40.50           C  
ANISOU 3633  CG  ARG B  99     4986   5309   5091     33     -3    206       C  
ATOM   3634  CD  ARG B  99     -44.744 -41.709 -41.329  1.00 36.88           C  
ANISOU 3634  CD  ARG B  99     4507   4834   4670    -16     -2    259       C  
ATOM   3635  NE  ARG B  99     -43.323 -41.541 -41.072  1.00 50.55           N  
ANISOU 3635  NE  ARG B  99     6171   6600   6435    -38     37    274       N  
ATOM   3636  CZ  ARG B  99     -42.712 -40.365 -41.027  1.00 64.98           C  
ANISOU 3636  CZ  ARG B  99     7966   8413   8310    -97     45    315       C  
ATOM   3637  NH1 ARG B  99     -43.401 -39.251 -41.221  1.00 63.83           N  
ANISOU 3637  NH1 ARG B  99     7857   8201   8193   -128     23    346       N  
ATOM   3638  NH2 ARG B  99     -41.410 -40.303 -40.790  1.00 69.33           N  
ANISOU 3638  NH2 ARG B  99     8437   9007   8898   -126     73    333       N  
ATOM   3639  N   GLY B 100     -49.459 -44.524 -41.474  1.00 24.66           N  
ANISOU 3639  N   GLY B 100     3082   3233   3054     53   -158    147       N  
ATOM   3640  CA  GLY B 100     -50.747 -44.029 -41.907  1.00 26.52           C  
ANISOU 3640  CA  GLY B 100     3314   3459   3305     40   -220    186       C  
ATOM   3641  C   GLY B 100     -50.950 -42.613 -41.391  1.00 24.23           C  
ANISOU 3641  C   GLY B 100     2981   3119   3106     47   -221    233       C  
ATOM   3642  O   GLY B 100     -50.323 -42.193 -40.416  1.00 22.54           O  
ANISOU 3642  O   GLY B 100     2749   2878   2936     48   -179    205       O  
ATOM   3643  N   PRO B 101     -51.826 -41.841 -42.038  1.00 21.21           N  
ANISOU 3643  N   PRO B 101     2581   2720   2759     46   -273    306       N  
ATOM   3644  CA  PRO B 101     -51.976 -40.427 -41.670  1.00 26.42           C  
ANISOU 3644  CA  PRO B 101     3202   3302   3535     61   -261    354       C  
ATOM   3645  C   PRO B 101     -53.056 -40.136 -40.642  1.00 28.51           C  
ANISOU 3645  C   PRO B 101     3410   3497   3925     92   -248    321       C  
ATOM   3646  O   PRO B 101     -53.112 -39.003 -40.143  1.00 24.99           O  
ANISOU 3646  O   PRO B 101     2939   2965   3592    107   -209    326       O  
ATOM   3647  CB  PRO B 101     -52.337 -39.771 -43.013  1.00 25.42           C  
ANISOU 3647  CB  PRO B 101     3077   3189   3393     51   -325    480       C  
ATOM   3648  CG  PRO B 101     -53.104 -40.856 -43.741  1.00 22.78           C  
ANISOU 3648  CG  PRO B 101     2757   2936   2964     33   -398    480       C  
ATOM   3649  CD  PRO B 101     -52.482 -42.163 -43.320  1.00 21.37           C  
ANISOU 3649  CD  PRO B 101     2622   2795   2702     23   -348    361       C  
ATOM   3650  N   GLN B 102     -53.926 -41.091 -40.339  1.00 24.87           N  
ANISOU 3650  N   GLN B 102     2927   3064   3458     98   -267    285       N  
ATOM   3651  CA  GLN B 102     -55.010 -40.862 -39.397  1.00 25.56           C  
ANISOU 3651  CA  GLN B 102     2951   3099   3664    126   -236    256       C  
ATOM   3652  C   GLN B 102     -54.542 -41.178 -37.971  1.00 23.64           C  
ANISOU 3652  C   GLN B 102     2730   2852   3399    112   -153    152       C  
ATOM   3653  O   GLN B 102     -53.469 -41.743 -37.756  1.00 23.52           O  
ANISOU 3653  O   GLN B 102     2768   2882   3287     86   -144    119       O  
ATOM   3654  CB  GLN B 102     -56.232 -41.706 -39.785  1.00 21.39           C  
ANISOU 3654  CB  GLN B 102     2372   2608   3146    123   -299    284       C  
ATOM   3655  CG  GLN B 102     -56.585 -41.638 -41.306  1.00 21.41           C  
ANISOU 3655  CG  GLN B 102     2369   2655   3110    107   -413    389       C  
ATOM   3656  CD  GLN B 102     -56.973 -40.248 -41.779  1.00 28.76           C  
ANISOU 3656  CD  GLN B 102     3241   3526   4160    146   -443    503       C  
ATOM   3657  OE1 GLN B 102     -57.369 -39.392 -40.982  1.00 27.39           O  
ANISOU 3657  OE1 GLN B 102     3007   3258   4143    196   -377    494       O  
ATOM   3658  NE2 GLN B 102     -56.880 -40.016 -43.098  1.00 30.39           N  
ANISOU 3658  NE2 GLN B 102     3469   3784   4294    120   -538    614       N  
ATOM   3659  N   ARG B 103     -55.362 -40.798 -36.990  1.00 24.21           N  
ANISOU 3659  N   ARG B 103     2757   2877   3563    129    -89    106       N  
ATOM   3660  CA  ARG B 103     -55.051 -41.023 -35.579  1.00 22.06           C  
ANISOU 3660  CA  ARG B 103     2514   2620   3248    101    -10     11       C  
ATOM   3661  C   ARG B 103     -56.328 -41.438 -34.852  1.00 23.65           C  
ANISOU 3661  C   ARG B 103     2660   2823   3505    110     42    -17       C  
ATOM   3662  O   ARG B 103     -57.396 -40.865 -35.094  1.00 24.43           O  
ANISOU 3662  O   ARG B 103     2678   2866   3738    153     59      9       O  
ATOM   3663  CB  ARG B 103     -54.469 -39.751 -34.905  1.00 23.67           C  
ANISOU 3663  CB  ARG B 103     2744   2759   3492     87     59    -54       C  
ATOM   3664  CG  ARG B 103     -53.095 -39.259 -35.425  1.00 24.82           C  
ANISOU 3664  CG  ARG B 103     2935   2903   3591     58     22    -31       C  
ATOM   3665  CD  ARG B 103     -51.985 -40.297 -35.200  1.00 25.39           C  
ANISOU 3665  CD  ARG B 103     3048   3076   3523     18    -12    -36       C  
ATOM   3666  NE  ARG B 103     -50.641 -39.812 -35.547  1.00 25.10           N  
ANISOU 3666  NE  ARG B 103     3032   3047   3458    -15    -32    -19       N  
ATOM   3667  CZ  ARG B 103     -50.118 -39.867 -36.774  1.00 27.62           C  
ANISOU 3667  CZ  ARG B 103     3350   3381   3764     -1    -70     58       C  
ATOM   3668  NH1 ARG B 103     -50.829 -40.363 -37.784  1.00 25.22           N  
ANISOU 3668  NH1 ARG B 103     3037   3088   3456     37   -107    116       N  
ATOM   3669  NH2 ARG B 103     -48.891 -39.419 -37.001  1.00 23.78           N  
ANISOU 3669  NH2 ARG B 103     2868   2906   3261    -37    -71     74       N  
ATOM   3670  N   LEU B 104     -56.220 -42.417 -33.949  1.00 22.82           N  
ANISOU 3670  N   LEU B 104     2584   2780   3307     71     71    -56       N  
ATOM   3671  CA  LEU B 104     -57.370 -42.765 -33.119  1.00 23.62           C  
ANISOU 3671  CA  LEU B 104     2633   2889   3451     65    145    -82       C  
ATOM   3672  C   LEU B 104     -57.784 -41.570 -32.262  1.00 26.59           C  
ANISOU 3672  C   LEU B 104     2989   3209   3906     80    267   -166       C  
ATOM   3673  O   LEU B 104     -56.925 -40.849 -31.737  1.00 25.73           O  
ANISOU 3673  O   LEU B 104     2945   3083   3746     54    304   -235       O  
ATOM   3674  CB  LEU B 104     -57.063 -43.955 -32.206  1.00 25.04           C  
ANISOU 3674  CB  LEU B 104     2862   3145   3506      9    160    -92       C  
ATOM   3675  CG  LEU B 104     -56.908 -45.334 -32.859  1.00 26.54           C  
ANISOU 3675  CG  LEU B 104     3066   3364   3654     -4     71    -25       C  
ATOM   3676  CD1 LEU B 104     -56.549 -46.383 -31.817  1.00 28.15           C  
ANISOU 3676  CD1 LEU B 104     3316   3621   3760    -53     94    -15       C  
ATOM   3677  CD2 LEU B 104     -58.183 -45.733 -33.565  1.00 18.74           C  
ANISOU 3677  CD2 LEU B 104     1997   2357   2766      6     41     15       C  
ATOM   3678  N   PRO B 105     -59.079 -41.324 -32.114  1.00 26.13           N  
ANISOU 3678  N   PRO B 105     2834   3112   3981    118    338   -169       N  
ATOM   3679  CA  PRO B 105     -59.540 -40.284 -31.195  1.00 30.83           C  
ANISOU 3679  CA  PRO B 105     3409   3643   4661    137    491   -272       C  
ATOM   3680  C   PRO B 105     -59.507 -40.781 -29.757  1.00 31.15           C  
ANISOU 3680  C   PRO B 105     3508   3764   4561     64    603   -365       C  
ATOM   3681  O   PRO B 105     -59.623 -41.979 -29.488  1.00 28.10           O  
ANISOU 3681  O   PRO B 105     3131   3470   4077     19    573   -317       O  
ATOM   3682  CB  PRO B 105     -60.979 -40.037 -31.658  1.00 29.41           C  
ANISOU 3682  CB  PRO B 105     3077   3406   4692    211    520   -217       C  
ATOM   3683  CG  PRO B 105     -61.435 -41.416 -32.096  1.00 28.58           C  
ANISOU 3683  CG  PRO B 105     2930   3391   4536    179    423   -125       C  
ATOM   3684  CD  PRO B 105     -60.199 -42.085 -32.707  1.00 22.68           C  
ANISOU 3684  CD  PRO B 105     2295   2695   3625    135    288    -86       C  
ATOM   3685  N   VAL B 106     -59.340 -39.843 -28.828  1.00 28.58           N  
ANISOU 3685  N   VAL B 106     3233   3403   4223     43    732   -497       N  
ATOM   3686  CA  VAL B 106     -59.501 -40.143 -27.402  1.00 34.18           C  
ANISOU 3686  CA  VAL B 106     3998   4196   4791    -34    864   -597       C  
ATOM   3687  C   VAL B 106     -60.988 -40.115 -27.064  1.00 36.20           C  
ANISOU 3687  C   VAL B 106     4138   4428   5188     11   1016   -620       C  
ATOM   3688  O   VAL B 106     -61.612 -39.042 -27.105  1.00 36.75           O  
ANISOU 3688  O   VAL B 106     4142   4380   5443     82   1131   -692       O  
ATOM   3689  CB  VAL B 106     -58.737 -39.155 -26.504  1.00 35.90           C  
ANISOU 3689  CB  VAL B 106     4328   4397   4915    -97    950   -755       C  
ATOM   3690  CG1 VAL B 106     -58.980 -39.500 -25.031  1.00 35.34           C  
ANISOU 3690  CG1 VAL B 106     4325   4441   4663   -193   1088   -856       C  
ATOM   3691  CG2 VAL B 106     -57.245 -39.170 -26.819  1.00 36.53           C  
ANISOU 3691  CG2 VAL B 106     4498   4511   4873   -150    797   -722       C  
ATOM   3692  N   PRO B 107     -61.596 -41.245 -26.718  1.00 30.77           N  
ANISOU 3692  N   PRO B 107     3412   3837   4441    -25   1031   -556       N  
ATOM   3693  CA  PRO B 107     -63.028 -41.242 -26.410  1.00 33.17           C  
ANISOU 3693  CA  PRO B 107     3582   4126   4894     12   1182   -568       C  
ATOM   3694  C   PRO B 107     -63.295 -40.686 -25.023  1.00 37.51           C  
ANISOU 3694  C   PRO B 107     4183   4702   5369    -33   1415   -734       C  
ATOM   3695  O   PRO B 107     -62.498 -40.856 -24.095  1.00 42.15           O  
ANISOU 3695  O   PRO B 107     4917   5383   5714   -136   1438   -804       O  
ATOM   3696  CB  PRO B 107     -63.408 -42.725 -26.486  1.00 38.37           C  
ANISOU 3696  CB  PRO B 107     4205   4885   5491    -40   1107   -440       C  
ATOM   3697  CG  PRO B 107     -62.167 -43.428 -26.053  1.00 30.65           C  
ANISOU 3697  CG  PRO B 107     3385   3998   4265   -129   1015   -422       C  
ATOM   3698  CD  PRO B 107     -61.011 -42.591 -26.601  1.00 34.38           C  
ANISOU 3698  CD  PRO B 107     3936   4410   4718   -101    915   -461       C  
ATOM   3699  N   VAL B 108     -64.445 -40.019 -24.893  1.00 43.14           N  
ANISOU 3699  N   VAL B 108     4766   5334   6292     43   1589   -795       N  
ATOM   3700  CA  VAL B 108     -64.824 -39.454 -23.601  1.00 52.75           C  
ANISOU 3700  CA  VAL B 108     6024   6565   7453      5   1851   -977       C  
ATOM   3701  C   VAL B 108     -65.116 -40.560 -22.590  1.00 57.22           C  
ANISOU 3701  C   VAL B 108     6628   7307   7805   -110   1934   -957       C  
ATOM   3702  O   VAL B 108     -64.715 -40.472 -21.422  1.00 58.68           O  
ANISOU 3702  O   VAL B 108     6954   7585   7755   -215   2056  -1081       O  
ATOM   3703  CB  VAL B 108     -66.022 -38.496 -23.756  1.00 54.08           C  
ANISOU 3703  CB  VAL B 108     6019   6589   7940    134   2036  -1040       C  
ATOM   3704  CG1 VAL B 108     -66.378 -37.879 -22.406  1.00 52.45           C  
ANISOU 3704  CG1 VAL B 108     5881   6390   7659     90   2308  -1246       C  
ATOM   3705  CG2 VAL B 108     -65.708 -37.401 -24.761  1.00 56.69           C  
ANISOU 3705  CG2 VAL B 108     6316   6737   8488    245   1943  -1029       C  
ATOM   3706  N   ASN B 109     -65.816 -41.614 -23.012  1.00 55.56           N  
ANISOU 3706  N   ASN B 109     6297   7147   7665   -105   1866   -795       N  
ATOM   3707  CA  ASN B 109     -66.198 -42.703 -22.124  1.00 53.51           C  
ANISOU 3707  CA  ASN B 109     6055   7036   7239   -213   1948   -745       C  
ATOM   3708  C   ASN B 109     -65.802 -44.039 -22.735  1.00 53.11           C  
ANISOU 3708  C   ASN B 109     6018   7040   7120   -259   1717   -553       C  
ATOM   3709  O   ASN B 109     -65.790 -44.203 -23.959  1.00 50.32           O  
ANISOU 3709  O   ASN B 109     5588   6609   6922   -191   1538   -456       O  
ATOM   3710  CB  ASN B 109     -67.704 -42.699 -21.846  1.00 56.23           C  
ANISOU 3710  CB  ASN B 109     6211   7375   7777   -176   2160   -753       C  
ATOM   3711  CG  ASN B 109     -68.204 -41.347 -21.373  1.00 63.09           C  
ANISOU 3711  CG  ASN B 109     7042   8151   8776   -100   2396   -942       C  
ATOM   3712  OD1 ASN B 109     -68.968 -40.676 -22.069  1.00 62.48           O  
ANISOU 3712  OD1 ASN B 109     6807   7940   8991     30   2388   -919       O  
ATOM   3713  ND2 ASN B 109     -67.767 -40.937 -20.189  1.00 59.63           N  
ANISOU 3713  ND2 ASN B 109     6785   7775   8098   -183   2514  -1092       N  
ATOM   3714  N   GLU B 110     -65.472 -44.994 -21.870  1.00 39.65           N  
ANISOU 3714  N   GLU B 110     4417   5467   5181   -381   1724   -499       N  
ATOM   3715  CA  GLU B 110     -65.289 -46.362 -22.328  1.00 43.74           C  
ANISOU 3715  CA  GLU B 110     4932   6016   5670   -425   1548   -318       C  
ATOM   3716  C   GLU B 110     -66.644 -46.971 -22.703  1.00 44.31           C  
ANISOU 3716  C   GLU B 110     4818   6067   5950   -412   1597   -228       C  
ATOM   3717  O   GLU B 110     -67.709 -46.460 -22.344  1.00 39.24           O  
ANISOU 3717  O   GLU B 110     4052   5423   5435   -386   1793   -293       O  
ATOM   3718  CB  GLU B 110     -64.608 -47.201 -21.247  1.00 46.83           C  
ANISOU 3718  CB  GLU B 110     5475   6543   5776   -555   1547   -259       C  
ATOM   3719  CG  GLU B 110     -65.520 -47.544 -20.076  1.00 52.59           C  
ANISOU 3719  CG  GLU B 110     6182   7382   6418   -647   1769   -259       C  
ATOM   3720  CD  GLU B 110     -64.839 -48.427 -19.037  1.00 68.16           C  
ANISOU 3720  CD  GLU B 110     8305   9497   8095   -784   1744   -161       C  
ATOM   3721  OE1 GLU B 110     -63.587 -48.492 -19.033  1.00 67.65           O  
ANISOU 3721  OE1 GLU B 110     8369   9455   7881   -803   1581   -134       O  
ATOM   3722  OE2 GLU B 110     -65.558 -49.057 -18.226  1.00 72.89           O  
ANISOU 3722  OE2 GLU B 110     8884  10189   8620   -875   1886    -94       O  
ATOM   3723  N   LEU B 111     -66.605 -48.062 -23.448  1.00 40.47           N  
ANISOU 3723  N   LEU B 111     4305   5559   5512   -434   1423    -85       N  
ATOM   3724  CA  LEU B 111     -67.849 -48.789 -23.673  1.00 34.33           C  
ANISOU 3724  CA  LEU B 111     3360   4778   4905   -462   1460      6       C  
ATOM   3725  C   LEU B 111     -68.170 -49.616 -22.433  1.00 41.77           C  
ANISOU 3725  C   LEU B 111     4341   5830   5700   -586   1607     63       C  
ATOM   3726  O   LEU B 111     -67.319 -50.383 -21.973  1.00 47.39           O  
ANISOU 3726  O   LEU B 111     5202   6590   6213   -663   1534    137       O  
ATOM   3727  CB  LEU B 111     -67.749 -49.680 -24.908  1.00 37.01           C  
ANISOU 3727  CB  LEU B 111     3667   5049   5348   -462   1230    120       C  
ATOM   3728  CG  LEU B 111     -67.673 -48.927 -26.244  1.00 43.04           C  
ANISOU 3728  CG  LEU B 111     4365   5721   6266   -354   1086     89       C  
ATOM   3729  CD1 LEU B 111     -67.577 -49.892 -27.432  1.00 36.77           C  
ANISOU 3729  CD1 LEU B 111     3560   4877   5533   -380    870    183       C  
ATOM   3730  CD2 LEU B 111     -68.862 -47.985 -26.403  1.00 43.67           C  
ANISOU 3730  CD2 LEU B 111     4247   5774   6570   -279   1202     49       C  
ATOM   3731  N   PRO B 112     -69.366 -49.485 -21.870  1.00 42.46           N  
ANISOU 3731  N   PRO B 112     4290   5959   5882   -608   1817     45       N  
ATOM   3732  CA  PRO B 112     -69.656 -50.067 -20.557  1.00 49.24           C  
ANISOU 3732  CA  PRO B 112     5198   6943   6567   -733   2001     84       C  
ATOM   3733  C   PRO B 112     -70.009 -51.550 -20.656  1.00 52.11           C  
ANISOU 3733  C   PRO B 112     5525   7313   6963   -837   1920    273       C  
ATOM   3734  O   PRO B 112     -70.096 -52.132 -21.736  1.00 46.89           O  
ANISOU 3734  O   PRO B 112     4796   6555   6465   -818   1732    351       O  
ATOM   3735  CB  PRO B 112     -70.858 -49.244 -20.086  1.00 48.49           C  
ANISOU 3735  CB  PRO B 112     4941   6873   6612   -696   2273    -23       C  
ATOM   3736  CG  PRO B 112     -71.594 -48.957 -21.352  1.00 51.58           C  
ANISOU 3736  CG  PRO B 112     5120   7145   7332   -588   2172     -2       C  
ATOM   3737  CD  PRO B 112     -70.520 -48.736 -22.402  1.00 50.08           C  
ANISOU 3737  CD  PRO B 112     5034   6865   7130   -515   1906     -5       C  
ATOM   3738  N   HIS B 113     -70.208 -52.156 -19.490  1.00 52.95           N  
ANISOU 3738  N   HIS B 113     5687   7532   6901   -960   2070    342       N  
ATOM   3739  CA  HIS B 113     -70.725 -53.515 -19.434  1.00 64.52           C  
ANISOU 3739  CA  HIS B 113     7099   8996   8421  -1074   2042    526       C  
ATOM   3740  C   HIS B 113     -72.175 -53.547 -19.910  1.00 65.17           C  
ANISOU 3740  C   HIS B 113     6925   9041   8796  -1068   2132    538       C  
ATOM   3741  O   HIS B 113     -72.950 -52.619 -19.657  1.00 68.26           O  
ANISOU 3741  O   HIS B 113     7193   9469   9273  -1005   2310    426       O  
ATOM   3742  CB  HIS B 113     -70.621 -54.066 -18.008  1.00 70.92           C  
ANISOU 3742  CB  HIS B 113     8028   9949   8969  -1214   2198    614       C  
ATOM   3743  CG  HIS B 113     -69.224 -54.415 -17.594  1.00 78.00           C  
ANISOU 3743  CG  HIS B 113     9152  10883   9601  -1249   2054    679       C  
ATOM   3744  ND1 HIS B 113     -68.665 -55.653 -17.832  1.00 81.17           N  
ANISOU 3744  ND1 HIS B 113     9623  11219   9999  -1301   1869    866       N  
ATOM   3745  CD2 HIS B 113     -68.272 -53.689 -16.959  1.00 78.92           C  
ANISOU 3745  CD2 HIS B 113     9431  11090   9464  -1240   2063    586       C  
ATOM   3746  CE1 HIS B 113     -67.430 -55.675 -17.361  1.00 82.36           C  
ANISOU 3746  CE1 HIS B 113     9953  11423   9915  -1312   1769    902       C  
ATOM   3747  NE2 HIS B 113     -67.167 -54.496 -16.827  1.00 82.27           N  
ANISOU 3747  NE2 HIS B 113    10002  11517   9740  -1284   1874    734       N  
ATOM   3748  N   GLY B 114     -72.538 -54.624 -20.612  1.00 63.00           N  
ANISOU 3748  N   GLY B 114     6572   8686   8680  -1127   1987    671       N  
ATOM   3749  CA  GLY B 114     -73.903 -54.768 -21.086  1.00 64.86           C  
ANISOU 3749  CA  GLY B 114     6555   8897   9191  -1145   2033    702       C  
ATOM   3750  C   GLY B 114     -74.871 -55.288 -20.043  1.00 77.69           C  
ANISOU 3750  C   GLY B 114     8127  10631  10760  -1249   2194    769       C  
ATOM   3751  O   GLY B 114     -76.061 -54.959 -20.087  1.00 79.84           O  
ANISOU 3751  O   GLY B 114     8213  10935  11188  -1222   2267    735       O  
ATOM   3752  N   TRP B 115     -74.383 -56.090 -19.092  1.00 82.40           N  
ANISOU 3752  N   TRP B 115     8880  11291  11136  -1369   2247    878       N  
ATOM   3753  CA  TRP B 115     -75.233 -56.745 -18.090  1.00 92.86           C  
ANISOU 3753  CA  TRP B 115    10165  12726  12390  -1492   2385    976       C  
ATOM   3754  C   TRP B 115     -76.344 -57.555 -18.759  1.00 86.40           C  
ANISOU 3754  C   TRP B 115     9167  11833  11826  -1566   2309   1044       C  
ATOM   3755  O   TRP B 115     -77.511 -57.504 -18.361  1.00 90.30           O  
ANISOU 3755  O   TRP B 115     9508  12408  12395  -1599   2437   1042       O  
ATOM   3756  CB  TRP B 115     -75.812 -55.731 -17.096  1.00101.98           C  
ANISOU 3756  CB  TRP B 115    11276  14030  13441  -1430   2618    871       C  
ATOM   3757  CG  TRP B 115     -74.776 -54.846 -16.461  1.00110.11           C  
ANISOU 3757  CG  TRP B 115    12497  15115  14224  -1356   2686    762       C  
ATOM   3758  CD1 TRP B 115     -74.369 -53.619 -16.900  1.00113.42           C  
ANISOU 3758  CD1 TRP B 115    12933  15485  14676  -1218   2682    575       C  
ATOM   3759  CD2 TRP B 115     -74.015 -55.120 -15.275  1.00114.38           C  
ANISOU 3759  CD2 TRP B 115    13250  15760  14448  -1424   2750    830       C  
ATOM   3760  NE1 TRP B 115     -73.403 -53.112 -16.063  1.00116.19           N  
ANISOU 3760  NE1 TRP B 115    13497  15909  14740  -1214   2738    499       N  
ATOM   3761  CE2 TRP B 115     -73.167 -54.014 -15.058  1.00117.21           C  
ANISOU 3761  CE2 TRP B 115    13751  16139  14644  -1338   2772    651       C  
ATOM   3762  CE3 TRP B 115     -73.968 -56.192 -14.377  1.00115.43           C  
ANISOU 3762  CE3 TRP B 115    13471  15959  14430  -1544   2783   1031       C  
ATOM   3763  CZ2 TRP B 115     -72.282 -53.948 -13.982  1.00117.97           C  
ANISOU 3763  CZ2 TRP B 115    14075  16338  14411  -1385   2802    652       C  
ATOM   3764  CZ3 TRP B 115     -73.089 -56.124 -13.308  1.00117.54           C  
ANISOU 3764  CZ3 TRP B 115    13968  16309  14382  -1570   2823   1043       C  
ATOM   3765  CH2 TRP B 115     -72.258 -55.011 -13.121  1.00118.82           C  
ANISOU 3765  CH2 TRP B 115    14265  16514  14365  -1500   2819    849       C  
ATOM   3766  N   LYS B 116     -75.976 -58.305 -19.795  1.00 73.62           N  
ANISOU 3766  N   LYS B 116     7568  10059  10345  -1589   2095   1100       N  
ATOM   3767  CA  LYS B 116     -76.926 -59.178 -20.462  1.00 70.29           C  
ANISOU 3767  CA  LYS B 116     7008   9555  10145  -1674   1993   1160       C  
ATOM   3768  C   LYS B 116     -77.200 -60.409 -19.601  1.00 64.98           C  
ANISOU 3768  C   LYS B 116     6405   8892   9393  -1846   2065   1299       C  
ATOM   3769  O   LYS B 116     -76.511 -60.679 -18.611  1.00 61.25           O  
ANISOU 3769  O   LYS B 116     6108   8471   8692  -1898   2153   1367       O  
ATOM   3770  CB  LYS B 116     -76.400 -59.594 -21.838  1.00 75.34           C  
ANISOU 3770  CB  LYS B 116     7667  10028  10930  -1649   1734   1161       C  
ATOM   3771  CG  LYS B 116     -76.365 -58.467 -22.859  1.00 77.50           C  
ANISOU 3771  CG  LYS B 116     7839  10285  11322  -1500   1639   1037       C  
ATOM   3772  CD  LYS B 116     -75.844 -58.947 -24.202  1.00 75.46           C  
ANISOU 3772  CD  LYS B 116     7615   9885  11173  -1502   1379   1039       C  
ATOM   3773  CE  LYS B 116     -76.069 -57.899 -25.283  1.00 74.41           C  
ANISOU 3773  CE  LYS B 116     7352   9749  11173  -1378   1269    936       C  
ATOM   3774  NZ  LYS B 116     -77.526 -57.686 -25.532  1.00 76.65           N  
ANISOU 3774  NZ  LYS B 116     7410  10085  11629  -1386   1282    925       N  
ATOM   3775  N   ALA B 117     -78.230 -61.159 -19.989  1.00 63.52           N  
ANISOU 3775  N   ALA B 117     6083   8655   9396  -1940   2021   1343       N  
ATOM   3776  CA  ALA B 117     -78.555 -62.395 -19.291  1.00 60.77           C  
ANISOU 3776  CA  ALA B 117     5794   8283   9014  -2107   2080   1476       C  
ATOM   3777  C   ALA B 117     -77.347 -63.323 -19.276  1.00 62.26           C  
ANISOU 3777  C   ALA B 117     6215   8331   9109  -2140   1960   1580       C  
ATOM   3778  O   ALA B 117     -76.602 -63.416 -20.256  1.00 64.55           O  
ANISOU 3778  O   ALA B 117     6562   8493   9471  -2073   1766   1555       O  
ATOM   3779  CB  ALA B 117     -79.749 -63.083 -19.956  1.00 59.59           C  
ANISOU 3779  CB  ALA B 117     5463   8066   9111  -2200   2007   1497       C  
ATOM   3780  N   TRP B 118     -77.134 -63.980 -18.139  1.00 72.94           N  
ANISOU 3780  N   TRP B 118     7705   9710  10298  -2235   2078   1701       N  
ATOM   3781  CA  TRP B 118     -76.028 -64.920 -18.006  1.00 83.57           C  
ANISOU 3781  CA  TRP B 118     9264  10921  11568  -2251   1965   1832       C  
ATOM   3782  C   TRP B 118     -76.139 -66.008 -19.068  1.00 77.23           C  
ANISOU 3782  C   TRP B 118     8441   9907  10996  -2299   1767   1868       C  
ATOM   3783  O   TRP B 118     -77.170 -66.681 -19.175  1.00 77.70           O  
ANISOU 3783  O   TRP B 118     8392   9925  11205  -2414   1789   1894       O  
ATOM   3784  CB  TRP B 118     -76.023 -65.528 -16.602  1.00104.00           C  
ANISOU 3784  CB  TRP B 118    11975  13565  13974  -2352   2127   1976       C  
ATOM   3785  CG  TRP B 118     -75.697 -64.541 -15.507  1.00123.49           C  
ANISOU 3785  CG  TRP B 118    14522  16221  16176  -2308   2317   1933       C  
ATOM   3786  CD1 TRP B 118     -76.584 -63.825 -14.750  1.00129.68           C  
ANISOU 3786  CD1 TRP B 118    15215  17176  16882  -2350   2559   1845       C  
ATOM   3787  CD2 TRP B 118     -74.388 -64.163 -15.053  1.00132.58           C  
ANISOU 3787  CD2 TRP B 118    15862  17409  17105  -2214   2279   1966       C  
ATOM   3788  NE1 TRP B 118     -75.908 -63.030 -13.854  1.00133.14           N  
ANISOU 3788  NE1 TRP B 118    15790  17715  17080  -2273   2700   1812       N  
ATOM   3789  CE2 TRP B 118     -74.560 -63.217 -14.020  1.00133.94           C  
ANISOU 3789  CE2 TRP B 118    16058  17755  17080  -2189   2512   1896       C  
ATOM   3790  CE3 TRP B 118     -73.088 -64.533 -15.421  1.00131.93           C  
ANISOU 3790  CE3 TRP B 118    15923  17230  16976  -2145   2067   2047       C  
ATOM   3791  CZ2 TRP B 118     -73.480 -62.637 -13.351  1.00132.62           C  
ANISOU 3791  CZ2 TRP B 118    16049  17684  16655  -2097   2509   1916       C  
ATOM   3792  CZ3 TRP B 118     -72.017 -63.957 -14.755  1.00129.31           C  
ANISOU 3792  CZ3 TRP B 118    15741  17007  16384  -2071   2062   2062       C  
ATOM   3793  CH2 TRP B 118     -72.221 -63.019 -13.731  1.00130.01           C  
ANISOU 3793  CH2 TRP B 118    15852  17286  16260  -2056   2269   1994       C  
ATOM   3794  N   GLY B 119     -75.089 -66.161 -19.867  1.00 65.04           N  
ANISOU 3794  N   GLY B 119     7001   8231   9480  -2218   1581   1854       N  
ATOM   3795  CA  GLY B 119     -75.107 -67.130 -20.948  1.00 56.16           C  
ANISOU 3795  CA  GLY B 119     5879   6896   8562  -2260   1398   1848       C  
ATOM   3796  C   GLY B 119     -73.789 -67.117 -21.689  1.00 55.60           C  
ANISOU 3796  C   GLY B 119     5942   6705   8479  -2152   1228   1818       C  
ATOM   3797  O   GLY B 119     -72.840 -66.418 -21.312  1.00 49.41           O  
ANISOU 3797  O   GLY B 119     5246   6001   7526  -2050   1243   1827       O  
ATOM   3798  N   LYS B 120     -73.743 -67.896 -22.775  1.00 54.59           N  
ANISOU 3798  N   LYS B 120     5829   6385   8529  -2182   1068   1770       N  
ATOM   3799  CA  LYS B 120     -72.474 -68.087 -23.475  1.00 56.88           C  
ANISOU 3799  CA  LYS B 120     6259   6529   8823  -2091    918   1742       C  
ATOM   3800  C   LYS B 120     -71.917 -66.791 -24.060  1.00 54.34           C  
ANISOU 3800  C   LYS B 120     5908   6303   8438  -1962    867   1622       C  
ATOM   3801  O   LYS B 120     -70.723 -66.738 -24.390  1.00 50.48           O  
ANISOU 3801  O   LYS B 120     5539   5737   7904  -1871    777   1616       O  
ATOM   3802  CB  LYS B 120     -72.625 -69.152 -24.570  1.00 60.73           C  
ANISOU 3802  CB  LYS B 120     6773   6792   9509  -2160    778   1675       C  
ATOM   3803  CG  LYS B 120     -73.417 -68.738 -25.799  1.00 62.69           C  
ANISOU 3803  CG  LYS B 120     6883   7053   9882  -2192    681   1501       C  
ATOM   3804  CD  LYS B 120     -73.243 -69.773 -26.903  1.00 62.03           C  
ANISOU 3804  CD  LYS B 120     6883   6743   9942  -2254    535   1412       C  
ATOM   3805  CE  LYS B 120     -73.778 -69.285 -28.239  1.00 68.47           C  
ANISOU 3805  CE  LYS B 120     7596   7586  10831  -2275    403   1229       C  
ATOM   3806  NZ  LYS B 120     -75.193 -69.682 -28.433  1.00 65.78           N  
ANISOU 3806  NZ  LYS B 120     7109   7279  10606  -2425    403   1209       N  
ATOM   3807  N   SER B 121     -72.732 -65.734 -24.163  1.00 51.56           N  
ANISOU 3807  N   SER B 121     5392   6111   8087  -1945    930   1533       N  
ATOM   3808  CA  SER B 121     -72.230 -64.462 -24.685  1.00 50.61           C  
ANISOU 3808  CA  SER B 121     5237   6076   7916  -1820    891   1425       C  
ATOM   3809  C   SER B 121     -71.104 -63.880 -23.835  1.00 49.98           C  
ANISOU 3809  C   SER B 121     5286   6086   7617  -1723    958   1480       C  
ATOM   3810  O   SER B 121     -70.328 -63.057 -24.333  1.00 47.23           O  
ANISOU 3810  O   SER B 121     5002   5766   7178  -1583    878   1354       O  
ATOM   3811  CB  SER B 121     -73.366 -63.440 -24.787  1.00 57.53           C  
ANISOU 3811  CB  SER B 121     5909   7106   8845  -1803    970   1336       C  
ATOM   3812  OG  SER B 121     -73.908 -63.158 -23.503  1.00 65.08           O  
ANISOU 3812  OG  SER B 121     6823   8209   9694  -1828   1178   1398       O  
ATOM   3813  N   TYR B 122     -71.012 -64.263 -22.561  1.00 52.57           N  
ANISOU 3813  N   TYR B 122     5687   6479   7809  -1774   1083   1621       N  
ATOM   3814  CA  TYR B 122     -69.923 -63.781 -21.722  1.00 56.10           C  
ANISOU 3814  CA  TYR B 122     6268   7029   8018  -1702   1122   1679       C  
ATOM   3815  C   TYR B 122     -68.592 -64.436 -22.053  1.00 53.10           C  
ANISOU 3815  C   TYR B 122     6055   6502   7617  -1637    960   1729       C  
ATOM   3816  O   TYR B 122     -67.556 -63.970 -21.566  1.00 42.32           O  
ANISOU 3816  O   TYR B 122     4803   5218   6058  -1550    941   1740       O  
ATOM   3817  CB  TYR B 122     -70.252 -64.012 -20.243  1.00 61.09           C  
ANISOU 3817  CB  TYR B 122     6944   7790   8478  -1781   1290   1800       C  
ATOM   3818  CG  TYR B 122     -71.251 -63.026 -19.683  1.00 72.28           C  
ANISOU 3818  CG  TYR B 122     8235   9395   9833  -1797   1486   1708       C  
ATOM   3819  CD1 TYR B 122     -72.618 -63.219 -19.845  1.00 71.21           C  
ANISOU 3819  CD1 TYR B 122     7938   9255   9863  -1872   1564   1669       C  
ATOM   3820  CD2 TYR B 122     -70.826 -61.895 -18.995  1.00 74.89           C  
ANISOU 3820  CD2 TYR B 122     8606   9904   9942  -1736   1595   1649       C  
ATOM   3821  CE1 TYR B 122     -73.534 -62.314 -19.334  1.00 73.86           C  
ANISOU 3821  CE1 TYR B 122     8147   9753  10163  -1873   1753   1578       C  
ATOM   3822  CE2 TYR B 122     -71.735 -60.987 -18.480  1.00 75.88           C  
ANISOU 3822  CE2 TYR B 122     8622  10178  10029  -1739   1798   1540       C  
ATOM   3823  CZ  TYR B 122     -73.085 -61.201 -18.653  1.00 74.22           C  
ANISOU 3823  CZ  TYR B 122     8243   9956  10003  -1802   1878   1508       C  
ATOM   3824  OH  TYR B 122     -73.984 -60.296 -18.143  1.00 75.21           O  
ANISOU 3824  OH  TYR B 122     8246  10231  10099  -1798   2075   1397       O  
ATOM   3825  N   PHE B 123     -68.593 -65.489 -22.863  1.00 50.96           N  
ANISOU 3825  N   PHE B 123     5797   6015   7549  -1679    849   1751       N  
ATOM   3826  CA  PHE B 123     -67.375 -66.265 -23.071  1.00 46.19           C  
ANISOU 3826  CA  PHE B 123     5341   5247   6961  -1620    730   1820       C  
ATOM   3827  C   PHE B 123     -66.999 -66.430 -24.536  1.00 40.03           C  
ANISOU 3827  C   PHE B 123     4583   4297   6328  -1549    583   1649       C  
ATOM   3828  O   PHE B 123     -65.811 -66.455 -24.854  1.00 40.80           O  
ANISOU 3828  O   PHE B 123     4788   4327   6387  -1433    496   1623       O  
ATOM   3829  CB  PHE B 123     -67.512 -67.640 -22.409  1.00 43.37           C  
ANISOU 3829  CB  PHE B 123     5051   4770   6658  -1701    751   1985       C  
ATOM   3830  CG  PHE B 123     -67.738 -67.575 -20.925  1.00 41.80           C  
ANISOU 3830  CG  PHE B 123     4876   4746   6261  -1751    881   2130       C  
ATOM   3831  CD1 PHE B 123     -66.685 -67.305 -20.064  1.00 41.66           C  
ANISOU 3831  CD1 PHE B 123     4965   4833   6030  -1685    871   2238       C  
ATOM   3832  CD2 PHE B 123     -69.000 -67.793 -20.392  1.00 43.68           C  
ANISOU 3832  CD2 PHE B 123     5029   5049   6517  -1871   1010   2152       C  
ATOM   3833  CE1 PHE B 123     -66.888 -67.248 -18.693  1.00 43.40           C  
ANISOU 3833  CE1 PHE B 123     5224   5224   6042  -1743    985   2357       C  
ATOM   3834  CE2 PHE B 123     -69.214 -67.736 -19.025  1.00 49.18           C  
ANISOU 3834  CE2 PHE B 123     5760   5906   7019  -1924   1145   2272       C  
ATOM   3835  CZ  PHE B 123     -68.158 -67.458 -18.177  1.00 45.27           C  
ANISOU 3835  CZ  PHE B 123     5387   5517   6295  -1862   1132   2370       C  
ATOM   3836  N   VAL B 124     -67.969 -66.546 -25.435  1.00 38.74           N  
ANISOU 3836  N   VAL B 124     4318   4073   6327  -1624    553   1533       N  
ATOM   3837  CA  VAL B 124     -67.664 -66.887 -26.820  1.00 38.17           C  
ANISOU 3837  CA  VAL B 124     4288   3834   6382  -1594    416   1377       C  
ATOM   3838  C   VAL B 124     -67.340 -65.630 -27.613  1.00 35.24           C  
ANISOU 3838  C   VAL B 124     3900   3585   5904  -1466    352   1190       C  
ATOM   3839  O   VAL B 124     -67.726 -64.512 -27.263  1.00 40.13           O  
ANISOU 3839  O   VAL B 124     4435   4395   6418  -1426    411   1159       O  
ATOM   3840  CB  VAL B 124     -68.812 -67.681 -27.481  1.00 46.33           C  
ANISOU 3840  CB  VAL B 124     5233   4743   7629  -1761    385   1340       C  
ATOM   3841  CG1 VAL B 124     -69.061 -68.956 -26.718  1.00 43.43           C  
ANISOU 3841  CG1 VAL B 124     4923   4266   7314  -1843    445   1478       C  
ATOM   3842  CG2 VAL B 124     -70.073 -66.845 -27.573  1.00 37.84           C  
ANISOU 3842  CG2 VAL B 124     3971   3846   6561  -1817    422   1280       C  
ATOM   3843  N   ARG B 125     -66.602 -65.823 -28.699  1.00 33.08           N  
ANISOU 3843  N   ARG B 125     3714   3190   5665  -1400    240   1065       N  
ATOM   3844  CA  ARG B 125     -66.308 -64.725 -29.601  1.00 31.27           C  
ANISOU 3844  CA  ARG B 125     3475   3058   5347  -1296    170    896       C  
ATOM   3845  C   ARG B 125     -67.593 -64.149 -30.175  1.00 33.83           C  
ANISOU 3845  C   ARG B 125     3645   3480   5729  -1370    144    814       C  
ATOM   3846  O   ARG B 125     -68.597 -64.849 -30.342  1.00 33.14           O  
ANISOU 3846  O   ARG B 125     3477   3329   5785  -1515    135    835       O  
ATOM   3847  CB  ARG B 125     -65.403 -65.186 -30.741  1.00 44.54           C  
ANISOU 3847  CB  ARG B 125     5274   4585   7063  -1241     70    774       C  
ATOM   3848  CG  ARG B 125     -64.003 -65.510 -30.310  1.00 52.49           C  
ANISOU 3848  CG  ARG B 125     6405   5517   8023  -1127     86    843       C  
ATOM   3849  CD  ARG B 125     -63.114 -65.777 -31.504  1.00 58.68           C  
ANISOU 3849  CD  ARG B 125     7287   6171   8836  -1055     15    695       C  
ATOM   3850  NE  ARG B 125     -61.896 -66.462 -31.094  1.00 67.97           N  
ANISOU 3850  NE  ARG B 125     8560   7216  10050   -965     38    786       N  
ATOM   3851  CZ  ARG B 125     -61.787 -67.783 -30.998  1.00 70.59           C  
ANISOU 3851  CZ  ARG B 125     8947   7321  10553  -1012     56    854       C  
ATOM   3852  NH1 ARG B 125     -62.824 -68.557 -31.294  1.00 61.20           N  
ANISOU 3852  NH1 ARG B 125     7737   6014   9502  -1165     53    826       N  
ATOM   3853  NH2 ARG B 125     -60.641 -68.331 -30.611  1.00 76.77           N  
ANISOU 3853  NH2 ARG B 125     9797   7987  11387   -909     73    957       N  
ATOM   3854  N   ALA B 126     -67.549 -62.852 -30.454  1.00 30.12           N  
ANISOU 3854  N   ALA B 126     3125   3160   5159  -1271    129    734       N  
ATOM   3855  CA  ALA B 126     -68.648 -62.172 -31.114  1.00 39.44           C  
ANISOU 3855  CA  ALA B 126     4148   4433   6402  -1310     83    665       C  
ATOM   3856  C   ALA B 126     -68.848 -62.722 -32.525  1.00 42.70           C  
ANISOU 3856  C   ALA B 126     4579   4748   6896  -1387    -71    554       C  
ATOM   3857  O   ALA B 126     -67.899 -63.138 -33.198  1.00 36.03           O  
ANISOU 3857  O   ALA B 126     3884   3798   6009  -1350   -136    475       O  
ATOM   3858  CB  ALA B 126     -68.360 -60.668 -31.169  1.00 30.50           C  
ANISOU 3858  CB  ALA B 126     2984   3449   5157  -1169     95    609       C  
ATOM   3859  N   ALA B 127     -70.098 -62.716 -32.978  1.00 36.22           N  
ANISOU 3859  N   ALA B 127     3600   3970   6190  -1502   -126    544       N  
ATOM   3860  CA  ALA B 127     -70.373 -63.039 -34.370  1.00 41.55           C  
ANISOU 3860  CA  ALA B 127     4282   4597   6907  -1590   -293    428       C  
ATOM   3861  C   ALA B 127     -69.687 -62.027 -35.281  1.00 39.78           C  
ANISOU 3861  C   ALA B 127     4116   4454   6545  -1463   -381    329       C  
ATOM   3862  O   ALA B 127     -69.641 -60.828 -34.983  1.00 35.71           O  
ANISOU 3862  O   ALA B 127     3531   4068   5969  -1342   -341    359       O  
ATOM   3863  CB  ALA B 127     -71.882 -63.055 -34.625  1.00 43.58           C  
ANISOU 3863  CB  ALA B 127     4325   4923   7310  -1735   -352    459       C  
ATOM   3864  N   LYS B 128     -69.116 -62.520 -36.379  1.00 39.26           N  
ANISOU 3864  N   LYS B 128     4186   4302   6427  -1495   -488    206       N  
ATOM   3865  CA  LYS B 128     -68.520 -61.626 -37.363  1.00 42.71           C  
ANISOU 3865  CA  LYS B 128     4679   4822   6726  -1402   -577    117       C  
ATOM   3866  C   LYS B 128     -69.599 -60.703 -37.915  1.00 42.21           C  
ANISOU 3866  C   LYS B 128     4432   4917   6689  -1434   -684    143       C  
ATOM   3867  O   LYS B 128     -70.756 -61.102 -38.043  1.00 39.52           O  
ANISOU 3867  O   LYS B 128     3953   4592   6472  -1577   -747    173       O  
ATOM   3868  CB  LYS B 128     -67.874 -62.435 -38.490  1.00 45.77           C  
ANISOU 3868  CB  LYS B 128     5240   5095   7053  -1463   -659    -31       C  
ATOM   3869  CG  LYS B 128     -66.733 -61.724 -39.200  1.00 56.55           C  
ANISOU 3869  CG  LYS B 128     6728   6507   8252  -1332   -678   -111       C  
ATOM   3870  CD  LYS B 128     -66.529 -62.256 -40.614  1.00 64.43           C  
ANISOU 3870  CD  LYS B 128     7849   7461   9170  -1430   -786   -275       C  
ATOM   3871  CE  LYS B 128     -65.110 -61.996 -41.125  1.00 60.96           C  
ANISOU 3871  CE  LYS B 128     7573   7003   8587  -1302   -740   -363       C  
ATOM   3872  NZ  LYS B 128     -64.609 -60.603 -40.910  1.00 47.16           N  
ANISOU 3872  NZ  LYS B 128     5779   5398   6743  -1143   -718   -285       N  
ATOM   3873  N   THR B 129     -69.237 -59.451 -38.193  1.00 42.83           N  
ANISOU 3873  N   THR B 129     4493   5108   6674  -1301   -703    149       N  
ATOM   3874  CA  THR B 129     -70.182 -58.478 -38.742  1.00 38.75           C  
ANISOU 3874  CA  THR B 129     3794   4730   6198  -1305   -809    198       C  
ATOM   3875  C   THR B 129     -69.751 -58.069 -40.151  1.00 43.68           C  
ANISOU 3875  C   THR B 129     4505   5410   6681  -1306   -968    124       C  
ATOM   3876  O   THR B 129     -68.735 -58.533 -40.680  1.00 39.53           O  
ANISOU 3876  O   THR B 129     4177   4817   6026  -1303   -973     19       O  
ATOM   3877  CB  THR B 129     -70.316 -57.229 -37.854  1.00 38.73           C  
ANISOU 3877  CB  THR B 129     3670   4810   6237  -1153   -692    290       C  
ATOM   3878  OG1 THR B 129     -69.157 -56.394 -38.003  1.00 34.65           O  
ANISOU 3878  OG1 THR B 129     3280   4307   5579  -1007   -665    256       O  
ATOM   3879  CG2 THR B 129     -70.506 -57.610 -36.380  1.00 37.01           C  
ANISOU 3879  CG2 THR B 129     3413   4551   6098  -1147   -505    350       C  
ATOM   3880  N   ASN B 130     -70.549 -57.169 -40.739  1.00 46.64           N  
ANISOU 3880  N   ASN B 130     4720   5913   7090  -1307  -1089    192       N  
ATOM   3881  CA  ASN B 130     -70.359 -56.619 -42.077  1.00 55.44           C  
ANISOU 3881  CA  ASN B 130     5879   7117   8070  -1319  -1258    168       C  
ATOM   3882  C   ASN B 130     -69.240 -55.594 -42.149  1.00 46.63           C  
ANISOU 3882  C   ASN B 130     4868   6020   6827  -1147  -1197    169       C  
ATOM   3883  O   ASN B 130     -68.829 -55.218 -43.251  1.00 43.56           O  
ANISOU 3883  O   ASN B 130     4563   5695   6292  -1155  -1311    142       O  
ATOM   3884  CB  ASN B 130     -71.650 -55.940 -42.545  1.00 70.55           C  
ANISOU 3884  CB  ASN B 130     7550   9160  10095  -1366  -1412    288       C  
ATOM   3885  CG  ASN B 130     -72.663 -56.911 -43.105  1.00 95.34           C  
ANISOU 3885  CG  ASN B 130    10637  12319  13267  -1553  -1532    256       C  
ATOM   3886  OD1 ASN B 130     -72.323 -58.018 -43.527  1.00 89.17           O  
ANISOU 3886  OD1 ASN B 130    10017  11464  12398  -1685  -1562    125       O  
ATOM   3887  ND2 ASN B 130     -73.930 -56.490 -43.116  1.00122.10           N  
ANISOU 3887  ND2 ASN B 130    13815  15798  16778  -1545  -1572    362       N  
ATOM   3888  N   ASN B 131     -68.764 -55.107 -41.013  1.00 36.86           N  
ANISOU 3888  N   ASN B 131     3628   4741   5636  -1005  -1023    202       N  
ATOM   3889  CA  ASN B 131     -67.892 -53.945 -40.973  1.00 31.63           C  
ANISOU 3889  CA  ASN B 131     3019   4104   4895   -848   -968    223       C  
ATOM   3890  C   ASN B 131     -66.575 -54.367 -40.344  1.00 36.48           C  
ANISOU 3890  C   ASN B 131     3814   4628   5417   -783   -828    147       C  
ATOM   3891  O   ASN B 131     -66.522 -54.659 -39.144  1.00 37.49           O  
ANISOU 3891  O   ASN B 131     3930   4704   5611   -752   -693    163       O  
ATOM   3892  CB  ASN B 131     -68.560 -52.812 -40.196  1.00 36.64           C  
ANISOU 3892  CB  ASN B 131     3467   4778   5678   -742   -895    329       C  
ATOM   3893  CG  ASN B 131     -69.857 -52.345 -40.858  1.00 44.16           C  
ANISOU 3893  CG  ASN B 131     4207   5816   6754   -789  -1043    430       C  
ATOM   3894  OD1 ASN B 131     -69.934 -52.240 -42.086  1.00 44.69           O  
ANISOU 3894  OD1 ASN B 131     4292   5951   6739   -850  -1223    446       O  
ATOM   3895  ND2 ASN B 131     -70.884 -52.083 -40.049  1.00 40.42           N  
ANISOU 3895  ND2 ASN B 131     3529   5352   6478   -767   -968    505       N  
ATOM   3896  N   SER B 132     -65.516 -54.404 -41.149  1.00 27.48           N  
ANISOU 3896  N   SER B 132     2835   3481   4124   -765   -860     75       N  
ATOM   3897  CA  SER B 132     -64.203 -54.842 -40.681  1.00 28.80           C  
ANISOU 3897  CA  SER B 132     3158   3565   4218   -700   -742     10       C  
ATOM   3898  C   SER B 132     -63.295 -53.641 -40.431  1.00 36.00           C  
ANISOU 3898  C   SER B 132     4095   4512   5071   -561   -678     42       C  
ATOM   3899  O   SER B 132     -62.999 -52.877 -41.355  1.00 37.08           O  
ANISOU 3899  O   SER B 132     4255   4710   5123   -536   -747     47       O  
ATOM   3900  CB  SER B 132     -63.557 -55.789 -41.690  1.00 31.77           C  
ANISOU 3900  CB  SER B 132     3694   3892   4487   -772   -787   -108       C  
ATOM   3901  OG  SER B 132     -64.415 -56.873 -41.963  1.00 38.96           O  
ANISOU 3901  OG  SER B 132     4589   4757   5456   -919   -852   -152       O  
ATOM   3902  N   PHE B 133     -62.846 -53.493 -39.186  1.00 31.62           N  
ANISOU 3902  N   PHE B 133     3540   3923   4552   -485   -551     66       N  
ATOM   3903  CA  PHE B 133     -61.804 -52.540 -38.802  1.00 30.54           C  
ANISOU 3903  CA  PHE B 133     3448   3801   4355   -372   -480     75       C  
ATOM   3904  C   PHE B 133     -60.482 -53.310 -38.831  1.00 28.05           C  
ANISOU 3904  C   PHE B 133     3274   3425   3957   -353   -437     17       C  
ATOM   3905  O   PHE B 133     -60.194 -54.100 -37.924  1.00 26.40           O  
ANISOU 3905  O   PHE B 133     3094   3157   3780   -354   -366     24       O  
ATOM   3906  CB  PHE B 133     -62.114 -51.960 -37.423  1.00 26.69           C  
ANISOU 3906  CB  PHE B 133     2879   3322   3939   -322   -373    123       C  
ATOM   3907  CG  PHE B 133     -61.182 -50.862 -36.974  1.00 29.94           C  
ANISOU 3907  CG  PHE B 133     3326   3750   4298   -227   -308    122       C  
ATOM   3908  CD1 PHE B 133     -61.401 -49.542 -37.362  1.00 28.84           C  
ANISOU 3908  CD1 PHE B 133     3127   3643   4190   -174   -329    147       C  
ATOM   3909  CD2 PHE B 133     -60.114 -51.141 -36.123  1.00 27.15           C  
ANISOU 3909  CD2 PHE B 133     3057   3377   3881   -199   -232    107       C  
ATOM   3910  CE1 PHE B 133     -60.552 -48.524 -36.933  1.00 26.91           C  
ANISOU 3910  CE1 PHE B 133     2918   3397   3910   -102   -267    136       C  
ATOM   3911  CE2 PHE B 133     -59.264 -50.128 -35.687  1.00 26.53           C  
ANISOU 3911  CE2 PHE B 133     3007   3321   3755   -134   -184    100       C  
ATOM   3912  CZ  PHE B 133     -59.483 -48.819 -36.088  1.00 24.40           C  
ANISOU 3912  CZ  PHE B 133     2686   3069   3514    -90   -196    105       C  
ATOM   3913  N   VAL B 134     -59.688 -53.117 -39.894  1.00 27.42           N  
ANISOU 3913  N   VAL B 134     3278   3362   3780   -337   -475    -30       N  
ATOM   3914  CA  VAL B 134     -58.584 -54.030 -40.196  1.00 25.10           C  
ANISOU 3914  CA  VAL B 134     3103   3001   3432   -328   -435   -101       C  
ATOM   3915  C   VAL B 134     -57.284 -53.483 -39.620  1.00 25.05           C  
ANISOU 3915  C   VAL B 134     3126   2999   3394   -228   -356    -79       C  
ATOM   3916  O   VAL B 134     -56.915 -52.325 -39.852  1.00 26.37           O  
ANISOU 3916  O   VAL B 134     3277   3230   3513   -181   -361    -55       O  
ATOM   3917  CB  VAL B 134     -58.462 -54.299 -41.708  1.00 25.65           C  
ANISOU 3917  CB  VAL B 134     3253   3089   3405   -386   -500   -185       C  
ATOM   3918  CG1 VAL B 134     -59.636 -55.185 -42.203  1.00 26.10           C  
ANISOU 3918  CG1 VAL B 134     3299   3125   3494   -514   -584   -228       C  
ATOM   3919  CG2 VAL B 134     -58.403 -53.009 -42.500  1.00 31.99           C  
ANISOU 3919  CG2 VAL B 134     4037   4000   4119   -363   -557   -146       C  
ATOM   3920  N   VAL B 135     -56.586 -54.318 -38.868  1.00 25.41           N  
ANISOU 3920  N   VAL B 135     3206   2971   3475   -200   -291    -75       N  
ATOM   3921  CA  VAL B 135     -55.292 -53.976 -38.299  1.00 24.54           C  
ANISOU 3921  CA  VAL B 135     3112   2868   3342   -117   -232    -46       C  
ATOM   3922  C   VAL B 135     -54.244 -54.725 -39.114  1.00 29.53           C  
ANISOU 3922  C   VAL B 135     3821   3440   3959    -88   -201   -111       C  
ATOM   3923  O   VAL B 135     -54.273 -55.960 -39.181  1.00 26.75           O  
ANISOU 3923  O   VAL B 135     3510   2985   3669   -109   -180   -146       O  
ATOM   3924  CB  VAL B 135     -55.218 -54.330 -36.802  1.00 25.29           C  
ANISOU 3924  CB  VAL B 135     3177   2943   3488   -104   -190     32       C  
ATOM   3925  CG1 VAL B 135     -53.845 -53.997 -36.234  1.00 26.00           C  
ANISOU 3925  CG1 VAL B 135     3274   3056   3548    -33   -156     71       C  
ATOM   3926  CG2 VAL B 135     -56.310 -53.602 -36.028  1.00 28.72           C  
ANISOU 3926  CG2 VAL B 135     3540   3439   3933   -136   -191     73       C  
ATOM   3927  N   ASP B 136     -53.352 -53.972 -39.773  1.00 22.50           N  
ANISOU 3927  N   ASP B 136     2948   2604   2997    -44   -185   -132       N  
ATOM   3928  CA  ASP B 136     -52.331 -54.545 -40.645  1.00 23.84           C  
ANISOU 3928  CA  ASP B 136     3181   2732   3145    -13   -129   -205       C  
ATOM   3929  C   ASP B 136     -52.940 -55.566 -41.602  1.00 34.24           C  
ANISOU 3929  C   ASP B 136     4573   3982   4453    -84   -138   -312       C  
ATOM   3930  O   ASP B 136     -54.061 -55.368 -42.084  1.00 33.32           O  
ANISOU 3930  O   ASP B 136     4458   3909   4292   -167   -217   -331       O  
ATOM   3931  CB  ASP B 136     -51.203 -55.149 -39.799  1.00 27.24           C  
ANISOU 3931  CB  ASP B 136     3590   3095   3663     67    -63   -159       C  
ATOM   3932  CG  ASP B 136     -50.665 -54.160 -38.781  1.00 31.93           C  
ANISOU 3932  CG  ASP B 136     4114   3769   4249    107    -74    -60       C  
ATOM   3933  OD1 ASP B 136     -50.420 -52.994 -39.166  1.00 29.47           O  
ANISOU 3933  OD1 ASP B 136     3788   3543   3866    110    -85    -60       O  
ATOM   3934  OD2 ASP B 136     -50.517 -54.524 -37.590  1.00 32.46           O  
ANISOU 3934  OD2 ASP B 136     4145   3814   4373    125    -77     21       O  
ATOM   3935  N   GLY B 137     -52.222 -56.657 -41.881  1.00 25.71           N  
ANISOU 3935  N   GLY B 137     3549   2792   3427    -55    -59   -386       N  
ATOM   3936  CA  GLY B 137     -52.734 -57.701 -42.751  1.00 29.00           C  
ANISOU 3936  CA  GLY B 137     4053   3122   3842   -133    -53   -516       C  
ATOM   3937  C   GLY B 137     -52.641 -57.326 -44.218  1.00 36.04           C  
ANISOU 3937  C   GLY B 137     5024   4099   4571   -185    -53   -629       C  
ATOM   3938  O   GLY B 137     -52.132 -56.268 -44.600  1.00 36.87           O  
ANISOU 3938  O   GLY B 137     5113   4322   4574   -154    -50   -592       O  
ATOM   3939  N   ASP B 138     -53.157 -58.229 -45.055  1.00 36.67           N  
ANISOU 3939  N   ASP B 138     5198   4117   4619   -282    -57   -768       N  
ATOM   3940  CA  ASP B 138     -53.209 -58.047 -46.508  1.00 39.95           C  
ANISOU 3940  CA  ASP B 138     5713   4622   4845   -367    -66   -892       C  
ATOM   3941  C   ASP B 138     -54.589 -57.505 -46.891  1.00 42.42           C  
ANISOU 3941  C   ASP B 138     6004   5054   5059   -495   -236   -853       C  
ATOM   3942  O   ASP B 138     -55.413 -58.163 -47.521  1.00 41.11           O  
ANISOU 3942  O   ASP B 138     5901   4874   4845   -627   -303   -954       O  
ATOM   3943  CB  ASP B 138     -52.888 -59.373 -47.208  1.00 42.91           C  
ANISOU 3943  CB  ASP B 138     6213   4856   5235   -408     39  -1091       C  
ATOM   3944  CG  ASP B 138     -52.967 -59.284 -48.715  1.00 55.22           C  
ANISOU 3944  CG  ASP B 138     7897   6517   6565   -521     37  -1243       C  
ATOM   3945  OD1 ASP B 138     -52.852 -58.162 -49.248  1.00 63.79           O  
ANISOU 3945  OD1 ASP B 138     8971   7781   7485   -530     -9  -1175       O  
ATOM   3946  OD2 ASP B 138     -53.142 -60.341 -49.367  1.00 55.93           O  
ANISOU 3946  OD2 ASP B 138     8106   6509   6636   -610     83  -1432       O  
ATOM   3947  N   THR B 139     -54.837 -56.264 -46.478  1.00 35.89           N  
ANISOU 3947  N   THR B 139     5076   4342   4217   -456   -310   -699       N  
ATOM   3948  CA  THR B 139     -56.197 -55.742 -46.414  1.00 39.97           C  
ANISOU 3948  CA  THR B 139     5516   4941   4730   -536   -463   -613       C  
ATOM   3949  C   THR B 139     -56.279 -54.334 -46.994  1.00 44.00           C  
ANISOU 3949  C   THR B 139     5989   5609   5119   -532   -539   -511       C  
ATOM   3950  O   THR B 139     -57.188 -53.566 -46.654  1.00 36.74           O  
ANISOU 3950  O   THR B 139     4962   4748   4248   -539   -641   -391       O  
ATOM   3951  CB  THR B 139     -56.706 -55.759 -44.969  1.00 36.61           C  
ANISOU 3951  CB  THR B 139     4974   4450   4486   -486   -467   -506       C  
ATOM   3952  OG1 THR B 139     -55.731 -55.135 -44.123  1.00 32.51           O  
ANISOU 3952  OG1 THR B 139     4412   3925   4014   -356   -381   -427       O  
ATOM   3953  CG2 THR B 139     -56.926 -57.199 -44.479  1.00 32.91           C  
ANISOU 3953  CG2 THR B 139     4537   3827   4142   -524   -425   -578       C  
ATOM   3954  N   LEU B 140     -55.342 -53.987 -47.880  1.00 44.88           N  
ANISOU 3954  N   LEU B 140     6184   5784   5085   -518   -480   -552       N  
ATOM   3955  CA  LEU B 140     -55.273 -52.623 -48.396  1.00 55.58           C  
ANISOU 3955  CA  LEU B 140     7509   7273   6337   -508   -538   -433       C  
ATOM   3956  C   LEU B 140     -56.451 -52.294 -49.303  1.00 51.58           C  
ANISOU 3956  C   LEU B 140     6996   6885   5716   -632   -712   -386       C  
ATOM   3957  O   LEU B 140     -56.867 -51.132 -49.371  1.00 45.22           O  
ANISOU 3957  O   LEU B 140     6108   6161   4912   -615   -803   -231       O  
ATOM   3958  CB  LEU B 140     -53.951 -52.407 -49.131  1.00 51.73           C  
ANISOU 3958  CB  LEU B 140     7110   6827   5718   -475   -417   -482       C  
ATOM   3959  CG  LEU B 140     -52.788 -52.231 -48.150  1.00 50.71           C  
ANISOU 3959  CG  LEU B 140     6928   6617   5722   -338   -281   -453       C  
ATOM   3960  CD1 LEU B 140     -51.455 -52.129 -48.881  1.00 56.17           C  
ANISOU 3960  CD1 LEU B 140     7687   7346   6309   -308   -145   -507       C  
ATOM   3961  CD2 LEU B 140     -53.018 -51.016 -47.254  1.00 50.43           C  
ANISOU 3961  CD2 LEU B 140     6772   6600   5789   -274   -336   -291       C  
ATOM   3962  N   LYS B 141     -57.019 -53.293 -49.977  1.00 53.11           N  
ANISOU 3962  N   LYS B 141     7268   7084   5826   -761   -768   -510       N  
ATOM   3963  CA  LYS B 141     -58.134 -53.024 -50.877  1.00 58.96           C  
ANISOU 3963  CA  LYS B 141     7998   7959   6446   -899   -959   -458       C  
ATOM   3964  C   LYS B 141     -59.341 -52.498 -50.108  1.00 56.85           C  
ANISOU 3964  C   LYS B 141     7550   7692   6357   -881  -1087   -302       C  
ATOM   3965  O   LYS B 141     -59.961 -51.505 -50.506  1.00 63.26           O  
ANISOU 3965  O   LYS B 141     8278   8615   7141   -897  -1221   -147       O  
ATOM   3966  CB  LYS B 141     -58.486 -54.290 -51.665  1.00 67.31           C  
ANISOU 3966  CB  LYS B 141     9180   9011   7383  -1061   -992   -648       C  
ATOM   3967  CG  LYS B 141     -59.150 -54.018 -53.005  1.00 72.00           C  
ANISOU 3967  CG  LYS B 141     9828   9791   7737  -1229  -1168   -631       C  
ATOM   3968  CD  LYS B 141     -59.170 -55.262 -53.888  1.00 77.54           C  
ANISOU 3968  CD  LYS B 141    10703  10487   8271  -1397  -1158   -870       C  
ATOM   3969  CE  LYS B 141     -59.450 -54.895 -55.338  1.00 79.18           C  
ANISOU 3969  CE  LYS B 141    10988  10897   8201  -1529  -1277   -852       C  
ATOM   3970  NZ  LYS B 141     -59.237 -56.039 -56.276  1.00 83.69           N  
ANISOU 3970  NZ  LYS B 141    11723  11442   8634  -1629  -1192  -1090       N  
ATOM   3971  N   GLU B 142     -59.671 -53.134 -48.983  1.00 53.08           N  
ANISOU 3971  N   GLU B 142     7004   7087   6076   -842  -1036   -330       N  
ATOM   3972  CA  GLU B 142     -60.836 -52.720 -48.208  1.00 55.11           C  
ANISOU 3972  CA  GLU B 142     7085   7343   6510   -828  -1125   -200       C  
ATOM   3973  C   GLU B 142     -60.576 -51.490 -47.343  1.00 52.65           C  
ANISOU 3973  C   GLU B 142     6667   7018   6318   -676  -1065    -60       C  
ATOM   3974  O   GLU B 142     -61.500 -50.705 -47.108  1.00 55.78           O  
ANISOU 3974  O   GLU B 142     6920   7454   6821   -658  -1151     73       O  
ATOM   3975  CB  GLU B 142     -61.317 -53.870 -47.331  1.00 61.13           C  
ANISOU 3975  CB  GLU B 142     7819   7983   7426   -860  -1081   -276       C  
ATOM   3976  CG  GLU B 142     -60.220 -54.593 -46.595  1.00 67.26           C  
ANISOU 3976  CG  GLU B 142     8683   8621   8253   -776   -903   -372       C  
ATOM   3977  CD  GLU B 142     -60.691 -55.933 -46.079  1.00 72.92           C  
ANISOU 3977  CD  GLU B 142     9408   9213   9084   -848   -879   -456       C  
ATOM   3978  OE1 GLU B 142     -61.610 -55.938 -45.229  1.00 64.73           O  
ANISOU 3978  OE1 GLU B 142     8242   8157   8196   -856   -908   -372       O  
ATOM   3979  OE2 GLU B 142     -60.161 -56.973 -46.540  1.00 72.22           O  
ANISOU 3979  OE2 GLU B 142     9453   9040   8945   -898   -821   -606       O  
ATOM   3980  N   CYS B 143     -59.362 -51.312 -46.831  1.00 39.27           N  
ANISOU 3980  N   CYS B 143     5032   5262   4625   -570   -917    -91       N  
ATOM   3981  CA  CYS B 143     -59.015 -50.100 -46.090  1.00 30.67           C  
ANISOU 3981  CA  CYS B 143     3864   4162   3628   -447   -861     20       C  
ATOM   3982  C   CYS B 143     -57.678 -49.598 -46.605  1.00 24.24           C  
ANISOU 3982  C   CYS B 143     3147   3373   2692   -401   -785      8       C  
ATOM   3983  O   CYS B 143     -56.623 -50.102 -46.181  1.00 29.72           O  
ANISOU 3983  O   CYS B 143     3904   4004   3385   -352   -659    -74       O  
ATOM   3984  CB  CYS B 143     -58.949 -50.330 -44.584  1.00 33.49           C  
ANISOU 3984  CB  CYS B 143     4161   4418   4144   -371   -755     10       C  
ATOM   3985  SG  CYS B 143     -58.681 -48.779 -43.693  1.00 35.17           S  
ANISOU 3985  SG  CYS B 143     4285   4620   4459   -249   -695    119       S  
ATOM   3986  N   PRO B 144     -57.676 -48.635 -47.525  1.00 30.32           N  
ANISOU 3986  N   PRO B 144     3920   4235   3365   -418   -857    103       N  
ATOM   3987  CA  PRO B 144     -56.406 -48.095 -48.027  1.00 25.59           C  
ANISOU 3987  CA  PRO B 144     3403   3666   2654   -383   -773    107       C  
ATOM   3988  C   PRO B 144     -55.597 -47.461 -46.909  1.00 32.62           C  
ANISOU 3988  C   PRO B 144     4246   4475   3673   -269   -657    134       C  
ATOM   3989  O   PRO B 144     -56.144 -46.984 -45.912  1.00 29.87           O  
ANISOU 3989  O   PRO B 144     3797   4071   3480   -215   -663    188       O  
ATOM   3990  CB  PRO B 144     -56.847 -47.045 -49.052  1.00 27.63           C  
ANISOU 3990  CB  PRO B 144     3644   4032   2822   -426   -897    253       C  
ATOM   3991  CG  PRO B 144     -58.240 -47.436 -49.433  1.00 38.70           C  
ANISOU 3991  CG  PRO B 144     4991   5487   4225   -516  -1059    281       C  
ATOM   3992  CD  PRO B 144     -58.843 -48.046 -48.204  1.00 33.50           C  
ANISOU 3992  CD  PRO B 144     4245   4724   3758   -478  -1025    226       C  
ATOM   3993  N   LEU B 145     -54.272 -47.428 -47.102  1.00 25.37           N  
ANISOU 3993  N   LEU B 145     3397   3559   2684   -239   -548     92       N  
ATOM   3994  CA  LEU B 145     -53.382 -46.895 -46.073  1.00 26.77           C  
ANISOU 3994  CA  LEU B 145     3531   3671   2968   -151   -450    109       C  
ATOM   3995  C   LEU B 145     -53.742 -45.466 -45.650  1.00 27.80           C  
ANISOU 3995  C   LEU B 145     3577   3785   3200   -113   -487    234       C  
ATOM   3996  O   LEU B 145     -53.552 -45.109 -44.485  1.00 25.80           O  
ANISOU 3996  O   LEU B 145     3269   3465   3067    -57   -435    232       O  
ATOM   3997  CB  LEU B 145     -51.936 -46.949 -46.566  1.00 33.39           C  
ANISOU 3997  CB  LEU B 145     4436   4535   3716   -138   -341     69       C  
ATOM   3998  CG  LEU B 145     -50.868 -46.407 -45.611  1.00 42.53           C  
ANISOU 3998  CG  LEU B 145     5543   5645   4972    -67   -253     90       C  
ATOM   3999  CD1 LEU B 145     -50.916 -47.081 -44.206  1.00 38.71           C  
ANISOU 3999  CD1 LEU B 145     5013   5082   4613    -21   -226     42       C  
ATOM   4000  CD2 LEU B 145     -49.475 -46.508 -46.248  1.00 43.52           C  
ANISOU 4000  CD2 LEU B 145     5712   5808   5017    -61   -145     60       C  
ATOM   4001  N   GLU B 146     -54.227 -44.623 -46.572  1.00 26.47           N  
ANISOU 4001  N   GLU B 146     3400   3672   2985   -144   -574    345       N  
ATOM   4002  CA  GLU B 146     -54.497 -43.231 -46.202  1.00 28.66           C  
ANISOU 4002  CA  GLU B 146     3597   3902   3392    -97   -594    467       C  
ATOM   4003  C   GLU B 146     -55.715 -43.082 -45.295  1.00 26.67           C  
ANISOU 4003  C   GLU B 146     3238   3585   3310    -59   -633    484       C  
ATOM   4004  O   GLU B 146     -55.964 -41.980 -44.792  1.00 25.78           O  
ANISOU 4004  O   GLU B 146     3055   3404   3339     -6   -620    555       O  
ATOM   4005  CB  GLU B 146     -54.666 -42.352 -47.462  1.00 21.29           C  
ANISOU 4005  CB  GLU B 146     2677   3036   2378   -136   -681    614       C  
ATOM   4006  CG  GLU B 146     -55.905 -42.615 -48.303  1.00 24.97           C  
ANISOU 4006  CG  GLU B 146     3120   3581   2788   -196   -834    684       C  
ATOM   4007  CD  GLU B 146     -55.700 -43.681 -49.386  1.00 34.75           C  
ANISOU 4007  CD  GLU B 146     4474   4938   3790   -298   -865    603       C  
ATOM   4008  OE1 GLU B 146     -54.706 -44.445 -49.325  1.00 30.24           O  
ANISOU 4008  OE1 GLU B 146     3991   4365   3135   -302   -746    465       O  
ATOM   4009  OE2 GLU B 146     -56.550 -43.757 -50.297  1.00 32.11           O  
ANISOU 4009  OE2 GLU B 146     4140   4699   3360   -376  -1007    676       O  
ATOM   4010  N   HIS B 147     -56.477 -44.152 -45.074  1.00 23.60           N  
ANISOU 4010  N   HIS B 147     2834   3210   2924    -89   -667    417       N  
ATOM   4011  CA  HIS B 147     -57.595 -44.129 -44.144  1.00 24.03           C  
ANISOU 4011  CA  HIS B 147     2779   3212   3140    -58   -677    424       C  
ATOM   4012  C   HIS B 147     -57.293 -44.902 -42.856  1.00 25.50           C  
ANISOU 4012  C   HIS B 147     2976   3346   3368    -38   -572    311       C  
ATOM   4013  O   HIS B 147     -58.217 -45.199 -42.097  1.00 29.09           O  
ANISOU 4013  O   HIS B 147     3355   3774   3925    -33   -565    299       O  
ATOM   4014  CB  HIS B 147     -58.847 -44.692 -44.817  1.00 20.27           C  
ANISOU 4014  CB  HIS B 147     2251   2796   2656   -123   -807    461       C  
ATOM   4015  CG  HIS B 147     -59.313 -43.900 -46.007  1.00 26.67           C  
ANISOU 4015  CG  HIS B 147     3030   3673   3431   -149   -939    606       C  
ATOM   4016  ND1 HIS B 147     -59.599 -42.551 -45.941  1.00 29.45           N  
ANISOU 4016  ND1 HIS B 147     3293   3978   3920    -79   -954    742       N  
ATOM   4017  CD2 HIS B 147     -59.569 -44.273 -47.284  1.00 30.77           C  
ANISOU 4017  CD2 HIS B 147     3597   4303   3792   -243  -1067    645       C  
ATOM   4018  CE1 HIS B 147     -59.994 -42.125 -47.129  1.00 30.26           C  
ANISOU 4018  CE1 HIS B 147     3381   4159   3957   -123  -1095    883       C  
ATOM   4019  NE2 HIS B 147     -59.979 -43.148 -47.964  1.00 32.93           N  
ANISOU 4019  NE2 HIS B 147     3805   4608   4097   -230  -1170    825       N  
ATOM   4020  N   ARG B 148     -56.029 -45.233 -42.592  1.00 24.79           N  
ANISOU 4020  N   ARG B 148     2968   3247   3205    -27   -490    244       N  
ATOM   4021  CA  ARG B 148     -55.643 -45.953 -41.382  1.00 23.92           C  
ANISOU 4021  CA  ARG B 148     2867   3097   3125    -10   -408    167       C  
ATOM   4022  C   ARG B 148     -54.944 -45.048 -40.376  1.00 21.79           C  
ANISOU 4022  C   ARG B 148     2582   2791   2907     35   -330    166       C  
ATOM   4023  O   ARG B 148     -54.193 -44.139 -40.742  1.00 22.79           O  
ANISOU 4023  O   ARG B 148     2726   2917   3017     49   -318    197       O  
ATOM   4024  CB  ARG B 148     -54.718 -47.125 -41.701  1.00 24.04           C  
ANISOU 4024  CB  ARG B 148     2968   3122   3044    -30   -377     96       C  
ATOM   4025  CG  ARG B 148     -55.308 -48.103 -42.688  1.00 23.45           C  
ANISOU 4025  CG  ARG B 148     2933   3072   2905    -92   -441     61       C  
ATOM   4026  CD  ARG B 148     -54.485 -49.372 -42.743  1.00 29.99           C  
ANISOU 4026  CD  ARG B 148     3839   3868   3687    -98   -381    -29       C  
ATOM   4027  NE  ARG B 148     -55.025 -50.315 -43.719  1.00 29.17           N  
ANISOU 4027  NE  ARG B 148     3792   3774   3516   -174   -432    -93       N  
ATOM   4028  CZ  ARG B 148     -54.983 -51.634 -43.581  1.00 33.85           C  
ANISOU 4028  CZ  ARG B 148     4431   4300   4130   -198   -399   -178       C  
ATOM   4029  NH1 ARG B 148     -54.435 -52.172 -42.492  1.00 27.94           N  
ANISOU 4029  NH1 ARG B 148     3670   3476   3470   -144   -323   -180       N  
ATOM   4030  NH2 ARG B 148     -55.494 -52.414 -44.529  1.00 29.37           N  
ANISOU 4030  NH2 ARG B 148     3927   3738   3496   -286   -448   -254       N  
ATOM   4031  N   ALA B 149     -55.162 -45.351 -39.093  1.00 23.53           N  
ANISOU 4031  N   ALA B 149     2778   2986   3178     43   -276    127       N  
ATOM   4032  CA  ALA B 149     -54.483 -44.678 -37.997  1.00 24.09           C  
ANISOU 4032  CA  ALA B 149     2850   3037   3266     61   -205    102       C  
ATOM   4033  C   ALA B 149     -53.147 -45.350 -37.695  1.00 27.72           C  
ANISOU 4033  C   ALA B 149     3363   3520   3649     55   -182     77       C  
ATOM   4034  O   ALA B 149     -52.997 -46.571 -37.814  1.00 24.10           O  
ANISOU 4034  O   ALA B 149     2930   3069   3156     48   -190     65       O  
ATOM   4035  CB  ALA B 149     -55.341 -44.679 -36.734  1.00 23.02           C  
ANISOU 4035  CB  ALA B 149     2670   2884   3193     59   -152     73       C  
ATOM   4036  N   TRP B 150     -52.182 -44.535 -37.279  1.00 24.54           N  
ANISOU 4036  N   TRP B 150     2967   3119   3239     56   -152     71       N  
ATOM   4037  CA  TRP B 150     -50.820 -44.988 -37.034  1.00 20.40           C  
ANISOU 4037  CA  TRP B 150     2463   2625   2662     53   -140     67       C  
ATOM   4038  C   TRP B 150     -50.223 -44.085 -35.964  1.00 21.68           C  
ANISOU 4038  C   TRP B 150     2615   2793   2829     28   -115     47       C  
ATOM   4039  O   TRP B 150     -50.456 -42.877 -35.983  1.00 21.34           O  
ANISOU 4039  O   TRP B 150     2564   2714   2829     19   -100     35       O  
ATOM   4040  CB  TRP B 150     -50.007 -44.951 -38.335  1.00 20.65           C  
ANISOU 4040  CB  TRP B 150     2513   2672   2661     64   -146     90       C  
ATOM   4041  CG  TRP B 150     -48.506 -45.146 -38.208  1.00 23.10           C  
ANISOU 4041  CG  TRP B 150     2814   3012   2950     69   -121     96       C  
ATOM   4042  CD1 TRP B 150     -47.816 -46.324 -38.315  1.00 23.79           C  
ANISOU 4042  CD1 TRP B 150     2902   3110   3027     96   -104     93       C  
ATOM   4043  CD2 TRP B 150     -47.516 -44.117 -38.036  1.00 21.88           C  
ANISOU 4043  CD2 TRP B 150     2634   2873   2807     47   -107    113       C  
ATOM   4044  NE1 TRP B 150     -46.464 -46.097 -38.184  1.00 20.33           N  
ANISOU 4044  NE1 TRP B 150     2424   2703   2598    100    -82    117       N  
ATOM   4045  CE2 TRP B 150     -46.253 -44.752 -38.005  1.00 22.67           C  
ANISOU 4045  CE2 TRP B 150     2704   3009   2900     61    -89    128       C  
ATOM   4046  CE3 TRP B 150     -47.579 -42.723 -37.892  1.00 21.56           C  
ANISOU 4046  CE3 TRP B 150     2587   2805   2800     15   -106    117       C  
ATOM   4047  CZ2 TRP B 150     -45.054 -44.037 -37.854  1.00 19.83           C  
ANISOU 4047  CZ2 TRP B 150     2297   2679   2557     33    -79    152       C  
ATOM   4048  CZ3 TRP B 150     -46.395 -42.015 -37.708  1.00 24.53           C  
ANISOU 4048  CZ3 TRP B 150     2935   3197   3189    -21    -94    129       C  
ATOM   4049  CH2 TRP B 150     -45.146 -42.673 -37.703  1.00 22.05           C  
ANISOU 4049  CH2 TRP B 150     2581   2939   2859    -17    -86    149       C  
ATOM   4050  N   ASN B 151     -49.504 -44.685 -35.005  1.00 24.07           N  
ANISOU 4050  N   ASN B 151     2918   3137   3091     10   -116     46       N  
ATOM   4051  CA  ASN B 151     -48.824 -43.949 -33.929  1.00 23.52           C  
ANISOU 4051  CA  ASN B 151     2845   3097   2993    -40   -111     22       C  
ATOM   4052  C   ASN B 151     -49.813 -43.250 -32.998  1.00 26.91           C  
ANISOU 4052  C   ASN B 151     3291   3506   3427    -72    -68    -41       C  
ATOM   4053  O   ASN B 151     -49.560 -42.140 -32.530  1.00 23.77           O  
ANISOU 4053  O   ASN B 151     2904   3093   3035   -115    -45    -95       O  
ATOM   4054  CB  ASN B 151     -47.800 -42.944 -34.493  1.00 23.04           C  
ANISOU 4054  CB  ASN B 151     2769   3031   2955    -58   -115     27       C  
ATOM   4055  CG  ASN B 151     -46.628 -42.693 -33.532  1.00 32.34           C  
ANISOU 4055  CG  ASN B 151     3928   4268   4093   -120   -141     22       C  
ATOM   4056  OD1 ASN B 151     -46.274 -43.562 -32.739  1.00 26.47           O  
ANISOU 4056  OD1 ASN B 151     3173   3585   3299   -130   -173     50       O  
ATOM   4057  ND2 ASN B 151     -46.035 -41.499 -33.601  1.00 26.74           N  
ANISOU 4057  ND2 ASN B 151     3211   3538   3411   -170   -136     -3       N  
ATOM   4058  N   SER B 152     -50.934 -43.909 -32.704  1.00 19.61           N  
ANISOU 4058  N   SER B 152     2366   2577   2507    -58    -46    -43       N  
ATOM   4059  CA  SER B 152     -51.956 -43.324 -31.841  1.00 24.58           C  
ANISOU 4059  CA  SER B 152     2999   3190   3151    -80     22   -108       C  
ATOM   4060  C   SER B 152     -51.700 -43.570 -30.361  1.00 25.25           C  
ANISOU 4060  C   SER B 152     3118   3351   3126   -149     46   -139       C  
ATOM   4061  O   SER B 152     -52.337 -42.921 -29.527  1.00 26.20           O  
ANISOU 4061  O   SER B 152     3255   3466   3233   -183    125   -219       O  
ATOM   4062  CB  SER B 152     -53.342 -43.874 -32.201  1.00 25.09           C  
ANISOU 4062  CB  SER B 152     3028   3225   3281    -43     43    -88       C  
ATOM   4063  OG  SER B 152     -53.631 -43.659 -33.578  1.00 26.69           O  
ANISOU 4063  OG  SER B 152     3202   3378   3561      5      1    -49       O  
ATOM   4064  N   PHE B 153     -50.794 -44.486 -30.022  1.00 24.82           N  
ANISOU 4064  N   PHE B 153     3072   3365   2992   -170    -16    -73       N  
ATOM   4065  CA  PHE B 153     -50.564 -44.914 -28.647  1.00 25.70           C  
ANISOU 4065  CA  PHE B 153     3215   3570   2979   -243    -18    -62       C  
ATOM   4066  C   PHE B 153     -49.341 -44.230 -28.048  1.00 27.88           C  
ANISOU 4066  C   PHE B 153     3509   3912   3174   -315    -66    -87       C  
ATOM   4067  O   PHE B 153     -48.393 -43.869 -28.755  1.00 22.64           O  
ANISOU 4067  O   PHE B 153     2815   3229   2559   -298   -116    -70       O  
ATOM   4068  CB  PHE B 153     -50.356 -46.429 -28.563  1.00 23.10           C  
ANISOU 4068  CB  PHE B 153     2873   3272   2631   -223    -72     58       C  
ATOM   4069  CG  PHE B 153     -51.586 -47.241 -28.861  1.00 21.77           C  
ANISOU 4069  CG  PHE B 153     2695   3053   2523   -188    -29     80       C  
ATOM   4070  CD1 PHE B 153     -52.724 -47.117 -28.084  1.00 30.55           C  
ANISOU 4070  CD1 PHE B 153     3819   4184   3605   -228     53     41       C  
ATOM   4071  CD2 PHE B 153     -51.595 -48.145 -29.923  1.00 31.68           C  
ANISOU 4071  CD2 PHE B 153     3927   4243   3867   -125    -64    134       C  
ATOM   4072  CE1 PHE B 153     -53.867 -47.864 -28.355  1.00 30.38           C  
ANISOU 4072  CE1 PHE B 153     3769   4120   3654   -208     89     70       C  
ATOM   4073  CE2 PHE B 153     -52.732 -48.899 -30.197  1.00 36.96           C  
ANISOU 4073  CE2 PHE B 153     4585   4863   4593   -115    -37    148       C  
ATOM   4074  CZ  PHE B 153     -53.876 -48.753 -29.406  1.00 32.50           C  
ANISOU 4074  CZ  PHE B 153     4015   4322   4011   -158     34    125       C  
ATOM   4075  N   LEU B 154     -49.376 -44.078 -26.720  1.00 27.92           N  
ANISOU 4075  N   LEU B 154     3562   4005   3042   -410    -49   -127       N  
ATOM   4076  CA  LEU B 154     -48.218 -43.776 -25.889  1.00 27.10           C  
ANISOU 4076  CA  LEU B 154     3475   4006   2816   -510   -126   -126       C  
ATOM   4077  C   LEU B 154     -48.176 -44.768 -24.738  1.00 27.30           C  
ANISOU 4077  C   LEU B 154     3525   4158   2689   -573   -169    -34       C  
ATOM   4078  O   LEU B 154     -49.220 -45.138 -24.191  1.00 30.66           O  
ANISOU 4078  O   LEU B 154     3990   4598   3062   -585    -89    -46       O  
ATOM   4079  CB  LEU B 154     -48.264 -42.350 -25.314  1.00 33.29           C  
ANISOU 4079  CB  LEU B 154     4317   4783   3548   -603    -66   -292       C  
ATOM   4080  CG  LEU B 154     -47.687 -41.238 -26.200  1.00 33.90           C  
ANISOU 4080  CG  LEU B 154     4370   4762   3750   -589    -73   -351       C  
ATOM   4081  CD1 LEU B 154     -47.736 -39.904 -25.471  1.00 36.04           C  
ANISOU 4081  CD1 LEU B 154     4710   5009   3974   -696     -8   -526       C  
ATOM   4082  CD2 LEU B 154     -46.256 -41.581 -26.656  1.00 28.88           C  
ANISOU 4082  CD2 LEU B 154     3665   4178   3131   -591   -201   -238       C  
ATOM   4083  N   VAL B 155     -46.972 -45.201 -24.377  1.00 25.27           N  
ANISOU 4083  N   VAL B 155     3236   3997   2370   -614   -296     75       N  
ATOM   4084  CA  VAL B 155     -46.814 -46.046 -23.203  1.00 26.44           C  
ANISOU 4084  CA  VAL B 155     3407   4281   2358   -688   -360    189       C  
ATOM   4085  C   VAL B 155     -47.138 -45.210 -21.974  1.00 34.75           C  
ANISOU 4085  C   VAL B 155     4558   5440   3205   -839   -313     59       C  
ATOM   4086  O   VAL B 155     -46.504 -44.178 -21.729  1.00 34.92           O  
ANISOU 4086  O   VAL B 155     4601   5498   3170   -928   -343    -49       O  
ATOM   4087  CB  VAL B 155     -45.394 -46.622 -23.125  1.00 28.59           C  
ANISOU 4087  CB  VAL B 155     3598   4630   2634   -693   -522    352       C  
ATOM   4088  CG1 VAL B 155     -45.155 -47.274 -21.763  1.00 29.57           C  
ANISOU 4088  CG1 VAL B 155     3750   4920   2564   -799   -613    482       C  
ATOM   4089  CG2 VAL B 155     -45.167 -47.624 -24.260  1.00 30.37           C  
ANISOU 4089  CG2 VAL B 155     3736   4741   3061   -538   -535    471       C  
ATOM   4090  N   GLU B 156     -48.150 -45.643 -21.221  1.00 29.43           N  
ANISOU 4090  N   GLU B 156     3946   4811   2423   -874   -226     59       N  
ATOM   4091  CA  GLU B 156     -48.575 -44.977 -19.995  1.00 32.85           C  
ANISOU 4091  CA  GLU B 156     4487   5357   2639  -1020   -148    -74       C  
ATOM   4092  C   GLU B 156     -47.691 -45.360 -18.819  1.00 38.58           C  
ANISOU 4092  C   GLU B 156     5247   6288   3122  -1166   -289     37       C  
ATOM   4093  O   GLU B 156     -47.344 -44.507 -17.993  1.00 44.08           O  
ANISOU 4093  O   GLU B 156     6023   7094   3632  -1316   -299    -91       O  
ATOM   4094  CB  GLU B 156     -50.032 -45.345 -19.693  1.00 32.34           C  
ANISOU 4094  CB  GLU B 156     4459   5268   2560   -999     17   -105       C  
ATOM   4095  CG  GLU B 156     -50.595 -44.735 -18.414  1.00 50.46           C  
ANISOU 4095  CG  GLU B 156     6869   7681   4623  -1145    141   -253       C  
ATOM   4096  CD  GLU B 156     -50.944 -43.261 -18.565  1.00 62.60           C  
ANISOU 4096  CD  GLU B 156     8446   9121   6217  -1157    277   -514       C  
ATOM   4097  OE1 GLU B 156     -51.611 -42.711 -17.666  1.00 64.81           O  
ANISOU 4097  OE1 GLU B 156     8815   9454   6354  -1250    431   -675       O  
ATOM   4098  OE2 GLU B 156     -50.557 -42.649 -19.585  1.00 62.33           O  
ANISOU 4098  OE2 GLU B 156     8355   8950   6378  -1072    241   -558       O  
ATOM   4099  N   ASP B 157     -47.336 -46.638 -18.720  1.00 35.96           N  
ANISOU 4099  N   ASP B 157     4862   6008   2793  -1129   -401    276       N  
ATOM   4100  CA  ASP B 157     -46.538 -47.132 -17.606  1.00 39.03           C  
ANISOU 4100  CA  ASP B 157     5269   6598   2962  -1258   -556    434       C  
ATOM   4101  C   ASP B 157     -46.133 -48.566 -17.917  1.00 35.45           C  
ANISOU 4101  C   ASP B 157     4717   6116   2635  -1152   -669    714       C  
ATOM   4102  O   ASP B 157     -46.656 -49.193 -18.845  1.00 34.31           O  
ANISOU 4102  O   ASP B 157     4522   5805   2708  -1003   -600    752       O  
ATOM   4103  CB  ASP B 157     -47.313 -47.057 -16.286  1.00 43.08           C  
ANISOU 4103  CB  ASP B 157     5915   7266   3187  -1414   -466    379       C  
ATOM   4104  CG  ASP B 157     -46.399 -47.070 -15.083  1.00 56.04           C  
ANISOU 4104  CG  ASP B 157     7568   9055   4669  -1540   -601    453       C  
ATOM   4105  OD1 ASP B 157     -45.176 -46.874 -15.265  1.00 61.78           O  
ANISOU 4105  OD1 ASP B 157     8216   9800   5456  -1546   -761    509       O  
ATOM   4106  OD2 ASP B 157     -46.897 -47.270 -13.957  1.00 74.25           O  
ANISOU 4106  OD2 ASP B 157     9954  11457   6802  -1634   -542    457       O  
ATOM   4107  N   HIS B 158     -45.173 -49.062 -17.145  1.00 35.89           N  
ANISOU 4107  N   HIS B 158     4742   6323   2573  -1229   -846    904       N  
ATOM   4108  CA  HIS B 158     -44.840 -50.476 -17.086  1.00 42.25           C  
ANISOU 4108  CA  HIS B 158     5463   7094   3495  -1141   -937   1178       C  
ATOM   4109  C   HIS B 158     -45.530 -51.096 -15.882  1.00 43.68           C  
ANISOU 4109  C   HIS B 158     5726   7357   3512  -1226   -890   1259       C  
ATOM   4110  O   HIS B 158     -45.823 -50.414 -14.899  1.00 48.45           O  
ANISOU 4110  O   HIS B 158     6429   8082   3898  -1368   -838   1129       O  
ATOM   4111  CB  HIS B 158     -43.322 -50.679 -17.002  1.00 36.10           C  
ANISOU 4111  CB  HIS B 158     4558   6346   2814  -1121  -1116   1316       C  
ATOM   4112  CG  HIS B 158     -42.624 -50.433 -18.306  1.00 41.26           C  
ANISOU 4112  CG  HIS B 158     5097   6893   3687  -1000  -1154   1297       C  
ATOM   4113  ND1 HIS B 158     -42.554 -49.186 -18.889  1.00 44.53           N  
ANISOU 4113  ND1 HIS B 158     5529   7304   4088  -1036  -1118   1086       N  
ATOM   4114  CD2 HIS B 158     -41.998 -51.280 -19.157  1.00 41.62           C  
ANISOU 4114  CD2 HIS B 158     5009   6821   3983   -842  -1206   1453       C  
ATOM   4115  CE1 HIS B 158     -41.907 -49.273 -20.039  1.00 44.19           C  
ANISOU 4115  CE1 HIS B 158     5366   7130   4296   -897  -1128   1104       C  
ATOM   4116  NE2 HIS B 158     -41.556 -50.532 -20.224  1.00 45.00           N  
ANISOU 4116  NE2 HIS B 158     5375   7182   4542   -783  -1190   1329       N  
ATOM   4117  N   GLY B 159     -45.799 -52.387 -15.963  1.00 46.13           N  
ANISOU 4117  N   GLY B 159     5998   7592   3938  -1142   -899   1468       N  
ATOM   4118  CA  GLY B 159     -46.421 -53.104 -14.860  1.00 48.90           C  
ANISOU 4118  CA  GLY B 159     6413   8011   4156  -1218   -862   1578       C  
ATOM   4119  C   GLY B 159     -45.662 -54.360 -14.490  1.00 44.19           C  
ANISOU 4119  C   GLY B 159     5728   7393   3670  -1168  -1002   1857       C  
ATOM   4120  O   GLY B 159     -45.176 -55.083 -15.357  1.00 43.93           O  
ANISOU 4120  O   GLY B 159     5590   7214   3887  -1025  -1057   1982       O  
ATOM   4121  N   PHE B 160     -45.573 -54.615 -13.188  1.00 44.07           N  
ANISOU 4121  N   PHE B 160     5755   7519   3470  -1287  -1050   1950       N  
ATOM   4122  CA  PHE B 160     -44.912 -55.823 -12.713  1.00 50.12           C  
ANISOU 4122  CA  PHE B 160     6440   8273   4328  -1252  -1179   2228       C  
ATOM   4123  C   PHE B 160     -45.637 -57.071 -13.208  1.00 55.80           C  
ANISOU 4123  C   PHE B 160     7143   8816   5244  -1137  -1108   2375       C  
ATOM   4124  O   PHE B 160     -46.865 -57.103 -13.328  1.00 50.21           O  
ANISOU 4124  O   PHE B 160     6518   8066   4494  -1154   -956   2298       O  
ATOM   4125  CB  PHE B 160     -44.851 -55.850 -11.186  1.00 52.70           C  
ANISOU 4125  CB  PHE B 160     6835   8799   4389  -1418  -1233   2301       C  
ATOM   4126  CG  PHE B 160     -44.391 -57.171 -10.627  1.00 54.36           C  
ANISOU 4126  CG  PHE B 160     6975   8997   4682  -1390  -1348   2604       C  
ATOM   4127  CD1 PHE B 160     -43.042 -57.477 -10.566  1.00 55.54           C  
ANISOU 4127  CD1 PHE B 160     6994   9162   4946  -1354  -1527   2765       C  
ATOM   4128  CD2 PHE B 160     -45.308 -58.113 -10.186  1.00 56.71           C  
ANISOU 4128  CD2 PHE B 160     7328   9258   4961  -1398  -1272   2734       C  
ATOM   4129  CE1 PHE B 160     -42.613 -58.692 -10.061  1.00 62.04           C  
ANISOU 4129  CE1 PHE B 160     7745   9964   5865  -1322  -1629   3049       C  
ATOM   4130  CE2 PHE B 160     -44.889 -59.330  -9.682  1.00 63.53           C  
ANISOU 4130  CE2 PHE B 160     8127  10096   5914  -1372  -1376   3018       C  
ATOM   4131  CZ  PHE B 160     -43.539 -59.621  -9.619  1.00 68.24           C  
ANISOU 4131  CZ  PHE B 160     8594  10706   6627  -1330  -1557   3176       C  
ATOM   4132  N   GLY B 161     -44.857 -58.112 -13.477  1.00 58.66           N  
ANISOU 4132  N   GLY B 161     7389   9064   5834  -1025  -1212   2587       N  
ATOM   4133  CA  GLY B 161     -45.409 -59.407 -13.821  1.00 62.83           C  
ANISOU 4133  CA  GLY B 161     7899   9408   6566   -927  -1159   2743       C  
ATOM   4134  C   GLY B 161     -44.380 -60.482 -13.571  1.00 65.52           C  
ANISOU 4134  C   GLY B 161     8122   9688   7083   -854  -1295   2993       C  
ATOM   4135  O   GLY B 161     -43.177 -60.256 -13.733  1.00 60.66           O  
ANISOU 4135  O   GLY B 161     7400   9098   6548   -811  -1410   3023       O  
ATOM   4136  N   VAL B 162     -44.857 -61.665 -13.175  1.00 60.81           N  
ANISOU 4136  N   VAL B 162     7539   9005   6561   -841  -1274   3177       N  
ATOM   4137  CA  VAL B 162     -43.949 -62.755 -12.818  1.00 57.97           C  
ANISOU 4137  CA  VAL B 162     7072   8586   6369   -778  -1397   3434       C  
ATOM   4138  C   VAL B 162     -43.216 -63.278 -14.052  1.00 57.65           C  
ANISOU 4138  C   VAL B 162     6903   8314   6688   -585  -1403   3449       C  
ATOM   4139  O   VAL B 162     -41.996 -63.483 -14.027  1.00 60.03           O  
ANISOU 4139  O   VAL B 162     7077   8619   7114   -525  -1518   3561       O  
ATOM   4140  CB  VAL B 162     -44.717 -63.881 -12.101  1.00 66.03           C  
ANISOU 4140  CB  VAL B 162     8147   9558   7382   -818  -1362   3622       C  
ATOM   4141  CG1 VAL B 162     -43.769 -65.006 -11.702  1.00 61.66           C  
ANISOU 4141  CG1 VAL B 162     7479   8941   7010   -754  -1492   3901       C  
ATOM   4142  CG2 VAL B 162     -45.450 -63.332 -10.882  1.00 78.41           C  
ANISOU 4142  CG2 VAL B 162     9845  11363   8583  -1012  -1334   3592       C  
ATOM   4143  N   PHE B 163     -43.947 -63.504 -15.146  1.00 50.94           N  
ANISOU 4143  N   PHE B 163     6082   7262   6011   -488  -1271   3334       N  
ATOM   4144  CA  PHE B 163     -43.380 -64.097 -16.353  1.00 55.22           C  
ANISOU 4144  CA  PHE B 163     6523   7562   6897   -305  -1245   3328       C  
ATOM   4145  C   PHE B 163     -43.138 -63.090 -17.463  1.00 54.35           C  
ANISOU 4145  C   PHE B 163     6392   7437   6823   -244  -1203   3106       C  
ATOM   4146  O   PHE B 163     -42.230 -63.289 -18.278  1.00 54.27           O  
ANISOU 4146  O   PHE B 163     6271   7305   7044   -109  -1215   3098       O  
ATOM   4147  CB  PHE B 163     -44.294 -65.209 -16.879  1.00 55.97           C  
ANISOU 4147  CB  PHE B 163     6662   7408   7196   -238  -1129   3359       C  
ATOM   4148  CG  PHE B 163     -44.488 -66.338 -15.908  1.00 64.04           C  
ANISOU 4148  CG  PHE B 163     7693   8405   8235   -280  -1164   3594       C  
ATOM   4149  CD1 PHE B 163     -43.475 -67.263 -15.681  1.00 64.97           C  
ANISOU 4149  CD1 PHE B 163     7695   8440   8552   -194  -1253   3795       C  
ATOM   4150  CD2 PHE B 163     -45.677 -66.472 -15.212  1.00 68.66           C  
ANISOU 4150  CD2 PHE B 163     8395   9051   8641   -406  -1102   3621       C  
ATOM   4151  CE1 PHE B 163     -43.646 -68.302 -14.783  1.00 73.15           C  
ANISOU 4151  CE1 PHE B 163     8737   9450   9607   -233  -1292   4029       C  
ATOM   4152  CE2 PHE B 163     -45.855 -67.510 -14.309  1.00 73.86           C  
ANISOU 4152  CE2 PHE B 163     9063   9689   9310   -450  -1133   3848       C  
ATOM   4153  CZ  PHE B 163     -44.837 -68.427 -14.095  1.00 76.62           C  
ANISOU 4153  CZ  PHE B 163     9302   9952   9858   -363  -1235   4058       C  
ATOM   4154  N   HIS B 164     -43.933 -62.024 -17.517  1.00 46.38           N  
ANISOU 4154  N   HIS B 164     5484   6543   5595   -338  -1144   2927       N  
ATOM   4155  CA  HIS B 164     -43.737 -60.950 -18.479  1.00 46.10           C  
ANISOU 4155  CA  HIS B 164     5436   6517   5562   -299  -1114   2724       C  
ATOM   4156  C   HIS B 164     -43.979 -59.612 -17.797  1.00 52.28           C  
ANISOU 4156  C   HIS B 164     6297   7546   6019   -457  -1134   2595       C  
ATOM   4157  O   HIS B 164     -44.827 -59.495 -16.909  1.00 53.93           O  
ANISOU 4157  O   HIS B 164     6610   7870   6010   -586  -1098   2595       O  
ATOM   4158  CB  HIS B 164     -44.666 -61.092 -19.697  1.00 50.19           C  
ANISOU 4158  CB  HIS B 164     6002   6839   6229   -217   -978   2598       C  
ATOM   4159  CG  HIS B 164     -44.549 -62.415 -20.382  1.00 70.47           C  
ANISOU 4159  CG  HIS B 164     8519   9143   9115    -77   -933   2682       C  
ATOM   4160  ND1 HIS B 164     -45.173 -63.552 -19.914  1.00 76.53           N  
ANISOU 4160  ND1 HIS B 164     9325   9803   9951    -95   -901   2816       N  
ATOM   4161  CD2 HIS B 164     -43.860 -62.790 -21.486  1.00 76.93           C  
ANISOU 4161  CD2 HIS B 164     9252   9777  10200     78   -904   2638       C  
ATOM   4162  CE1 HIS B 164     -44.884 -64.567 -20.709  1.00 84.60           C  
ANISOU 4162  CE1 HIS B 164    10294  10577  11274     40   -857   2841       C  
ATOM   4163  NE2 HIS B 164     -44.088 -64.132 -21.670  1.00 83.05           N  
ANISOU 4163  NE2 HIS B 164    10025  10332  11200    149   -851   2728       N  
ATOM   4164  N   THR B 165     -43.226 -58.605 -18.225  1.00 47.87           N  
ANISOU 4164  N   THR B 165     5690   7062   5437   -449  -1178   2473       N  
ATOM   4165  CA  THR B 165     -43.430 -57.244 -17.758  1.00 40.80           C  
ANISOU 4165  CA  THR B 165     4872   6365   4263   -592  -1180   2306       C  
ATOM   4166  C   THR B 165     -44.416 -56.560 -18.689  1.00 37.46           C  
ANISOU 4166  C   THR B 165     4524   5881   3826   -574  -1053   2112       C  
ATOM   4167  O   THR B 165     -44.245 -56.581 -19.912  1.00 38.90           O  
ANISOU 4167  O   THR B 165     4649   5920   4210   -447  -1024   2063       O  
ATOM   4168  CB  THR B 165     -42.107 -56.482 -17.697  1.00 43.67           C  
ANISOU 4168  CB  THR B 165     5144   6836   4614   -611  -1296   2276       C  
ATOM   4169  OG1 THR B 165     -41.282 -57.075 -16.688  1.00 42.41           O  
ANISOU 4169  OG1 THR B 165     4920   6760   4434   -654  -1420   2468       O  
ATOM   4170  CG2 THR B 165     -42.342 -55.006 -17.368  1.00 39.40           C  
ANISOU 4170  CG2 THR B 165     4692   6461   3815   -757  -1280   2062       C  
ATOM   4171  N   SER B 166     -45.469 -55.993 -18.108  1.00 37.84           N  
ANISOU 4171  N   SER B 166     4697   6037   3643   -701   -968   2005       N  
ATOM   4172  CA  SER B 166     -46.515 -55.356 -18.895  1.00 35.26           C  
ANISOU 4172  CA  SER B 166     4434   5640   3321   -688   -819   1794       C  
ATOM   4173  C   SER B 166     -46.094 -53.956 -19.306  1.00 32.00           C  
ANISOU 4173  C   SER B 166     4019   5282   2859   -707   -812   1561       C  
ATOM   4174  O   SER B 166     -45.421 -53.241 -18.555  1.00 36.98           O  
ANISOU 4174  O   SER B 166     4660   6091   3297   -820   -907   1555       O  
ATOM   4175  CB  SER B 166     -47.824 -55.285 -18.108  1.00 40.09           C  
ANISOU 4175  CB  SER B 166     5162   6328   3743   -807   -693   1744       C  
ATOM   4176  OG  SER B 166     -48.242 -56.573 -17.712  1.00 46.28           O  
ANISOU 4176  OG  SER B 166     5951   7057   4577   -805   -693   1969       O  
ATOM   4177  N   VAL B 167     -46.505 -53.574 -20.506  1.00 29.72           N  
ANISOU 4177  N   VAL B 167     3716   4836   2741   -607   -703   1377       N  
ATOM   4178  CA  VAL B 167     -46.319 -52.238 -21.045  1.00 36.43           C  
ANISOU 4178  CA  VAL B 167     4569   5695   3577   -615   -667   1152       C  
ATOM   4179  C   VAL B 167     -47.706 -51.737 -21.442  1.00 33.32           C  
ANISOU 4179  C   VAL B 167     4244   5222   3193   -612   -496    958       C  
ATOM   4180  O   VAL B 167     -48.286 -52.217 -22.423  1.00 34.71           O  
ANISOU 4180  O   VAL B 167     4397   5241   3552   -508   -426    932       O  
ATOM   4181  CB  VAL B 167     -45.354 -52.243 -22.240  1.00 33.92           C  
ANISOU 4181  CB  VAL B 167     4146   5265   3477   -487   -712   1148       C  
ATOM   4182  CG1 VAL B 167     -45.078 -50.834 -22.708  1.00 32.01           C  
ANISOU 4182  CG1 VAL B 167     3907   5043   3212   -514   -685    947       C  
ATOM   4183  CG2 VAL B 167     -44.049 -52.981 -21.873  1.00 32.66           C  
ANISOU 4183  CG2 VAL B 167     3882   5160   3365   -463   -872   1378       C  
ATOM   4184  N   TRP B 168     -48.246 -50.791 -20.675  1.00 34.20           N  
ANISOU 4184  N   TRP B 168     4437   5443   3115   -728   -427    821       N  
ATOM   4185  CA  TRP B 168     -49.620 -50.323 -20.860  1.00 27.00           C  
ANISOU 4185  CA  TRP B 168     3573   4469   2215   -728   -256    657       C  
ATOM   4186  C   TRP B 168     -49.668 -49.197 -21.883  1.00 29.27           C  
ANISOU 4186  C   TRP B 168     3840   4657   2626   -665   -203    463       C  
ATOM   4187  O   TRP B 168     -48.966 -48.191 -21.739  1.00 32.40           O  
ANISOU 4187  O   TRP B 168     4249   5107   2956   -715   -239    368       O  
ATOM   4188  CB  TRP B 168     -50.207 -49.822 -19.539  1.00 31.45           C  
ANISOU 4188  CB  TRP B 168     4232   5187   2529   -876   -176    588       C  
ATOM   4189  CG  TRP B 168     -50.116 -50.801 -18.424  1.00 41.63           C  
ANISOU 4189  CG  TRP B 168     5556   6609   3651   -966   -234    792       C  
ATOM   4190  CD1 TRP B 168     -49.284 -50.751 -17.345  1.00 40.78           C  
ANISOU 4190  CD1 TRP B 168     5492   6691   3313  -1093   -352    884       C  
ATOM   4191  CD2 TRP B 168     -50.894 -51.986 -18.280  1.00 41.99           C  
ANISOU 4191  CD2 TRP B 168     5597   6611   3746   -948   -187    945       C  
ATOM   4192  NE1 TRP B 168     -49.497 -51.836 -16.532  1.00 46.67           N  
ANISOU 4192  NE1 TRP B 168     6262   7518   3953  -1149   -382   1102       N  
ATOM   4193  CE2 TRP B 168     -50.483 -52.612 -17.087  1.00 45.75           C  
ANISOU 4193  CE2 TRP B 168     6117   7251   4016  -1060   -275   1143       C  
ATOM   4194  CE3 TRP B 168     -51.903 -52.579 -19.048  1.00 35.95           C  
ANISOU 4194  CE3 TRP B 168     4793   5686   3181   -859    -88    941       C  
ATOM   4195  CZ2 TRP B 168     -51.046 -53.802 -16.637  1.00 45.56           C  
ANISOU 4195  CZ2 TRP B 168     6101   7221   3988  -1081   -254   1344       C  
ATOM   4196  CZ3 TRP B 168     -52.463 -53.764 -18.596  1.00 46.92           C  
ANISOU 4196  CZ3 TRP B 168     6188   7067   4572   -887    -67   1123       C  
ATOM   4197  CH2 TRP B 168     -52.031 -54.361 -17.408  1.00 45.50           C  
ANISOU 4197  CH2 TRP B 168     6055   7038   4196   -993   -143   1325       C  
ATOM   4198  N   LEU B 169     -50.504 -49.361 -22.905  1.00 31.95           N  
ANISOU 4198  N   LEU B 169     4146   4852   3142   -566   -124    415       N  
ATOM   4199  CA  LEU B 169     -50.634 -48.386 -23.976  1.00 30.17           C  
ANISOU 4199  CA  LEU B 169     3895   4525   3043   -499    -81    268       C  
ATOM   4200  C   LEU B 169     -51.961 -47.640 -23.866  1.00 37.25           C  
ANISOU 4200  C   LEU B 169     4815   5390   3947   -514     67    124       C  
ATOM   4201  O   LEU B 169     -53.012 -48.240 -23.610  1.00 30.81           O  
ANISOU 4201  O   LEU B 169     3997   4567   3142   -518    144    154       O  
ATOM   4202  CB  LEU B 169     -50.523 -49.057 -25.344  1.00 27.52           C  
ANISOU 4202  CB  LEU B 169     3498   4058   2899   -380   -116    322       C  
ATOM   4203  CG  LEU B 169     -49.130 -49.120 -25.995  1.00 34.97           C  
ANISOU 4203  CG  LEU B 169     4395   4987   3905   -329   -219    375       C  
ATOM   4204  CD1 LEU B 169     -48.109 -49.835 -25.146  1.00 44.31           C  
ANISOU 4204  CD1 LEU B 169     5561   6264   5012   -365   -324    527       C  
ATOM   4205  CD2 LEU B 169     -49.204 -49.771 -27.381  1.00 40.10           C  
ANISOU 4205  CD2 LEU B 169     5004   5506   4725   -219   -215    392       C  
ATOM   4206  N   LYS B 170     -51.904 -46.329 -24.073  1.00 30.43           N  
ANISOU 4206  N   LYS B 170     3963   4499   3101   -518    111    -25       N  
ATOM   4207  CA  LYS B 170     -53.072 -45.471 -24.004  1.00 29.00           C  
ANISOU 4207  CA  LYS B 170     3788   4266   2965   -514    258   -166       C  
ATOM   4208  C   LYS B 170     -53.154 -44.643 -25.280  1.00 28.84           C  
ANISOU 4208  C   LYS B 170     3717   4111   3128   -421    260   -231       C  
ATOM   4209  O   LYS B 170     -52.128 -44.257 -25.845  1.00 25.43           O  
ANISOU 4209  O   LYS B 170     3280   3658   2722   -407    173   -224       O  
ATOM   4210  CB  LYS B 170     -52.982 -44.568 -22.768  1.00 30.90           C  
ANISOU 4210  CB  LYS B 170     4110   4598   3034   -630    334   -298       C  
ATOM   4211  CG  LYS B 170     -54.180 -43.695 -22.488  1.00 45.97           C  
ANISOU 4211  CG  LYS B 170     6025   6452   4988   -627    519   -458       C  
ATOM   4212  CD  LYS B 170     -54.042 -43.096 -21.076  1.00 57.81           C  
ANISOU 4212  CD  LYS B 170     7630   8070   6264   -768    604   -588       C  
ATOM   4213  CE  LYS B 170     -55.180 -42.147 -20.720  1.00 57.68           C  
ANISOU 4213  CE  LYS B 170     7624   7988   6303   -763    822   -777       C  
ATOM   4214  NZ  LYS B 170     -54.916 -41.427 -19.434  1.00 60.34           N  
ANISOU 4214  NZ  LYS B 170     8085   8427   6414   -911    912   -946       N  
ATOM   4215  N   VAL B 171     -54.379 -44.363 -25.729  1.00 29.45           N  
ANISOU 4215  N   VAL B 171     3749   4105   3336   -363    356   -279       N  
ATOM   4216  CA  VAL B 171     -54.557 -43.499 -26.893  1.00 27.88           C  
ANISOU 4216  CA  VAL B 171     3501   3785   3307   -281    354   -320       C  
ATOM   4217  C   VAL B 171     -54.178 -42.074 -26.514  1.00 30.75           C  
ANISOU 4217  C   VAL B 171     3907   4115   3663   -317    411   -455       C  
ATOM   4218  O   VAL B 171     -54.681 -41.527 -25.526  1.00 31.73           O  
ANISOU 4218  O   VAL B 171     4068   4257   3732   -369    533   -570       O  
ATOM   4219  CB  VAL B 171     -56.001 -43.581 -27.411  1.00 29.23           C  
ANISOU 4219  CB  VAL B 171     3592   3886   3628   -214    426   -314       C  
ATOM   4220  CG1 VAL B 171     -56.197 -42.668 -28.654  1.00 26.78           C  
ANISOU 4220  CG1 VAL B 171     3226   3458   3490   -130    403   -325       C  
ATOM   4221  CG2 VAL B 171     -56.351 -45.035 -27.732  1.00 31.20           C  
ANISOU 4221  CG2 VAL B 171     3811   4163   3882   -205    367   -194       C  
ATOM   4222  N   ARG B 172     -53.276 -41.471 -27.287  1.00 25.74           N  
ANISOU 4222  N   ARG B 172     3271   3428   3082   -297    333   -449       N  
ATOM   4223  CA  ARG B 172     -52.762 -40.146 -26.970  1.00 27.10           C  
ANISOU 4223  CA  ARG B 172     3487   3552   3257   -347    371   -571       C  
ATOM   4224  C   ARG B 172     -53.638 -39.049 -27.568  1.00 30.30           C  
ANISOU 4224  C   ARG B 172     3851   3801   3859   -272    466   -636       C  
ATOM   4225  O   ARG B 172     -54.381 -39.262 -28.528  1.00 30.44           O  
ANISOU 4225  O   ARG B 172     3795   3758   4014   -177    454   -555       O  
ATOM   4226  CB  ARG B 172     -51.343 -39.983 -27.498  1.00 25.01           C  
ANISOU 4226  CB  ARG B 172     3227   3301   2974   -373    249   -520       C  
ATOM   4227  CG  ARG B 172     -51.309 -39.928 -29.028  1.00 24.74           C  
ANISOU 4227  CG  ARG B 172     3131   3178   3091   -275    196   -427       C  
ATOM   4228  CD  ARG B 172     -49.980 -40.403 -29.535  1.00 26.39           C  
ANISOU 4228  CD  ARG B 172     3327   3446   3255   -288     82   -337       C  
ATOM   4229  NE  ARG B 172     -48.874 -39.522 -29.183  1.00 33.46           N  
ANISOU 4229  NE  ARG B 172     4245   4350   4118   -373     54   -390       N  
ATOM   4230  CZ  ARG B 172     -47.603 -39.835 -29.428  1.00 37.49           C  
ANISOU 4230  CZ  ARG B 172     4726   4925   4593   -401    -39   -317       C  
ATOM   4231  NH1 ARG B 172     -46.643 -38.985 -29.106  1.00 29.58           N  
ANISOU 4231  NH1 ARG B 172     3733   3933   3575   -493    -68   -366       N  
ATOM   4232  NH2 ARG B 172     -47.304 -41.015 -29.995  1.00 31.40           N  
ANISOU 4232  NH2 ARG B 172     3911   4203   3816   -338    -95   -200       N  
ATOM   4233  N   GLU B 173     -53.508 -37.849 -27.004  1.00 26.75           N  
ANISOU 4233  N   GLU B 173     3451   3283   3429   -322    552   -781       N  
ATOM   4234  CA  GLU B 173     -54.219 -36.678 -27.502  1.00 33.42           C  
ANISOU 4234  CA  GLU B 173     4257   3951   4490   -248    647   -841       C  
ATOM   4235  C   GLU B 173     -53.464 -35.951 -28.614  1.00 38.08           C  
ANISOU 4235  C   GLU B 173     4831   4439   5198   -220    559   -775       C  
ATOM   4236  O   GLU B 173     -54.095 -35.423 -29.537  1.00 38.13           O  
ANISOU 4236  O   GLU B 173     4770   4319   5398   -123    573   -714       O  
ATOM   4237  CB  GLU B 173     -54.491 -35.707 -26.346  1.00 38.45           C  
ANISOU 4237  CB  GLU B 173     4964   4532   5113   -314    810  -1048       C  
ATOM   4238  CG  GLU B 173     -55.734 -34.857 -26.528  1.00 62.90           C  
ANISOU 4238  CG  GLU B 173     7996   7457   8448   -211    967  -1114       C  
ATOM   4239  CD  GLU B 173     -56.995 -35.547 -26.023  1.00 79.49           C  
ANISOU 4239  CD  GLU B 173    10039   9618  10547   -167   1080  -1118       C  
ATOM   4240  OE1 GLU B 173     -56.981 -36.055 -24.878  1.00 86.52           O  
ANISOU 4240  OE1 GLU B 173    11000  10643  11231   -263   1145  -1202       O  
ATOM   4241  OE2 GLU B 173     -57.996 -35.585 -26.773  1.00 80.43           O  
ANISOU 4241  OE2 GLU B 173    10035   9660  10866    -47   1098  -1026       O  
ATOM   4242  N   ASP B 174     -52.134 -35.927 -28.557  1.00 34.20           N  
ANISOU 4242  N   ASP B 174     4388   4008   4598   -307    466   -768       N  
ATOM   4243  CA  ASP B 174     -51.298 -35.153 -29.470  1.00 32.19           C  
ANISOU 4243  CA  ASP B 174     4124   3666   4443   -308    402   -717       C  
ATOM   4244  C   ASP B 174     -51.002 -35.917 -30.760  1.00 33.12           C  
ANISOU 4244  C   ASP B 174     4181   3830   4574   -238    287   -536       C  
ATOM   4245  O   ASP B 174     -50.947 -37.148 -30.782  1.00 35.63           O  
ANISOU 4245  O   ASP B 174     4484   4270   4783   -225    229   -465       O  
ATOM   4246  CB  ASP B 174     -49.973 -34.787 -28.792  1.00 33.55           C  
ANISOU 4246  CB  ASP B 174     4358   3894   4495   -448    355   -794       C  
ATOM   4247  CG  ASP B 174     -49.180 -36.021 -28.352  1.00 45.73           C  
ANISOU 4247  CG  ASP B 174     5902   5635   5837   -504    248   -726       C  
ATOM   4248  OD1 ASP B 174     -49.782 -36.886 -27.691  1.00 37.66           O  
ANISOU 4248  OD1 ASP B 174     4892   4707   4711   -496    271   -728       O  
ATOM   4249  OD2 ASP B 174     -47.970 -36.148 -28.674  1.00 49.38           O  
ANISOU 4249  OD2 ASP B 174     6342   6157   6262   -551    144   -656       O  
ATOM   4250  N   TYR B 175     -50.768 -35.161 -31.833  1.00 30.22           N  
ANISOU 4250  N   TYR B 175     3787   3359   4338   -203    263   -463       N  
ATOM   4251  CA  TYR B 175     -50.331 -35.714 -33.107  1.00 29.34           C  
ANISOU 4251  CA  TYR B 175     3636   3294   4217   -159    168   -309       C  
ATOM   4252  C   TYR B 175     -48.807 -35.769 -33.140  1.00 28.69           C  
ANISOU 4252  C   TYR B 175     3568   3285   4048   -242    106   -290       C  
ATOM   4253  O   TYR B 175     -48.143 -34.761 -32.874  1.00 31.46           O  
ANISOU 4253  O   TYR B 175     3941   3569   4444   -317    123   -346       O  
ATOM   4254  CB  TYR B 175     -50.847 -34.849 -34.255  1.00 34.22           C  
ANISOU 4254  CB  TYR B 175     4219   3781   5003    -92    172   -218       C  
ATOM   4255  CG  TYR B 175     -50.401 -35.315 -35.617  1.00 29.55           C  
ANISOU 4255  CG  TYR B 175     3603   3248   4375    -64     86    -68       C  
ATOM   4256  CD1 TYR B 175     -49.176 -34.907 -36.159  1.00 33.85           C  
ANISOU 4256  CD1 TYR B 175     4159   3800   4902   -119     57    -17       C  
ATOM   4257  CD2 TYR B 175     -51.201 -36.160 -36.366  1.00 27.89           C  
ANISOU 4257  CD2 TYR B 175     3361   3092   4143      3     42     16       C  
ATOM   4258  CE1 TYR B 175     -48.772 -35.339 -37.417  1.00 27.96           C  
ANISOU 4258  CE1 TYR B 175     3399   3119   4107    -99      3    109       C  
ATOM   4259  CE2 TYR B 175     -50.806 -36.591 -37.625  1.00 30.10           C  
ANISOU 4259  CE2 TYR B 175     3637   3434   4364     14    -26    131       C  
ATOM   4260  CZ  TYR B 175     -49.598 -36.180 -38.141  1.00 30.75           C  
ANISOU 4260  CZ  TYR B 175     3737   3527   4419    -33    -35    175       C  
ATOM   4261  OH  TYR B 175     -49.221 -36.626 -39.392  1.00 32.26           O  
ANISOU 4261  OH  TYR B 175     3932   3792   4535    -27    -78    277       O  
ATOM   4262  N   SER B 176     -48.250 -36.928 -33.492  1.00 26.79           N  
ANISOU 4262  N   SER B 176     3305   3168   3705   -228     39   -212       N  
ATOM   4263  CA  SER B 176     -46.796 -37.056 -33.502  1.00 29.63           C  
ANISOU 4263  CA  SER B 176     3649   3604   4003   -295    -15   -183       C  
ATOM   4264  C   SER B 176     -46.331 -38.052 -34.551  1.00 24.19           C  
ANISOU 4264  C   SER B 176     2921   2991   3281   -237    -58    -69       C  
ATOM   4265  O   SER B 176     -47.015 -39.034 -34.844  1.00 25.11           O  
ANISOU 4265  O   SER B 176     3037   3138   3365   -170    -64    -39       O  
ATOM   4266  CB  SER B 176     -46.262 -37.493 -32.138  1.00 32.42           C  
ANISOU 4266  CB  SER B 176     4017   4059   4240   -375    -42   -253       C  
ATOM   4267  OG  SER B 176     -44.849 -37.596 -32.178  1.00 33.68           O  
ANISOU 4267  OG  SER B 176     4134   4297   4367   -437   -107   -206       O  
ATOM   4268  N   LEU B 177     -45.142 -37.793 -35.098  1.00 23.39           N  
ANISOU 4268  N   LEU B 177     2784   2914   3189   -273    -77    -16       N  
ATOM   4269  CA  LEU B 177     -44.432 -38.728 -35.969  1.00 27.12           C  
ANISOU 4269  CA  LEU B 177     3215   3465   3625   -230    -93     69       C  
ATOM   4270  C   LEU B 177     -43.331 -39.486 -35.243  1.00 30.87           C  
ANISOU 4270  C   LEU B 177     3636   4043   4049   -261   -133     76       C  
ATOM   4271  O   LEU B 177     -42.675 -40.337 -35.851  1.00 26.52           O  
ANISOU 4271  O   LEU B 177     3038   3549   3490   -216   -131    138       O  
ATOM   4272  CB  LEU B 177     -43.810 -37.984 -37.153  1.00 27.20           C  
ANISOU 4272  CB  LEU B 177     3205   3446   3686   -245    -68    140       C  
ATOM   4273  CG  LEU B 177     -44.741 -37.183 -38.056  1.00 31.14           C  
ANISOU 4273  CG  LEU B 177     3743   3848   4241   -216    -45    182       C  
ATOM   4274  CD1 LEU B 177     -43.913 -36.507 -39.144  1.00 31.68           C  
ANISOU 4274  CD1 LEU B 177     3791   3910   4337   -250    -21    274       C  
ATOM   4275  CD2 LEU B 177     -45.807 -38.080 -38.668  1.00 28.41           C  
ANISOU 4275  CD2 LEU B 177     3423   3525   3848   -133    -56    205       C  
ATOM   4276  N   GLU B 178     -43.114 -39.190 -33.968  1.00 25.33           N  
ANISOU 4276  N   GLU B 178     2939   3369   3316   -340   -168     16       N  
ATOM   4277  CA  GLU B 178     -41.942 -39.650 -33.237  1.00 27.78           C  
ANISOU 4277  CA  GLU B 178     3182   3786   3587   -394   -233     45       C  
ATOM   4278  C   GLU B 178     -42.156 -41.052 -32.676  1.00 23.35           C  
ANISOU 4278  C   GLU B 178     2613   3296   2962   -338   -268     83       C  
ATOM   4279  O   GLU B 178     -43.276 -41.441 -32.325  1.00 24.61           O  
ANISOU 4279  O   GLU B 178     2838   3432   3082   -305   -248     48       O  
ATOM   4280  CB  GLU B 178     -41.637 -38.641 -32.121  1.00 33.75           C  
ANISOU 4280  CB  GLU B 178     3960   4548   4314   -530   -269    -39       C  
ATOM   4281  CG  GLU B 178     -40.888 -39.118 -30.906  1.00 50.55           C  
ANISOU 4281  CG  GLU B 178     6049   6805   6351   -611   -363    -30       C  
ATOM   4282  CD  GLU B 178     -40.864 -38.052 -29.811  1.00 55.24           C  
ANISOU 4282  CD  GLU B 178     6703   7400   6886   -763   -387   -154       C  
ATOM   4283  OE1 GLU B 178     -41.525 -38.249 -28.762  1.00 40.57           O  
ANISOU 4283  OE1 GLU B 178     4920   5581   4914   -800   -391   -224       O  
ATOM   4284  OE2 GLU B 178     -40.207 -37.004 -30.025  1.00 53.15           O  
ANISOU 4284  OE2 GLU B 178     6418   7090   6688   -852   -390   -188       O  
ATOM   4285  N   CYS B 179     -41.067 -41.820 -32.614  1.00 21.29           N  
ANISOU 4285  N   CYS B 179     2261   3116   2712   -325   -316    168       N  
ATOM   4286  CA  CYS B 179     -41.101 -43.111 -31.936  1.00 24.52           C  
ANISOU 4286  CA  CYS B 179     2652   3584   3080   -282   -362    228       C  
ATOM   4287  C   CYS B 179     -41.265 -42.883 -30.439  1.00 26.13           C  
ANISOU 4287  C   CYS B 179     2894   3861   3174   -387   -433    195       C  
ATOM   4288  O   CYS B 179     -40.649 -41.976 -29.874  1.00 28.61           O  
ANISOU 4288  O   CYS B 179     3194   4220   3456   -502   -480    157       O  
ATOM   4289  CB  CYS B 179     -39.812 -43.890 -32.185  1.00 22.12           C  
ANISOU 4289  CB  CYS B 179     2220   3339   2847   -237   -396    339       C  
ATOM   4290  SG  CYS B 179     -39.443 -44.199 -33.954  1.00 28.40           S  
ANISOU 4290  SG  CYS B 179     2972   4069   3751   -125   -285    360       S  
ATOM   4291  N   ASP B 180     -42.059 -43.730 -29.796  1.00 20.92           N  
ANISOU 4291  N   ASP B 180     2285   3217   2448   -361   -438    211       N  
ATOM   4292  CA  ASP B 180     -42.329 -43.578 -28.360  1.00 24.18           C  
ANISOU 4292  CA  ASP B 180     2753   3714   2721   -468   -488    179       C  
ATOM   4293  C   ASP B 180     -41.041 -43.635 -27.544  1.00 27.81           C  
ANISOU 4293  C   ASP B 180     3133   4306   3128   -559   -615    259       C  
ATOM   4294  O   ASP B 180     -40.361 -44.672 -27.548  1.00 25.32           O  
ANISOU 4294  O   ASP B 180     2726   4038   2858   -500   -680    403       O  
ATOM   4295  CB  ASP B 180     -43.284 -44.673 -27.906  1.00 26.66           C  
ANISOU 4295  CB  ASP B 180     3115   4031   2984   -419   -469    222       C  
ATOM   4296  CG  ASP B 180     -43.894 -44.399 -26.531  1.00 29.10           C  
ANISOU 4296  CG  ASP B 180     3510   4419   3128   -532   -473    162       C  
ATOM   4297  OD1 ASP B 180     -43.258 -43.742 -25.680  1.00 26.52           O  
ANISOU 4297  OD1 ASP B 180     3192   4188   2696   -658   -538    127       O  
ATOM   4298  OD2 ASP B 180     -45.016 -44.874 -26.308  1.00 30.84           O  
ANISOU 4298  OD2 ASP B 180     3788   4611   3317   -503   -408    148       O  
ATOM   4299  N   PRO B 181     -40.682 -42.570 -26.812  1.00 27.16           N  
ANISOU 4299  N   PRO B 181     2898   3949   3474    -67    -81   -131       N  
ATOM   4300  CA  PRO B 181     -39.430 -42.587 -26.042  1.00 26.02           C  
ANISOU 4300  CA  PRO B 181     2877   3654   3355   -118    -66    -36       C  
ATOM   4301  C   PRO B 181     -39.497 -43.412 -24.759  1.00 28.29           C  
ANISOU 4301  C   PRO B 181     3172   3937   3641   -244      1    -31       C  
ATOM   4302  O   PRO B 181     -38.446 -43.690 -24.167  1.00 25.26           O  
ANISOU 4302  O   PRO B 181     2885   3443   3269   -287      9     43       O  
ATOM   4303  CB  PRO B 181     -39.202 -41.096 -25.721  1.00 25.93           C  
ANISOU 4303  CB  PRO B 181     2935   3601   3316      5    -98    -19       C  
ATOM   4304  CG  PRO B 181     -40.612 -40.552 -25.581  1.00 30.89           C  
ANISOU 4304  CG  PRO B 181     3463   4375   3896     98    -98   -113       C  
ATOM   4305  CD  PRO B 181     -41.401 -41.284 -26.675  1.00 25.74           C  
ANISOU 4305  CD  PRO B 181     2690   3845   3245     90   -113   -179       C  
ATOM   4306  N   ALA B 182     -40.688 -43.819 -24.318  1.00 24.41           N  
ANISOU 4306  N   ALA B 182     2583   3569   3122   -305     53   -114       N  
ATOM   4307  CA  ALA B 182     -40.788 -44.581 -23.078  1.00 25.29           C  
ANISOU 4307  CA  ALA B 182     2730   3665   3216   -435    130   -110       C  
ATOM   4308  C   ALA B 182     -39.990 -45.877 -23.136  1.00 30.38           C  
ANISOU 4308  C   ALA B 182     3480   4190   3874   -546    158    -46       C  
ATOM   4309  O   ALA B 182     -39.567 -46.385 -22.095  1.00 28.67           O  
ANISOU 4309  O   ALA B 182     3362   3896   3635   -611    202     -1       O  
ATOM   4310  CB  ALA B 182     -42.251 -44.890 -22.763  1.00 29.04           C  
ANISOU 4310  CB  ALA B 182     3073   4312   3650   -513    195   -226       C  
ATOM   4311  N   VAL B 183     -39.773 -46.431 -24.329  1.00 27.09           N  
ANISOU 4311  N   VAL B 183     3058   3753   3482   -553    134    -43       N  
ATOM   4312  CA  VAL B 183     -39.078 -47.701 -24.477  1.00 23.86           C  
ANISOU 4312  CA  VAL B 183     2762   3230   3075   -638    163      8       C  
ATOM   4313  C   VAL B 183     -37.726 -47.538 -25.170  1.00 24.44           C  
ANISOU 4313  C   VAL B 183     2902   3200   3185   -543     94     90       C  
ATOM   4314  O   VAL B 183     -37.148 -48.528 -25.623  1.00 28.32           O  
ANISOU 4314  O   VAL B 183     3471   3611   3678   -575    104    124       O  
ATOM   4315  CB  VAL B 183     -39.953 -48.731 -25.211  1.00 28.62           C  
ANISOU 4315  CB  VAL B 183     3321   3890   3663   -760    212    -68       C  
ATOM   4316  CG1 VAL B 183     -41.131 -49.134 -24.332  1.00 28.96           C  
ANISOU 4316  CG1 VAL B 183     3319   4029   3655   -902    306   -152       C  
ATOM   4317  CG2 VAL B 183     -40.451 -48.167 -26.531  1.00 34.54           C  
ANISOU 4317  CG2 VAL B 183     3938   4750   4434   -685    151   -128       C  
ATOM   4318  N   ILE B 184     -37.201 -46.306 -25.261  1.00 23.07           N  
ANISOU 4318  N   ILE B 184     2709   3027   3030   -431     34    118       N  
ATOM   4319  CA  ILE B 184     -35.901 -46.058 -25.880  1.00 22.66           C  
ANISOU 4319  CA  ILE B 184     2707   2898   3003   -364    -19    182       C  
ATOM   4320  C   ILE B 184     -34.834 -46.028 -24.798  1.00 26.91           C  
ANISOU 4320  C   ILE B 184     3324   3374   3527   -356    -22    244       C  
ATOM   4321  O   ILE B 184     -35.033 -45.433 -23.733  1.00 22.85           O  
ANISOU 4321  O   ILE B 184     2814   2876   2991   -356    -12    240       O  
ATOM   4322  CB  ILE B 184     -35.902 -44.741 -26.679  1.00 21.15           C  
ANISOU 4322  CB  ILE B 184     2477   2736   2822   -270    -71    169       C  
ATOM   4323  CG1 ILE B 184     -36.911 -44.838 -27.821  1.00 25.02           C  
ANISOU 4323  CG1 ILE B 184     2891   3304   3314   -253    -81    106       C  
ATOM   4324  CG2 ILE B 184     -34.490 -44.423 -27.223  1.00 22.85           C  
ANISOU 4324  CG2 ILE B 184     2748   2881   3054   -232   -107    227       C  
ATOM   4325  CD1 ILE B 184     -36.885 -43.644 -28.762  1.00 24.74           C  
ANISOU 4325  CD1 ILE B 184     2854   3277   3269   -140   -135    100       C  
ATOM   4326  N   GLY B 185     -33.707 -46.676 -25.072  1.00 21.65           N  
ANISOU 4326  N   GLY B 185     2713   2648   2864   -339    -40    293       N  
ATOM   4327  CA  GLY B 185     -32.517 -46.583 -24.244  1.00 23.51           C  
ANISOU 4327  CA  GLY B 185     2999   2856   3079   -304    -63    342       C  
ATOM   4328  C   GLY B 185     -31.301 -46.362 -25.130  1.00 22.87           C  
ANISOU 4328  C   GLY B 185     2901   2773   3016   -253   -108    364       C  
ATOM   4329  O   GLY B 185     -31.037 -47.157 -26.041  1.00 22.16           O  
ANISOU 4329  O   GLY B 185     2822   2660   2939   -240   -108    371       O  
ATOM   4330  N   THR B 186     -30.563 -45.283 -24.889  1.00 20.60           N  
ANISOU 4330  N   THR B 186     2590   2513   2723   -235   -138    367       N  
ATOM   4331  CA  THR B 186     -29.380 -44.937 -25.669  1.00 21.42           C  
ANISOU 4331  CA  THR B 186     2667   2636   2834   -214   -167    373       C  
ATOM   4332  C   THR B 186     -28.231 -44.698 -24.703  1.00 24.71           C  
ANISOU 4332  C   THR B 186     3077   3098   3213   -205   -193    382       C  
ATOM   4333  O   THR B 186     -28.410 -44.013 -23.694  1.00 26.39           O  
ANISOU 4333  O   THR B 186     3303   3322   3403   -229   -193    374       O  
ATOM   4334  CB  THR B 186     -29.636 -43.699 -26.535  1.00 22.17           C  
ANISOU 4334  CB  THR B 186     2749   2729   2945   -227   -169    349       C  
ATOM   4335  OG1 THR B 186     -30.557 -44.041 -27.591  1.00 22.29           O  
ANISOU 4335  OG1 THR B 186     2757   2726   2985   -214   -160    335       O  
ATOM   4336  CG2 THR B 186     -28.339 -43.166 -27.134  1.00 19.94           C  
ANISOU 4336  CG2 THR B 186     2452   2471   2654   -241   -182    347       C  
ATOM   4337  N   ALA B 187     -27.064 -45.271 -24.987  1.00 21.50           N  
ANISOU 4337  N   ALA B 187     2645   2733   2792   -165   -216    390       N  
ATOM   4338  CA  ALA B 187     -25.946 -45.084 -24.069  1.00 21.12           C  
ANISOU 4338  CA  ALA B 187     2565   2766   2694   -147   -250    383       C  
ATOM   4339  C   ALA B 187     -24.625 -45.144 -24.812  1.00 25.68           C  
ANISOU 4339  C   ALA B 187     3065   3432   3261   -124   -272    361       C  
ATOM   4340  O   ALA B 187     -24.476 -45.870 -25.802  1.00 25.78           O  
ANISOU 4340  O   ALA B 187     3073   3429   3292    -81   -265    369       O  
ATOM   4341  CB  ALA B 187     -25.950 -46.138 -22.957  1.00 20.73           C  
ANISOU 4341  CB  ALA B 187     2575   2705   2596    -77   -263    414       C  
ATOM   4342  N   VAL B 188     -23.653 -44.411 -24.287  1.00 20.68           N  
ANISOU 4342  N   VAL B 188     2365   2904   2587   -157   -294    325       N  
ATOM   4343  CA  VAL B 188     -22.290 -44.443 -24.798  1.00 21.46           C  
ANISOU 4343  CA  VAL B 188     2361   3136   2659   -146   -313    283       C  
ATOM   4344  C   VAL B 188     -21.366 -44.516 -23.601  1.00 23.15           C  
ANISOU 4344  C   VAL B 188     2512   3486   2800   -104   -363    255       C  
ATOM   4345  O   VAL B 188     -21.617 -43.891 -22.563  1.00 22.98           O  
ANISOU 4345  O   VAL B 188     2515   3463   2753   -153   -371    248       O  
ATOM   4346  CB  VAL B 188     -21.960 -43.223 -25.692  1.00 22.41           C  
ANISOU 4346  CB  VAL B 188     2446   3277   2793   -278   -274    239       C  
ATOM   4347  CG1 VAL B 188     -22.270 -41.888 -24.972  1.00 21.35           C  
ANISOU 4347  CG1 VAL B 188     2357   3116   2640   -393   -256    216       C  
ATOM   4348  CG2 VAL B 188     -20.485 -43.262 -26.152  1.00 19.02           C  
ANISOU 4348  CG2 VAL B 188     1885   3017   2323   -290   -282    178       C  
ATOM   4349  N   LYS B 189     -20.306 -45.291 -23.742  1.00 21.23           N  
ANISOU 4349  N   LYS B 189     2186   3368   2512      2   -401    233       N  
ATOM   4350  CA  LYS B 189     -19.371 -45.515 -22.653  1.00 27.71           C  
ANISOU 4350  CA  LYS B 189     2936   4348   3246     84   -465    199       C  
ATOM   4351  C   LYS B 189     -18.017 -45.787 -23.284  1.00 27.42           C  
ANISOU 4351  C   LYS B 189     2743   4508   3168    143   -491    132       C  
ATOM   4352  O   LYS B 189     -17.872 -46.769 -24.018  1.00 28.25           O  
ANISOU 4352  O   LYS B 189     2862   4593   3280    266   -492    155       O  
ATOM   4353  CB  LYS B 189     -19.853 -46.698 -21.805  1.00 25.05           C  
ANISOU 4353  CB  LYS B 189     2723   3924   2870    244   -498    266       C  
ATOM   4354  CG  LYS B 189     -18.908 -47.188 -20.734  1.00 31.57           C  
ANISOU 4354  CG  LYS B 189     3507   4902   3585    390   -577    243       C  
ATOM   4355  CD  LYS B 189     -19.678 -48.154 -19.827  1.00 35.17           C  
ANISOU 4355  CD  LYS B 189     4153   5210   3998    505   -585    323       C  
ATOM   4356  CE  LYS B 189     -18.800 -48.864 -18.832  1.00 38.35           C  
ANISOU 4356  CE  LYS B 189     4563   5736   4271    702   -668    316       C  
ATOM   4357  NZ  LYS B 189     -19.622 -49.687 -17.892  1.00 38.25           N  
ANISOU 4357  NZ  LYS B 189     4776   5553   4205    783   -660    397       N  
ATOM   4358  N   GLY B 190     -17.035 -44.922 -23.023  1.00 23.73           N  
ANISOU 4358  N   GLY B 190     2126   4237   2652     47   -504     42       N  
ATOM   4359  CA  GLY B 190     -15.721 -45.115 -23.610  1.00 24.80           C  
ANISOU 4359  CA  GLY B 190     2081   4600   2739     87   -521    -43       C  
ATOM   4360  C   GLY B 190     -15.749 -45.099 -25.128  1.00 33.34           C  
ANISOU 4360  C   GLY B 190     3157   5628   3884     26   -454    -44       C  
ATOM   4361  O   GLY B 190     -16.025 -44.053 -25.729  1.00 27.45           O  
ANISOU 4361  O   GLY B 190     2433   4817   3181   -172   -385    -61       O  
ATOM   4362  N   ARG B 191     -15.490 -46.250 -25.760  1.00 27.73           N  
ANISOU 4362  N   ARG B 191     2439   4928   3169    201   -471    -24       N  
ATOM   4363  CA  ARG B 191     -15.373 -46.354 -27.214  1.00 23.73           C  
ANISOU 4363  CA  ARG B 191     1912   4397   2707    165   -412    -33       C  
ATOM   4364  C   ARG B 191     -16.525 -47.095 -27.879  1.00 28.25           C  
ANISOU 4364  C   ARG B 191     2665   4719   3351    228   -386     65       C  
ATOM   4365  O   ARG B 191     -16.406 -47.440 -29.059  1.00 25.36           O  
ANISOU 4365  O   ARG B 191     2292   4332   3010    243   -350     61       O  
ATOM   4366  CB  ARG B 191     -14.073 -47.067 -27.605  1.00 30.18           C  
ANISOU 4366  CB  ARG B 191     2562   5451   3456    311   -443   -109       C  
ATOM   4367  CG  ARG B 191     -12.828 -46.454 -27.047  1.00 42.02           C  
ANISOU 4367  CG  ARG B 191     3839   7255   4869    257   -472   -232       C  
ATOM   4368  CD  ARG B 191     -11.591 -47.235 -27.484  1.00 45.44           C  
ANISOU 4368  CD  ARG B 191     4091   7947   5229    432   -504   -316       C  
ATOM   4369  NE  ARG B 191     -10.398 -46.678 -26.860  1.00 64.63           N  
ANISOU 4369  NE  ARG B 191     6279  10713   7564    382   -540   -452       N  
ATOM   4370  CZ  ARG B 191      -9.158 -47.085 -27.106  1.00 72.66           C  
ANISOU 4370  CZ  ARG B 191     7090  12019   8496    497   -562   -563       C  
ATOM   4371  NH1 ARG B 191      -8.936 -48.065 -27.975  1.00 71.32           N  
ANISOU 4371  NH1 ARG B 191     6929  11842   8326    684   -557   -549       N  
ATOM   4372  NH2 ARG B 191      -8.139 -46.505 -26.483  1.00 67.58           N  
ANISOU 4372  NH2 ARG B 191     6318  11591   7770    412   -558   -682       N  
ATOM   4373  N   GLU B 192     -17.616 -47.375 -27.171  1.00 25.28           N  
ANISOU 4373  N   GLU B 192     2442   4164   3000    257   -399    143       N  
ATOM   4374  CA  GLU B 192     -18.760 -48.023 -27.798  1.00 25.98           C  
ANISOU 4374  CA  GLU B 192     2686   4035   3149    281   -366    217       C  
ATOM   4375  C   GLU B 192     -20.048 -47.367 -27.335  1.00 27.11           C  
ANISOU 4375  C   GLU B 192     2936   4023   3343    163   -342    262       C  
ATOM   4376  O   GLU B 192     -20.140 -46.861 -26.212  1.00 24.96           O  
ANISOU 4376  O   GLU B 192     2664   3774   3045    130   -364    259       O  
ATOM   4377  CB  GLU B 192     -18.824 -49.529 -27.486  1.00 24.98           C  
ANISOU 4377  CB  GLU B 192     2664   3846   2980    484   -398    263       C  
ATOM   4378  CG  GLU B 192     -17.774 -50.355 -28.211  1.00 38.96           C  
ANISOU 4378  CG  GLU B 192     4368   5730   4706    637   -414    227       C  
ATOM   4379  CD  GLU B 192     -18.135 -51.830 -28.278  1.00 48.71           C  
ANISOU 4379  CD  GLU B 192     5777   6820   5909    812   -419    284       C  
ATOM   4380  OE1 GLU B 192     -18.669 -52.377 -27.282  1.00 39.16           O  
ANISOU 4380  OE1 GLU B 192     4713   5504   4662    876   -437    336       O  
ATOM   4381  OE2 GLU B 192     -17.883 -52.438 -29.342  1.00 39.67           O  
ANISOU 4381  OE2 GLU B 192     4643   5661   4769    876   -396    275       O  
ATOM   4382  N   ALA B 193     -21.053 -47.433 -28.199  1.00 23.42           N  
ANISOU 4382  N   ALA B 193     2555   3406   2937    114   -300    297       N  
ATOM   4383  CA  ALA B 193     -22.362 -46.860 -27.941  1.00 22.67           C  
ANISOU 4383  CA  ALA B 193     2547   3182   2886     23   -276    328       C  
ATOM   4384  C   ALA B 193     -23.435 -47.759 -28.533  1.00 25.92           C  
ANISOU 4384  C   ALA B 193     3061   3454   3334     53   -252    368       C  
ATOM   4385  O   ALA B 193     -23.190 -48.530 -29.472  1.00 26.31           O  
ANISOU 4385  O   ALA B 193     3120   3490   3388    108   -243    368       O  
ATOM   4386  CB  ALA B 193     -22.506 -45.452 -28.543  1.00 17.97           C  
ANISOU 4386  CB  ALA B 193     1927   2584   2317   -115   -243    300       C  
ATOM   4387  N   ALA B 194     -24.643 -47.619 -27.991  1.00 19.68           N  
ANISOU 4387  N   ALA B 194     2342   2573   2565      7   -237    391       N  
ATOM   4388  CA  ALA B 194     -25.823 -48.307 -28.504  1.00 24.83           C  
ANISOU 4388  CA  ALA B 194     3073   3115   3246     -6   -207    408       C  
ATOM   4389  C   ALA B 194     -27.024 -47.370 -28.476  1.00 26.47           C  
ANISOU 4389  C   ALA B 194     3282   3288   3488    -93   -189    398       C  
ATOM   4390  O   ALA B 194     -27.320 -46.774 -27.435  1.00 23.80           O  
ANISOU 4390  O   ALA B 194     2946   2958   3138   -120   -193    398       O  
ATOM   4391  CB  ALA B 194     -26.116 -49.565 -27.674  1.00 23.51           C  
ANISOU 4391  CB  ALA B 194     3010   2882   3039     51   -200    439       C  
ATOM   4392  N   HIS B 195     -27.701 -47.222 -29.616  1.00 22.02           N  
ANISOU 4392  N   HIS B 195     2718   2693   2957   -121   -174    384       N  
ATOM   4393  CA  HIS B 195     -29.047 -46.651 -29.672  1.00 21.53           C  
ANISOU 4393  CA  HIS B 195     2661   2606   2913   -166   -161    367       C  
ATOM   4394  C   HIS B 195     -30.028 -47.820 -29.737  1.00 24.18           C  
ANISOU 4394  C   HIS B 195     3035   2901   3252   -182   -136    360       C  
ATOM   4395  O   HIS B 195     -29.879 -48.701 -30.593  1.00 23.64           O  
ANISOU 4395  O   HIS B 195     2991   2805   3186   -170   -127    359       O  
ATOM   4396  CB  HIS B 195     -29.231 -45.738 -30.892  1.00 21.15           C  
ANISOU 4396  CB  HIS B 195     2595   2562   2878   -173   -167    348       C  
ATOM   4397  CG  HIS B 195     -28.447 -44.455 -30.841  1.00 24.12           C  
ANISOU 4397  CG  HIS B 195     2969   2959   3237   -191   -172    346       C  
ATOM   4398  ND1 HIS B 195     -27.083 -44.410 -31.026  1.00 22.37           N  
ANISOU 4398  ND1 HIS B 195     2720   2778   3001   -202   -171    346       N  
ATOM   4399  CD2 HIS B 195     -28.842 -43.169 -30.648  1.00 19.24           C  
ANISOU 4399  CD2 HIS B 195     2381   2326   2602   -209   -171    334       C  
ATOM   4400  CE1 HIS B 195     -26.667 -43.155 -30.939  1.00 23.67           C  
ANISOU 4400  CE1 HIS B 195     2899   2952   3141   -253   -162    332       C  
ATOM   4401  NE2 HIS B 195     -27.715 -42.383 -30.718  1.00 21.59           N  
ANISOU 4401  NE2 HIS B 195     2688   2640   2874   -253   -161    330       N  
ATOM   4402  N   SER B 196     -31.001 -47.866 -28.822  1.00 20.87           N  
ANISOU 4402  N   SER B 196     2628   2478   2823   -222   -115    348       N  
ATOM   4403  CA  SER B 196     -31.819 -49.071 -28.756  1.00 22.20           C  
ANISOU 4403  CA  SER B 196     2847   2608   2978   -272    -73    334       C  
ATOM   4404  C   SER B 196     -33.261 -48.756 -28.382  1.00 23.55           C  
ANISOU 4404  C   SER B 196     2977   2823   3149   -340    -45    285       C  
ATOM   4405  O   SER B 196     -33.565 -47.730 -27.769  1.00 23.14           O  
ANISOU 4405  O   SER B 196     2880   2815   3098   -328    -57    276       O  
ATOM   4406  CB  SER B 196     -31.241 -50.101 -27.755  1.00 23.72           C  
ANISOU 4406  CB  SER B 196     3146   2740   3127   -256    -53    373       C  
ATOM   4407  OG  SER B 196     -31.577 -49.783 -26.405  1.00 21.30           O  
ANISOU 4407  OG  SER B 196     2856   2443   2796   -282    -39    380       O  
ATOM   4408  N   ASP B 197     -34.147 -49.670 -28.765  1.00 23.27           N  
ANISOU 4408  N   ASP B 197     2955   2783   3103   -414     -4    244       N  
ATOM   4409  CA  ASP B 197     -35.504 -49.744 -28.225  1.00 23.94           C  
ANISOU 4409  CA  ASP B 197     3001   2928   3170   -505     42    184       C  
ATOM   4410  C   ASP B 197     -35.902 -51.221 -28.223  1.00 25.77           C  
ANISOU 4410  C   ASP B 197     3327   3100   3365   -617    112    163       C  
ATOM   4411  O   ASP B 197     -35.037 -52.103 -28.179  1.00 25.39           O  
ANISOU 4411  O   ASP B 197     3409   2942   3295   -596    124    215       O  
ATOM   4412  CB  ASP B 197     -36.462 -48.806 -28.998  1.00 21.05           C  
ANISOU 4412  CB  ASP B 197     2500   2678   2820   -483     10    117       C  
ATOM   4413  CG  ASP B 197     -36.626 -49.182 -30.477  1.00 32.28           C  
ANISOU 4413  CG  ASP B 197     3894   4119   4251   -482    -10     84       C  
ATOM   4414  OD1 ASP B 197     -36.351 -50.326 -30.882  1.00 27.17           O  
ANISOU 4414  OD1 ASP B 197     3322   3406   3597   -539     21     90       O  
ATOM   4415  OD2 ASP B 197     -37.051 -48.309 -31.256  1.00 40.64           O  
ANISOU 4415  OD2 ASP B 197     4869   5256   5315   -415    -57     49       O  
ATOM   4416  N   LEU B 198     -37.204 -51.507 -28.264  1.00 23.67           N  
ANISOU 4416  N   LEU B 198     3005   2910   3079   -736    163     79       N  
ATOM   4417  CA  LEU B 198     -37.603 -52.908 -28.186  1.00 26.54           C  
ANISOU 4417  CA  LEU B 198     3487   3205   3393   -880    248     51       C  
ATOM   4418  C   LEU B 198     -37.467 -53.626 -29.514  1.00 28.93           C  
ANISOU 4418  C   LEU B 198     3819   3473   3699   -897    242     30       C  
ATOM   4419  O   LEU B 198     -37.695 -54.837 -29.563  1.00 25.04           O  
ANISOU 4419  O   LEU B 198     3458   2897   3157  -1018    317      8       O  
ATOM   4420  CB  LEU B 198     -39.040 -53.050 -27.679  1.00 25.83           C  
ANISOU 4420  CB  LEU B 198     3324   3224   3265  -1041    324    -49       C  
ATOM   4421  CG  LEU B 198     -39.269 -52.584 -26.239  1.00 32.99           C  
ANISOU 4421  CG  LEU B 198     4234   4151   4150  -1053    356    -35       C  
ATOM   4422  CD1 LEU B 198     -40.722 -52.771 -25.880  1.00 31.96           C  
ANISOU 4422  CD1 LEU B 198     4010   4155   3977  -1225    441   -152       C  
ATOM   4423  CD2 LEU B 198     -38.360 -53.345 -25.261  1.00 29.93           C  
ANISOU 4423  CD2 LEU B 198     4069   3587   3717  -1048    394     59       C  
ATOM   4424  N   GLY B 199     -37.109 -52.919 -30.585  1.00 23.69           N  
ANISOU 4424  N   GLY B 199     3059   2860   3083   -788    164     35       N  
ATOM   4425  CA  GLY B 199     -36.987 -53.574 -31.871  1.00 23.14           C  
ANISOU 4425  CA  GLY B 199     3016   2762   3012   -802    158     12       C  
ATOM   4426  C   GLY B 199     -35.662 -53.341 -32.570  1.00 25.08           C  
ANISOU 4426  C   GLY B 199     3298   2940   3289   -656     97     87       C  
ATOM   4427  O   GLY B 199     -35.305 -54.101 -33.473  1.00 23.73           O  
ANISOU 4427  O   GLY B 199     3198   2710   3109   -658    104     86       O  
ATOM   4428  N   TYR B 200     -34.926 -52.300 -32.169  1.00 23.66           N  
ANISOU 4428  N   TYR B 200     3073   2777   3140   -541     44    144       N  
ATOM   4429  CA  TYR B 200     -33.665 -51.910 -32.796  1.00 21.59           C  
ANISOU 4429  CA  TYR B 200     2818   2483   2902   -422     -6    200       C  
ATOM   4430  C   TYR B 200     -32.538 -51.969 -31.768  1.00 23.74           C  
ANISOU 4430  C   TYR B 200     3159   2698   3165   -354    -10    270       C  
ATOM   4431  O   TYR B 200     -32.678 -51.434 -30.666  1.00 22.07           O  
ANISOU 4431  O   TYR B 200     2929   2508   2949   -359     -9    283       O  
ATOM   4432  CB  TYR B 200     -33.721 -50.475 -33.337  1.00 23.21           C  
ANISOU 4432  CB  TYR B 200     2909   2773   3136   -357    -63    192       C  
ATOM   4433  CG  TYR B 200     -34.546 -50.216 -34.575  1.00 26.73           C  
ANISOU 4433  CG  TYR B 200     3287   3289   3580   -364    -87    133       C  
ATOM   4434  CD1 TYR B 200     -35.356 -51.200 -35.142  1.00 23.48           C  
ANISOU 4434  CD1 TYR B 200     2878   2894   3148   -451    -58     70       C  
ATOM   4435  CD2 TYR B 200     -34.499 -48.966 -35.189  1.00 24.57           C  
ANISOU 4435  CD2 TYR B 200     2960   3064   3312   -282   -138    134       C  
ATOM   4436  CE1 TYR B 200     -36.101 -50.936 -36.299  1.00 23.55           C  
ANISOU 4436  CE1 TYR B 200     2811   2991   3144   -446    -91      7       C  
ATOM   4437  CE2 TYR B 200     -35.229 -48.696 -36.326  1.00 23.08           C  
ANISOU 4437  CE2 TYR B 200     2722   2943   3105   -260   -169     82       C  
ATOM   4438  CZ  TYR B 200     -36.022 -49.677 -36.877  1.00 22.97           C  
ANISOU 4438  CZ  TYR B 200     2685   2969   3073   -336   -152     17       C  
ATOM   4439  OH  TYR B 200     -36.735 -49.382 -38.010  1.00 26.08           O  
ANISOU 4439  OH  TYR B 200     3019   3452   3439   -302   -195    -42       O  
ATOM   4440  N   TRP B 201     -31.418 -52.587 -32.134  1.00 24.02           N  
ANISOU 4440  N   TRP B 201     3265   2675   3188   -280    -17    307       N  
ATOM   4441  CA  TRP B 201     -30.187 -52.530 -31.338  1.00 23.15           C  
ANISOU 4441  CA  TRP B 201     3185   2552   3060   -183    -40    361       C  
ATOM   4442  C   TRP B 201     -29.072 -52.091 -32.278  1.00 26.43           C  
ANISOU 4442  C   TRP B 201     3535   3011   3494   -100    -79    370       C  
ATOM   4443  O   TRP B 201     -28.636 -52.872 -33.126  1.00 24.03           O  
ANISOU 4443  O   TRP B 201     3280   2671   3178    -60    -70    368       O  
ATOM   4444  CB  TRP B 201     -29.876 -53.881 -30.696  1.00 23.43           C  
ANISOU 4444  CB  TRP B 201     3385   2484   3033   -152     -4    389       C  
ATOM   4445  CG  TRP B 201     -28.610 -53.908 -29.867  1.00 26.30           C  
ANISOU 4445  CG  TRP B 201     3775   2858   3359    -22    -40    436       C  
ATOM   4446  CD1 TRP B 201     -27.386 -54.383 -30.257  1.00 24.19           C  
ANISOU 4446  CD1 TRP B 201     3532   2595   3064    112    -67    454       C  
ATOM   4447  CD2 TRP B 201     -28.444 -53.433 -28.518  1.00 24.57           C  
ANISOU 4447  CD2 TRP B 201     3549   2670   3118     -4    -57    460       C  
ATOM   4448  NE1 TRP B 201     -26.472 -54.241 -29.231  1.00 24.33           N  
ANISOU 4448  NE1 TRP B 201     3544   2660   3038    217   -106    482       N  
ATOM   4449  CE2 TRP B 201     -27.094 -53.659 -28.156  1.00 27.04           C  
ANISOU 4449  CE2 TRP B 201     3875   3013   3384    144   -101    489       C  
ATOM   4450  CE3 TRP B 201     -29.306 -52.850 -27.580  1.00 20.90           C  
ANISOU 4450  CE3 TRP B 201     3062   2219   2659    -92    -40    454       C  
ATOM   4451  CZ2 TRP B 201     -26.587 -53.324 -26.897  1.00 27.76           C  
ANISOU 4451  CZ2 TRP B 201     3961   3152   3434    200   -134    511       C  
ATOM   4452  CZ3 TRP B 201     -28.799 -52.510 -26.322  1.00 28.96           C  
ANISOU 4452  CZ3 TRP B 201     4092   3269   3644    -41    -66    482       C  
ATOM   4453  CH2 TRP B 201     -27.453 -52.763 -25.988  1.00 27.27           C  
ANISOU 4453  CH2 TRP B 201     3896   3085   3382    102   -115    511       C  
ATOM   4454  N   ILE B 202     -28.635 -50.842 -32.145  1.00 21.64           N  
ANISOU 4454  N   ILE B 202     2831   2481   2911    -86   -112    374       N  
ATOM   4455  CA  ILE B 202     -27.793 -50.171 -33.140  1.00 23.59           C  
ANISOU 4455  CA  ILE B 202     3011   2781   3173    -54   -132    367       C  
ATOM   4456  C   ILE B 202     -26.488 -49.777 -32.460  1.00 24.16           C  
ANISOU 4456  C   ILE B 202     3037   2918   3225     -1   -155    382       C  
ATOM   4457  O   ILE B 202     -26.469 -48.843 -31.645  1.00 24.57           O  
ANISOU 4457  O   ILE B 202     3049   3009   3277    -31   -168    383       O  
ATOM   4458  CB  ILE B 202     -28.494 -48.941 -33.734  1.00 22.29           C  
ANISOU 4458  CB  ILE B 202     2793   2644   3033   -107   -141    346       C  
ATOM   4459  CG1 ILE B 202     -29.770 -49.358 -34.472  1.00 22.04           C  
ANISOU 4459  CG1 ILE B 202     2778   2586   3009   -146   -131    315       C  
ATOM   4460  CG2 ILE B 202     -27.549 -48.155 -34.662  1.00 19.00           C  
ANISOU 4460  CG2 ILE B 202     2338   2266   2614    -93   -148    342       C  
ATOM   4461  CD1 ILE B 202     -30.705 -48.187 -34.754  1.00 19.18           C  
ANISOU 4461  CD1 ILE B 202     2373   2263   2653   -164   -149    289       C  
ATOM   4462  N   GLU B 203     -25.399 -50.471 -32.795  1.00 20.34           N  
ANISOU 4462  N   GLU B 203     2552   2461   2715     82   -159    383       N  
ATOM   4463  CA  GLU B 203     -24.117 -50.284 -32.125  1.00 21.92           C  
ANISOU 4463  CA  GLU B 203     2688   2761   2880    149   -186    381       C  
ATOM   4464  C   GLU B 203     -23.192 -49.405 -32.946  1.00 25.97           C  
ANISOU 4464  C   GLU B 203     3093   3376   3397    119   -183    346       C  
ATOM   4465  O   GLU B 203     -23.099 -49.551 -34.167  1.00 25.15           O  
ANISOU 4465  O   GLU B 203     2988   3262   3304    115   -162    333       O  
ATOM   4466  CB  GLU B 203     -23.398 -51.615 -31.874  1.00 21.92           C  
ANISOU 4466  CB  GLU B 203     2748   2755   2826    289   -197    392       C  
ATOM   4467  CG  GLU B 203     -24.119 -52.566 -30.961  1.00 24.77           C  
ANISOU 4467  CG  GLU B 203     3255   3002   3155    318   -187    427       C  
ATOM   4468  CD  GLU B 203     -23.217 -53.689 -30.485  1.00 30.34           C  
ANISOU 4468  CD  GLU B 203     4042   3707   3780    489   -207    442       C  
ATOM   4469  OE1 GLU B 203     -23.715 -54.822 -30.339  1.00 28.88           O  
ANISOU 4469  OE1 GLU B 203     4033   3386   3555    526   -179    468       O  
ATOM   4470  OE2 GLU B 203     -22.015 -53.440 -30.233  1.00 32.95           O  
ANISOU 4470  OE2 GLU B 203     4269   4176   4075    589   -250    423       O  
ATOM   4471  N   SER B 204     -22.473 -48.522 -32.260  1.00 20.86           N  
ANISOU 4471  N   SER B 204     2363   2832   2732     88   -198    326       N  
ATOM   4472  CA  SER B 204     -21.432 -47.713 -32.875  1.00 20.55           C  
ANISOU 4472  CA  SER B 204     2221   2909   2677     36   -183    281       C  
ATOM   4473  C   SER B 204     -20.168 -47.847 -32.050  1.00 23.53           C  
ANISOU 4473  C   SER B 204     2492   3447   3000     98   -214    245       C  
ATOM   4474  O   SER B 204     -20.195 -48.317 -30.907  1.00 24.31           O  
ANISOU 4474  O   SER B 204     2611   3552   3073    176   -252    263       O  
ATOM   4475  CB  SER B 204     -21.853 -46.246 -32.989  1.00 23.51           C  
ANISOU 4475  CB  SER B 204     2607   3258   3067   -106   -158    271       C  
ATOM   4476  OG  SER B 204     -22.361 -45.769 -31.748  1.00 22.97           O  
ANISOU 4476  OG  SER B 204     2562   3167   2998   -132   -179    286       O  
ATOM   4477  N   GLU B 205     -19.053 -47.403 -32.638  1.00 23.13           N  
ANISOU 4477  N   GLU B 205     2326   3541   2922     60   -194    185       N  
ATOM   4478  CA  GLU B 205     -17.739 -47.597 -32.050  1.00 25.36           C  
ANISOU 4478  CA  GLU B 205     2467   4028   3140    130   -225    127       C  
ATOM   4479  C   GLU B 205     -16.816 -46.476 -32.501  1.00 27.69           C  
ANISOU 4479  C   GLU B 205     2635   4477   3409    -25   -181     47       C  
ATOM   4480  O   GLU B 205     -16.983 -45.910 -33.588  1.00 27.13           O  
ANISOU 4480  O   GLU B 205     2598   4349   3359   -139   -121     41       O  
ATOM   4481  CB  GLU B 205     -17.128 -48.943 -32.466  1.00 27.15           C  
ANISOU 4481  CB  GLU B 205     2674   4309   3334    322   -245    120       C  
ATOM   4482  CG  GLU B 205     -16.844 -48.993 -33.982  1.00 27.27           C  
ANISOU 4482  CG  GLU B 205     2664   4332   3363    289   -191     93       C  
ATOM   4483  CD  GLU B 205     -16.348 -50.348 -34.453  1.00 34.98           C  
ANISOU 4483  CD  GLU B 205     3648   5337   4305    489   -205     88       C  
ATOM   4484  OE1 GLU B 205     -16.267 -50.563 -35.681  1.00 35.48           O  
ANISOU 4484  OE1 GLU B 205     3721   5379   4381    480   -161     75       O  
ATOM   4485  OE2 GLU B 205     -16.037 -51.191 -33.589  1.00 35.19           O  
ANISOU 4485  OE2 GLU B 205     3689   5400   4282    664   -260     96       O  
ATOM   4486  N   LYS B 206     -15.820 -46.182 -31.670  1.00 27.00           N  
ANISOU 4486  N   LYS B 206     2406   4590   3262    -33   -208    -22       N  
ATOM   4487  CA  LYS B 206     -14.786 -45.212 -32.013  1.00 24.98           C  
ANISOU 4487  CA  LYS B 206     2009   4520   2962   -198   -158   -121       C  
ATOM   4488  C   LYS B 206     -13.637 -45.948 -32.687  1.00 29.95           C  
ANISOU 4488  C   LYS B 206     2481   5355   3545    -94   -155   -193       C  
ATOM   4489  O   LYS B 206     -12.891 -46.680 -32.032  1.00 35.23           O  
ANISOU 4489  O   LYS B 206     3029   6199   4157     75   -220   -233       O  
ATOM   4490  CB  LYS B 206     -14.300 -44.461 -30.773  1.00 26.14           C  
ANISOU 4490  CB  LYS B 206     2067   4807   3059   -285   -186   -179       C  
ATOM   4491  CG  LYS B 206     -13.095 -43.536 -31.023  1.00 30.02           C  
ANISOU 4491  CG  LYS B 206     2391   5532   3483   -477   -129   -307       C  
ATOM   4492  CD  LYS B 206     -13.412 -42.497 -32.100  1.00 28.65           C  
ANISOU 4492  CD  LYS B 206     2330   5226   3330   -702    -22   -306       C  
ATOM   4493  CE  LYS B 206     -12.282 -41.481 -32.248  1.00 34.93           C  
ANISOU 4493  CE  LYS B 206     2996   6231   4046   -943     55   -438       C  
ATOM   4494  NZ  LYS B 206     -12.066 -40.716 -30.987  1.00 51.01           N  
ANISOU 4494  NZ  LYS B 206     4994   8350   6036  -1057     32   -490       N  
ATOM   4495  N   ASN B 207     -13.512 -45.758 -33.992  1.00 32.56           N  
ANISOU 4495  N   ASN B 207     2820   5663   3887   -179    -81   -210       N  
ATOM   4496  CA  ASN B 207     -12.353 -46.174 -34.773  1.00 40.27           C  
ANISOU 4496  CA  ASN B 207     3631   6856   4813   -135    -51   -299       C  
ATOM   4497  C   ASN B 207     -11.453 -44.949 -34.947  1.00 42.76           C  
ANISOU 4497  C   ASN B 207     3812   7361   5073   -388     26   -413       C  
ATOM   4498  O   ASN B 207     -11.163 -44.296 -33.942  1.00 46.37           O  
ANISOU 4498  O   ASN B 207     4201   7922   5496   -482      5   -460       O  
ATOM   4499  CB  ASN B 207     -12.823 -46.844 -36.070  1.00 46.60           C  
ANISOU 4499  CB  ASN B 207     4544   7507   5656    -64    -16   -246       C  
ATOM   4500  CG  ASN B 207     -11.689 -47.458 -36.889  1.00 55.38           C  
ANISOU 4500  CG  ASN B 207     5498   8831   6714     25     12   -332       C  
ATOM   4501  OD1 ASN B 207     -11.076 -46.788 -37.727  1.00 53.72           O  
ANISOU 4501  OD1 ASN B 207     5209   8730   6474   -144     99   -406       O  
ATOM   4502  ND2 ASN B 207     -11.423 -48.744 -36.666  1.00 65.69           N  
ANISOU 4502  ND2 ASN B 207     6776  10187   7996    292    -53   -325       N  
ATOM   4503  N   ASP B 208     -11.022 -44.577 -36.156  1.00 47.14           N  
ANISOU 4503  N   ASP B 208     4345   7959   5610   -523    122   -463       N  
ATOM   4504  CA  ASP B 208     -10.461 -43.241 -36.331  1.00 51.97           C  
ANISOU 4504  CA  ASP B 208     4914   8667   6167   -823    220   -553       C  
ATOM   4505  C   ASP B 208     -11.515 -42.185 -36.025  1.00 44.87           C  
ANISOU 4505  C   ASP B 208     4243   7505   5303   -981    242   -475       C  
ATOM   4506  O   ASP B 208     -11.221 -41.143 -35.426  1.00 45.64           O  
ANISOU 4506  O   ASP B 208     4329   7658   5353  -1183    278   -534       O  
ATOM   4507  CB  ASP B 208      -9.913 -43.066 -37.748  1.00 60.84           C  
ANISOU 4507  CB  ASP B 208     6013   9846   7256   -942    331   -610       C  
ATOM   4508  CG  ASP B 208      -8.705 -43.942 -38.019  1.00 76.39           C  
ANISOU 4508  CG  ASP B 208     7723  12130   9172   -808    323   -718       C  
ATOM   4509  OD1 ASP B 208      -7.982 -44.280 -37.057  1.00 73.09           O  
ANISOU 4509  OD1 ASP B 208     7102  11958   8710   -705    252   -794       O  
ATOM   4510  OD2 ASP B 208      -8.480 -44.295 -39.198  1.00 90.18           O  
ANISOU 4510  OD2 ASP B 208     9470  13884  10911   -792    385   -732       O  
ATOM   4511  N   THR B 209     -12.754 -42.452 -36.415  1.00 39.69           N  
ANISOU 4511  N   THR B 209     3793   6569   4718   -886    220   -351       N  
ATOM   4512  CA  THR B 209     -13.905 -41.632 -36.087  1.00 34.20           C  
ANISOU 4512  CA  THR B 209     3312   5627   4057   -965    220   -270       C  
ATOM   4513  C   THR B 209     -14.992 -42.551 -35.544  1.00 36.73           C  
ANISOU 4513  C   THR B 209     3707   5796   4453   -744    122   -165       C  
ATOM   4514  O   THR B 209     -14.889 -43.781 -35.623  1.00 30.07           O  
ANISOU 4514  O   THR B 209     2796   4999   3631   -551     70   -147       O  
ATOM   4515  CB  THR B 209     -14.410 -40.862 -37.318  1.00 48.02           C  
ANISOU 4515  CB  THR B 209     5256   7191   5798  -1098    310   -237       C  
ATOM   4516  OG1 THR B 209     -14.946 -41.787 -38.271  1.00 50.20           O  
ANISOU 4516  OG1 THR B 209     5583   7369   6121   -941    290   -174       O  
ATOM   4517  CG2 THR B 209     -13.271 -40.090 -37.986  1.00 48.33           C  
ANISOU 4517  CG2 THR B 209     5235   7379   5749  -1329    428   -345       C  
ATOM   4518  N   TRP B 210     -16.040 -41.949 -34.985  1.00 23.74           N  
ANISOU 4518  N   TRP B 210     2214   3968   2837   -776    104   -101       N  
ATOM   4519  CA  TRP B 210     -17.209 -42.725 -34.594  1.00 27.95           C  
ANISOU 4519  CA  TRP B 210     2835   4348   3437   -606     32     -8       C  
ATOM   4520  C   TRP B 210     -17.952 -43.202 -35.840  1.00 28.23           C  
ANISOU 4520  C   TRP B 210     2976   4240   3511   -542     48     46       C  
ATOM   4521  O   TRP B 210     -18.101 -42.462 -36.812  1.00 25.87           O  
ANISOU 4521  O   TRP B 210     2772   3865   3193   -647    110     45       O  
ATOM   4522  CB  TRP B 210     -18.122 -41.889 -33.696  1.00 25.86           C  
ANISOU 4522  CB  TRP B 210     2688   3953   3185   -661     17     30       C  
ATOM   4523  CG  TRP B 210     -17.692 -41.931 -32.261  1.00 25.12           C  
ANISOU 4523  CG  TRP B 210     2498   3977   3070   -644    -33      1       C  
ATOM   4524  CD1 TRP B 210     -16.853 -41.066 -31.628  1.00 28.14           C  
ANISOU 4524  CD1 TRP B 210     2807   4492   3393   -788    -11    -76       C  
ATOM   4525  CD2 TRP B 210     -18.063 -42.920 -31.293  1.00 22.73           C  
ANISOU 4525  CD2 TRP B 210     2171   3673   2793   -478   -111     44       C  
ATOM   4526  NE1 TRP B 210     -16.677 -41.452 -30.307  1.00 21.95           N  
ANISOU 4526  NE1 TRP B 210     1942   3802   2597   -706    -82    -83       N  
ATOM   4527  CE2 TRP B 210     -17.409 -42.591 -30.084  1.00 27.05           C  
ANISOU 4527  CE2 TRP B 210     2628   4360   3292   -511   -141     -6       C  
ATOM   4528  CE3 TRP B 210     -18.870 -44.065 -31.338  1.00 27.18           C  
ANISOU 4528  CE3 TRP B 210     2795   4131   3403   -317   -150    114       C  
ATOM   4529  CZ2 TRP B 210     -17.551 -43.362 -28.913  1.00 26.47           C  
ANISOU 4529  CZ2 TRP B 210     2532   4313   3212   -368   -215     22       C  
ATOM   4530  CZ3 TRP B 210     -19.016 -44.834 -30.175  1.00 22.37           C  
ANISOU 4530  CZ3 TRP B 210     2177   3536   2786   -194   -212    140       C  
ATOM   4531  CH2 TRP B 210     -18.350 -44.472 -28.976  1.00 24.80           C  
ANISOU 4531  CH2 TRP B 210     2404   3977   3042   -212   -246     98       C  
ATOM   4532  N   ARG B 211     -18.400 -44.453 -35.822  1.00 25.46           N  
ANISOU 4532  N   ARG B 211     2624   3849   3200   -372     -4     90       N  
ATOM   4533  CA  ARG B 211     -19.043 -45.030 -36.996  1.00 24.31           C  
ANISOU 4533  CA  ARG B 211     2564   3590   3084   -313      7    128       C  
ATOM   4534  C   ARG B 211     -19.972 -46.142 -36.548  1.00 25.67           C  
ANISOU 4534  C   ARG B 211     2789   3664   3300   -173    -50    185       C  
ATOM   4535  O   ARG B 211     -19.813 -46.711 -35.464  1.00 23.49           O  
ANISOU 4535  O   ARG B 211     2473   3431   3021    -92    -93    191       O  
ATOM   4536  CB  ARG B 211     -18.005 -45.592 -37.984  1.00 26.94           C  
ANISOU 4536  CB  ARG B 211     2808   4040   3387   -285     43     80       C  
ATOM   4537  CG  ARG B 211     -17.300 -46.816 -37.378  1.00 30.73           C  
ANISOU 4537  CG  ARG B 211     3176   4645   3855   -119     -5     60       C  
ATOM   4538  CD  ARG B 211     -16.091 -47.250 -38.133  1.00 36.18           C  
ANISOU 4538  CD  ARG B 211     3743   5504   4501    -79     28     -9       C  
ATOM   4539  NE  ARG B 211     -15.569 -48.519 -37.633  1.00 32.87           N  
ANISOU 4539  NE  ARG B 211     3256   5173   4059    130    -27    -19       N  
ATOM   4540  CZ  ARG B 211     -14.520 -49.139 -38.163  1.00 37.17           C  
ANISOU 4540  CZ  ARG B 211     3686   5880   4557    229    -13    -82       C  
ATOM   4541  NH1 ARG B 211     -13.896 -48.605 -39.208  1.00 35.01           N  
ANISOU 4541  NH1 ARG B 211     3341   5702   4259    113     61   -142       N  
ATOM   4542  NH2 ARG B 211     -14.097 -50.292 -37.661  1.00 34.00           N  
ANISOU 4542  NH2 ARG B 211     3255   5543   4120    452    -69    -87       N  
ATOM   4543  N   LEU B 212     -20.932 -46.459 -37.413  1.00 21.84           N  
ANISOU 4543  N   LEU B 212     2404   3052   2844   -151    -46    220       N  
ATOM   4544  CA  LEU B 212     -21.785 -47.615 -37.191  1.00 22.35           C  
ANISOU 4544  CA  LEU B 212     2525   3028   2939    -48    -81    257       C  
ATOM   4545  C   LEU B 212     -20.952 -48.889 -37.180  1.00 23.89           C  
ANISOU 4545  C   LEU B 212     2678   3287   3113     77    -91    244       C  
ATOM   4546  O   LEU B 212     -20.158 -49.129 -38.094  1.00 24.60           O  
ANISOU 4546  O   LEU B 212     2723   3443   3180    101    -64    212       O  
ATOM   4547  CB  LEU B 212     -22.854 -47.693 -38.285  1.00 23.19           C  
ANISOU 4547  CB  LEU B 212     2723   3021   3066    -63    -71    275       C  
ATOM   4548  CG  LEU B 212     -23.825 -48.869 -38.192  1.00 25.13           C  
ANISOU 4548  CG  LEU B 212     3034   3179   3334      1    -93    297       C  
ATOM   4549  CD1 LEU B 212     -24.734 -48.698 -36.985  1.00 23.19           C  
ANISOU 4549  CD1 LEU B 212     2812   2891   3108    -18   -117    319       C  
ATOM   4550  CD2 LEU B 212     -24.657 -48.996 -39.503  1.00 23.76           C  
ANISOU 4550  CD2 LEU B 212     2923   2938   3167    -17    -84    292       C  
ATOM   4551  N   LYS B 213     -21.133 -49.702 -36.135  1.00 22.12           N  
ANISOU 4551  N   LYS B 213     2482   3038   2884    167   -126    268       N  
ATOM   4552  CA  LYS B 213     -20.406 -50.951 -35.940  1.00 27.46           C  
ANISOU 4552  CA  LYS B 213     3160   3754   3520    322   -143    262       C  
ATOM   4553  C   LYS B 213     -21.192 -52.165 -36.427  1.00 28.02           C  
ANISOU 4553  C   LYS B 213     3374   3677   3597    383   -133    291       C  
ATOM   4554  O   LYS B 213     -20.665 -53.009 -37.166  1.00 24.64           O  
ANISOU 4554  O   LYS B 213     2968   3254   3141    478   -120    275       O  
ATOM   4555  CB  LYS B 213     -20.078 -51.125 -34.449  1.00 23.93           C  
ANISOU 4555  CB  LYS B 213     2695   3358   3039    395   -187    272       C  
ATOM   4556  CG  LYS B 213     -19.476 -52.471 -34.091  1.00 28.00           C  
ANISOU 4556  CG  LYS B 213     3260   3885   3492    591   -212    276       C  
ATOM   4557  CD  LYS B 213     -19.503 -52.664 -32.581  1.00 29.31           C  
ANISOU 4557  CD  LYS B 213     3464   4054   3619    658   -256    302       C  
ATOM   4558  CE  LYS B 213     -18.876 -53.971 -32.151  1.00 33.85           C  
ANISOU 4558  CE  LYS B 213     4121   4632   4108    882   -287    310       C  
ATOM   4559  NZ  LYS B 213     -19.336 -54.297 -30.766  1.00 37.29           N  
ANISOU 4559  NZ  LYS B 213     4675   4989   4504    926   -315    356       N  
ATOM   4560  N   ARG B 214     -22.446 -52.271 -36.000  1.00 25.01           N  
ANISOU 4560  N   ARG B 214     3089   3170   3243    322   -133    325       N  
ATOM   4561  CA  ARG B 214     -23.329 -53.398 -36.286  1.00 26.09           C  
ANISOU 4561  CA  ARG B 214     3370   3165   3376    337   -115    341       C  
ATOM   4562  C   ARG B 214     -24.711 -52.995 -35.810  1.00 29.41           C  
ANISOU 4562  C   ARG B 214     3829   3513   3833    218   -111    355       C  
ATOM   4563  O   ARG B 214     -24.852 -52.083 -34.990  1.00 26.79           O  
ANISOU 4563  O   ARG B 214     3436   3225   3516    172   -128    363       O  
ATOM   4564  CB  ARG B 214     -22.884 -54.687 -35.576  1.00 22.75           C  
ANISOU 4564  CB  ARG B 214     3059   2694   2891    480   -120    359       C  
ATOM   4565  CG  ARG B 214     -22.946 -54.578 -34.055  1.00 27.69           C  
ANISOU 4565  CG  ARG B 214     3705   3324   3494    500   -146    387       C  
ATOM   4566  CD  ARG B 214     -22.574 -55.889 -33.364  1.00 34.33           C  
ANISOU 4566  CD  ARG B 214     4702   4090   4250    657   -150    412       C  
ATOM   4567  NE  ARG B 214     -23.418 -56.990 -33.816  1.00 35.11           N  
ANISOU 4567  NE  ARG B 214     4995   4013   4331    629   -100    422       N  
ATOM   4568  CZ  ARG B 214     -24.521 -57.400 -33.195  1.00 46.43           C  
ANISOU 4568  CZ  ARG B 214     6569   5317   5755    532    -65    443       C  
ATOM   4569  NH1 ARG B 214     -25.237 -58.401 -33.709  1.00 40.19           N  
ANISOU 4569  NH1 ARG B 214     5952   4378   4939    479    -10    436       N  
ATOM   4570  NH2 ARG B 214     -24.908 -56.819 -32.056  1.00 33.38           N  
ANISOU 4570  NH2 ARG B 214     4887   3687   4111    474    -78    462       N  
ATOM   4571  N   ALA B 215     -25.731 -53.682 -36.324  1.00 27.40           N  
ANISOU 4571  N   ALA B 215     3668   3160   3584    167    -85    349       N  
ATOM   4572  CA  ALA B 215     -27.091 -53.420 -35.875  1.00 21.69           C  
ANISOU 4572  CA  ALA B 215     2963   2396   2883     57    -77    344       C  
ATOM   4573  C   ALA B 215     -27.919 -54.681 -36.043  1.00 31.18           C  
ANISOU 4573  C   ALA B 215     4299   3489   4058     13    -37    330       C  
ATOM   4574  O   ALA B 215     -27.691 -55.476 -36.959  1.00 28.79           O  
ANISOU 4574  O   ALA B 215     4065   3140   3736     42    -19    315       O  
ATOM   4575  CB  ALA B 215     -27.739 -52.260 -36.648  1.00 21.45           C  
ANISOU 4575  CB  ALA B 215     2841   2418   2892    -19    -92    321       C  
ATOM   4576  N   HIS B 216     -28.877 -54.868 -35.144  1.00 24.97           N  
ANISOU 4576  N   HIS B 216     3560   2663   3264    -68    -16    328       N  
ATOM   4577  CA  HIS B 216     -29.860 -55.927 -35.316  1.00 23.51           C  
ANISOU 4577  CA  HIS B 216     3497   2388   3049   -166     38    295       C  
ATOM   4578  C   HIS B 216     -31.245 -55.315 -35.185  1.00 30.53           C  
ANISOU 4578  C   HIS B 216     4296   3339   3964   -302     44    249       C  
ATOM   4579  O   HIS B 216     -31.508 -54.557 -34.243  1.00 27.61           O  
ANISOU 4579  O   HIS B 216     3861   3019   3611   -315     31    261       O  
ATOM   4580  CB  HIS B 216     -29.670 -57.076 -34.324  1.00 27.60           C  
ANISOU 4580  CB  HIS B 216     4204   2784   3498   -141     82    325       C  
ATOM   4581  CG  HIS B 216     -30.330 -58.341 -34.778  1.00 48.26           C  
ANISOU 4581  CG  HIS B 216     6993   5279   6063   -233    150    290       C  
ATOM   4582  ND1 HIS B 216     -29.736 -59.210 -35.668  1.00 59.32           N  
ANISOU 4582  ND1 HIS B 216     8508   6603   7430   -162    164    287       N  
ATOM   4583  CD2 HIS B 216     -31.564 -58.840 -34.531  1.00 46.93           C  
ANISOU 4583  CD2 HIS B 216     6898   5066   5869   -410    214    243       C  
ATOM   4584  CE1 HIS B 216     -30.561 -60.211 -35.920  1.00 58.10           C  
ANISOU 4584  CE1 HIS B 216     8510   6339   7225   -292    235    245       C  
ATOM   4585  NE2 HIS B 216     -31.677 -60.011 -35.243  1.00 48.94           N  
ANISOU 4585  NE2 HIS B 216     7323   5204   6069   -454    269    214       N  
ATOM   4586  N   LEU B 217     -32.115 -55.608 -36.155  1.00 26.73           N  
ANISOU 4586  N   LEU B 217     3803   2872   3482   -393     60    188       N  
ATOM   4587  CA  LEU B 217     -33.468 -55.054 -36.195  1.00 22.94           C  
ANISOU 4587  CA  LEU B 217     3212   2490   3015   -504     58    124       C  
ATOM   4588  C   LEU B 217     -34.452 -56.205 -36.327  1.00 26.57           C  
ANISOU 4588  C   LEU B 217     3758   2911   3428   -659    126     54       C  
ATOM   4589  O   LEU B 217     -34.344 -57.012 -37.256  1.00 27.75           O  
ANISOU 4589  O   LEU B 217     3988   3004   3553   -682    146     29       O  
ATOM   4590  CB  LEU B 217     -33.638 -54.073 -37.361  1.00 30.25           C  
ANISOU 4590  CB  LEU B 217     4005   3518   3969   -460     -1     97       C  
ATOM   4591  CG  LEU B 217     -32.484 -53.146 -37.774  1.00 32.72           C  
ANISOU 4591  CG  LEU B 217     4277   3843   4310   -331    -50    153       C  
ATOM   4592  CD1 LEU B 217     -32.933 -52.349 -38.984  1.00 32.87           C  
ANISOU 4592  CD1 LEU B 217     4215   3943   4332   -312    -94    117       C  
ATOM   4593  CD2 LEU B 217     -32.039 -52.201 -36.673  1.00 27.81           C  
ANISOU 4593  CD2 LEU B 217     3612   3244   3709   -283    -70    200       C  
ATOM   4594  N   ILE B 218     -35.389 -56.313 -35.387  1.00 25.75           N  
ANISOU 4594  N   ILE B 218     3647   2833   3303   -778    172     17       N  
ATOM   4595  CA  ILE B 218     -36.401 -57.362 -35.464  1.00 22.95           C  
ANISOU 4595  CA  ILE B 218     3368   2458   2893   -968    253    -66       C  
ATOM   4596  C   ILE B 218     -37.752 -56.807 -35.918  1.00 27.16           C  
ANISOU 4596  C   ILE B 218     3704   3183   3431  -1073    237   -177       C  
ATOM   4597  O   ILE B 218     -38.775 -57.508 -35.853  1.00 24.19           O  
ANISOU 4597  O   ILE B 218     3340   2847   3006  -1264    308   -273       O  
ATOM   4598  CB  ILE B 218     -36.501 -58.133 -34.135  1.00 26.66           C  
ANISOU 4598  CB  ILE B 218     4007   2814   3309  -1058    340    -44       C  
ATOM   4599  CG1 ILE B 218     -36.876 -57.203 -32.978  1.00 21.99           C  
ANISOU 4599  CG1 ILE B 218     3299   2314   2740  -1052    328    -32       C  
ATOM   4600  CG2 ILE B 218     -35.173 -58.834 -33.860  1.00 27.70           C  
ANISOU 4600  CG2 ILE B 218     4352   2763   3412   -924    347     55       C  
ATOM   4601  CD1 ILE B 218     -37.100 -57.928 -31.622  1.00 29.43           C  
ANISOU 4601  CD1 ILE B 218     4412   3153   3617  -1157    421    -16       C  
ATOM   4602  N   GLU B 219     -37.759 -55.569 -36.410  1.00 26.90           N  
ANISOU 4602  N   GLU B 219     3499   3276   3444   -950    148   -174       N  
ATOM   4603  CA  GLU B 219     -38.898 -54.888 -37.011  1.00 29.64           C  
ANISOU 4603  CA  GLU B 219     3654   3821   3786   -976    104   -274       C  
ATOM   4604  C   GLU B 219     -38.323 -53.823 -37.938  1.00 27.58           C  
ANISOU 4604  C   GLU B 219     3324   3596   3559   -793      7   -229       C  
ATOM   4605  O   GLU B 219     -37.136 -53.500 -37.878  1.00 28.61           O  
ANISOU 4605  O   GLU B 219     3527   3621   3722   -677    -15   -130       O  
ATOM   4606  CB  GLU B 219     -39.814 -54.249 -35.950  1.00 27.87           C  
ANISOU 4606  CB  GLU B 219     3307   3725   3559  -1016    116   -318       C  
ATOM   4607  CG  GLU B 219     -39.176 -53.001 -35.249  1.00 26.58           C  
ANISOU 4607  CG  GLU B 219     3110   3548   3440   -848     61   -227       C  
ATOM   4608  CD  GLU B 219     -39.936 -52.550 -34.000  1.00 27.19           C  
ANISOU 4608  CD  GLU B 219     3112   3713   3508   -893     91   -259       C  
ATOM   4609  OE1 GLU B 219     -39.420 -51.695 -33.244  1.00 27.69           O  
ANISOU 4609  OE1 GLU B 219     3178   3744   3598   -787     64   -188       O  
ATOM   4610  OE2 GLU B 219     -41.044 -53.059 -33.771  1.00 26.45           O  
ANISOU 4610  OE2 GLU B 219     2952   3724   3373  -1045    148   -362       O  
ATOM   4611  N   MET B 220     -39.177 -53.280 -38.802  1.00 26.21           N  
ANISOU 4611  N   MET B 220     3012   3581   3364   -770    -48   -311       N  
ATOM   4612  CA  MET B 220     -38.803 -52.193 -39.712  1.00 29.90           C  
ANISOU 4612  CA  MET B 220     3435   4085   3841   -599   -136   -277       C  
ATOM   4613  C   MET B 220     -39.871 -51.121 -39.538  1.00 27.84           C  
ANISOU 4613  C   MET B 220     3016   4005   3555   -532   -190   -342       C  
ATOM   4614  O   MET B 220     -40.911 -51.171 -40.201  1.00 29.33           O  
ANISOU 4614  O   MET B 220     3090   4357   3696   -554   -221   -450       O  
ATOM   4615  CB  MET B 220     -38.723 -52.670 -41.171  1.00 36.06           C  
ANISOU 4615  CB  MET B 220     4240   4869   4593   -600   -160   -311       C  
ATOM   4616  CG  MET B 220     -38.052 -54.025 -41.362  1.00 34.81           C  
ANISOU 4616  CG  MET B 220     4231   4560   4436   -697    -92   -290       C  
ATOM   4617  SD  MET B 220     -36.272 -53.921 -41.167  1.00 37.41           S  
ANISOU 4617  SD  MET B 220     4698   4705   4811   -574    -85   -148       S  
ATOM   4618  CE  MET B 220     -35.920 -55.533 -40.449  1.00 32.92           C  
ANISOU 4618  CE  MET B 220     4302   3980   4226   -692     13   -136       C  
ATOM   4619  N   LYS B 221     -39.641 -50.182 -38.624  1.00 23.06           N  
ANISOU 4619  N   LYS B 221     2404   3382   2974   -447   -201   -285       N  
ATOM   4620  CA  LYS B 221     -40.654 -49.176 -38.335  1.00 29.51           C  
ANISOU 4620  CA  LYS B 221     3090   4363   3760   -364   -246   -347       C  
ATOM   4621  C   LYS B 221     -40.290 -47.857 -38.998  1.00 24.43           C  
ANISOU 4621  C   LYS B 221     2477   3708   3099   -165   -326   -297       C  
ATOM   4622  O   LYS B 221     -39.146 -47.636 -39.399  1.00 23.56           O  
ANISOU 4622  O   LYS B 221     2486   3453   3011   -118   -330   -205       O  
ATOM   4623  CB  LYS B 221     -40.827 -48.979 -36.827  1.00 24.44           C  
ANISOU 4623  CB  LYS B 221     2431   3717   3138   -406   -199   -333       C  
ATOM   4624  CG  LYS B 221     -39.555 -48.800 -36.047  1.00 28.07           C  
ANISOU 4624  CG  LYS B 221     3023   3994   3646   -383   -173   -209       C  
ATOM   4625  CD  LYS B 221     -39.930 -48.557 -34.584  1.00 28.97           C  
ANISOU 4625  CD  LYS B 221     3108   4134   3765   -420   -133   -213       C  
ATOM   4626  CE  LYS B 221     -38.728 -48.188 -33.757  1.00 24.23           C  
ANISOU 4626  CE  LYS B 221     2620   3385   3201   -379   -123   -101       C  
ATOM   4627  NZ  LYS B 221     -37.771 -49.335 -33.606  1.00 28.34           N  
ANISOU 4627  NZ  LYS B 221     3259   3766   3741   -461    -76    -42       N  
ATOM   4628  N   THR B 222     -41.287 -46.980 -39.108  1.00 23.79           N  
ANISOU 4628  N   THR B 222     2291   3784   2963    -48   -384   -366       N  
ATOM   4629  CA  THR B 222     -41.145 -45.752 -39.884  1.00 25.76           C  
ANISOU 4629  CA  THR B 222     2597   4026   3164    153   -461   -334       C  
ATOM   4630  C   THR B 222     -41.416 -44.489 -39.075  1.00 29.33           C  
ANISOU 4630  C   THR B 222     3056   4496   3593    291   -483   -319       C  
ATOM   4631  O   THR B 222     -41.614 -43.425 -39.674  1.00 26.44           O  
ANISOU 4631  O   THR B 222     2739   4148   3157    477   -549   -316       O  
ATOM   4632  CB  THR B 222     -42.074 -45.783 -41.108  1.00 23.46           C  
ANISOU 4632  CB  THR B 222     2215   3906   2794    232   -534   -434       C  
ATOM   4633  OG1 THR B 222     -43.444 -45.862 -40.689  1.00 25.94           O  
ANISOU 4633  OG1 THR B 222     2338   4453   3066    227   -550   -565       O  
ATOM   4634  CG2 THR B 222     -41.744 -46.981 -42.008  1.00 25.44           C  
ANISOU 4634  CG2 THR B 222     2484   4122   3060     98   -512   -449       C  
ATOM   4635  N   CYS B 223     -41.487 -44.575 -37.745  1.00 22.53           N  
ANISOU 4635  N   CYS B 223     2161   3628   2772    214   -430   -314       N  
ATOM   4636  CA  CYS B 223     -41.570 -43.360 -36.940  1.00 25.15           C  
ANISOU 4636  CA  CYS B 223     2530   3943   3083    339   -443   -288       C  
ATOM   4637  C   CYS B 223     -40.202 -42.661 -36.933  1.00 26.24           C  
ANISOU 4637  C   CYS B 223     2860   3866   3244    372   -432   -164       C  
ATOM   4638  O   CYS B 223     -39.199 -43.184 -37.435  1.00 24.18           O  
ANISOU 4638  O   CYS B 223     2676   3490   3021    292   -410   -103       O  
ATOM   4639  CB  CYS B 223     -42.049 -43.681 -35.507  1.00 23.00           C  
ANISOU 4639  CB  CYS B 223     2167   3732   2841    237   -383   -324       C  
ATOM   4640  SG  CYS B 223     -41.140 -45.068 -34.749  1.00 27.11           S  
ANISOU 4640  SG  CYS B 223     2739   4113   3446     -3   -289   -262       S  
ATOM   4641  N   GLU B 224     -40.162 -41.453 -36.375  1.00 23.99           N  
ANISOU 4641  N   GLU B 224     2653   3535   2926    486   -443   -136       N  
ATOM   4642  CA  GLU B 224     -38.920 -40.686 -36.278  1.00 22.66           C  
ANISOU 4642  CA  GLU B 224     2666   3179   2766    492   -423    -36       C  
ATOM   4643  C   GLU B 224     -38.259 -40.928 -34.926  1.00 23.99           C  
ANISOU 4643  C   GLU B 224     2837   3278   2999    365   -363      7       C  
ATOM   4644  O   GLU B 224     -38.880 -40.695 -33.889  1.00 25.11           O  
ANISOU 4644  O   GLU B 224     2923   3480   3138    378   -351    -26       O  
ATOM   4645  CB  GLU B 224     -39.186 -39.189 -36.455  1.00 24.67           C  
ANISOU 4645  CB  GLU B 224     3050   3394   2928    679   -461    -30       C  
ATOM   4646  CG  GLU B 224     -39.689 -38.814 -37.836  1.00 31.82           C  
ANISOU 4646  CG  GLU B 224     4002   4343   3745    836   -527    -58       C  
ATOM   4647  CD  GLU B 224     -39.862 -37.314 -37.971  1.00 36.51           C  
ANISOU 4647  CD  GLU B 224     4781   4860   4229   1036   -557    -40       C  
ATOM   4648  OE1 GLU B 224     -39.749 -36.598 -36.945  1.00 38.29           O  
ANISOU 4648  OE1 GLU B 224     5075   5022   4451   1049   -527    -22       O  
ATOM   4649  OE2 GLU B 224     -40.101 -36.856 -39.096  1.00 39.74           O  
ANISOU 4649  OE2 GLU B 224     5289   5265   4547   1182   -608    -45       O  
ATOM   4650  N   TRP B 225     -37.001 -41.385 -34.941  1.00 22.03           N  
ANISOU 4650  N   TRP B 225     2650   2919   2801    255   -327     75       N  
ATOM   4651  CA  TRP B 225     -36.222 -41.546 -33.708  1.00 20.02           C  
ANISOU 4651  CA  TRP B 225     2411   2602   2592    157   -282    118       C  
ATOM   4652  C   TRP B 225     -35.971 -40.165 -33.105  1.00 23.66           C  
ANISOU 4652  C   TRP B 225     2978   2998   3014    218   -280    141       C  
ATOM   4653  O   TRP B 225     -35.407 -39.296 -33.785  1.00 21.43           O  
ANISOU 4653  O   TRP B 225     2821   2631   2689    261   -287    171       O  
ATOM   4654  CB  TRP B 225     -34.893 -42.261 -34.008  1.00 16.69           C  
ANISOU 4654  CB  TRP B 225     2025   2104   2214     63   -257    173       C  
ATOM   4655  CG  TRP B 225     -34.171 -42.745 -32.784  1.00 18.32           C  
ANISOU 4655  CG  TRP B 225     2221   2280   2459    -24   -222    206       C  
ATOM   4656  CD1 TRP B 225     -33.519 -41.981 -31.844  1.00 25.23           C  
ANISOU 4656  CD1 TRP B 225     3147   3113   3327    -39   -209    234       C  
ATOM   4657  CD2 TRP B 225     -34.050 -44.103 -32.350  1.00 23.04           C  
ANISOU 4657  CD2 TRP B 225     2772   2888   3092   -101   -196    209       C  
ATOM   4658  NE1 TRP B 225     -33.000 -42.791 -30.856  1.00 23.73           N  
ANISOU 4658  NE1 TRP B 225     2928   2922   3167   -107   -187    255       N  
ATOM   4659  CE2 TRP B 225     -33.318 -44.096 -31.141  1.00 21.33           C  
ANISOU 4659  CE2 TRP B 225     2579   2641   2886   -139   -177    244       C  
ATOM   4660  CE3 TRP B 225     -34.491 -45.328 -32.865  1.00 23.80           C  
ANISOU 4660  CE3 TRP B 225     2830   3011   3202   -144   -186    182       C  
ATOM   4661  CZ2 TRP B 225     -33.006 -45.264 -30.451  1.00 25.07           C  
ANISOU 4661  CZ2 TRP B 225     3050   3101   3374   -193   -152    261       C  
ATOM   4662  CZ3 TRP B 225     -34.183 -46.493 -32.166  1.00 25.98           C  
ANISOU 4662  CZ3 TRP B 225     3120   3257   3495   -215   -149    199       C  
ATOM   4663  CH2 TRP B 225     -33.445 -46.448 -30.976  1.00 27.17           C  
ANISOU 4663  CH2 TRP B 225     3307   3370   3648   -227   -135    242       C  
ATOM   4664  N   PRO B 226     -36.372 -39.911 -31.859  1.00 23.41           N  
ANISOU 4664  N   PRO B 226     2918   2993   2984    213   -264    126       N  
ATOM   4665  CA  PRO B 226     -36.266 -38.547 -31.312  1.00 24.40           C  
ANISOU 4665  CA  PRO B 226     3160   3052   3058    280   -262    137       C  
ATOM   4666  C   PRO B 226     -34.827 -38.134 -31.014  1.00 22.98           C  
ANISOU 4666  C   PRO B 226     3090   2756   2887    185   -231    195       C  
ATOM   4667  O   PRO B 226     -34.053 -38.883 -30.410  1.00 22.72           O  
ANISOU 4667  O   PRO B 226     3004   2725   2904     74   -209    219       O  
ATOM   4668  CB  PRO B 226     -37.101 -38.607 -30.022  1.00 22.36           C  
ANISOU 4668  CB  PRO B 226     2820   2873   2805    284   -247     97       C  
ATOM   4669  CG  PRO B 226     -37.040 -40.074 -29.600  1.00 23.62           C  
ANISOU 4669  CG  PRO B 226     2858   3086   3029    154   -220     96       C  
ATOM   4670  CD  PRO B 226     -37.009 -40.865 -30.924  1.00 19.48           C  
ANISOU 4670  CD  PRO B 226     2297   2583   2523    143   -240     91       C  
ATOM   4671  N   LYS B 227     -34.496 -36.899 -31.415  1.00 20.56           N  
ANISOU 4671  N   LYS B 227     2946   2353   2514    233   -227    210       N  
ATOM   4672  CA  LYS B 227     -33.169 -36.346 -31.166  1.00 22.13           C  
ANISOU 4672  CA  LYS B 227     3251   2456   2700    122   -188    244       C  
ATOM   4673  C   LYS B 227     -32.855 -36.278 -29.675  1.00 26.03           C  
ANISOU 4673  C   LYS B 227     3715   2960   3213     47   -167    243       C  
ATOM   4674  O   LYS B 227     -31.685 -36.372 -29.285  1.00 22.14           O  
ANISOU 4674  O   LYS B 227     3222   2453   2736    -74   -142    260       O  
ATOM   4675  CB  LYS B 227     -33.066 -34.944 -31.788  1.00 20.87           C  
ANISOU 4675  CB  LYS B 227     3311   2176   2444    179   -173    251       C  
ATOM   4676  CG  LYS B 227     -32.907 -34.923 -33.322  1.00 25.28           C  
ANISOU 4676  CG  LYS B 227     3944   2695   2967    215   -181    265       C  
ATOM   4677  CD  LYS B 227     -33.136 -33.499 -33.797  1.00 29.92           C  
ANISOU 4677  CD  LYS B 227     4784   3151   3433    313   -169    269       C  
ATOM   4678  CE  LYS B 227     -32.820 -33.284 -35.254  1.00 29.58           C  
ANISOU 4678  CE  LYS B 227     4872   3038   3330    333   -162    290       C  
ATOM   4679  NZ  LYS B 227     -33.005 -31.822 -35.588  1.00 25.67           N  
ANISOU 4679  NZ  LYS B 227     4677   2382   2692    429   -139    299       N  
ATOM   4680  N   SER B 228     -33.887 -36.119 -28.832  1.00 22.47           N  
ANISOU 4680  N   SER B 228     3231   2553   2754    122   -176    214       N  
ATOM   4681  CA  SER B 228     -33.687 -36.109 -27.384  1.00 21.97           C  
ANISOU 4681  CA  SER B 228     3141   2504   2703     57   -157    211       C  
ATOM   4682  C   SER B 228     -32.963 -37.358 -26.915  1.00 24.68           C  
ANISOU 4682  C   SER B 228     3363   2902   3111    -53   -153    233       C  
ATOM   4683  O   SER B 228     -32.213 -37.308 -25.930  1.00 24.64           O  
ANISOU 4683  O   SER B 228     3362   2893   3105   -131   -139    243       O  
ATOM   4684  CB  SER B 228     -35.041 -35.996 -26.663  1.00 26.00           C  
ANISOU 4684  CB  SER B 228     3601   3080   3198    157   -163    169       C  
ATOM   4685  OG  SER B 228     -35.876 -37.112 -26.967  1.00 22.79           O  
ANISOU 4685  OG  SER B 228     3041   2784   2835    177   -178    145       O  
ATOM   4686  N   HIS B 229     -33.167 -38.490 -27.613  1.00 20.05           N  
ANISOU 4686  N   HIS B 229     2682   2366   2571    -50   -166    238       N  
ATOM   4687  CA  HIS B 229     -32.603 -39.786 -27.239  1.00 22.35           C  
ANISOU 4687  CA  HIS B 229     2888   2695   2910   -124   -161    259       C  
ATOM   4688  C   HIS B 229     -31.524 -40.225 -28.227  1.00 23.83           C  
ANISOU 4688  C   HIS B 229     3073   2866   3114   -160   -166    284       C  
ATOM   4689  O   HIS B 229     -31.338 -41.421 -28.474  1.00 22.96           O  
ANISOU 4689  O   HIS B 229     2903   2782   3038   -175   -169    296       O  
ATOM   4690  CB  HIS B 229     -33.698 -40.861 -27.148  1.00 22.02           C  
ANISOU 4690  CB  HIS B 229     2757   2716   2894   -110   -157    237       C  
ATOM   4691  CG  HIS B 229     -34.675 -40.655 -26.027  1.00 22.08           C  
ANISOU 4691  CG  HIS B 229     2740   2766   2882    -97   -139    205       C  
ATOM   4692  ND1 HIS B 229     -35.422 -39.502 -25.885  1.00 23.95           N  
ANISOU 4692  ND1 HIS B 229     3008   3012   3080    -17   -144    171       N  
ATOM   4693  CD2 HIS B 229     -35.043 -41.469 -25.006  1.00 18.80           C  
ANISOU 4693  CD2 HIS B 229     2284   2386   2473   -150   -110    199       C  
ATOM   4694  CE1 HIS B 229     -36.187 -39.605 -24.811  1.00 22.10           C  
ANISOU 4694  CE1 HIS B 229     2732   2832   2834    -22   -120    140       C  
ATOM   4695  NE2 HIS B 229     -35.982 -40.790 -24.264  1.00 22.25           N  
ANISOU 4695  NE2 HIS B 229     2709   2866   2880   -113    -95    158       N  
ATOM   4696  N   THR B 230     -30.814 -39.263 -28.807  1.00 21.83           N  
ANISOU 4696  N   THR B 230     2899   2565   2829   -178   -160    288       N  
ATOM   4697  CA  THR B 230     -29.832 -39.546 -29.840  1.00 20.80           C  
ANISOU 4697  CA  THR B 230     2766   2430   2706   -216   -154    301       C  
ATOM   4698  C   THR B 230     -28.519 -38.867 -29.485  1.00 20.32           C  
ANISOU 4698  C   THR B 230     2739   2367   2613   -311   -131    297       C  
ATOM   4699  O   THR B 230     -28.515 -37.725 -29.023  1.00 20.98           O  
ANISOU 4699  O   THR B 230     2915   2405   2650   -341   -113    283       O  
ATOM   4700  CB  THR B 230     -30.324 -39.043 -31.191  1.00 24.01           C  
ANISOU 4700  CB  THR B 230     3245   2791   3086   -161   -157    297       C  
ATOM   4701  OG1 THR B 230     -31.626 -39.580 -31.433  1.00 20.69           O  
ANISOU 4701  OG1 THR B 230     2772   2404   2684    -76   -183    281       O  
ATOM   4702  CG2 THR B 230     -29.362 -39.468 -32.313  1.00 17.63           C  
ANISOU 4702  CG2 THR B 230     2428   1985   2285   -204   -144    308       C  
ATOM   4703  N   LEU B 231     -27.410 -39.574 -29.688  1.00 18.82           N  
ANISOU 4703  N   LEU B 231     2475   2238   2440   -358   -130    299       N  
ATOM   4704  CA  LEU B 231     -26.101 -38.973 -29.486  1.00 25.78           C  
ANISOU 4704  CA  LEU B 231     3354   3157   3282   -462   -105    275       C  
ATOM   4705  C   LEU B 231     -25.666 -38.190 -30.724  1.00 24.19           C  
ANISOU 4705  C   LEU B 231     3241   2909   3042   -522    -63    262       C  
ATOM   4706  O   LEU B 231     -25.935 -38.597 -31.854  1.00 25.72           O  
ANISOU 4706  O   LEU B 231     3442   3078   3250   -474    -63    278       O  
ATOM   4707  CB  LEU B 231     -25.077 -40.060 -29.165  1.00 17.65           C  
ANISOU 4707  CB  LEU B 231     2193   2243   2271   -464   -125    269       C  
ATOM   4708  CG  LEU B 231     -25.365 -40.830 -27.865  1.00 19.55           C  
ANISOU 4708  CG  LEU B 231     2383   2519   2527   -407   -161    285       C  
ATOM   4709  CD1 LEU B 231     -24.556 -42.111 -27.844  1.00 24.15           C  
ANISOU 4709  CD1 LEU B 231     2871   3187   3117   -353   -186    291       C  
ATOM   4710  CD2 LEU B 231     -25.024 -39.959 -26.654  1.00 20.18           C  
ANISOU 4710  CD2 LEU B 231     2478   2627   2564   -473   -161    259       C  
ATOM   4711  N   TRP B 232     -25.034 -37.042 -30.495  1.00 20.90           N  
ANISOU 4711  N   TRP B 232     2907   2470   2563   -636    -20    232       N  
ATOM   4712  CA  TRP B 232     -24.258 -36.309 -31.497  1.00 22.39           C  
ANISOU 4712  CA  TRP B 232     3183   2630   2695   -747     41    208       C  
ATOM   4713  C   TRP B 232     -25.067 -36.074 -32.781  1.00 29.43           C  
ANISOU 4713  C   TRP B 232     4205   3406   3570   -668     50    240       C  
ATOM   4714  O   TRP B 232     -24.836 -36.705 -33.821  1.00 23.48           O  
ANISOU 4714  O   TRP B 232     3407   2679   2835   -649     52    248       O  
ATOM   4715  CB  TRP B 232     -22.940 -37.043 -31.796  1.00 19.60           C  
ANISOU 4715  CB  TRP B 232     2672   2423   2352   -819     53    175       C  
ATOM   4716  CG  TRP B 232     -21.913 -36.162 -32.507  1.00 22.76           C  
ANISOU 4716  CG  TRP B 232     3140   2831   2677   -993    136    125       C  
ATOM   4717  CD1 TRP B 232     -22.026 -34.829 -32.779  1.00 23.17           C  
ANISOU 4717  CD1 TRP B 232     3404   2752   2649  -1097    202    114       C  
ATOM   4718  CD2 TRP B 232     -20.632 -36.568 -33.015  1.00 28.97           C  
ANISOU 4718  CD2 TRP B 232     3793   3765   3448  -1086    170     74       C  
ATOM   4719  NE1 TRP B 232     -20.901 -34.380 -33.440  1.00 25.26           N  
ANISOU 4719  NE1 TRP B 232     3685   3065   2848  -1276    285     59       N  
ATOM   4720  CE2 TRP B 232     -20.028 -35.426 -33.589  1.00 27.26           C  
ANISOU 4720  CE2 TRP B 232     3709   3506   3143  -1273    266     29       C  
ATOM   4721  CE3 TRP B 232     -19.944 -37.788 -33.048  1.00 25.89           C  
ANISOU 4721  CE3 TRP B 232     3196   3540   3101  -1022    133     58       C  
ATOM   4722  CZ2 TRP B 232     -18.754 -35.462 -34.181  1.00 26.95           C  
ANISOU 4722  CZ2 TRP B 232     3572   3606   3061  -1420    331    -41       C  
ATOM   4723  CZ3 TRP B 232     -18.674 -37.826 -33.632  1.00 27.04           C  
ANISOU 4723  CZ3 TRP B 232     3238   3831   3204  -1135    186    -11       C  
ATOM   4724  CH2 TRP B 232     -18.097 -36.666 -34.197  1.00 31.64           C  
ANISOU 4724  CH2 TRP B 232     3928   4389   3703  -1342    287    -63       C  
ATOM   4725  N   THR B 233     -26.002 -35.124 -32.682  1.00 25.12           N  
ANISOU 4725  N   THR B 233     3829   2738   2980   -612     52    252       N  
ATOM   4726  CA  THR B 233     -27.026 -34.873 -33.700  1.00 25.85           C  
ANISOU 4726  CA  THR B 233     4045   2733   3044   -484     37    280       C  
ATOM   4727  C   THR B 233     -26.751 -33.653 -34.573  1.00 30.64           C  
ANISOU 4727  C   THR B 233     4895   3204   3541   -541    103    278       C  
ATOM   4728  O   THR B 233     -27.526 -33.382 -35.501  1.00 30.27           O  
ANISOU 4728  O   THR B 233     4976   3075   3450   -420     87    301       O  
ATOM   4729  CB  THR B 233     -28.404 -34.696 -33.044  1.00 25.86           C  
ANISOU 4729  CB  THR B 233     4069   2704   3053   -334    -13    289       C  
ATOM   4730  OG1 THR B 233     -28.357 -33.602 -32.114  1.00 25.07           O  
ANISOU 4730  OG1 THR B 233     4096   2535   2895   -379     16    273       O  
ATOM   4731  CG2 THR B 233     -28.813 -35.960 -32.307  1.00 29.32           C  
ANISOU 4731  CG2 THR B 233     4295   3260   3587   -285    -65    291       C  
ATOM   4732  N   ASP B 234     -25.704 -32.891 -34.296  1.00 28.53           N  
ANISOU 4732  N   ASP B 234     4712   2913   3215   -723    177    247       N  
ATOM   4733  CA  ASP B 234     -25.474 -31.654 -35.028  1.00 25.54           C  
ANISOU 4733  CA  ASP B 234     4615   2378   2711   -801    257    243       C  
ATOM   4734  C   ASP B 234     -24.524 -31.899 -36.197  1.00 32.03           C  
ANISOU 4734  C   ASP B 234     5430   3230   3510   -921    317    232       C  
ATOM   4735  O   ASP B 234     -23.613 -32.727 -36.109  1.00 29.27           O  
ANISOU 4735  O   ASP B 234     4859   3038   3222  -1017    321    203       O  
ATOM   4736  CB  ASP B 234     -24.923 -30.571 -34.099  1.00 29.36           C  
ANISOU 4736  CB  ASP B 234     5234   2801   3122   -963    323    203       C  
ATOM   4737  CG  ASP B 234     -23.521 -30.875 -33.614  1.00 33.64           C  
ANISOU 4737  CG  ASP B 234     5598   3497   3688  -1187    367    143       C  
ATOM   4738  OD1 ASP B 234     -23.387 -31.745 -32.726  1.00 29.74           O  
ANISOU 4738  OD1 ASP B 234     4858   3157   3285  -1157    305    133       O  
ATOM   4739  OD2 ASP B 234     -22.560 -30.244 -34.119  1.00 30.35           O  
ANISOU 4739  OD2 ASP B 234     5290   3055   3186  -1391    466    101       O  
ATOM   4740  N   GLY B 235     -24.766 -31.196 -37.303  1.00 35.98           N  
ANISOU 4740  N   GLY B 235     6180   3583   3910   -898    361    255       N  
ATOM   4741  CA  GLY B 235     -23.948 -31.352 -38.490  1.00 32.83           C  
ANISOU 4741  CA  GLY B 235     5806   3196   3472  -1010    428    246       C  
ATOM   4742  C   GLY B 235     -24.033 -32.709 -39.149  1.00 34.48           C  
ANISOU 4742  C   GLY B 235     5784   3536   3780   -908    365    262       C  
ATOM   4743  O   GLY B 235     -23.118 -33.083 -39.876  1.00 37.08           O  
ANISOU 4743  O   GLY B 235     6048   3937   4104  -1022    419    239       O  
ATOM   4744  N   VAL B 236     -25.094 -33.473 -38.893  1.00 32.52           N  
ANISOU 4744  N   VAL B 236     5411   3329   3615   -708    259    293       N  
ATOM   4745  CA  VAL B 236     -25.319 -34.754 -39.557  1.00 33.73           C  
ANISOU 4745  CA  VAL B 236     5385   3582   3850   -609    202    306       C  
ATOM   4746  C   VAL B 236     -26.082 -34.503 -40.849  1.00 37.09           C  
ANISOU 4746  C   VAL B 236     5982   3906   4205   -483    186    337       C  
ATOM   4747  O   VAL B 236     -27.049 -33.729 -40.870  1.00 38.08           O  
ANISOU 4747  O   VAL B 236     6284   3923   4262   -356    157    357       O  
ATOM   4748  CB  VAL B 236     -26.106 -35.727 -38.658  1.00 32.89           C  
ANISOU 4748  CB  VAL B 236     5075   3570   3854   -483    108    313       C  
ATOM   4749  CG1 VAL B 236     -26.022 -37.123 -39.230  1.00 46.59           C  
ANISOU 4749  CG1 VAL B 236     6628   5408   5666   -437     73    315       C  
ATOM   4750  CG2 VAL B 236     -25.599 -35.708 -37.230  1.00 34.83           C  
ANISOU 4750  CG2 VAL B 236     5213   3882   4141   -570    113    290       C  
ATOM   4751  N   GLU B 237     -25.654 -35.159 -41.924  1.00 28.20           N  
ANISOU 4751  N   GLU B 237     4807   2824   3084   -503    202    337       N  
ATOM   4752  CA  GLU B 237     -26.375 -35.126 -43.191  1.00 30.35           C  
ANISOU 4752  CA  GLU B 237     5211   3028   3294   -373    174    363       C  
ATOM   4753  C   GLU B 237     -27.273 -36.348 -43.259  1.00 27.64           C  
ANISOU 4753  C   GLU B 237     4668   2788   3045   -222     73    364       C  
ATOM   4754  O   GLU B 237     -26.789 -37.477 -43.130  1.00 33.48           O  
ANISOU 4754  O   GLU B 237     5202   3639   3878   -268     67    349       O  
ATOM   4755  CB  GLU B 237     -25.400 -35.110 -44.368  1.00 42.30           C  
ANISOU 4755  CB  GLU B 237     6802   4525   4746   -493    260    356       C  
ATOM   4756  CG  GLU B 237     -24.687 -33.798 -44.534  1.00 51.22           C  
ANISOU 4756  CG  GLU B 237     8189   5527   5747   -651    374    351       C  
ATOM   4757  CD  GLU B 237     -25.588 -32.750 -45.132  1.00 66.79           C  
ANISOU 4757  CD  GLU B 237    10483   7312   7581   -518    364    391       C  
ATOM   4758  OE1 GLU B 237     -25.857 -32.845 -46.345  1.00 82.82           O  
ANISOU 4758  OE1 GLU B 237    12624   9299   9545   -436    357    412       O  
ATOM   4759  OE2 GLU B 237     -26.042 -31.848 -44.395  1.00 64.37           O  
ANISOU 4759  OE2 GLU B 237    10326   6905   7225   -479    360    399       O  
ATOM   4760  N   GLU B 238     -28.576 -36.127 -43.456  1.00 30.92           N  
ANISOU 4760  N   GLU B 238     5151   3172   3426    -42     -3    374       N  
ATOM   4761  CA  GLU B 238     -29.511 -37.249 -43.494  1.00 32.43           C  
ANISOU 4761  CA  GLU B 238     5152   3474   3695     75    -91    358       C  
ATOM   4762  C   GLU B 238     -29.156 -38.243 -44.587  1.00 27.00           C  
ANISOU 4762  C   GLU B 238     4389   2838   3029     53    -88    352       C  
ATOM   4763  O   GLU B 238     -29.385 -39.445 -44.421  1.00 23.36           O  
ANISOU 4763  O   GLU B 238     3741   2475   2658     61   -126    333       O  
ATOM   4764  CB  GLU B 238     -30.942 -36.760 -43.700  1.00 36.22           C  
ANISOU 4764  CB  GLU B 238     5710   3944   4109    274   -171    352       C  
ATOM   4765  CG  GLU B 238     -31.558 -36.095 -42.491  1.00 41.15           C  
ANISOU 4765  CG  GLU B 238     6346   4556   4732    333   -192    345       C  
ATOM   4766  CD  GLU B 238     -32.971 -35.627 -42.766  1.00 52.01           C  
ANISOU 4766  CD  GLU B 238     7782   5952   6029    557   -275    325       C  
ATOM   4767  OE1 GLU B 238     -33.518 -35.956 -43.843  1.00 63.03           O  
ANISOU 4767  OE1 GLU B 238     9175   7392   7380    662   -326    311       O  
ATOM   4768  OE2 GLU B 238     -33.533 -34.929 -41.906  1.00 54.29           O  
ANISOU 4768  OE2 GLU B 238     8113   6222   6291    636   -291    316       O  
ATOM   4769  N   SER B 239     -28.598 -37.763 -45.706  1.00 26.11           N  
ANISOU 4769  N   SER B 239     4441   2653   2828     19    -37    366       N  
ATOM   4770  CA  SER B 239     -28.205 -38.658 -46.795  1.00 28.05           C  
ANISOU 4770  CA  SER B 239     4630   2945   3084     -3    -26    358       C  
ATOM   4771  C   SER B 239     -27.024 -39.561 -46.436  1.00 26.54           C  
ANISOU 4771  C   SER B 239     4266   2834   2984   -141     27    342       C  
ATOM   4772  O   SER B 239     -26.707 -40.468 -47.211  1.00 27.19           O  
ANISOU 4772  O   SER B 239     4278   2966   3088   -147     33    330       O  
ATOM   4773  CB  SER B 239     -27.873 -37.849 -48.052  1.00 30.51           C  
ANISOU 4773  CB  SER B 239     5178   3151   3261    -11     26    377       C  
ATOM   4774  OG  SER B 239     -26.899 -36.855 -47.789  1.00 32.26           O  
ANISOU 4774  OG  SER B 239     5545   3288   3424   -157    128    387       O  
ATOM   4775  N   ASP B 240     -26.370 -39.339 -45.298  1.00 28.56           N  
ANISOU 4775  N   ASP B 240     4455   3112   3284   -237     63    337       N  
ATOM   4776  CA  ASP B 240     -25.275 -40.184 -44.831  1.00 29.72           C  
ANISOU 4776  CA  ASP B 240     4426   3361   3506   -333     98    314       C  
ATOM   4777  C   ASP B 240     -25.709 -41.204 -43.791  1.00 28.83           C  
ANISOU 4777  C   ASP B 240     4137   3322   3496   -274     35    310       C  
ATOM   4778  O   ASP B 240     -24.886 -42.035 -43.382  1.00 26.57           O  
ANISOU 4778  O   ASP B 240     3714   3118   3263   -313     51    293       O  
ATOM   4779  CB  ASP B 240     -24.156 -39.334 -44.227  1.00 34.39           C  
ANISOU 4779  CB  ASP B 240     5044   3959   4065   -486    179    298       C  
ATOM   4780  CG  ASP B 240     -23.353 -38.596 -45.267  1.00 40.33           C  
ANISOU 4780  CG  ASP B 240     5944   4665   4716   -600    275    287       C  
ATOM   4781  OD1 ASP B 240     -23.359 -39.020 -46.449  1.00 37.45           O  
ANISOU 4781  OD1 ASP B 240     5612   4294   4324   -565    283    290       O  
ATOM   4782  OD2 ASP B 240     -22.703 -37.596 -44.886  1.00 38.49           O  
ANISOU 4782  OD2 ASP B 240     5800   4401   4424   -740    349    270       O  
ATOM   4783  N   LEU B 241     -26.973 -41.166 -43.359  1.00 25.35           N  
ANISOU 4783  N   LEU B 241     3703   2858   3072   -178    -32    319       N  
ATOM   4784  CA  LEU B 241     -27.462 -42.038 -42.289  1.00 26.59           C  
ANISOU 4784  CA  LEU B 241     3719   3071   3311   -145    -78    313       C  
ATOM   4785  C   LEU B 241     -27.726 -43.443 -42.819  1.00 31.96           C  
ANISOU 4785  C   LEU B 241     4313   3795   4035   -106   -103    299       C  
ATOM   4786  O   LEU B 241     -28.638 -43.639 -43.632  1.00 25.96           O  
ANISOU 4786  O   LEU B 241     3583   3029   3253    -42   -140    287       O  
ATOM   4787  CB  LEU B 241     -28.744 -41.473 -41.694  1.00 22.33           C  
ANISOU 4787  CB  LEU B 241     3212   2510   2763    -69   -129    313       C  
ATOM   4788  CG  LEU B 241     -28.630 -40.106 -41.013  1.00 24.86           C  
ANISOU 4788  CG  LEU B 241     3641   2771   3036    -93   -107    325       C  
ATOM   4789  CD1 LEU B 241     -30.019 -39.688 -40.576  1.00 24.06           C  
ANISOU 4789  CD1 LEU B 241     3559   2663   2918     21   -164    317       C  
ATOM   4790  CD2 LEU B 241     -27.683 -40.173 -39.834  1.00 23.02           C  
ANISOU 4790  CD2 LEU B 241     3328   2572   2847   -193    -73    324       C  
ATOM   4791  N   ILE B 242     -26.978 -44.428 -42.306  1.00 25.60           N  
ANISOU 4791  N   ILE B 242     3408   3037   3282   -134    -87    294       N  
ATOM   4792  CA  ILE B 242     -27.044 -45.790 -42.844  1.00 27.93           C  
ANISOU 4792  CA  ILE B 242     3658   3351   3604   -103    -96    281       C  
ATOM   4793  C   ILE B 242     -28.463 -46.340 -42.742  1.00 29.77           C  
ANISOU 4793  C   ILE B 242     3879   3578   3855    -63   -144    265       C  
ATOM   4794  O   ILE B 242     -29.074 -46.737 -43.743  1.00 22.94           O  
ANISOU 4794  O   ILE B 242     3036   2712   2968    -38   -162    242       O  
ATOM   4795  CB  ILE B 242     -26.026 -46.696 -42.129  1.00 23.09           C  
ANISOU 4795  CB  ILE B 242     2966   2780   3026   -109    -74    280       C  
ATOM   4796  CG1 ILE B 242     -24.616 -46.121 -42.314  1.00 22.50           C  
ANISOU 4796  CG1 ILE B 242     2869   2756   2922   -157    -25    273       C  
ATOM   4797  CG2 ILE B 242     -26.109 -48.143 -42.658  1.00 23.16           C  
ANISOU 4797  CG2 ILE B 242     2968   2782   3050    -66    -76    267       C  
ATOM   4798  CD1 ILE B 242     -24.180 -46.022 -43.779  1.00 23.91           C  
ANISOU 4798  CD1 ILE B 242     3096   2932   3057   -173     14    260       C  
ATOM   4799  N   ILE B 243     -29.011 -46.362 -41.534  1.00 21.77           N  
ANISOU 4799  N   ILE B 243     2825   2575   2873    -67   -162    266       N  
ATOM   4800  CA  ILE B 243     -30.422 -46.686 -41.341  1.00 20.44           C  
ANISOU 4800  CA  ILE B 243     2630   2427   2711    -51   -198    236       C  
ATOM   4801  C   ILE B 243     -31.190 -45.397 -41.600  1.00 22.82           C  
ANISOU 4801  C   ILE B 243     2968   2736   2966      0   -231    229       C  
ATOM   4802  O   ILE B 243     -31.011 -44.428 -40.847  1.00 24.07           O  
ANISOU 4802  O   ILE B 243     3153   2877   3118      3   -226    250       O  
ATOM   4803  CB  ILE B 243     -30.689 -47.217 -39.919  1.00 22.85           C  
ANISOU 4803  CB  ILE B 243     2886   2741   3056    -81   -192    238       C  
ATOM   4804  CG1 ILE B 243     -29.867 -48.486 -39.671  1.00 23.04           C  
ANISOU 4804  CG1 ILE B 243     2913   2739   3103   -100   -161    251       C  
ATOM   4805  CG2 ILE B 243     -32.203 -47.433 -39.723  1.00 22.06           C  
ANISOU 4805  CG2 ILE B 243     2745   2687   2952    -87   -217    190       C  
ATOM   4806  CD1 ILE B 243     -29.864 -48.940 -38.183  1.00 27.23           C  
ANISOU 4806  CD1 ILE B 243     3430   3260   3654   -119   -150    266       C  
ATOM   4807  N   PRO B 244     -32.020 -45.323 -42.650  1.00 20.74           N  
ANISOU 4807  N   PRO B 244     2723   2500   2658     51   -267    197       N  
ATOM   4808  CA  PRO B 244     -32.638 -44.041 -43.020  1.00 19.86           C  
ANISOU 4808  CA  PRO B 244     2679   2388   2478    140   -303    194       C  
ATOM   4809  C   PRO B 244     -33.480 -43.451 -41.892  1.00 25.68           C  
ANISOU 4809  C   PRO B 244     3378   3162   3219    177   -327    179       C  
ATOM   4810  O   PRO B 244     -34.087 -44.171 -41.099  1.00 23.00           O  
ANISOU 4810  O   PRO B 244     2934   2882   2923    140   -330    148       O  
ATOM   4811  CB  PRO B 244     -33.520 -44.402 -44.231  1.00 22.71           C  
ANISOU 4811  CB  PRO B 244     3031   2809   2790    200   -352    146       C  
ATOM   4812  CG  PRO B 244     -32.909 -45.642 -44.809  1.00 24.48           C  
ANISOU 4812  CG  PRO B 244     3230   3021   3049    125   -320    141       C  
ATOM   4813  CD  PRO B 244     -32.336 -46.402 -43.601  1.00 24.39           C  
ANISOU 4813  CD  PRO B 244     3161   2990   3117     40   -276    160       C  
ATOM   4814  N   LYS B 245     -33.526 -42.115 -41.853  1.00 21.07           N  
ANISOU 4814  N   LYS B 245     2899   2532   2575    249   -336    199       N  
ATOM   4815  CA  LYS B 245     -34.462 -41.411 -40.979  1.00 25.44           C  
ANISOU 4815  CA  LYS B 245     3435   3124   3109    324   -366    177       C  
ATOM   4816  C   LYS B 245     -35.883 -41.945 -41.131  1.00 24.85           C  
ANISOU 4816  C   LYS B 245     3233   3188   3022    390   -422    101       C  
ATOM   4817  O   LYS B 245     -36.599 -42.130 -40.138  1.00 25.39           O  
ANISOU 4817  O   LYS B 245     3197   3332   3118    380   -426     64       O  
ATOM   4818  CB  LYS B 245     -34.433 -39.911 -41.292  1.00 27.60           C  
ANISOU 4818  CB  LYS B 245     3886   3315   3287    427   -374    202       C  
ATOM   4819  CG  LYS B 245     -35.553 -39.100 -40.654  1.00 32.11           C  
ANISOU 4819  CG  LYS B 245     4460   3930   3809    560   -417    169       C  
ATOM   4820  CD  LYS B 245     -35.517 -37.635 -41.080  1.00 38.70           C  
ANISOU 4820  CD  LYS B 245     5523   4655   4526    684   -422    197       C  
ATOM   4821  CE  LYS B 245     -36.603 -36.838 -40.393  1.00 44.38           C  
ANISOU 4821  CE  LYS B 245     6253   5419   5190    841   -464    161       C  
ATOM   4822  NZ  LYS B 245     -36.692 -35.449 -40.930  1.00 47.03           N  
ANISOU 4822  NZ  LYS B 245     6849   5634   5385    999   -476    185       N  
ATOM   4823  N   SER B 246     -36.304 -42.196 -42.372  1.00 19.75           N  
ANISOU 4823  N   SER B 246     2587   2590   2326    448   -463     69       N  
ATOM   4824  CA  SER B 246     -37.635 -42.705 -42.684  1.00 21.62           C  
ANISOU 4824  CA  SER B 246     2688   2989   2535    500   -520    -22       C  
ATOM   4825  C   SER B 246     -37.854 -44.133 -42.195  1.00 22.37           C  
ANISOU 4825  C   SER B 246     2639   3153   2709    346   -486    -66       C  
ATOM   4826  O   SER B 246     -38.977 -44.642 -42.314  1.00 25.99           O  
ANISOU 4826  O   SER B 246     2967   3763   3146    343   -518   -158       O  
ATOM   4827  CB  SER B 246     -37.853 -42.654 -44.204  1.00 25.13           C  
ANISOU 4827  CB  SER B 246     3186   3463   2900    589   -571    -44       C  
ATOM   4828  OG  SER B 246     -36.886 -43.481 -44.831  1.00 26.90           O  
ANISOU 4828  OG  SER B 246     3446   3608   3167    473   -527     -8       O  
ATOM   4829  N   LEU B 247     -36.824 -44.786 -41.664  1.00 20.08           N  
ANISOU 4829  N   LEU B 247     2376   2760   2494    220   -422    -10       N  
ATOM   4830  CA  LEU B 247     -36.947 -46.100 -41.038  1.00 22.96           C  
ANISOU 4830  CA  LEU B 247     2658   3149   2918     82   -378    -39       C  
ATOM   4831  C   LEU B 247     -36.539 -46.031 -39.571  1.00 18.61           C  
ANISOU 4831  C   LEU B 247     2108   2545   2418     28   -334      4       C  
ATOM   4832  O   LEU B 247     -35.930 -46.955 -39.020  1.00 19.74           O  
ANISOU 4832  O   LEU B 247     2265   2627   2607    -70   -285     30       O  
ATOM   4833  CB  LEU B 247     -36.123 -47.147 -41.782  1.00 25.26           C  
ANISOU 4833  CB  LEU B 247     2998   3368   3233      6   -347    -17       C  
ATOM   4834  CG  LEU B 247     -36.780 -47.696 -43.044  1.00 40.83           C  
ANISOU 4834  CG  LEU B 247     4938   5416   5160      8   -380    -86       C  
ATOM   4835  CD1 LEU B 247     -35.763 -48.507 -43.792  1.00 43.27           C  
ANISOU 4835  CD1 LEU B 247     5327   5628   5486    -42   -345    -50       C  
ATOM   4836  CD2 LEU B 247     -37.994 -48.552 -42.718  1.00 35.87           C  
ANISOU 4836  CD2 LEU B 247     4191   4913   4525    -85   -376   -186       C  
ATOM   4837  N   ALA B 248     -36.858 -44.909 -38.935  1.00 21.68           N  
ANISOU 4837  N   ALA B 248     2500   2952   2785    107   -353      9       N  
ATOM   4838  CA  ALA B 248     -36.554 -44.690 -37.530  1.00 21.46           C  
ANISOU 4838  CA  ALA B 248     2475   2884   2793     67   -318     43       C  
ATOM   4839  C   ALA B 248     -35.053 -44.754 -37.245  1.00 25.02           C  
ANISOU 4839  C   ALA B 248     3012   3212   3282     17   -281    124       C  
ATOM   4840  O   ALA B 248     -34.643 -45.101 -36.129  1.00 24.05           O  
ANISOU 4840  O   ALA B 248     2883   3061   3195    -44   -248    149       O  
ATOM   4841  CB  ALA B 248     -37.327 -45.678 -36.645  1.00 25.39           C  
ANISOU 4841  CB  ALA B 248     2875   3455   3316    -34   -284     -9       C  
ATOM   4842  N   GLY B 249     -34.217 -44.416 -38.239  1.00 20.18           N  
ANISOU 4842  N   GLY B 249     2476   2540   2652     45   -286    159       N  
ATOM   4843  CA  GLY B 249     -32.791 -44.295 -38.007  1.00 21.37           C  
ANISOU 4843  CA  GLY B 249     2685   2611   2824      2   -251    217       C  
ATOM   4844  C   GLY B 249     -32.470 -43.106 -37.113  1.00 18.18           C  
ANISOU 4844  C   GLY B 249     2329   2173   2405     12   -243    242       C  
ATOM   4845  O   GLY B 249     -33.001 -42.009 -37.312  1.00 21.71           O  
ANISOU 4845  O   GLY B 249     2837   2611   2802     84   -264    234       O  
ATOM   4846  N   PRO B 250     -31.618 -43.300 -36.093  1.00 21.11           N  
ANISOU 4846  N   PRO B 250     2686   2527   2808    -49   -215    269       N  
ATOM   4847  CA  PRO B 250     -31.169 -42.147 -35.285  1.00 21.34           C  
ANISOU 4847  CA  PRO B 250     2769   2524   2816    -61   -203    287       C  
ATOM   4848  C   PRO B 250     -30.453 -41.118 -36.161  1.00 21.60           C  
ANISOU 4848  C   PRO B 250     2910   2499   2798    -65   -186    301       C  
ATOM   4849  O   PRO B 250     -29.647 -41.470 -37.026  1.00 22.77           O  
ANISOU 4849  O   PRO B 250     3064   2642   2946    -98   -168    309       O  
ATOM   4850  CB  PRO B 250     -30.218 -42.773 -34.249  1.00 22.12           C  
ANISOU 4850  CB  PRO B 250     2818   2637   2951   -126   -183    306       C  
ATOM   4851  CG  PRO B 250     -30.691 -44.229 -34.115  1.00 21.26           C  
ANISOU 4851  CG  PRO B 250     2646   2555   2878   -127   -186    298       C  
ATOM   4852  CD  PRO B 250     -31.128 -44.589 -35.564  1.00 19.67           C  
ANISOU 4852  CD  PRO B 250     2450   2355   2669   -100   -197    279       C  
ATOM   4853  N   LEU B 251     -30.780 -39.838 -35.955  1.00 18.88           N  
ANISOU 4853  N   LEU B 251     2668   2106   2400    -32   -186    300       N  
ATOM   4854  CA  LEU B 251     -30.173 -38.756 -36.740  1.00 19.89           C  
ANISOU 4854  CA  LEU B 251     2949   2152   2457    -49   -155    313       C  
ATOM   4855  C   LEU B 251     -28.843 -38.392 -36.084  1.00 21.45           C  
ANISOU 4855  C   LEU B 251     3159   2338   2654   -181   -103    319       C  
ATOM   4856  O   LEU B 251     -28.694 -37.354 -35.432  1.00 22.32           O  
ANISOU 4856  O   LEU B 251     3364   2396   2720   -217    -80    316       O  
ATOM   4857  CB  LEU B 251     -31.097 -37.545 -36.834  1.00 25.93           C  
ANISOU 4857  CB  LEU B 251     3858   2852   3142     57   -172    307       C  
ATOM   4858  CG  LEU B 251     -32.567 -37.777 -37.196  1.00 26.97           C  
ANISOU 4858  CG  LEU B 251     3944   3042   3262    210   -236    280       C  
ATOM   4859  CD1 LEU B 251     -33.284 -36.436 -37.356  1.00 26.72           C  
ANISOU 4859  CD1 LEU B 251     4086   2941   3126    347   -253    274       C  
ATOM   4860  CD2 LEU B 251     -32.675 -38.596 -38.474  1.00 29.64           C  
ANISOU 4860  CD2 LEU B 251     4236   3419   3605    232   -258    274       C  
ATOM   4861  N   SER B 252     -27.851 -39.259 -36.298  1.00 25.07           N  
ANISOU 4861  N   SER B 252     3519   2856   3152   -252    -86    318       N  
ATOM   4862  CA  SER B 252     -26.640 -39.286 -35.486  1.00 19.55           C  
ANISOU 4862  CA  SER B 252     2755   2210   2464   -358    -55    307       C  
ATOM   4863  C   SER B 252     -25.412 -39.589 -36.332  1.00 26.01           C  
ANISOU 4863  C   SER B 252     3538   3075   3270   -434    -14    293       C  
ATOM   4864  O   SER B 252     -25.475 -40.399 -37.264  1.00 22.98           O  
ANISOU 4864  O   SER B 252     3120   2707   2906   -386    -23    299       O  
ATOM   4865  CB  SER B 252     -26.757 -40.354 -34.385  1.00 22.38           C  
ANISOU 4865  CB  SER B 252     2976   2641   2886   -327    -92    310       C  
ATOM   4866  OG  SER B 252     -25.582 -40.413 -33.594  1.00 24.97           O  
ANISOU 4866  OG  SER B 252     3233   3044   3212   -403    -76    294       O  
ATOM   4867  N   HIS B 253     -24.282 -38.963 -35.980  1.00 21.86           N  
ANISOU 4867  N   HIS B 253     3011   2589   2707   -558     34    264       N  
ATOM   4868  CA  HIS B 253     -22.998 -39.408 -36.533  1.00 24.65           C  
ANISOU 4868  CA  HIS B 253     3271   3043   3051   -633     73    232       C  
ATOM   4869  C   HIS B 253     -22.688 -40.860 -36.206  1.00 25.78           C  
ANISOU 4869  C   HIS B 253     3245   3294   3256   -549     28    232       C  
ATOM   4870  O   HIS B 253     -21.901 -41.493 -36.924  1.00 22.95           O  
ANISOU 4870  O   HIS B 253     2813   3011   2896   -549     48    212       O  
ATOM   4871  CB  HIS B 253     -21.862 -38.540 -36.011  1.00 23.60           C  
ANISOU 4871  CB  HIS B 253     3129   2975   2863   -795    130    181       C  
ATOM   4872  CG  HIS B 253     -21.894 -37.148 -36.545  1.00 24.56           C  
ANISOU 4872  CG  HIS B 253     3455   2978   2900   -908    201    173       C  
ATOM   4873  ND1 HIS B 253     -21.463 -36.834 -37.814  1.00 25.69           N  
ANISOU 4873  ND1 HIS B 253     3688   3088   2986   -980    268    162       N  
ATOM   4874  CD2 HIS B 253     -22.329 -35.990 -35.998  1.00 22.62           C  
ANISOU 4874  CD2 HIS B 253     3371   2622   2602   -956    220    176       C  
ATOM   4875  CE1 HIS B 253     -21.616 -35.539 -38.024  1.00 28.67           C  
ANISOU 4875  CE1 HIS B 253     4289   3330   3275  -1071    328    162       C  
ATOM   4876  NE2 HIS B 253     -22.134 -35.000 -36.934  1.00 28.68           N  
ANISOU 4876  NE2 HIS B 253     4340   3280   3276  -1054    300    169       N  
ATOM   4877  N   HIS B 254     -23.263 -41.392 -35.121  1.00 19.09           N  
ANISOU 4877  N   HIS B 254     2350   2451   2450   -475    -25    252       N  
ATOM   4878  CA  HIS B 254     -23.096 -42.799 -34.796  1.00 19.71           C  
ANISOU 4878  CA  HIS B 254     2324   2594   2570   -381    -63    261       C  
ATOM   4879  C   HIS B 254     -23.743 -43.705 -35.842  1.00 25.40           C  
ANISOU 4879  C   HIS B 254     3070   3260   3319   -302    -73    283       C  
ATOM   4880  O   HIS B 254     -23.366 -44.875 -35.948  1.00 24.48           O  
ANISOU 4880  O   HIS B 254     2896   3186   3218   -235    -85    283       O  
ATOM   4881  CB  HIS B 254     -23.692 -43.082 -33.418  1.00 20.35           C  
ANISOU 4881  CB  HIS B 254     2392   2666   2674   -336   -104    280       C  
ATOM   4882  CG  HIS B 254     -22.951 -42.412 -32.290  1.00 25.33           C  
ANISOU 4882  CG  HIS B 254     2980   3372   3273   -402   -104    253       C  
ATOM   4883  ND1 HIS B 254     -22.061 -43.086 -31.482  1.00 23.86           N  
ANISOU 4883  ND1 HIS B 254     2689   3304   3073   -365   -132    235       N  
ATOM   4884  CD2 HIS B 254     -22.971 -41.132 -31.839  1.00 26.73           C  
ANISOU 4884  CD2 HIS B 254     3215   3524   3417   -498    -82    235       C  
ATOM   4885  CE1 HIS B 254     -21.565 -42.253 -30.577  1.00 22.21           C  
ANISOU 4885  CE1 HIS B 254     2454   3156   2828   -444   -130    202       C  
ATOM   4886  NE2 HIS B 254     -22.098 -41.059 -30.773  1.00 24.58           N  
ANISOU 4886  NE2 HIS B 254     2858   3363   3117   -537    -95    201       N  
ATOM   4887  N   ASN B 255     -24.711 -43.192 -36.599  1.00 24.49           N  
ANISOU 4887  N   ASN B 255     3050   3055   3200   -300    -70    297       N  
ATOM   4888  CA  ASN B 255     -25.425 -43.938 -37.644  1.00 24.02           C  
ANISOU 4888  CA  ASN B 255     3016   2953   3156   -237    -83    306       C  
ATOM   4889  C   ASN B 255     -24.833 -43.623 -39.014  1.00 23.82           C  
ANISOU 4889  C   ASN B 255     3033   2926   3094   -270    -44    295       C  
ATOM   4890  O   ASN B 255     -25.554 -43.403 -39.987  1.00 22.74           O  
ANISOU 4890  O   ASN B 255     2974   2729   2937   -244    -49    301       O  
ATOM   4891  CB  ASN B 255     -26.925 -43.599 -37.564  1.00 22.52           C  
ANISOU 4891  CB  ASN B 255     2884   2699   2971   -197   -114    316       C  
ATOM   4892  CG  ASN B 255     -27.822 -44.355 -38.587  1.00 22.75           C  
ANISOU 4892  CG  ASN B 255     2926   2710   3010   -142   -135    310       C  
ATOM   4893  OD1 ASN B 255     -27.449 -45.374 -39.171  1.00 22.49           O  
ANISOU 4893  OD1 ASN B 255     2865   2690   2990   -130   -128    305       O  
ATOM   4894  ND2 ASN B 255     -29.039 -43.851 -38.754  1.00 19.79           N  
ANISOU 4894  ND2 ASN B 255     2590   2313   2618   -102   -164    301       N  
ATOM   4895  N   THR B 256     -23.503 -43.551 -39.114  1.00 21.83           N  
ANISOU 4895  N   THR B 256     2725   2751   2820   -328     -3    270       N  
ATOM   4896  CA  THR B 256     -22.840 -43.265 -40.382  1.00 20.44           C  
ANISOU 4896  CA  THR B 256     2584   2584   2599   -379     50    251       C  
ATOM   4897  C   THR B 256     -21.660 -44.216 -40.544  1.00 26.42           C  
ANISOU 4897  C   THR B 256     3216   3461   3362   -362     68    218       C  
ATOM   4898  O   THR B 256     -21.178 -44.812 -39.575  1.00 23.62           O  
ANISOU 4898  O   THR B 256     2759   3188   3028   -320     42    207       O  
ATOM   4899  CB  THR B 256     -22.357 -41.793 -40.487  1.00 27.98           C  
ANISOU 4899  CB  THR B 256     3627   3518   3487   -509    109    234       C  
ATOM   4900  OG1 THR B 256     -21.334 -41.536 -39.518  1.00 28.46           O  
ANISOU 4900  OG1 THR B 256     3589   3686   3540   -593    131    196       O  
ATOM   4901  CG2 THR B 256     -23.504 -40.795 -40.249  1.00 29.01           C  
ANISOU 4901  CG2 THR B 256     3904   3523   3596   -494     89    265       C  
ATOM   4902  N   ARG B 257     -21.180 -44.338 -41.783  1.00 23.04           N  
ANISOU 4902  N   ARG B 257     2804   3048   2902   -380    112    200       N  
ATOM   4903  CA  ARG B 257     -20.013 -45.169 -42.074  1.00 29.19           C  
ANISOU 4903  CA  ARG B 257     3462   3956   3672   -352    137    158       C  
ATOM   4904  C   ARG B 257     -19.359 -44.646 -43.345  1.00 30.54           C  
ANISOU 4904  C   ARG B 257     3669   4153   3784   -443    216    125       C  
ATOM   4905  O   ARG B 257     -20.016 -44.572 -44.384  1.00 26.66           O  
ANISOU 4905  O   ARG B 257     3295   3559   3278   -433    224    151       O  
ATOM   4906  CB  ARG B 257     -20.407 -46.636 -42.244  1.00 26.23           C  
ANISOU 4906  CB  ARG B 257     3074   3557   3337   -207     93    176       C  
ATOM   4907  CG  ARG B 257     -19.223 -47.582 -42.456  1.00 29.37           C  
ANISOU 4907  CG  ARG B 257     3361   4084   3716   -132    111    132       C  
ATOM   4908  CD  ARG B 257     -18.747 -48.222 -41.132  1.00 24.47           C  
ANISOU 4908  CD  ARG B 257     2644   3550   3105    -39     65    124       C  
ATOM   4909  NE  ARG B 257     -17.673 -49.179 -41.408  1.00 27.36           N  
ANISOU 4909  NE  ARG B 257     2917   4041   3439     76     75     79       N  
ATOM   4910  CZ  ARG B 257     -17.288 -50.168 -40.610  1.00 31.36           C  
ANISOU 4910  CZ  ARG B 257     3380   4601   3934    229     30     76       C  
ATOM   4911  NH1 ARG B 257     -17.877 -50.364 -39.422  1.00 24.35           N  
ANISOU 4911  NH1 ARG B 257     2536   3648   3067    270    -23    118       N  
ATOM   4912  NH2 ARG B 257     -16.303 -50.969 -41.012  1.00 27.85           N  
ANISOU 4912  NH2 ARG B 257     2860   4276   3446    353     41     28       N  
ATOM   4913  N   GLU B 258     -18.071 -44.312 -43.267  1.00 26.19           N  
ANISOU 4913  N   GLU B 258     3010   3750   3189   -535    276     62       N  
ATOM   4914  CA  GLU B 258     -17.354 -43.764 -44.416  1.00 33.88           C  
ANISOU 4914  CA  GLU B 258     4016   4764   4095   -655    370     19       C  
ATOM   4915  C   GLU B 258     -17.492 -44.663 -45.644  1.00 33.29           C  
ANISOU 4915  C   GLU B 258     3968   4659   4020   -560    376     28       C  
ATOM   4916  O   GLU B 258     -17.316 -45.882 -45.567  1.00 29.27           O  
ANISOU 4916  O   GLU B 258     3366   4210   3547   -421    336     21       O  
ATOM   4917  CB  GLU B 258     -15.875 -43.570 -44.065  1.00 35.92           C  
ANISOU 4917  CB  GLU B 258     4097   5243   4308   -757    431    -73       C  
ATOM   4918  CG  GLU B 258     -14.998 -43.256 -45.265  1.00 60.13           C  
ANISOU 4918  CG  GLU B 258     7158   8390   7298   -880    541   -135       C  
ATOM   4919  CD  GLU B 258     -14.394 -41.865 -45.210  1.00 85.27           C  
ANISOU 4919  CD  GLU B 258    10389  11609  10401  -1131    643   -189       C  
ATOM   4920  OE1 GLU B 258     -13.198 -41.725 -45.544  1.00 92.09           O  
ANISOU 4920  OE1 GLU B 258    11125  12664  11202  -1257    733   -286       O  
ATOM   4921  OE2 GLU B 258     -15.114 -40.913 -44.833  1.00 89.05           O  
ANISOU 4921  OE2 GLU B 258    11036  11928  10870  -1205    639   -141       O  
ATOM   4922  N   GLY B 259     -17.810 -44.050 -46.783  1.00 27.55           N  
ANISOU 4922  N   GLY B 259     3394   3832   3241   -631    427     44       N  
ATOM   4923  CA  GLY B 259     -17.969 -44.786 -48.016  1.00 31.20           C  
ANISOU 4923  CA  GLY B 259     3901   4262   3693   -557    435     50       C  
ATOM   4924  C   GLY B 259     -19.363 -45.310 -48.290  1.00 34.00           C  
ANISOU 4924  C   GLY B 259     4362   4467   4087   -433    352    111       C  
ATOM   4925  O   GLY B 259     -19.571 -45.931 -49.341  1.00 30.53           O  
ANISOU 4925  O   GLY B 259     3970   3997   3633   -376    355    112       O  
ATOM   4926  N   TYR B 260     -20.324 -45.087 -47.386  1.00 23.63           N  
ANISOU 4926  N   TYR B 260     3082   3078   2819   -398    282    153       N  
ATOM   4927  CA  TYR B 260     -21.701 -45.509 -47.587  1.00 23.91           C  
ANISOU 4927  CA  TYR B 260     3197   3004   2885   -300    206    193       C  
ATOM   4928  C   TYR B 260     -22.627 -44.324 -47.380  1.00 27.20           C  
ANISOU 4928  C   TYR B 260     3739   3322   3274   -328    183    227       C  
ATOM   4929  O   TYR B 260     -22.370 -43.462 -46.533  1.00 25.10           O  
ANISOU 4929  O   TYR B 260     3476   3060   3002   -397    200    229       O  
ATOM   4930  CB  TYR B 260     -22.076 -46.673 -46.648  1.00 21.30           C  
ANISOU 4930  CB  TYR B 260     2772   2691   2631   -204    142    199       C  
ATOM   4931  CG  TYR B 260     -21.233 -47.875 -46.965  1.00 27.91           C  
ANISOU 4931  CG  TYR B 260     3529   3602   3475   -141    163    168       C  
ATOM   4932  CD1 TYR B 260     -21.618 -48.771 -47.959  1.00 25.50           C  
ANISOU 4932  CD1 TYR B 260     3276   3251   3163    -79    156    163       C  
ATOM   4933  CD2 TYR B 260     -20.011 -48.074 -46.339  1.00 25.53           C  
ANISOU 4933  CD2 TYR B 260     3102   3427   3172   -137    191    134       C  
ATOM   4934  CE1 TYR B 260     -20.822 -49.857 -48.291  1.00 22.45           C  
ANISOU 4934  CE1 TYR B 260     2839   2921   2770     -7    180    131       C  
ATOM   4935  CE2 TYR B 260     -19.204 -49.161 -46.674  1.00 22.63           C  
ANISOU 4935  CE2 TYR B 260     2667   3137   2796    -47    208     99       C  
ATOM   4936  CZ  TYR B 260     -19.615 -50.047 -47.643  1.00 27.67           C  
ANISOU 4936  CZ  TYR B 260     3378   3706   3428     21    206    101       C  
ATOM   4937  OH  TYR B 260     -18.815 -51.126 -47.965  1.00 29.80           O  
ANISOU 4937  OH  TYR B 260     3601   4042   3680    127    226     65       O  
ATOM   4938  N   ARG B 261     -23.685 -44.270 -48.181  1.00 25.53           N  
ANISOU 4938  N   ARG B 261     3635   3030   3034   -265    142    247       N  
ATOM   4939  CA  ARG B 261     -24.757 -43.300 -48.004  1.00 24.43           C  
ANISOU 4939  CA  ARG B 261     3613   2807   2862   -234     99    275       C  
ATOM   4940  C   ARG B 261     -26.000 -44.029 -47.494  1.00 22.37           C  
ANISOU 4940  C   ARG B 261     3286   2552   2662   -136      9    276       C  
ATOM   4941  O   ARG B 261     -25.982 -45.237 -47.241  1.00 24.62           O  
ANISOU 4941  O   ARG B 261     3463   2882   3010   -114     -9    261       O  
ATOM   4942  CB  ARG B 261     -25.020 -42.538 -49.309  1.00 28.23           C  
ANISOU 4942  CB  ARG B 261     4277   3212   3238   -225    119    286       C  
ATOM   4943  CG  ARG B 261     -24.098 -41.329 -49.528  1.00 33.47           C  
ANISOU 4943  CG  ARG B 261     5073   3830   3815   -348    216    290       C  
ATOM   4944  CD  ARG B 261     -24.262 -40.745 -50.937  1.00 40.06           C  
ANISOU 4944  CD  ARG B 261     6114   4578   4528   -335    247    305       C  
ATOM   4945  NE  ARG B 261     -23.447 -41.487 -51.898  1.00 68.08           N  
ANISOU 4945  NE  ARG B 261     9614   8186   8068   -381    303    278       N  
ATOM   4946  CZ  ARG B 261     -23.667 -41.544 -53.209  1.00 75.95           C  
ANISOU 4946  CZ  ARG B 261    10733   9141   8985   -340    310    283       C  
ATOM   4947  NH1 ARG B 261     -22.853 -42.253 -53.984  1.00 64.62           N  
ANISOU 4947  NH1 ARG B 261     9238   7768   7545   -386    369    253       N  
ATOM   4948  NH2 ARG B 261     -24.702 -40.911 -53.745  1.00 82.35           N  
ANISOU 4948  NH2 ARG B 261    11723   9856   9712   -238    254    313       N  
ATOM   4949  N   THR B 262     -27.087 -43.280 -47.334  1.00 22.88           N  
ANISOU 4949  N   THR B 262     3425   2572   2696    -79    -41    288       N  
ATOM   4950  CA  THR B 262     -28.275 -43.827 -46.693  1.00 22.07           C  
ANISOU 4950  CA  THR B 262     3241   2500   2644    -10   -115    275       C  
ATOM   4951  C   THR B 262     -28.835 -45.004 -47.500  1.00 27.66           C  
ANISOU 4951  C   THR B 262     3902   3244   3364     30   -150    244       C  
ATOM   4952  O   THR B 262     -28.936 -44.949 -48.735  1.00 25.68           O  
ANISOU 4952  O   THR B 262     3727   2980   3050     60   -154    236       O  
ATOM   4953  CB  THR B 262     -29.321 -42.716 -46.508  1.00 26.58           C  
ANISOU 4953  CB  THR B 262     3899   3038   3160     66   -162    282       C  
ATOM   4954  OG1 THR B 262     -30.447 -43.234 -45.786  1.00 28.69           O  
ANISOU 4954  OG1 THR B 262     4059   3366   3475    117   -224    255       O  
ATOM   4955  CG2 THR B 262     -29.785 -42.147 -47.853  1.00 27.04           C  
ANISOU 4955  CG2 THR B 262     4100   3059   3112    145   -184    282       C  
ATOM   4956  N   GLN B 263     -29.151 -46.094 -46.797  1.00 25.34           N  
ANISOU 4956  N   GLN B 263     3499   2988   3140     19   -167    225       N  
ATOM   4957  CA  GLN B 263     -29.524 -47.363 -47.432  1.00 23.80           C  
ANISOU 4957  CA  GLN B 263     3272   2815   2957     23   -181    189       C  
ATOM   4958  C   GLN B 263     -31.038 -47.432 -47.644  1.00 20.42           C  
ANISOU 4958  C   GLN B 263     2820   2435   2504     63   -248    144       C  
ATOM   4959  O   GLN B 263     -31.732 -48.315 -47.132  1.00 26.88           O  
ANISOU 4959  O   GLN B 263     3566   3288   3359     31   -263    107       O  
ATOM   4960  CB  GLN B 263     -29.020 -48.542 -46.596  1.00 21.49           C  
ANISOU 4960  CB  GLN B 263     2912   2521   2731    -15   -152    188       C  
ATOM   4961  CG  GLN B 263     -27.491 -48.589 -46.442  1.00 20.84           C  
ANISOU 4961  CG  GLN B 263     2824   2434   2661    -30    -95    214       C  
ATOM   4962  CD  GLN B 263     -26.774 -48.813 -47.785  1.00 25.79           C  
ANISOU 4962  CD  GLN B 263     3495   3058   3244    -24    -59    202       C  
ATOM   4963  OE1 GLN B 263     -27.016 -49.810 -48.467  1.00 24.03           O  
ANISOU 4963  OE1 GLN B 263     3289   2825   3015     -7    -62    176       O  
ATOM   4964  NE2 GLN B 263     -25.887 -47.899 -48.148  1.00 22.19           N  
ANISOU 4964  NE2 GLN B 263     3066   2612   2752    -51    -17    217       N  
ATOM   4965  N   VAL B 264     -31.550 -46.477 -48.425  1.00 24.39           N  
ANISOU 4965  N   VAL B 264     3390   2945   2930    133   -287    141       N  
ATOM   4966  CA  VAL B 264     -33.001 -46.391 -48.604  1.00 25.03           C  
ANISOU 4966  CA  VAL B 264     3429   3111   2972    198   -363     86       C  
ATOM   4967  C   VAL B 264     -33.565 -47.581 -49.376  1.00 26.05           C  
ANISOU 4967  C   VAL B 264     3506   3301   3093    168   -384     20       C  
ATOM   4968  O   VAL B 264     -34.753 -47.890 -49.234  1.00 27.35           O  
ANISOU 4968  O   VAL B 264     3581   3567   3246    173   -434    -48       O  
ATOM   4969  CB  VAL B 264     -33.409 -45.067 -49.284  1.00 30.63           C  
ANISOU 4969  CB  VAL B 264     4246   3815   3578    319   -408     97       C  
ATOM   4970  CG1 VAL B 264     -33.273 -43.907 -48.291  1.00 31.33           C  
ANISOU 4970  CG1 VAL B 264     4383   3855   3668    348   -396    141       C  
ATOM   4971  CG2 VAL B 264     -32.605 -44.814 -50.554  1.00 31.05           C  
ANISOU 4971  CG2 VAL B 264     4435   3798   3563    328   -378    128       C  
ATOM   4972  N   LYS B 265     -32.758 -48.253 -50.200  1.00 20.86           N  
ANISOU 4972  N   LYS B 265     2899   2594   2433    130   -344     29       N  
ATOM   4973  CA  LYS B 265     -33.212 -49.430 -50.943  1.00 24.16           C  
ANISOU 4973  CA  LYS B 265     3291   3051   2837     89   -354    -36       C  
ATOM   4974  C   LYS B 265     -32.613 -50.726 -50.394  1.00 24.33           C  
ANISOU 4974  C   LYS B 265     3298   3018   2930     -5   -290    -36       C  
ATOM   4975  O   LYS B 265     -32.439 -51.699 -51.130  1.00 26.96           O  
ANISOU 4975  O   LYS B 265     3665   3329   3248    -41   -269    -68       O  
ATOM   4976  CB  LYS B 265     -32.909 -49.283 -52.434  1.00 25.61           C  
ANISOU 4976  CB  LYS B 265     3568   3222   2943    135   -362    -39       C  
ATOM   4977  CG  LYS B 265     -33.674 -48.154 -53.087  1.00 24.32           C  
ANISOU 4977  CG  LYS B 265     3447   3113   2681    250   -436    -48       C  
ATOM   4978  CD  LYS B 265     -33.417 -48.071 -54.603  1.00 25.97           C  
ANISOU 4978  CD  LYS B 265     3767   3305   2796    297   -445    -52       C  
ATOM   4979  CE  LYS B 265     -34.194 -46.872 -55.142  1.00 33.08           C  
ANISOU 4979  CE  LYS B 265     4739   4250   3580    443   -524    -54       C  
ATOM   4980  NZ  LYS B 265     -33.992 -46.661 -56.591  1.00 37.86           N  
ANISOU 4980  NZ  LYS B 265     5479   4833   4073    503   -536    -51       N  
ATOM   4981  N   GLY B 266     -32.310 -50.763 -49.092  1.00 24.67           N  
ANISOU 4981  N   GLY B 266     3305   3030   3038    -36   -260     -2       N  
ATOM   4982  CA  GLY B 266     -31.942 -52.005 -48.452  1.00 21.64           C  
ANISOU 4982  CA  GLY B 266     2927   2594   2702   -103   -209     -5       C  
ATOM   4983  C   GLY B 266     -33.094 -52.992 -48.497  1.00 24.03           C  
ANISOU 4983  C   GLY B 266     3206   2935   2989   -186   -218    -87       C  
ATOM   4984  O   GLY B 266     -34.207 -52.662 -48.922  1.00 24.80           O  
ANISOU 4984  O   GLY B 266     3244   3134   3046   -190   -272   -148       O  
ATOM   4985  N   PRO B 267     -32.837 -54.295 -48.035  1.00 29.60           N  
ANISOU 4985  N   PRO B 267     3970   3562   3715   -258   -160    -96       N  
ATOM   4986  CA  PRO B 267     -33.881 -55.337 -48.061  1.00 26.85           C  
ANISOU 4986  CA  PRO B 267     3629   3232   3340   -378   -146   -183       C  
ATOM   4987  C   PRO B 267     -34.847 -55.215 -46.884  1.00 29.51           C  
ANISOU 4987  C   PRO B 267     3888   3629   3695   -454   -146   -213       C  
ATOM   4988  O   PRO B 267     -35.004 -56.132 -46.075  1.00 27.34           O  
ANISOU 4988  O   PRO B 267     3670   3292   3427   -551    -89   -226       O  
ATOM   4989  CB  PRO B 267     -33.052 -56.628 -48.014  1.00 24.55           C  
ANISOU 4989  CB  PRO B 267     3478   2801   3048   -402    -74   -165       C  
ATOM   4990  CG  PRO B 267     -31.864 -56.240 -47.171  1.00 25.02           C  
ANISOU 4990  CG  PRO B 267     3551   2803   3154   -305    -57    -72       C  
ATOM   4991  CD  PRO B 267     -31.549 -54.805 -47.530  1.00 29.29           C  
ANISOU 4991  CD  PRO B 267     4003   3419   3706   -220   -106    -34       C  
ATOM   4992  N   TRP B 268     -35.512 -54.062 -46.788  1.00 28.00           N  
ANISOU 4992  N   TRP B 268     3580   3558   3501   -404   -208   -225       N  
ATOM   4993  CA  TRP B 268     -36.357 -53.751 -45.634  1.00 28.83           C  
ANISOU 4993  CA  TRP B 268     3595   3737   3622   -450   -210   -250       C  
ATOM   4994  C   TRP B 268     -37.688 -54.484 -45.656  1.00 36.19           C  
ANISOU 4994  C   TRP B 268     4458   4779   4513   -595   -199   -373       C  
ATOM   4995  O   TRP B 268     -38.518 -54.262 -44.767  1.00 26.94           O  
ANISOU 4995  O   TRP B 268     3193   3699   3345   -648   -195   -415       O  
ATOM   4996  CB  TRP B 268     -36.630 -52.249 -45.557  1.00 25.10           C  
ANISOU 4996  CB  TRP B 268     3035   3355   3146   -327   -279   -229       C  
ATOM   4997  CG  TRP B 268     -35.409 -51.404 -45.615  1.00 25.78           C  
ANISOU 4997  CG  TRP B 268     3190   3350   3257   -215   -283   -126       C  
ATOM   4998  CD1 TRP B 268     -35.104 -50.472 -46.572  1.00 22.40           C  
ANISOU 4998  CD1 TRP B 268     2791   2930   2791   -109   -326   -101       C  
ATOM   4999  CD2 TRP B 268     -34.325 -51.397 -44.681  1.00 24.47           C  
ANISOU 4999  CD2 TRP B 268     3075   3080   3143   -210   -237    -44       C  
ATOM   5000  NE1 TRP B 268     -33.900 -49.876 -46.281  1.00 22.06           N  
ANISOU 5000  NE1 TRP B 268     2811   2796   2777    -64   -299    -13       N  
ATOM   5001  CE2 TRP B 268     -33.395 -50.432 -45.130  1.00 23.01           C  
ANISOU 5001  CE2 TRP B 268     2930   2859   2953   -120   -250     18       C  
ATOM   5002  CE3 TRP B 268     -34.058 -52.099 -43.494  1.00 27.61           C  
ANISOU 5002  CE3 TRP B 268     3495   3417   3579   -273   -187    -22       C  
ATOM   5003  CZ2 TRP B 268     -32.211 -50.156 -44.442  1.00 24.98           C  
ANISOU 5003  CZ2 TRP B 268     3211   3041   3239   -102   -216     88       C  
ATOM   5004  CZ3 TRP B 268     -32.884 -51.832 -42.813  1.00 25.33           C  
ANISOU 5004  CZ3 TRP B 268     3244   3056   3323   -226   -165     56       C  
ATOM   5005  CH2 TRP B 268     -31.971 -50.864 -43.285  1.00 26.30           C  
ANISOU 5005  CH2 TRP B 268     3377   3172   3446   -147   -181    104       C  
ATOM   5006  N   HIS B 269     -37.929 -55.321 -46.661  1.00 27.48           N  
ANISOU 5006  N   HIS B 269     3392   3684   3364   -669   -191   -442       N  
ATOM   5007  CA  HIS B 269     -39.060 -56.224 -46.587  1.00 25.68           C  
ANISOU 5007  CA  HIS B 269     3121   3543   3092   -855   -155   -568       C  
ATOM   5008  C   HIS B 269     -38.801 -57.373 -45.627  1.00 27.45           C  
ANISOU 5008  C   HIS B 269     3484   3616   3330  -1000    -47   -553       C  
ATOM   5009  O   HIS B 269     -39.730 -58.135 -45.326  1.00 29.68           O  
ANISOU 5009  O   HIS B 269     3754   3952   3571  -1191      9   -656       O  
ATOM   5010  CB  HIS B 269     -39.371 -56.781 -47.979  1.00 29.23           C  
ANISOU 5010  CB  HIS B 269     3584   4045   3478   -902   -176   -654       C  
ATOM   5011  CG  HIS B 269     -38.274 -57.640 -48.517  1.00 28.56           C  
ANISOU 5011  CG  HIS B 269     3690   3763   3397   -899   -124   -596       C  
ATOM   5012  ND1 HIS B 269     -37.025 -57.143 -48.809  1.00 26.11           N  
ANISOU 5012  ND1 HIS B 269     3453   3345   3124   -734   -140   -479       N  
ATOM   5013  CD2 HIS B 269     -38.221 -58.970 -48.769  1.00 34.62           C  
ANISOU 5013  CD2 HIS B 269     4600   4424   4129  -1041    -48   -643       C  
ATOM   5014  CE1 HIS B 269     -36.249 -58.127 -49.229  1.00 31.17           C  
ANISOU 5014  CE1 HIS B 269     4251   3837   3754   -755    -83   -459       C  
ATOM   5015  NE2 HIS B 269     -36.950 -59.247 -49.209  1.00 35.01           N  
ANISOU 5015  NE2 HIS B 269     4798   4308   4195   -932    -27   -552       N  
ATOM   5016  N   SER B 270     -37.566 -57.534 -45.160  1.00 28.69           N  
ANISOU 5016  N   SER B 270     3781   3591   3530   -916    -13   -434       N  
ATOM   5017  CA  SER B 270     -37.216 -58.709 -44.370  1.00 29.30           C  
ANISOU 5017  CA  SER B 270     4037   3500   3597  -1017     85   -412       C  
ATOM   5018  C   SER B 270     -37.876 -58.638 -42.993  1.00 31.54           C  
ANISOU 5018  C   SER B 270     4279   3816   3887  -1114    126   -426       C  
ATOM   5019  O   SER B 270     -38.138 -57.556 -42.467  1.00 27.91           O  
ANISOU 5019  O   SER B 270     3673   3469   3464  -1042     75   -407       O  
ATOM   5020  CB  SER B 270     -35.691 -58.821 -44.233  1.00 30.28           C  
ANISOU 5020  CB  SER B 270     4296   3456   3752   -861     95   -289       C  
ATOM   5021  OG  SER B 270     -35.041 -58.837 -45.504  1.00 27.91           O  
ANISOU 5021  OG  SER B 270     4026   3137   3444   -770     65   -279       O  
ATOM   5022  N   GLU B 271     -38.153 -59.812 -42.414  1.00 29.80           N  
ANISOU 5022  N   GLU B 271     4213   3488   3621  -1283    226   -461       N  
ATOM   5023  CA  GLU B 271     -38.755 -59.848 -41.080  1.00 26.54           C  
ANISOU 5023  CA  GLU B 271     3790   3092   3202  -1394    283   -475       C  
ATOM   5024  C   GLU B 271     -37.783 -59.338 -40.025  1.00 31.43           C  
ANISOU 5024  C   GLU B 271     4458   3615   3871  -1236    269   -342       C  
ATOM   5025  O   GLU B 271     -38.188 -58.686 -39.057  1.00 33.13           O  
ANISOU 5025  O   GLU B 271     4573   3908   4108  -1242    264   -335       O  
ATOM   5026  CB  GLU B 271     -39.199 -61.268 -40.730  1.00 30.71           C  
ANISOU 5026  CB  GLU B 271     4522   3496   3650  -1624    409   -538       C  
ATOM   5027  CG  GLU B 271     -40.576 -61.656 -41.206  1.00 59.78           C  
ANISOU 5027  CG  GLU B 271     8103   7339   7272  -1867    448   -706       C  
ATOM   5028  CD  GLU B 271     -41.005 -62.999 -40.633  1.00 83.56           C  
ANISOU 5028  CD  GLU B 271    11345  10209  10194  -2128    597   -766       C  
ATOM   5029  OE1 GLU B 271     -41.576 -63.815 -41.389  1.00 87.71           O  
ANISOU 5029  OE1 GLU B 271    11928  10747  10650  -2320    650   -883       O  
ATOM   5030  OE2 GLU B 271     -40.761 -63.240 -39.425  1.00 91.36           O  
ANISOU 5030  OE2 GLU B 271    12475  11067  11172  -2146    665   -699       O  
ATOM   5031  N   GLU B 272     -36.501 -59.649 -40.181  1.00 29.61           N  
ANISOU 5031  N   GLU B 272     4373   3226   3650  -1093    264   -246       N  
ATOM   5032  CA  GLU B 272     -35.483 -59.089 -39.311  1.00 32.31           C  
ANISOU 5032  CA  GLU B 272     4729   3512   4034   -928    235   -132       C  
ATOM   5033  C   GLU B 272     -34.175 -59.054 -40.085  1.00 29.33           C  
ANISOU 5033  C   GLU B 272     4398   3070   3675   -750    194    -65       C  
ATOM   5034  O   GLU B 272     -33.997 -59.758 -41.087  1.00 27.84           O  
ANISOU 5034  O   GLU B 272     4296   2826   3455   -759    210    -94       O  
ATOM   5035  CB  GLU B 272     -35.378 -59.872 -37.985  1.00 40.94           C  
ANISOU 5035  CB  GLU B 272     6004   4468   5084   -983    315    -95       C  
ATOM   5036  CG  GLU B 272     -34.442 -61.063 -37.925  1.00 58.29           C  
ANISOU 5036  CG  GLU B 272     8468   6456   7222   -919    367    -42       C  
ATOM   5037  CD  GLU B 272     -34.742 -61.941 -36.716  1.00 76.56           C  
ANISOU 5037  CD  GLU B 272    10996   8632   9461  -1025    462    -32       C  
ATOM   5038  OE1 GLU B 272     -33.803 -62.281 -35.959  1.00 78.56           O  
ANISOU 5038  OE1 GLU B 272    11408   8758   9683   -883    467     55       O  
ATOM   5039  OE2 GLU B 272     -35.934 -62.261 -36.507  1.00 82.80           O  
ANISOU 5039  OE2 GLU B 272    11790   9454  10215  -1251    532   -118       O  
ATOM   5040  N   LEU B 273     -33.279 -58.177 -39.648  1.00 22.98           N  
ANISOU 5040  N   LEU B 273     3524   2292   2917   -598    142     15       N  
ATOM   5041  CA  LEU B 273     -32.037 -57.941 -40.377  1.00 34.55           C  
ANISOU 5041  CA  LEU B 273     4986   3742   4400   -440    104     65       C  
ATOM   5042  C   LEU B 273     -30.906 -57.687 -39.403  1.00 30.90           C  
ANISOU 5042  C   LEU B 273     4542   3250   3949   -307     91    147       C  
ATOM   5043  O   LEU B 273     -31.078 -56.959 -38.426  1.00 30.87           O  
ANISOU 5043  O   LEU B 273     4462   3296   3971   -312     73    170       O  
ATOM   5044  CB  LEU B 273     -32.118 -56.722 -41.316  1.00 32.00           C  
ANISOU 5044  CB  LEU B 273     4493   3549   4116   -399     38     52       C  
ATOM   5045  CG  LEU B 273     -32.882 -56.830 -42.625  1.00 39.00           C  
ANISOU 5045  CG  LEU B 273     5346   4490   4982   -466     25    -23       C  
ATOM   5046  CD1 LEU B 273     -32.847 -55.475 -43.309  1.00 29.49           C  
ANISOU 5046  CD1 LEU B 273     4006   3398   3802   -390    -44    -15       C  
ATOM   5047  CD2 LEU B 273     -32.267 -57.922 -43.506  1.00 33.87           C  
ANISOU 5047  CD2 LEU B 273     4835   3738   4294   -446     60    -31       C  
ATOM   5048  N   GLU B 274     -29.741 -58.248 -39.704  1.00 26.74           N  
ANISOU 5048  N   GLU B 274     4103   2659   3399   -180     96    181       N  
ATOM   5049  CA  GLU B 274     -28.501 -57.868 -39.048  1.00 24.86           C  
ANISOU 5049  CA  GLU B 274     3831   2448   3167    -30     67    241       C  
ATOM   5050  C   GLU B 274     -27.664 -57.083 -40.046  1.00 31.07           C  
ANISOU 5050  C   GLU B 274     4491   3332   3984     47     30    241       C  
ATOM   5051  O   GLU B 274     -27.471 -57.527 -41.186  1.00 28.97           O  
ANISOU 5051  O   GLU B 274     4261   3045   3700     65     43    215       O  
ATOM   5052  CB  GLU B 274     -27.743 -59.102 -38.545  1.00 29.07           C  
ANISOU 5052  CB  GLU B 274     4556   2861   3630     82     99    270       C  
ATOM   5053  CG  GLU B 274     -26.364 -58.808 -37.958  1.00 33.64           C  
ANISOU 5053  CG  GLU B 274     5081   3502   4198    264     60    315       C  
ATOM   5054  CD  GLU B 274     -25.491 -60.063 -37.867  1.00 41.38           C  
ANISOU 5054  CD  GLU B 274     6247   4383   5092    431     80    332       C  
ATOM   5055  OE1 GLU B 274     -26.017 -61.180 -38.074  1.00 43.13           O  
ANISOU 5055  OE1 GLU B 274     6679   4450   5258    391    135    319       O  
ATOM   5056  OE2 GLU B 274     -24.278 -59.935 -37.605  1.00 42.21           O  
ANISOU 5056  OE2 GLU B 274     6292   4570   5174    606     43    350       O  
ATOM   5057  N   ILE B 275     -27.211 -55.905 -39.643  1.00 24.23           N  
ANISOU 5057  N   ILE B 275     3487   2566   3154     75     -8    265       N  
ATOM   5058  CA  ILE B 275     -26.255 -55.150 -40.443  1.00 23.49           C  
ANISOU 5058  CA  ILE B 275     3290   2562   3073    134    -26    264       C  
ATOM   5059  C   ILE B 275     -24.865 -55.518 -39.942  1.00 31.44           C  
ANISOU 5059  C   ILE B 275     4296   3602   4049    272    -28    285       C  
ATOM   5060  O   ILE B 275     -24.560 -55.377 -38.749  1.00 29.60           O  
ANISOU 5060  O   ILE B 275     4045   3392   3810    310    -45    310       O  
ATOM   5061  CB  ILE B 275     -26.508 -53.639 -40.362  1.00 31.57           C  
ANISOU 5061  CB  ILE B 275     4190   3672   4135     74    -55    269       C  
ATOM   5062  CG1 ILE B 275     -27.932 -53.317 -40.841  1.00 27.20           C  
ANISOU 5062  CG1 ILE B 275     3634   3106   3594    -24    -64    240       C  
ATOM   5063  CG2 ILE B 275     -25.442 -52.881 -41.167  1.00 29.57           C  
ANISOU 5063  CG2 ILE B 275     3859   3498   3877    109    -55    265       C  
ATOM   5064  CD1 ILE B 275     -28.298 -51.850 -40.794  1.00 27.10           C  
ANISOU 5064  CD1 ILE B 275     3536   3158   3601    -55    -94    244       C  
ATOM   5065  N   ARG B 276     -24.046 -56.047 -40.844  1.00 29.05           N  
ANISOU 5065  N   ARG B 276     4010   3311   3717    357    -12    267       N  
ATOM   5066  CA  ARG B 276     -22.730 -56.562 -40.509  1.00 29.87           C  
ANISOU 5066  CA  ARG B 276     4107   3467   3774    519    -15    269       C  
ATOM   5067  C   ARG B 276     -21.761 -56.091 -41.579  1.00 32.84           C  
ANISOU 5067  C   ARG B 276     4369   3962   4148    551     -5    235       C  
ATOM   5068  O   ARG B 276     -22.065 -56.180 -42.774  1.00 29.61           O  
ANISOU 5068  O   ARG B 276     3988   3519   3742    505     19    214       O  
ATOM   5069  CB  ARG B 276     -22.746 -58.099 -40.426  1.00 29.54           C  
ANISOU 5069  CB  ARG B 276     4262   3292   3671    624      8    273       C  
ATOM   5070  CG  ARG B 276     -21.440 -58.712 -39.918  1.00 37.00           C  
ANISOU 5070  CG  ARG B 276     5221   4292   4547    839     -7    275       C  
ATOM   5071  CD  ARG B 276     -21.377 -60.231 -40.132  1.00 39.67           C  
ANISOU 5071  CD  ARG B 276     5790   4478   4804    967     25    276       C  
ATOM   5072  NE  ARG B 276     -22.420 -60.932 -39.390  1.00 40.99           N  
ANISOU 5072  NE  ARG B 276     6166   4462   4947    894     49    306       N  
ATOM   5073  CZ  ARG B 276     -22.616 -62.246 -39.426  1.00 42.82           C  
ANISOU 5073  CZ  ARG B 276     6657   4515   5098    957     92    310       C  
ATOM   5074  NH1 ARG B 276     -21.829 -63.024 -40.162  1.00 43.63           N  
ANISOU 5074  NH1 ARG B 276     6844   4595   5138   1122    107    289       N  
ATOM   5075  NH2 ARG B 276     -23.603 -62.786 -38.725  1.00 47.13           N  
ANISOU 5075  NH2 ARG B 276     7391   4902   5617    848    129    331       N  
ATOM   5076  N   PHE B 277     -20.615 -55.562 -41.156  1.00 28.69           N  
ANISOU 5076  N   PHE B 277     3708   3587   3608    617    -19    222       N  
ATOM   5077  CA  PHE B 277     -19.595 -55.106 -42.101  1.00 26.62           C  
ANISOU 5077  CA  PHE B 277     3323   3461   3330    631      5    177       C  
ATOM   5078  C   PHE B 277     -18.647 -56.268 -42.327  1.00 32.66           C  
ANISOU 5078  C   PHE B 277     4119   4261   4031    825     14    149       C  
ATOM   5079  O   PHE B 277     -17.652 -56.440 -41.622  1.00 28.10           O  
ANISOU 5079  O   PHE B 277     3459   3809   3408    960     -9    129       O  
ATOM   5080  CB  PHE B 277     -18.916 -53.839 -41.597  1.00 27.41           C  
ANISOU 5080  CB  PHE B 277     3254   3722   3440    561     -2    159       C  
ATOM   5081  CG  PHE B 277     -19.817 -52.653 -41.679  1.00 28.30           C  
ANISOU 5081  CG  PHE B 277     3368   3784   3602    384      1    181       C  
ATOM   5082  CD1 PHE B 277     -20.720 -52.381 -40.656  1.00 28.41           C  
ANISOU 5082  CD1 PHE B 277     3424   3723   3647    335    -32    220       C  
ATOM   5083  CD2 PHE B 277     -19.852 -51.878 -42.824  1.00 26.06           C  
ANISOU 5083  CD2 PHE B 277     3070   3513   3321    280     38    164       C  
ATOM   5084  CE1 PHE B 277     -21.602 -51.320 -40.758  1.00 24.45           C  
ANISOU 5084  CE1 PHE B 277     2933   3175   3180    203    -32    236       C  
ATOM   5085  CE2 PHE B 277     -20.737 -50.812 -42.941  1.00 24.57           C  
ANISOU 5085  CE2 PHE B 277     2915   3262   3159    152     36    186       C  
ATOM   5086  CZ  PHE B 277     -21.615 -50.530 -41.900  1.00 22.92           C  
ANISOU 5086  CZ  PHE B 277     2734   2991   2982    122     -2    220       C  
ATOM   5087  N   GLU B 278     -18.984 -57.076 -43.334  1.00 26.40           N  
ANISOU 5087  N   GLU B 278     3449   3360   3222    849     44    142       N  
ATOM   5088  CA  GLU B 278     -18.323 -58.346 -43.604  1.00 30.09           C  
ANISOU 5088  CA  GLU B 278     4010   3805   3620   1045     57    121       C  
ATOM   5089  C   GLU B 278     -18.822 -58.866 -44.942  1.00 26.77           C  
ANISOU 5089  C   GLU B 278     3704   3273   3196   1001    100    105       C  
ATOM   5090  O   GLU B 278     -20.011 -58.725 -45.252  1.00 26.47           O  
ANISOU 5090  O   GLU B 278     3747   3113   3198    848    104    125       O  
ATOM   5091  CB  GLU B 278     -18.629 -59.360 -42.496  1.00 28.78           C  
ANISOU 5091  CB  GLU B 278     4016   3507   3410   1162     33    159       C  
ATOM   5092  CG  GLU B 278     -18.051 -60.730 -42.723  1.00 30.27           C  
ANISOU 5092  CG  GLU B 278     4363   3631   3508   1384     48    144       C  
ATOM   5093  CD  GLU B 278     -18.355 -61.649 -41.552  1.00 45.52           C  
ANISOU 5093  CD  GLU B 278     6502   5414   5380   1495     30    189       C  
ATOM   5094  OE1 GLU B 278     -17.850 -61.363 -40.448  1.00 51.46           O  
ANISOU 5094  OE1 GLU B 278     7176   6267   6111   1584    -17    203       O  
ATOM   5095  OE2 GLU B 278     -19.121 -62.623 -41.724  1.00 43.60           O  
ANISOU 5095  OE2 GLU B 278     6510   4953   5104   1476     66    207       O  
ATOM   5096  N   GLU B 279     -17.916 -59.448 -45.732  1.00 26.08           N  
ANISOU 5096  N   GLU B 279     3612   3245   3052   1138    129     61       N  
ATOM   5097  CA  GLU B 279     -18.304 -60.037 -47.012  1.00 32.20           C  
ANISOU 5097  CA  GLU B 279     4509   3914   3811   1112    171     40       C  
ATOM   5098  C   GLU B 279     -19.380 -61.099 -46.816  1.00 36.51           C  
ANISOU 5098  C   GLU B 279     5303   4229   4341   1095    175     67       C  
ATOM   5099  O   GLU B 279     -19.363 -61.856 -45.839  1.00 33.64           O  
ANISOU 5099  O   GLU B 279     5064   3780   3937   1204    162     92       O  
ATOM   5100  CB  GLU B 279     -17.096 -60.671 -47.718  1.00 35.20           C  
ANISOU 5100  CB  GLU B 279     4866   4390   4119   1302    203    -15       C  
ATOM   5101  CG  GLU B 279     -16.045 -59.685 -48.212  1.00 39.08           C  
ANISOU 5101  CG  GLU B 279     5114   5122   4613   1280    225    -65       C  
ATOM   5102  CD  GLU B 279     -15.088 -59.234 -47.112  1.00 55.76           C  
ANISOU 5102  CD  GLU B 279     7044   7432   6712   1368    191    -83       C  
ATOM   5103  OE1 GLU B 279     -15.280 -59.627 -45.932  1.00 54.28           O  
ANISOU 5103  OE1 GLU B 279     6921   7186   6515   1455    142    -45       O  
ATOM   5104  OE2 GLU B 279     -14.144 -58.476 -47.430  1.00 60.71           O  
ANISOU 5104  OE2 GLU B 279     7462   8277   7326   1339    217   -140       O  
ATOM   5105  N   CYS B 280     -20.329 -61.144 -47.748  1.00 31.24           N  
ANISOU 5105  N   CYS B 280     4714   3462   3693    948    196     57       N  
ATOM   5106  CA  CYS B 280     -21.238 -62.274 -47.801  1.00 31.21           C  
ANISOU 5106  CA  CYS B 280     4949   3254   3654    915    219     56       C  
ATOM   5107  C   CYS B 280     -20.436 -63.562 -48.001  1.00 38.55           C  
ANISOU 5107  C   CYS B 280     6049   4108   4491   1126    253     35       C  
ATOM   5108  O   CYS B 280     -19.385 -63.551 -48.653  1.00 36.36           O  
ANISOU 5108  O   CYS B 280     5687   3945   4183   1262    266      3       O  
ATOM   5109  CB  CYS B 280     -22.257 -62.087 -48.927  1.00 30.68           C  
ANISOU 5109  CB  CYS B 280     4907   3141   3611    733    232     27       C  
ATOM   5110  SG  CYS B 280     -23.501 -60.788 -48.575  1.00 29.91           S  
ANISOU 5110  SG  CYS B 280     4671   3096   3597    513    187     47       S  
ATOM   5111  N   PRO B 281     -20.894 -64.679 -47.433  1.00 39.15           N  
ANISOU 5111  N   PRO B 281     6376   3991   4508   1162    274     49       N  
ATOM   5112  CA  PRO B 281     -20.158 -65.943 -47.580  1.00 33.73           C  
ANISOU 5112  CA  PRO B 281     5901   3203   3713   1388    308     33       C  
ATOM   5113  C   PRO B 281     -19.903 -66.298 -49.042  1.00 37.84           C  
ANISOU 5113  C   PRO B 281     6454   3720   4204   1409    349    -22       C  
ATOM   5114  O   PRO B 281     -20.795 -66.210 -49.891  1.00 38.45           O  
ANISOU 5114  O   PRO B 281     6560   3738   4309   1212    369    -47       O  
ATOM   5115  CB  PRO B 281     -21.080 -66.964 -46.904  1.00 41.45           C  
ANISOU 5115  CB  PRO B 281     7185   3929   4634   1324    343     55       C  
ATOM   5116  CG  PRO B 281     -21.885 -66.144 -45.918  1.00 38.16           C  
ANISOU 5116  CG  PRO B 281     6655   3549   4295   1146    309     94       C  
ATOM   5117  CD  PRO B 281     -22.114 -64.836 -46.620  1.00 39.71           C  
ANISOU 5117  CD  PRO B 281     6566   3926   4596    994    277     77       C  
ATOM   5118  N   GLY B 282     -18.661 -66.688 -49.335  1.00 34.36           N  
ANISOU 5118  N   GLY B 282     5996   3362   3697   1659    357    -49       N  
ATOM   5119  CA  GLY B 282     -18.277 -67.068 -50.684  1.00 38.45           C  
ANISOU 5119  CA  GLY B 282     6548   3887   4175   1710    401   -105       C  
ATOM   5120  C   GLY B 282     -18.114 -65.929 -51.673  1.00 41.12           C  
ANISOU 5120  C   GLY B 282     6625   4416   4584   1580    399   -133       C  
ATOM   5121  O   GLY B 282     -18.052 -66.189 -52.881  1.00 38.69           O  
ANISOU 5121  O   GLY B 282     6360   4093   4247   1568    440   -178       O  
ATOM   5122  N   THR B 283     -18.031 -64.675 -51.209  1.00 34.37           N  
ANISOU 5122  N   THR B 283     5521   3729   3809   1483    360   -109       N  
ATOM   5123  CA  THR B 283     -17.979 -63.510 -52.090  1.00 36.97           C  
ANISOU 5123  CA  THR B 283     5644   4210   4194   1335    365   -128       C  
ATOM   5124  C   THR B 283     -16.811 -62.590 -51.734  1.00 35.53           C  
ANISOU 5124  C   THR B 283     5200   4274   4026   1405    355   -141       C  
ATOM   5125  O   THR B 283     -16.337 -62.556 -50.596  1.00 36.77           O  
ANISOU 5125  O   THR B 283     5292   4499   4180   1511    321   -123       O  
ATOM   5126  CB  THR B 283     -19.288 -62.696 -52.035  1.00 37.16           C  
ANISOU 5126  CB  THR B 283     5646   4179   4296   1082    335    -94       C  
ATOM   5127  OG1 THR B 283     -19.375 -61.994 -50.785  1.00 33.30           O  
ANISOU 5127  OG1 THR B 283     5045   3747   3860   1048    291    -49       O  
ATOM   5128  CG2 THR B 283     -20.501 -63.611 -52.169  1.00 32.50           C  
ANISOU 5128  CG2 THR B 283     5288   3373   3686    988    343    -95       C  
ATOM   5129  N   LYS B 284     -16.369 -61.810 -52.722  1.00 35.12           N  
ANISOU 5129  N   LYS B 284     5002   4361   3981   1328    390   -177       N  
ATOM   5130  CA  LYS B 284     -15.338 -60.797 -52.526  1.00 32.44           C  
ANISOU 5130  CA  LYS B 284     4411   4265   3651   1325    399   -204       C  
ATOM   5131  C   LYS B 284     -15.768 -59.509 -53.212  1.00 37.72           C  
ANISOU 5131  C   LYS B 284     4995   4973   4365   1089    418   -194       C  
ATOM   5132  O   LYS B 284     -16.342 -59.545 -54.305  1.00 34.50           O  
ANISOU 5132  O   LYS B 284     4685   4475   3947   1001    443   -198       O  
ATOM   5133  CB  LYS B 284     -13.977 -61.259 -53.070  1.00 40.66           C  
ANISOU 5133  CB  LYS B 284     5361   5476   4612   1516    448   -282       C  
ATOM   5134  CG  LYS B 284     -13.354 -62.374 -52.244  1.00 60.01           C  
ANISOU 5134  CG  LYS B 284     7872   7931   6999   1797    419   -296       C  
ATOM   5135  CD  LYS B 284     -12.016 -62.826 -52.802  1.00 71.65           C  
ANISOU 5135  CD  LYS B 284     9239   9601   8384   2013    464   -386       C  
ATOM   5136  CE  LYS B 284     -11.426 -63.955 -51.959  1.00 74.20           C  
ANISOU 5136  CE  LYS B 284     9648   9921   8624   2336    424   -398       C  
ATOM   5137  NZ  LYS B 284     -10.166 -64.495 -52.546  1.00 72.96           N  
ANISOU 5137  NZ  LYS B 284     9395   9959   8366   2584    464   -495       N  
ATOM   5138  N   VAL B 285     -15.489 -58.375 -52.566  1.00 31.28           N  
ANISOU 5138  N   VAL B 285     4014   4286   3586    991    406   -183       N  
ATOM   5139  CA  VAL B 285     -15.832 -57.051 -53.077  1.00 28.32           C  
ANISOU 5139  CA  VAL B 285     3584   3939   3238    778    427   -170       C  
ATOM   5140  C   VAL B 285     -14.548 -56.314 -53.436  1.00 38.97           C  
ANISOU 5140  C   VAL B 285     4748   5513   4544    746    496   -234       C  
ATOM   5141  O   VAL B 285     -13.588 -56.311 -52.653  1.00 34.35           O  
ANISOU 5141  O   VAL B 285     4008   5099   3945    830    495   -273       O  
ATOM   5142  CB  VAL B 285     -16.658 -56.237 -52.066  1.00 30.41           C  
ANISOU 5142  CB  VAL B 285     3841   4146   3568    661    370   -109       C  
ATOM   5143  CG1 VAL B 285     -17.030 -54.876 -52.667  1.00 26.49           C  
ANISOU 5143  CG1 VAL B 285     3331   3656   3079    466    394    -94       C  
ATOM   5144  CG2 VAL B 285     -17.914 -57.010 -51.638  1.00 29.61           C  
ANISOU 5144  CG2 VAL B 285     3902   3847   3500    679    312    -61       C  
ATOM   5145  N   TYR B 286     -14.538 -55.689 -54.618  1.00 32.41           N  
ANISOU 5145  N   TYR B 286     3937   4692   3683    617    559   -251       N  
ATOM   5146  CA  TYR B 286     -13.403 -54.940 -55.150  1.00 30.39           C  
ANISOU 5146  CA  TYR B 286     3536   4639   3374    537    649   -319       C  
ATOM   5147  C   TYR B 286     -13.805 -53.480 -55.324  1.00 40.96           C  
ANISOU 5147  C   TYR B 286     4897   5947   4718    304    675   -286       C  
ATOM   5148  O   TYR B 286     -14.878 -53.191 -55.855  1.00 38.66           O  
ANISOU 5148  O   TYR B 286     4768   5484   4438    230    650   -229       O  
ATOM   5149  CB  TYR B 286     -12.953 -55.516 -56.495  1.00 29.23           C  
ANISOU 5149  CB  TYR B 286     3429   4519   3159    590    721   -372       C  
ATOM   5150  CG  TYR B 286     -12.486 -56.959 -56.428  1.00 43.12           C  
ANISOU 5150  CG  TYR B 286     5192   6300   4891    838    706   -412       C  
ATOM   5151  CD1 TYR B 286     -13.395 -58.006 -56.439  1.00 38.51           C  
ANISOU 5151  CD1 TYR B 286     4801   5505   4327    944    648   -367       C  
ATOM   5152  CD2 TYR B 286     -11.133 -57.269 -56.364  1.00 49.81           C  
ANISOU 5152  CD2 TYR B 286     5859   7385   5680    968    754   -504       C  
ATOM   5153  CE1 TYR B 286     -12.974 -59.328 -56.376  1.00 43.61           C  
ANISOU 5153  CE1 TYR B 286     5499   6140   4932   1176    642   -401       C  
ATOM   5154  CE2 TYR B 286     -10.699 -58.587 -56.307  1.00 55.36           C  
ANISOU 5154  CE2 TYR B 286     6590   8100   6342   1230    738   -541       C  
ATOM   5155  CZ  TYR B 286     -11.624 -59.611 -56.310  1.00 52.35           C  
ANISOU 5155  CZ  TYR B 286     6441   7472   5978   1335    683   -483       C  
ATOM   5156  OH  TYR B 286     -11.202 -60.919 -56.251  1.00 63.10           O  
ANISOU 5156  OH  TYR B 286     7876   8815   7283   1599    675   -517       O  
ATOM   5157  N   VAL B 287     -12.950 -52.562 -54.887  1.00 38.69           N  
ANISOU 5157  N   VAL B 287     4459   5831   4410    194    726   -329       N  
ATOM   5158  CA  VAL B 287     -13.211 -51.133 -55.033  1.00 38.61           C  
ANISOU 5158  CA  VAL B 287     4500   5784   4385    -31    768   -303       C  
ATOM   5159  C   VAL B 287     -12.640 -50.675 -56.374  1.00 39.25           C  
ANISOU 5159  C   VAL B 287     4614   5923   4377   -151    887   -352       C  
ATOM   5160  O   VAL B 287     -11.438 -50.813 -56.626  1.00 34.23           O  
ANISOU 5160  O   VAL B 287     3821   5497   3687   -154    970   -446       O  
ATOM   5161  CB  VAL B 287     -12.605 -50.333 -53.870  1.00 40.19           C  
ANISOU 5161  CB  VAL B 287     4549   6126   4597   -123    773   -331       C  
ATOM   5162  CG1 VAL B 287     -12.937 -48.848 -54.008  1.00 35.63           C  
ANISOU 5162  CG1 VAL B 287     4073   5472   3991   -356    822   -302       C  
ATOM   5163  CG2 VAL B 287     -13.100 -50.875 -52.537  1.00 32.43           C  
ANISOU 5163  CG2 VAL B 287     3535   5095   3691     11    659   -286       C  
ATOM   5164  N   GLU B 288     -13.500 -50.136 -57.241  1.00 33.30           N  
ANISOU 5164  N   GLU B 288     4063   4993   3596   -241    895   -295       N  
ATOM   5165  CA  GLU B 288     -13.056 -49.684 -58.558  1.00 29.65           C  
ANISOU 5165  CA  GLU B 288     3675   4555   3035   -357   1010   -331       C  
ATOM   5166  C   GLU B 288     -14.118 -48.768 -59.151  1.00 34.16           C  
ANISOU 5166  C   GLU B 288     4488   4921   3571   -461    997   -252       C  
ATOM   5167  O   GLU B 288     -15.311 -49.092 -59.102  1.00 28.59           O  
ANISOU 5167  O   GLU B 288     3896   4054   2911   -367    890   -185       O  
ATOM   5168  CB  GLU B 288     -12.786 -50.873 -59.488  1.00 32.14           C  
ANISOU 5168  CB  GLU B 288     3987   4901   3324   -213   1028   -372       C  
ATOM   5169  CG  GLU B 288     -13.918 -51.906 -59.549  1.00 30.08           C  
ANISOU 5169  CG  GLU B 288     3847   4463   3121    -47    913   -313       C  
ATOM   5170  CD  GLU B 288     -13.440 -53.232 -60.118  1.00 40.25           C  
ANISOU 5170  CD  GLU B 288     5101   5803   4388    120    931   -369       C  
ATOM   5171  OE1 GLU B 288     -12.244 -53.542 -59.951  1.00 45.10           O  
ANISOU 5171  OE1 GLU B 288     5543   6616   4977    175    992   -448       O  
ATOM   5172  OE2 GLU B 288     -14.241 -53.962 -60.740  1.00 39.58           O  
ANISOU 5172  OE2 GLU B 288     5163   5573   4304    197    885   -342       O  
ATOM   5173  N   GLU B 289     -13.681 -47.629 -59.702  1.00 33.58           N  
ANISOU 5173  N   GLU B 289     4497   4860   3403   -653   1109   -268       N  
ATOM   5174  CA  GLU B 289     -14.603 -46.616 -60.219  1.00 38.21           C  
ANISOU 5174  CA  GLU B 289     5339   5250   3929   -739   1103   -193       C  
ATOM   5175  C   GLU B 289     -15.403 -47.089 -61.431  1.00 37.57           C  
ANISOU 5175  C   GLU B 289     5432   5040   3805   -643   1065   -158       C  
ATOM   5176  O   GLU B 289     -16.384 -46.430 -61.797  1.00 36.73           O  
ANISOU 5176  O   GLU B 289     5533   4770   3652   -649   1019    -91       O  
ATOM   5177  CB  GLU B 289     -13.844 -45.356 -60.626  1.00 45.64           C  
ANISOU 5177  CB  GLU B 289     6369   6221   4752   -974   1253   -225       C  
ATOM   5178  CG  GLU B 289     -13.309 -44.515 -59.501  1.00 60.30           C  
ANISOU 5178  CG  GLU B 289     8131   8157   6624  -1120   1292   -251       C  
ATOM   5179  CD  GLU B 289     -12.460 -43.375 -60.035  1.00 74.48           C  
ANISOU 5179  CD  GLU B 289    10026   9990   8283  -1384   1468   -301       C  
ATOM   5180  OE1 GLU B 289     -12.290 -43.301 -61.279  1.00 75.16           O  
ANISOU 5180  OE1 GLU B 289    10251  10040   8266  -1438   1558   -311       O  
ATOM   5181  OE2 GLU B 289     -11.965 -42.563 -59.223  1.00 76.18           O  
ANISOU 5181  OE2 GLU B 289    10191  10267   8486  -1550   1523   -336       O  
ATOM   5182  N   THR B 290     -14.986 -48.178 -62.085  1.00 34.16           N  
ANISOU 5182  N   THR B 290     4925   4684   3371   -550   1085   -207       N  
ATOM   5183  CA  THR B 290     -15.713 -48.735 -63.225  1.00 37.10           C  
ANISOU 5183  CA  THR B 290     5450   4948   3700   -460   1047   -185       C  
ATOM   5184  C   THR B 290     -16.969 -49.487 -62.812  1.00 32.67           C  
ANISOU 5184  C   THR B 290     4911   4277   3225   -309    892   -138       C  
ATOM   5185  O   THR B 290     -17.723 -49.924 -63.686  1.00 32.76           O  
ANISOU 5185  O   THR B 290     5046   4200   3200   -242    844   -126       O  
ATOM   5186  CB  THR B 290     -14.822 -49.694 -64.004  1.00 37.71           C  
ANISOU 5186  CB  THR B 290     5441   5143   3744   -408   1125   -262       C  
ATOM   5187  OG1 THR B 290     -14.271 -50.645 -63.087  1.00 32.62           O  
ANISOU 5187  OG1 THR B 290     4580   4622   3192   -294   1095   -306       O  
ATOM   5188  CG2 THR B 290     -13.706 -48.948 -64.707  1.00 37.11           C  
ANISOU 5188  CG2 THR B 290     5370   5175   3555   -577   1292   -318       C  
ATOM   5189  N   CYS B 291     -17.181 -49.677 -61.511  1.00 26.91           N  
ANISOU 5189  N   CYS B 291     4062   3563   2601   -264    819   -122       N  
ATOM   5190  CA  CYS B 291     -18.332 -50.416 -61.014  1.00 25.76           C  
ANISOU 5190  CA  CYS B 291     3927   3327   2534   -147    689    -88       C  
ATOM   5191  C   CYS B 291     -19.637 -49.734 -61.408  1.00 25.94           C  
ANISOU 5191  C   CYS B 291     4119   3218   2518   -156    612    -34       C  
ATOM   5192  O   CYS B 291     -19.684 -48.536 -61.681  1.00 28.92           O  
ANISOU 5192  O   CYS B 291     4610   3556   2823   -241    646     -4       O  
ATOM   5193  CB  CYS B 291     -18.285 -50.517 -59.489  1.00 25.00           C  
ANISOU 5193  CB  CYS B 291     3690   3268   2540   -121    639    -76       C  
ATOM   5194  SG  CYS B 291     -19.357 -51.806 -58.846  1.00 31.03           S  
ANISOU 5194  SG  CYS B 291     4443   3953   3395     14    517    -61       S  
ATOM   5195  N   GLY B 292     -20.711 -50.511 -61.401  1.00 26.85           N  
ANISOU 5195  N   GLY B 292     4257   3273   2672    -66    510    -27       N  
ATOM   5196  CA  GLY B 292     -22.036 -49.937 -61.515  1.00 28.68           C  
ANISOU 5196  CA  GLY B 292     4597   3421   2877    -49    415     11       C  
ATOM   5197  C   GLY B 292     -22.332 -48.975 -60.378  1.00 35.40           C  
ANISOU 5197  C   GLY B 292     5422   4257   3773    -81    382     54       C  
ATOM   5198  O   GLY B 292     -21.644 -48.909 -59.357  1.00 31.58           O  
ANISOU 5198  O   GLY B 292     4820   3823   3356   -117    415     55       O  
ATOM   5199  N   THR B 293     -23.407 -48.216 -60.570  1.00 31.33           N  
ANISOU 5199  N   THR B 293     5020   3678   3207    -54    309     86       N  
ATOM   5200  CA  THR B 293     -23.810 -47.172 -59.642  1.00 34.00           C  
ANISOU 5200  CA  THR B 293     5374   3984   3561    -69    277    128       C  
ATOM   5201  C   THR B 293     -24.645 -47.757 -58.496  1.00 31.19           C  
ANISOU 5201  C   THR B 293     4888   3648   3315    -17    183    125       C  
ATOM   5202  O   THR B 293     -25.123 -48.895 -58.553  1.00 31.82           O  
ANISOU 5202  O   THR B 293     4903   3748   3439     27    135     91       O  
ATOM   5203  CB  THR B 293     -24.595 -46.086 -60.391  1.00 33.50           C  
ANISOU 5203  CB  THR B 293     5511   3846   3374    -30    239    160       C  
ATOM   5204  OG1 THR B 293     -24.986 -45.050 -59.481  1.00 53.51           O  
ANISOU 5204  OG1 THR B 293     8080   6338   5913    -29    211    199       O  
ATOM   5205  CG2 THR B 293     -25.841 -46.663 -61.010  1.00 43.20           C  
ANISOU 5205  CG2 THR B 293     6758   5083   4574     81    126    137       C  
ATOM   5206  N   ARG B 294     -24.807 -46.962 -57.438  1.00 26.29           N  
ANISOU 5206  N   ARG B 294     4245   3014   2729    -35    166    156       N  
ATOM   5207  CA  ARG B 294     -25.692 -47.331 -56.332  1.00 28.28           C  
ANISOU 5207  CA  ARG B 294     4393   3281   3069      8     82    155       C  
ATOM   5208  C   ARG B 294     -27.054 -47.758 -56.857  1.00 30.24           C  
ANISOU 5208  C   ARG B 294     4664   3536   3292     86    -16    129       C  
ATOM   5209  O   ARG B 294     -27.600 -47.139 -57.772  1.00 30.92           O  
ANISOU 5209  O   ARG B 294     4871   3602   3276    136    -50    132       O  
ATOM   5210  CB  ARG B 294     -25.884 -46.141 -55.381  1.00 35.10           C  
ANISOU 5210  CB  ARG B 294     5281   4117   3938     -8     71    193       C  
ATOM   5211  CG  ARG B 294     -25.239 -46.278 -54.028  1.00 37.77           C  
ANISOU 5211  CG  ARG B 294     5490   4490   4371    -61    100    199       C  
ATOM   5212  CD  ARG B 294     -25.224 -44.941 -53.286  1.00 36.55           C  
ANISOU 5212  CD  ARG B 294     5395   4297   4196    -99    112    233       C  
ATOM   5213  NE  ARG B 294     -26.553 -44.458 -52.910  1.00 34.77           N  
ANISOU 5213  NE  ARG B 294     5210   4040   3961    -16     22    247       N  
ATOM   5214  CZ  ARG B 294     -27.136 -44.678 -51.731  1.00 32.16           C  
ANISOU 5214  CZ  ARG B 294     4773   3737   3709      6    -30    245       C  
ATOM   5215  NH1 ARG B 294     -28.345 -44.179 -51.476  1.00 34.02           N  
ANISOU 5215  NH1 ARG B 294     5039   3964   3923     87   -107    247       N  
ATOM   5216  NH2 ARG B 294     -26.514 -45.384 -50.793  1.00 24.02           N  
ANISOU 5216  NH2 ARG B 294     3608   2748   2769    -42     -6    238       N  
ATOM   5217  N   GLY B 295     -27.619 -48.801 -56.254  1.00 27.24           N  
ANISOU 5217  N   GLY B 295     4172   3189   2990     93    -61     96       N  
ATOM   5218  CA  GLY B 295     -28.920 -49.274 -56.664  1.00 26.78           C  
ANISOU 5218  CA  GLY B 295     4105   3166   2906    136   -148     50       C  
ATOM   5219  C   GLY B 295     -29.595 -50.115 -55.600  1.00 29.80           C  
ANISOU 5219  C   GLY B 295     4369   3580   3375    110   -183     19       C  
ATOM   5220  O   GLY B 295     -29.122 -50.211 -54.462  1.00 28.11           O  
ANISOU 5220  O   GLY B 295     4092   3350   3239     79   -151     46       O  
ATOM   5221  N   PRO B 296     -30.723 -50.733 -55.955  1.00 31.17           N  
ANISOU 5221  N   PRO B 296     4512   3805   3525    113   -246    -44       N  
ATOM   5222  CA  PRO B 296     -31.413 -51.620 -55.007  1.00 28.04           C  
ANISOU 5222  CA  PRO B 296     4020   3437   3197     56   -263    -86       C  
ATOM   5223  C   PRO B 296     -30.452 -52.664 -54.466  1.00 28.83           C  
ANISOU 5223  C   PRO B 296     4122   3466   3365      6   -186    -71       C  
ATOM   5224  O   PRO B 296     -29.598 -53.183 -55.194  1.00 23.55           O  
ANISOU 5224  O   PRO B 296     3514   2756   2678     12   -136    -70       O  
ATOM   5225  CB  PRO B 296     -32.515 -52.268 -55.857  1.00 34.91           C  
ANISOU 5225  CB  PRO B 296     4879   4380   4006     38   -320   -176       C  
ATOM   5226  CG  PRO B 296     -32.730 -51.327 -57.000  1.00 39.01           C  
ANISOU 5226  CG  PRO B 296     5465   4936   4422    131   -370   -172       C  
ATOM   5227  CD  PRO B 296     -31.391 -50.682 -57.269  1.00 34.47           C  
ANISOU 5227  CD  PRO B 296     4987   4267   3841    157   -300    -90       C  
ATOM   5228  N   SER B 297     -30.582 -52.953 -53.176  1.00 24.91           N  
ANISOU 5228  N   SER B 297     3568   2959   2938    -29   -177    -61       N  
ATOM   5229  CA  SER B 297     -29.743 -53.970 -52.569  1.00 23.27           C  
ANISOU 5229  CA  SER B 297     3379   2682   2779    -49   -114    -46       C  
ATOM   5230  C   SER B 297     -30.002 -55.327 -53.223  1.00 23.67           C  
ANISOU 5230  C   SER B 297     3499   2694   2800    -91    -93   -107       C  
ATOM   5231  O   SER B 297     -31.143 -55.693 -53.530  1.00 25.10           O  
ANISOU 5231  O   SER B 297     3672   2913   2950   -154   -129   -174       O  
ATOM   5232  CB  SER B 297     -29.995 -54.015 -51.055  1.00 25.96           C  
ANISOU 5232  CB  SER B 297     3666   3016   3182    -77   -114    -26       C  
ATOM   5233  OG  SER B 297     -29.541 -55.227 -50.476  1.00 33.35           O  
ANISOU 5233  OG  SER B 297     4651   3878   4141    -92    -65    -27       O  
ATOM   5234  N   LEU B 298     -28.925 -56.067 -53.454  1.00 23.14           N  
ANISOU 5234  N   LEU B 298     3499   2562   2733    -54    -33    -94       N  
ATOM   5235  CA  LEU B 298     -28.981 -57.335 -54.165  1.00 22.87           C  
ANISOU 5235  CA  LEU B 298     3565   2468   2658    -78     -2   -148       C  
ATOM   5236  C   LEU B 298     -28.591 -58.459 -53.222  1.00 31.54           C  
ANISOU 5236  C   LEU B 298     4734   3469   3780    -74     49   -140       C  
ATOM   5237  O   LEU B 298     -27.712 -58.288 -52.369  1.00 24.92           O  
ANISOU 5237  O   LEU B 298     3870   2620   2980     -3     70    -85       O  
ATOM   5238  CB  LEU B 298     -28.034 -57.333 -55.368  1.00 21.68           C  
ANISOU 5238  CB  LEU B 298     3463   2313   2462    -12     31   -146       C  
ATOM   5239  CG  LEU B 298     -28.299 -56.261 -56.424  1.00 28.12           C  
ANISOU 5239  CG  LEU B 298     4255   3201   3229     -5     -9   -147       C  
ATOM   5240  CD1 LEU B 298     -27.199 -56.320 -57.463  1.00 26.48           C  
ANISOU 5240  CD1 LEU B 298     4103   2982   2976     50     46   -142       C  
ATOM   5241  CD2 LEU B 298     -29.672 -56.447 -57.095  1.00 25.31           C  
ANISOU 5241  CD2 LEU B 298     3909   2886   2821    -67    -70   -218       C  
ATOM   5242  N   ARG B 299     -29.240 -59.608 -53.382  1.00 28.90           N  
ANISOU 5242  N   ARG B 299     4504   3065   3411   -152     71   -200       N  
ATOM   5243  CA  ARG B 299     -28.893 -60.762 -52.568  1.00 28.82           C  
ANISOU 5243  CA  ARG B 299     4620   2930   3398   -142    128   -193       C  
ATOM   5244  C   ARG B 299     -27.716 -61.500 -53.201  1.00 28.70           C  
ANISOU 5244  C   ARG B 299     4717   2842   3344    -21    179   -187       C  
ATOM   5245  O   ARG B 299     -27.544 -61.494 -54.422  1.00 27.28           O  
ANISOU 5245  O   ARG B 299     4551   2686   3126     -7    182   -219       O  
ATOM   5246  CB  ARG B 299     -30.096 -61.691 -52.419  1.00 26.33           C  
ANISOU 5246  CB  ARG B 299     4401   2557   3048   -301    148   -266       C  
ATOM   5247  CG  ARG B 299     -30.008 -62.623 -51.200  1.00 29.46           C  
ANISOU 5247  CG  ARG B 299     4934   2820   3440   -318    205   -247       C  
ATOM   5248  CD  ARG B 299     -31.245 -63.498 -51.099  1.00 26.32           C  
ANISOU 5248  CD  ARG B 299     4640   2368   2994   -518    242   -332       C  
ATOM   5249  NE  ARG B 299     -31.290 -64.478 -52.184  1.00 30.29           N  
ANISOU 5249  NE  ARG B 299     5298   2788   3422   -565    283   -401       N  
ATOM   5250  CZ  ARG B 299     -32.377 -65.159 -52.534  1.00 35.82           C  
ANISOU 5250  CZ  ARG B 299     6071   3476   4065   -765    311   -504       C  
ATOM   5251  NH1 ARG B 299     -33.527 -64.946 -51.904  1.00 37.53           N  
ANISOU 5251  NH1 ARG B 299     6193   3776   4290   -935    303   -554       N  
ATOM   5252  NH2 ARG B 299     -32.319 -66.037 -53.527  1.00 41.58           N  
ANISOU 5252  NH2 ARG B 299     6956   4122   4722   -802    351   -566       N  
ATOM   5253  N   SER B 300     -26.890 -62.123 -52.352  1.00 29.90           N  
ANISOU 5253  N   SER B 300     4948   2915   3496     82    218   -149       N  
ATOM   5254  CA  SER B 300     -25.670 -62.761 -52.839  1.00 32.38           C  
ANISOU 5254  CA  SER B 300     5348   3187   3768    238    262   -146       C  
ATOM   5255  C   SER B 300     -25.951 -64.067 -53.574  1.00 32.70           C  
ANISOU 5255  C   SER B 300     5602   3091   3732    210    311   -206       C  
ATOM   5256  O   SER B 300     -25.077 -64.566 -54.287  1.00 32.42           O  
ANISOU 5256  O   SER B 300     5639   3030   3650    334    347   -220       O  
ATOM   5257  CB  SER B 300     -24.696 -63.007 -51.673  1.00 31.62           C  
ANISOU 5257  CB  SER B 300     5266   3069   3679    390    275    -93       C  
ATOM   5258  OG  SER B 300     -25.179 -63.995 -50.764  1.00 33.95           O  
ANISOU 5258  OG  SER B 300     5740   3216   3944    364    302    -91       O  
ATOM   5259  N   THR B 301     -27.145 -64.626 -53.420  1.00 30.04           N  
ANISOU 5259  N   THR B 301     5366   2674   3373     43    321   -252       N  
ATOM   5260  CA  THR B 301     -27.541 -65.866 -54.065  1.00 31.02           C  
ANISOU 5260  CA  THR B 301     5712   2659   3416    -27    376   -322       C  
ATOM   5261  C   THR B 301     -28.708 -65.592 -55.001  1.00 35.10           C  
ANISOU 5261  C   THR B 301     6162   3254   3920   -215    344   -400       C  
ATOM   5262  O   THR B 301     -29.618 -64.826 -54.662  1.00 32.92           O  
ANISOU 5262  O   THR B 301     5734   3089   3687   -331    293   -409       O  
ATOM   5263  CB  THR B 301     -27.943 -66.915 -53.029  1.00 31.46           C  
ANISOU 5263  CB  THR B 301     5980   2543   3430    -90    432   -325       C  
ATOM   5264  OG1 THR B 301     -28.714 -66.274 -51.999  1.00 32.42           O  
ANISOU 5264  OG1 THR B 301     5977   2732   3610   -204    400   -304       O  
ATOM   5265  CG2 THR B 301     -26.707 -67.565 -52.409  1.00 35.66           C  
ANISOU 5265  CG2 THR B 301     6662   2962   3926    140    470   -267       C  
ATOM   5266  N   THR B 302     -28.672 -66.212 -56.179  1.00 33.79           N  
ANISOU 5266  N   THR B 302     6109   3044   3687   -229    371   -461       N  
ATOM   5267  CA  THR B 302     -29.769 -66.107 -57.121  1.00 34.09           C  
ANISOU 5267  CA  THR B 302     6103   3159   3690   -400    339   -550       C  
ATOM   5268  C   THR B 302     -30.958 -66.919 -56.619  1.00 38.68           C  
ANISOU 5268  C   THR B 302     6793   3671   4231   -620    374   -629       C  
ATOM   5269  O   THR B 302     -30.900 -67.589 -55.585  1.00 35.12           O  
ANISOU 5269  O   THR B 302     6485   3085   3774   -640    432   -606       O  
ATOM   5270  CB  THR B 302     -29.336 -66.598 -58.501  1.00 31.50           C  
ANISOU 5270  CB  THR B 302     5880   2798   3291   -353    364   -598       C  
ATOM   5271  OG1 THR B 302     -29.107 -68.008 -58.434  1.00 33.45           O  
ANISOU 5271  OG1 THR B 302     6400   2844   3465   -358    451   -632       O  
ATOM   5272  CG2 THR B 302     -28.050 -65.899 -58.939  1.00 34.01           C  
ANISOU 5272  CG2 THR B 302     6106   3180   3637   -145    354   -527       C  
ATOM   5273  N   ALA B 303     -32.054 -66.867 -57.380  1.00 41.07           N  
ANISOU 5273  N   ALA B 303     7035   4076   4495   -794    342   -730       N  
ATOM   5274  CA  ALA B 303     -33.234 -67.651 -57.030  1.00 46.01           C  
ANISOU 5274  CA  ALA B 303     7747   4668   5068  -1043    384   -833       C  
ATOM   5275  C   ALA B 303     -32.927 -69.142 -56.978  1.00 46.74           C  
ANISOU 5275  C   ALA B 303     8171   4513   5076  -1093    499   -864       C  
ATOM   5276  O   ALA B 303     -33.537 -69.871 -56.188  1.00 49.07           O  
ANISOU 5276  O   ALA B 303     8605   4705   5333  -1265    569   -906       O  
ATOM   5277  CB  ALA B 303     -34.364 -67.368 -58.024  1.00 46.47           C  
ANISOU 5277  CB  ALA B 303     7666   4911   5079  -1201    323   -956       C  
ATOM   5278  N   SER B 304     -31.986 -69.616 -57.794  1.00 43.46           N  
ANISOU 5278  N   SER B 304     7902   3992   4619   -945    528   -847       N  
ATOM   5279  CA  SER B 304     -31.628 -71.031 -57.786  1.00 48.77           C  
ANISOU 5279  CA  SER B 304     8923   4411   5197   -956    637   -874       C  
ATOM   5280  C   SER B 304     -30.651 -71.390 -56.672  1.00 47.21           C  
ANISOU 5280  C   SER B 304     8877   4047   5012   -763    685   -766       C  
ATOM   5281  O   SER B 304     -30.326 -72.574 -56.513  1.00 50.27           O  
ANISOU 5281  O   SER B 304     9590   4202   5309   -739    778   -777       O  
ATOM   5282  CB  SER B 304     -31.034 -71.434 -59.139  1.00 50.91           C  
ANISOU 5282  CB  SER B 304     9298   4641   5405   -860    650   -910       C  
ATOM   5283  OG  SER B 304     -29.673 -71.048 -59.233  1.00 48.17           O  
ANISOU 5283  OG  SER B 304     8908   4295   5098   -567    634   -809       O  
ATOM   5284  N   GLY B 305     -30.191 -70.411 -55.898  1.00 44.55           N  
ANISOU 5284  N   GLY B 305     8331   3822   4774   -622    625   -667       N  
ATOM   5285  CA  GLY B 305     -29.210 -70.633 -54.857  1.00 44.14           C  
ANISOU 5285  CA  GLY B 305     8382   3656   4732   -415    651   -568       C  
ATOM   5286  C   GLY B 305     -27.772 -70.403 -55.273  1.00 43.95           C  
ANISOU 5286  C   GLY B 305     8316   3662   4722   -118    631   -504       C  
ATOM   5287  O   GLY B 305     -26.874 -70.556 -54.436  1.00 42.28           O  
ANISOU 5287  O   GLY B 305     8164   3391   4510     83    642   -430       O  
ATOM   5288  N   ARG B 306     -27.522 -70.023 -56.524  1.00 42.74           N  
ANISOU 5288  N   ARG B 306     8054   3615   4571    -83    603   -536       N  
ATOM   5289  CA  ARG B 306     -26.156 -69.816 -56.984  1.00 42.01           C  
ANISOU 5289  CA  ARG B 306     7910   3571   4482    177    598   -492       C  
ATOM   5290  C   ARG B 306     -25.541 -68.584 -56.318  1.00 35.25           C  
ANISOU 5290  C   ARG B 306     6778   2890   3725    294    534   -408       C  
ATOM   5291  O   ARG B 306     -26.138 -67.503 -56.304  1.00 36.29           O  
ANISOU 5291  O   ARG B 306     6689   3171   3929    177    473   -399       O  
ATOM   5292  CB  ARG B 306     -26.133 -69.677 -58.508  1.00 40.52           C  
ANISOU 5292  CB  ARG B 306     7678   3454   4262    154    591   -552       C  
ATOM   5293  CG  ARG B 306     -24.756 -69.410 -59.102  1.00 41.32           C  
ANISOU 5293  CG  ARG B 306     7707   3632   4360    396    598   -522       C  
ATOM   5294  CD  ARG B 306     -24.766 -69.504 -60.625  1.00 43.89           C  
ANISOU 5294  CD  ARG B 306     8057   3989   4631    365    611   -589       C  
ATOM   5295  NE  ARG B 306     -25.657 -68.528 -61.265  1.00 44.09           N  
ANISOU 5295  NE  ARG B 306     7897   4162   4693    188    545   -612       N  
ATOM   5296  CZ  ARG B 306     -25.281 -67.322 -61.688  1.00 45.36           C  
ANISOU 5296  CZ  ARG B 306     7836   4498   4902    234    499   -575       C  
ATOM   5297  NH1 ARG B 306     -26.160 -66.512 -62.269  1.00 44.45           N  
ANISOU 5297  NH1 ARG B 306     7596   4496   4797     94    436   -598       N  
ATOM   5298  NH2 ARG B 306     -24.026 -66.924 -61.544  1.00 43.90           N  
ANISOU 5298  NH2 ARG B 306     7559   4381   4740    419    519   -523       N  
ATOM   5299  N   VAL B 307     -24.339 -68.750 -55.768  1.00 32.33           N  
ANISOU 5299  N   VAL B 307     6428   2509   3347    531    549   -355       N  
ATOM   5300  CA  VAL B 307     -23.606 -67.639 -55.171  1.00 36.53           C  
ANISOU 5300  CA  VAL B 307     6704   3216   3959    642    497   -290       C  
ATOM   5301  C   VAL B 307     -22.914 -66.840 -56.270  1.00 36.61           C  
ANISOU 5301  C   VAL B 307     6529   3394   3987    701    484   -302       C  
ATOM   5302  O   VAL B 307     -22.257 -67.402 -57.158  1.00 41.36           O  
ANISOU 5302  O   VAL B 307     7218   3972   4523    812    527   -340       O  
ATOM   5303  CB  VAL B 307     -22.597 -68.148 -54.128  1.00 40.64           C  
ANISOU 5303  CB  VAL B 307     7304   3688   4448    874    513   -243       C  
ATOM   5304  CG1 VAL B 307     -21.787 -66.991 -53.559  1.00 36.21           C  
ANISOU 5304  CG1 VAL B 307     6462   3333   3961    973    462   -193       C  
ATOM   5305  CG2 VAL B 307     -23.313 -68.883 -53.003  1.00 39.38           C  
ANISOU 5305  CG2 VAL B 307     7354   3350   4260    804    533   -224       C  
ATOM   5306  N   ILE B 308     -23.083 -65.527 -56.230  1.00 34.66           N  
ANISOU 5306  N   ILE B 308     6046   3307   3817    620    432   -273       N  
ATOM   5307  CA  ILE B 308     -22.354 -64.617 -57.107  1.00 34.72           C  
ANISOU 5307  CA  ILE B 308     5882   3473   3835    664    429   -275       C  
ATOM   5308  C   ILE B 308     -21.010 -64.326 -56.444  1.00 33.00           C  
ANISOU 5308  C   ILE B 308     5543   3364   3631    847    440   -242       C  
ATOM   5309  O   ILE B 308     -20.964 -63.774 -55.340  1.00 34.64           O  
ANISOU 5309  O   ILE B 308     5645   3624   3894    847    405   -196       O  
ATOM   5310  CB  ILE B 308     -23.157 -63.328 -57.347  1.00 32.03           C  
ANISOU 5310  CB  ILE B 308     5383   3237   3550    500    374   -259       C  
ATOM   5311  CG1 ILE B 308     -24.560 -63.654 -57.894  1.00 33.51           C  
ANISOU 5311  CG1 ILE B 308     5667   3352   3714    329    351   -307       C  
ATOM   5312  CG2 ILE B 308     -22.401 -62.369 -58.261  1.00 28.48           C  
ANISOU 5312  CG2 ILE B 308     4800   2927   3093    530    385   -258       C  
ATOM   5313  CD1 ILE B 308     -24.576 -64.469 -59.200  1.00 30.65           C  
ANISOU 5313  CD1 ILE B 308     5450   2926   3269    326    389   -375       C  
ATOM   5314  N   GLU B 309     -19.911 -64.719 -57.095  1.00 32.22           N  
ANISOU 5314  N   GLU B 309     5452   3315   3476   1006    488   -275       N  
ATOM   5315  CA  GLU B 309     -18.623 -64.690 -56.397  1.00 40.79           C  
ANISOU 5315  CA  GLU B 309     6429   4517   4554   1205    498   -266       C  
ATOM   5316  C   GLU B 309     -18.026 -63.285 -56.295  1.00 37.98           C  
ANISOU 5316  C   GLU B 309     5804   4377   4251   1155    485   -251       C  
ATOM   5317  O   GLU B 309     -17.507 -62.914 -55.237  1.00 34.31           O  
ANISOU 5317  O   GLU B 309     5216   4005   3814   1219    460   -226       O  
ATOM   5318  CB  GLU B 309     -17.622 -65.633 -57.072  1.00 35.97           C  
ANISOU 5318  CB  GLU B 309     5906   3909   3851   1414    555   -320       C  
ATOM   5319  CG  GLU B 309     -17.907 -67.115 -56.850  1.00 47.96           C  
ANISOU 5319  CG  GLU B 309     7722   5205   5297   1524    576   -332       C  
ATOM   5320  CD  GLU B 309     -16.806 -68.014 -57.388  1.00 47.15           C  
ANISOU 5320  CD  GLU B 309     7707   5115   5093   1781    629   -385       C  
ATOM   5321  OE1 GLU B 309     -16.517 -69.052 -56.750  1.00 47.17           O  
ANISOU 5321  OE1 GLU B 309     7902   4996   5025   1977    637   -383       O  
ATOM   5322  OE2 GLU B 309     -16.227 -67.683 -58.445  1.00 44.37           O  
ANISOU 5322  OE2 GLU B 309     7243   4892   4723   1796    665   -432       O  
ATOM   5323  N   GLU B 310     -18.061 -62.488 -57.365  1.00 33.05           N  
ANISOU 5323  N   GLU B 310     5099   3830   3627   1039    506   -268       N  
ATOM   5324  CA  GLU B 310     -17.302 -61.239 -57.400  1.00 30.09           C  
ANISOU 5324  CA  GLU B 310     4507   3651   3274    994    521   -267       C  
ATOM   5325  C   GLU B 310     -18.224 -60.032 -57.499  1.00 32.52           C  
ANISOU 5325  C   GLU B 310     4772   3952   3633    788    486   -225       C  
ATOM   5326  O   GLU B 310     -19.125 -59.991 -58.349  1.00 27.49           O  
ANISOU 5326  O   GLU B 310     4234   3228   2981    687    474   -227       O  
ATOM   5327  CB  GLU B 310     -16.292 -61.235 -58.556  1.00 34.35           C  
ANISOU 5327  CB  GLU B 310     4993   4311   3746   1053    597   -328       C  
ATOM   5328  CG  GLU B 310     -15.190 -62.301 -58.398  1.00 41.12           C  
ANISOU 5328  CG  GLU B 310     5855   5225   4543   1297    633   -380       C  
ATOM   5329  CD  GLU B 310     -13.991 -62.064 -59.313  1.00 49.20           C  
ANISOU 5329  CD  GLU B 310     6747   6442   5505   1353    714   -451       C  
ATOM   5330  OE1 GLU B 310     -13.987 -61.057 -60.052  1.00 40.46           O  
ANISOU 5330  OE1 GLU B 310     5562   5412   4399   1186    751   -456       O  
ATOM   5331  OE2 GLU B 310     -13.044 -62.879 -59.284  1.00 61.90           O  
ANISOU 5331  OE2 GLU B 310     8338   8131   7052   1571    744   -507       O  
ATOM   5332  N   TRP B 311     -17.961 -59.041 -56.644  1.00 25.98           N  
ANISOU 5332  N   TRP B 311     3797   3224   2852    739    467   -195       N  
ATOM   5333  CA  TRP B 311     -18.742 -57.820 -56.512  1.00 26.11           C  
ANISOU 5333  CA  TRP B 311     3776   3235   2909    575    431   -151       C  
ATOM   5334  C   TRP B 311     -17.799 -56.626 -56.571  1.00 25.00           C  
ANISOU 5334  C   TRP B 311     3486   3254   2757    514    478   -159       C  
ATOM   5335  O   TRP B 311     -16.581 -56.769 -56.450  1.00 33.43           O  
ANISOU 5335  O   TRP B 311     4443   4461   3800    595    528   -202       O  
ATOM   5336  CB  TRP B 311     -19.528 -57.805 -55.183  1.00 23.98           C  
ANISOU 5336  CB  TRP B 311     3509   2897   2705    553    363   -105       C  
ATOM   5337  CG  TRP B 311     -20.530 -58.913 -55.099  1.00 27.06           C  
ANISOU 5337  CG  TRP B 311     4055   3130   3096    566    332   -105       C  
ATOM   5338  CD1 TRP B 311     -20.271 -60.242 -54.940  1.00 29.68           C  
ANISOU 5338  CD1 TRP B 311     4498   3383   3396    688    350   -127       C  
ATOM   5339  CD2 TRP B 311     -21.951 -58.787 -55.190  1.00 26.75           C  
ANISOU 5339  CD2 TRP B 311     4087   3000   3077    444    283    -94       C  
ATOM   5340  NE1 TRP B 311     -21.446 -60.958 -54.923  1.00 28.25           N  
ANISOU 5340  NE1 TRP B 311     4467   3052   3213    621    327   -130       N  
ATOM   5341  CE2 TRP B 311     -22.492 -60.085 -55.076  1.00 27.95           C  
ANISOU 5341  CE2 TRP B 311     4386   3023   3209    468    284   -116       C  
ATOM   5342  CE3 TRP B 311     -22.821 -57.700 -55.361  1.00 29.02           C  
ANISOU 5342  CE3 TRP B 311     4333   3309   3384    325    241    -74       C  
ATOM   5343  CZ2 TRP B 311     -23.863 -60.332 -55.128  1.00 23.97           C  
ANISOU 5343  CZ2 TRP B 311     3961   2436   2709    348    249   -131       C  
ATOM   5344  CZ3 TRP B 311     -24.187 -57.945 -55.408  1.00 30.57           C  
ANISOU 5344  CZ3 TRP B 311     4597   3435   3585    242    193    -86       C  
ATOM   5345  CH2 TRP B 311     -24.693 -59.258 -55.296  1.00 24.30           C  
ANISOU 5345  CH2 TRP B 311     3922   2537   2776    241    200   -120       C  
ATOM   5346  N   CYS B 312     -18.368 -55.432 -56.731  1.00 29.51           N  
ANISOU 5346  N   CYS B 312     4061   3812   3338    372    465   -126       N  
ATOM   5347  CA  CYS B 312     -17.558 -54.221 -56.738  1.00 29.97           C  
ANISOU 5347  CA  CYS B 312     4016   3995   3376    278    521   -133       C  
ATOM   5348  C   CYS B 312     -18.351 -53.073 -56.126  1.00 29.31           C  
ANISOU 5348  C   CYS B 312     3949   3861   3328    165    475    -78       C  
ATOM   5349  O   CYS B 312     -19.559 -53.174 -55.899  1.00 26.98           O  
ANISOU 5349  O   CYS B 312     3735   3451   3066    162    401    -40       O  
ATOM   5350  CB  CYS B 312     -17.071 -53.863 -58.162  1.00 29.69           C  
ANISOU 5350  CB  CYS B 312     4021   4001   3257    219    604   -168       C  
ATOM   5351  SG  CYS B 312     -18.391 -53.542 -59.437  1.00 33.99           S  
ANISOU 5351  SG  CYS B 312     4768   4391   3755    149    571   -135       S  
ATOM   5352  N   CYS B 313     -17.646 -51.968 -55.861  1.00 26.90           N  
ANISOU 5352  N   CYS B 313     3565   3651   3005     66    525    -84       N  
ATOM   5353  CA  CYS B 313     -18.266 -50.697 -55.508  1.00 23.23           C  
ANISOU 5353  CA  CYS B 313     3151   3130   2545    -49    504    -37       C  
ATOM   5354  C   CYS B 313     -17.350 -49.580 -55.990  1.00 28.75           C  
ANISOU 5354  C   CYS B 313     3839   3913   3171   -187    606    -63       C  
ATOM   5355  O   CYS B 313     -16.131 -49.752 -56.072  1.00 26.86           O  
ANISOU 5355  O   CYS B 313     3478   3823   2905   -200    683   -125       O  
ATOM   5356  CB  CYS B 313     -18.527 -50.558 -54.000  1.00 29.00           C  
ANISOU 5356  CB  CYS B 313     3805   3865   3350    -36    442     -9       C  
ATOM   5357  SG  CYS B 313     -17.015 -50.432 -52.998  1.00 32.25           S  
ANISOU 5357  SG  CYS B 313     4014   4471   3768    -44    492    -60       S  
ATOM   5358  N   ARG B 314     -17.950 -48.435 -56.334  1.00 27.78           N  
ANISOU 5358  N   ARG B 314     3856   3696   3004   -288    611    -23       N  
ATOM   5359  CA  ARG B 314     -17.165 -47.351 -56.919  1.00 30.30           C  
ANISOU 5359  CA  ARG B 314     4225   4057   3232   -442    725    -46       C  
ATOM   5360  C   ARG B 314     -16.211 -46.733 -55.907  1.00 35.54           C  
ANISOU 5360  C   ARG B 314     4750   4848   3907   -550    778    -83       C  
ATOM   5361  O   ARG B 314     -15.053 -46.452 -56.232  1.00 34.50           O  
ANISOU 5361  O   ARG B 314     4542   4852   3716   -659    890   -149       O  
ATOM   5362  CB  ARG B 314     -18.089 -46.278 -57.498  1.00 37.59           C  
ANISOU 5362  CB  ARG B 314     5375   4822   4084   -500    713     12       C  
ATOM   5363  CG  ARG B 314     -18.643 -46.631 -58.867  1.00 38.85           C  
ANISOU 5363  CG  ARG B 314     5680   4903   4179   -440    703     22       C  
ATOM   5364  CD  ARG B 314     -19.646 -45.589 -59.379  1.00 38.31           C  
ANISOU 5364  CD  ARG B 314     5844   4686   4027   -452    669     80       C  
ATOM   5365  NE  ARG B 314     -20.237 -46.005 -60.651  1.00 46.88           N  
ANISOU 5365  NE  ARG B 314     7054   5713   5045   -375    640     85       N  
ATOM   5366  CZ  ARG B 314     -21.193 -45.337 -61.294  1.00 57.24           C  
ANISOU 5366  CZ  ARG B 314     8568   6913   6268   -333    590    127       C  
ATOM   5367  NH1 ARG B 314     -21.682 -44.210 -60.794  1.00 56.21           N  
ANISOU 5367  NH1 ARG B 314     8552   6700   6103   -349    566    172       N  
ATOM   5368  NH2 ARG B 314     -21.663 -45.793 -62.446  1.00 55.00           N  
ANISOU 5368  NH2 ARG B 314     8378   6601   5919   -261    560    120       N  
ATOM   5369  N   GLU B 315     -16.672 -46.501 -54.684  1.00 29.67           N  
ANISOU 5369  N   GLU B 315     3965   4076   3232   -532    705    -50       N  
ATOM   5370  CA  GLU B 315     -15.791 -45.869 -53.715  1.00 33.37           C  
ANISOU 5370  CA  GLU B 315     4306   4671   3703   -643    752    -90       C  
ATOM   5371  C   GLU B 315     -16.229 -46.172 -52.291  1.00 28.02           C  
ANISOU 5371  C   GLU B 315     3536   3992   3119   -556    650    -63       C  
ATOM   5372  O   GLU B 315     -16.088 -45.330 -51.401  1.00 37.97           O  
ANISOU 5372  O   GLU B 315     4773   5272   4382   -653    656    -63       O  
ATOM   5373  CB  GLU B 315     -15.730 -44.360 -53.959  1.00 45.09           C  
ANISOU 5373  CB  GLU B 315     5946   6086   5099   -841    835    -82       C  
ATOM   5374  CG  GLU B 315     -17.081 -43.697 -54.100  1.00 57.96           C  
ANISOU 5374  CG  GLU B 315     7805   7499   6716   -811    770      5       C  
ATOM   5375  CD  GLU B 315     -16.969 -42.206 -54.366  1.00 73.42           C  
ANISOU 5375  CD  GLU B 315     9964   9366   8565   -989    861     15       C  
ATOM   5376  OE1 GLU B 315     -15.899 -41.762 -54.842  1.00 63.95           O  
ANISOU 5376  OE1 GLU B 315     8762   8251   7284  -1159    994    -45       O  
ATOM   5377  OE2 GLU B 315     -17.951 -41.479 -54.091  1.00 83.85           O  
ANISOU 5377  OE2 GLU B 315    11454  10531   9873   -960    805     78       O  
ATOM   5378  N   CYS B 316     -16.757 -47.367 -52.057  1.00 24.72           N  
ANISOU 5378  N   CYS B 316     3080   3544   2769   -384    563    -41       N  
ATOM   5379  CA  CYS B 316     -17.120 -47.727 -50.695  1.00 28.97           C  
ANISOU 5379  CA  CYS B 316     3542   4082   3385   -305    478    -17       C  
ATOM   5380  C   CYS B 316     -15.866 -48.194 -49.951  1.00 30.95           C  
ANISOU 5380  C   CYS B 316     3588   4531   3639   -266    497    -82       C  
ATOM   5381  O   CYS B 316     -14.764 -48.245 -50.515  1.00 31.47           O  
ANISOU 5381  O   CYS B 316     3558   4749   3651   -300    576   -153       O  
ATOM   5382  CB  CYS B 316     -18.234 -48.780 -50.699  1.00 28.88           C  
ANISOU 5382  CB  CYS B 316     3598   3948   3428   -163    389     28       C  
ATOM   5383  SG  CYS B 316     -17.719 -50.481 -51.079  1.00 34.82           S  
ANISOU 5383  SG  CYS B 316     4291   4753   4186      4    386    -10       S  
ATOM   5384  N   THR B 317     -16.015 -48.516 -48.661  1.00 27.70           N  
ANISOU 5384  N   THR B 317     3105   4139   3282   -191    425    -66       N  
ATOM   5385  CA  THR B 317     -14.893 -48.958 -47.836  1.00 30.78           C  
ANISOU 5385  CA  THR B 317     3304   4727   3665   -122    423   -128       C  
ATOM   5386  C   THR B 317     -15.093 -50.390 -47.351  1.00 32.17           C  
ANISOU 5386  C   THR B 317     3473   4876   3875     98    348   -108       C  
ATOM   5387  O   THR B 317     -16.224 -50.837 -47.118  1.00 28.04           O  
ANISOU 5387  O   THR B 317     3077   4178   3399    152    288    -41       O  
ATOM   5388  CB  THR B 317     -14.685 -48.057 -46.610  1.00 29.35           C  
ANISOU 5388  CB  THR B 317     3046   4614   3491   -220    408   -136       C  
ATOM   5389  OG1 THR B 317     -15.854 -48.103 -45.784  1.00 33.34           O  
ANISOU 5389  OG1 THR B 317     3653   4958   4059   -175    326    -57       O  
ATOM   5390  CG2 THR B 317     -14.395 -46.618 -47.031  1.00 32.06           C  
ANISOU 5390  CG2 THR B 317     3425   4973   3782   -454    497   -163       C  
ATOM   5391  N   MET B 318     -13.972 -51.093 -47.174  1.00 29.42           N  
ANISOU 5391  N   MET B 318     2978   4710   3489    223    356   -175       N  
ATOM   5392  CA  MET B 318     -13.956 -52.449 -46.614  1.00 27.05           C  
ANISOU 5392  CA  MET B 318     2689   4394   3194    454    291   -164       C  
ATOM   5393  C   MET B 318     -13.785 -52.401 -45.087  1.00 33.74           C  
ANISOU 5393  C   MET B 318     3457   5310   4052    512    225   -157       C  
ATOM   5394  O   MET B 318     -13.136 -51.492 -44.569  1.00 31.16           O  
ANISOU 5394  O   MET B 318     2985   5145   3707    405    240   -204       O  
ATOM   5395  CB  MET B 318     -12.825 -53.282 -47.236  1.00 28.31           C  
ANISOU 5395  CB  MET B 318     2749   4718   3289    607    328   -243       C  
ATOM   5396  CG  MET B 318     -12.866 -53.390 -48.774  1.00 33.11           C  
ANISOU 5396  CG  MET B 318     3429   5277   3874    560    400   -259       C  
ATOM   5397  SD  MET B 318     -14.340 -54.252 -49.361  1.00 37.15           S  
ANISOU 5397  SD  MET B 318     4205   5483   4428    610    362   -172       S  
ATOM   5398  CE  MET B 318     -15.393 -52.895 -49.843  1.00 38.81           C  
ANISOU 5398  CE  MET B 318     4511   5561   4675    362    379   -119       C  
ATOM   5399  N   PRO B 319     -14.355 -53.383 -44.361  1.00 34.90           N  
ANISOU 5399  N   PRO B 319     3709   5334   4217    670    157   -104       N  
ATOM   5400  CA  PRO B 319     -15.181 -54.486 -44.877  1.00 33.18           C  
ANISOU 5400  CA  PRO B 319     3682   4913   4011    768    146    -56       C  
ATOM   5401  C   PRO B 319     -16.550 -53.986 -45.355  1.00 33.42           C  
ANISOU 5401  C   PRO B 319     3852   4746   4099    603    151      4       C  
ATOM   5402  O   PRO B 319     -17.012 -52.941 -44.882  1.00 29.97           O  
ANISOU 5402  O   PRO B 319     3395   4295   3698    463    140     29       O  
ATOM   5403  CB  PRO B 319     -15.302 -55.433 -43.677  1.00 33.67           C  
ANISOU 5403  CB  PRO B 319     3813   4920   4058    945     81    -23       C  
ATOM   5404  CG  PRO B 319     -15.059 -54.575 -42.485  1.00 38.72           C  
ANISOU 5404  CG  PRO B 319     4330   5671   4709    884     45    -24       C  
ATOM   5405  CD  PRO B 319     -14.097 -53.508 -42.911  1.00 34.59           C  
ANISOU 5405  CD  PRO B 319     3608   5367   4168    762     92    -99       C  
ATOM   5406  N   PRO B 320     -17.168 -54.708 -46.288  1.00 28.38           N  
ANISOU 5406  N   PRO B 320     3351   3971   3461    628    165     18       N  
ATOM   5407  CA  PRO B 320     -18.363 -54.187 -46.967  1.00 28.29           C  
ANISOU 5407  CA  PRO B 320     3442   3821   3485    482    169     54       C  
ATOM   5408  C   PRO B 320     -19.632 -54.271 -46.122  1.00 30.39           C  
ANISOU 5408  C   PRO B 320     3802   3948   3798    444    117    107       C  
ATOM   5409  O   PRO B 320     -19.814 -55.176 -45.303  1.00 26.15           O  
ANISOU 5409  O   PRO B 320     3326   3350   3259    537     90    125       O  
ATOM   5410  CB  PRO B 320     -18.470 -55.084 -48.210  1.00 29.72           C  
ANISOU 5410  CB  PRO B 320     3724   3933   3636    538    199     34       C  
ATOM   5411  CG  PRO B 320     -17.871 -56.400 -47.754  1.00 25.57           C  
ANISOU 5411  CG  PRO B 320     3231   3411   3075    732    190     18       C  
ATOM   5412  CD  PRO B 320     -16.729 -56.008 -46.834  1.00 28.93           C  
ANISOU 5412  CD  PRO B 320     3486   4022   3482    799    180     -9       C  
ATOM   5413  N   LEU B 321     -20.540 -53.322 -46.367  1.00 25.76           N  
ANISOU 5413  N   LEU B 321     3238   3309   3240    309    109    130       N  
ATOM   5414  CA  LEU B 321     -21.847 -53.328 -45.708  1.00 24.90           C  
ANISOU 5414  CA  LEU B 321     3200   3092   3171    262     66    166       C  
ATOM   5415  C   LEU B 321     -22.704 -54.478 -46.237  1.00 29.27           C  
ANISOU 5415  C   LEU B 321     3879   3526   3717    284     62    160       C  
ATOM   5416  O   LEU B 321     -22.953 -54.578 -47.445  1.00 24.15           O  
ANISOU 5416  O   LEU B 321     3275   2852   3047    259     79    139       O  
ATOM   5417  CB  LEU B 321     -22.557 -51.986 -45.933  1.00 24.76           C  
ANISOU 5417  CB  LEU B 321     3173   3067   3168    143     55    180       C  
ATOM   5418  CG  LEU B 321     -23.786 -51.605 -45.084  1.00 30.19           C  
ANISOU 5418  CG  LEU B 321     3885   3694   3890     93     11    208       C  
ATOM   5419  CD1 LEU B 321     -24.097 -50.107 -45.233  1.00 29.84           C  
ANISOU 5419  CD1 LEU B 321     3831   3667   3841     14      6    219       C  
ATOM   5420  CD2 LEU B 321     -25.008 -52.399 -45.490  1.00 28.91           C  
ANISOU 5420  CD2 LEU B 321     3805   3446   3732     84     -9    198       C  
ATOM   5421  N   SER B 322     -23.178 -55.334 -45.335  1.00 24.87           N  
ANISOU 5421  N   SER B 322     3392   2892   3166    317     47    175       N  
ATOM   5422  CA  SER B 322     -24.054 -56.436 -45.701  1.00 23.78           C  
ANISOU 5422  CA  SER B 322     3391   2632   3011    302     55    161       C  
ATOM   5423  C   SER B 322     -25.237 -56.485 -44.737  1.00 27.67           C  
ANISOU 5423  C   SER B 322     3921   3062   3529    218     35    175       C  
ATOM   5424  O   SER B 322     -25.164 -55.991 -43.607  1.00 28.51           O  
ANISOU 5424  O   SER B 322     3974   3199   3658    219     16    204       O  
ATOM   5425  CB  SER B 322     -23.296 -57.785 -45.688  1.00 28.76           C  
ANISOU 5425  CB  SER B 322     4127   3207   3592    436     84    151       C  
ATOM   5426  OG  SER B 322     -23.014 -58.167 -44.350  1.00 28.75           O  
ANISOU 5426  OG  SER B 322     4156   3186   3582    512     72    180       O  
ATOM   5427  N   PHE B 323     -26.334 -57.073 -45.210  1.00 25.58           N  
ANISOU 5427  N   PHE B 323     3743   2723   3254    135     43    144       N  
ATOM   5428  CA  PHE B 323     -27.523 -57.335 -44.408  1.00 23.48           C  
ANISOU 5428  CA  PHE B 323     3518   2406   2996     35     41    137       C  
ATOM   5429  C   PHE B 323     -27.722 -58.844 -44.345  1.00 30.12           C  
ANISOU 5429  C   PHE B 323     4543   3115   3787     27     88    116       C  
ATOM   5430  O   PHE B 323     -27.731 -59.508 -45.383  1.00 31.37           O  
ANISOU 5430  O   PHE B 323     4781   3227   3910     23    111     79       O  
ATOM   5431  CB  PHE B 323     -28.787 -56.690 -45.012  1.00 23.16           C  
ANISOU 5431  CB  PHE B 323     3412   2419   2970    -82     13     96       C  
ATOM   5432  CG  PHE B 323     -28.642 -55.235 -45.395  1.00 28.91           C  
ANISOU 5432  CG  PHE B 323     4015   3247   3722    -63    -28    112       C  
ATOM   5433  CD1 PHE B 323     -28.202 -54.877 -46.672  1.00 26.98           C  
ANISOU 5433  CD1 PHE B 323     3761   3034   3456    -31    -31    102       C  
ATOM   5434  CD2 PHE B 323     -28.991 -54.226 -44.501  1.00 26.19           C  
ANISOU 5434  CD2 PHE B 323     3589   2953   3408    -82    -57    135       C  
ATOM   5435  CE1 PHE B 323     -28.097 -53.539 -47.048  1.00 26.53           C  
ANISOU 5435  CE1 PHE B 323     3635   3044   3401    -23    -57    118       C  
ATOM   5436  CE2 PHE B 323     -28.878 -52.884 -44.869  1.00 30.55           C  
ANISOU 5436  CE2 PHE B 323     4070   3571   3965    -65    -86    150       C  
ATOM   5437  CZ  PHE B 323     -28.435 -52.545 -46.157  1.00 25.78           C  
ANISOU 5437  CZ  PHE B 323     3479   2984   3332    -39    -84    143       C  
ATOM   5438  N   ARG B 324     -27.890 -59.385 -43.142  1.00 26.92           N  
ANISOU 5438  N   ARG B 324     4227   2636   3366     21    109    138       N  
ATOM   5439  CA  ARG B 324     -28.109 -60.812 -42.959  1.00 28.80           C  
ANISOU 5439  CA  ARG B 324     4687   2719   3538      3    167    123       C  
ATOM   5440  C   ARG B 324     -29.583 -61.027 -42.650  1.00 31.88           C  
ANISOU 5440  C   ARG B 324     5113   3079   3923   -200    195     76       C  
ATOM   5441  O   ARG B 324     -30.101 -60.479 -41.668  1.00 31.76           O  
ANISOU 5441  O   ARG B 324     5025   3109   3936   -260    184     90       O  
ATOM   5442  CB  ARG B 324     -27.221 -61.387 -41.846  1.00 30.31           C  
ANISOU 5442  CB  ARG B 324     4996   2833   3685    148    180    177       C  
ATOM   5443  CG  ARG B 324     -25.720 -61.054 -41.976  1.00 30.89           C  
ANISOU 5443  CG  ARG B 324     4981   2995   3760    356    144    209       C  
ATOM   5444  CD  ARG B 324     -25.165 -61.453 -43.351  1.00 34.69           C  
ANISOU 5444  CD  ARG B 324     5487   3477   4219    424    159    175       C  
ATOM   5445  NE  ARG B 324     -23.856 -60.862 -43.672  1.00 30.96           N  
ANISOU 5445  NE  ARG B 324     4863   3143   3757    574    130    183       N  
ATOM   5446  CZ  ARG B 324     -22.715 -61.546 -43.721  1.00 29.39           C  
ANISOU 5446  CZ  ARG B 324     4724   2945   3498    771    138    183       C  
ATOM   5447  NH1 ARG B 324     -22.705 -62.844 -43.450  1.00 32.49           N  
ANISOU 5447  NH1 ARG B 324     5357   3179   3810    862    172    187       N  
ATOM   5448  NH2 ARG B 324     -21.586 -60.936 -44.047  1.00 29.48           N  
ANISOU 5448  NH2 ARG B 324     4564   3120   3517    876    118    172       N  
ATOM   5449  N   ALA B 325     -30.257 -61.808 -43.496  1.00 28.93           N  
ANISOU 5449  N   ALA B 325     4839   2645   3506   -313    235     10       N  
ATOM   5450  CA  ALA B 325     -31.681 -62.081 -43.366  1.00 31.76           C  
ANISOU 5450  CA  ALA B 325     5212   3008   3846   -532    270    -63       C  
ATOM   5451  C   ALA B 325     -31.924 -63.584 -43.420  1.00 35.46           C  
ANISOU 5451  C   ALA B 325     5954   3294   4224   -625    361   -103       C  
ATOM   5452  O   ALA B 325     -31.018 -64.380 -43.691  1.00 36.64           O  
ANISOU 5452  O   ALA B 325     6285   3312   4325   -498    389    -73       O  
ATOM   5453  CB  ALA B 325     -32.489 -61.370 -44.466  1.00 29.97           C  
ANISOU 5453  CB  ALA B 325     4806   2934   3648   -618    222   -133       C  
ATOM   5454  N   LYS B 326     -33.178 -63.969 -43.171  1.00 35.61           N  
ANISOU 5454  N   LYS B 326     6008   3312   4210   -855    413   -179       N  
ATOM   5455  CA  LYS B 326     -33.527 -65.385 -43.151  1.00 38.55           C  
ANISOU 5455  CA  LYS B 326     6667   3499   4481   -993    519   -228       C  
ATOM   5456  C   LYS B 326     -33.272 -66.051 -44.494  1.00 36.42           C  
ANISOU 5456  C   LYS B 326     6502   3167   4168   -982    533   -276       C  
ATOM   5457  O   LYS B 326     -32.966 -67.248 -44.538  1.00 34.34           O  
ANISOU 5457  O   LYS B 326     6534   2698   3814   -984    612   -279       O  
ATOM   5458  CB  LYS B 326     -34.990 -65.571 -42.752  1.00 48.70           C  
ANISOU 5458  CB  LYS B 326     7928   4839   5736  -1282    579   -327       C  
ATOM   5459  CG  LYS B 326     -35.262 -65.349 -41.271  1.00 73.93           C  
ANISOU 5459  CG  LYS B 326    11129   8025   8936  -1324    609   -287       C  
ATOM   5460  CD  LYS B 326     -36.754 -65.227 -40.980  1.00 82.50           C  
ANISOU 5460  CD  LYS B 326    12094   9245  10007  -1603    653   -400       C  
ATOM   5461  CE  LYS B 326     -37.018 -65.224 -39.480  1.00 81.86           C  
ANISOU 5461  CE  LYS B 326    12075   9119   9907  -1666    710   -364       C  
ATOM   5462  NZ  LYS B 326     -38.441 -64.916 -39.165  1.00 77.23           N  
ANISOU 5462  NZ  LYS B 326    11312   8715   9316  -1918    746   -481       N  
ATOM   5463  N   ASP B 327     -33.393 -65.308 -45.594  1.00 33.32           N  
ANISOU 5463  N   ASP B 327     5896   2937   3826   -962    459   -312       N  
ATOM   5464  CA  ASP B 327     -33.207 -65.897 -46.915  1.00 35.85           C  
ANISOU 5464  CA  ASP B 327     6307   3213   4102   -960    470   -363       C  
ATOM   5465  C   ASP B 327     -31.794 -65.706 -47.440  1.00 38.90           C  
ANISOU 5465  C   ASP B 327     6699   3571   4510   -697    430   -285       C  
ATOM   5466  O   ASP B 327     -31.508 -66.090 -48.577  1.00 35.85           O  
ANISOU 5466  O   ASP B 327     6372   3158   4090   -666    435   -320       O  
ATOM   5467  CB  ASP B 327     -34.237 -65.335 -47.913  1.00 36.34           C  
ANISOU 5467  CB  ASP B 327     6161   3469   4178  -1103    420   -465       C  
ATOM   5468  CG  ASP B 327     -33.950 -63.887 -48.339  1.00 44.14           C  
ANISOU 5468  CG  ASP B 327     6876   4647   5250   -954    309   -421       C  
ATOM   5469  OD1 ASP B 327     -33.361 -63.116 -47.549  1.00 35.71           O  
ANISOU 5469  OD1 ASP B 327     5719   3604   4243   -821    274   -331       O  
ATOM   5470  OD2 ASP B 327     -34.342 -63.529 -49.480  1.00 36.23           O  
ANISOU 5470  OD2 ASP B 327     5764   3763   4239   -978    259   -482       O  
ATOM   5471  N   GLY B 328     -30.901 -65.141 -46.636  1.00 32.91           N  
ANISOU 5471  N   GLY B 328     5877   2829   3798   -516    395   -189       N  
ATOM   5472  CA  GLY B 328     -29.507 -65.095 -47.010  1.00 34.91           C  
ANISOU 5472  CA  GLY B 328     6143   3067   4056   -276    373   -129       C  
ATOM   5473  C   GLY B 328     -28.853 -63.756 -46.765  1.00 33.66           C  
ANISOU 5473  C   GLY B 328     5735   3072   3982   -149    296    -67       C  
ATOM   5474  O   GLY B 328     -29.268 -63.000 -45.879  1.00 31.76           O  
ANISOU 5474  O   GLY B 328     5369   2907   3791   -198    266    -42       O  
ATOM   5475  N   CYS B 329     -27.837 -63.448 -47.566  1.00 32.77           N  
ANISOU 5475  N   CYS B 329     5556   3017   3879      2    271    -50       N  
ATOM   5476  CA  CYS B 329     -26.970 -62.298 -47.348  1.00 30.73           C  
ANISOU 5476  CA  CYS B 329     5098   2899   3680    125    219      3       C  
ATOM   5477  C   CYS B 329     -27.165 -61.310 -48.485  1.00 31.98           C  
ANISOU 5477  C   CYS B 329     5093   3186   3873     77    180    -22       C  
ATOM   5478  O   CYS B 329     -27.119 -61.693 -49.661  1.00 31.23           O  
ANISOU 5478  O   CYS B 329     5050   3073   3741     75    196    -63       O  
ATOM   5479  CB  CYS B 329     -25.502 -62.731 -47.259  1.00 34.57           C  
ANISOU 5479  CB  CYS B 329     5636   3367   4131    344    232     36       C  
ATOM   5480  SG  CYS B 329     -24.337 -61.413 -46.805  1.00 37.11           S  
ANISOU 5480  SG  CYS B 329     5713   3878   4510    469    182     84       S  
ATOM   5481  N   TRP B 330     -27.388 -60.047 -48.128  1.00 26.21           N  
ANISOU 5481  N   TRP B 330     4187   2572   3199     45    132      4       N  
ATOM   5482  CA  TRP B 330     -27.629 -58.968 -49.073  1.00 31.87           C  
ANISOU 5482  CA  TRP B 330     4774   3399   3934     11     93    -10       C  
ATOM   5483  C   TRP B 330     -26.529 -57.926 -48.944  1.00 28.49           C  
ANISOU 5483  C   TRP B 330     4228   3062   3536    106     79     38       C  
ATOM   5484  O   TRP B 330     -25.933 -57.765 -47.875  1.00 25.45           O  
ANISOU 5484  O   TRP B 330     3806   2689   3173    163     79     78       O  
ATOM   5485  CB  TRP B 330     -28.971 -58.307 -48.806  1.00 28.18           C  
ANISOU 5485  CB  TRP B 330     4227   2991   3491   -112     51    -33       C  
ATOM   5486  CG  TRP B 330     -30.173 -59.193 -48.934  1.00 25.32           C  
ANISOU 5486  CG  TRP B 330     3942   2584   3094   -246     67   -104       C  
ATOM   5487  CD1 TRP B 330     -30.547 -60.218 -48.104  1.00 28.84           C  
ANISOU 5487  CD1 TRP B 330     4507   2930   3521   -317    115   -119       C  
ATOM   5488  CD2 TRP B 330     -31.198 -59.083 -49.928  1.00 26.12           C  
ANISOU 5488  CD2 TRP B 330     4005   2754   3164   -339     37   -178       C  
ATOM   5489  NE1 TRP B 330     -31.730 -60.773 -48.549  1.00 25.84           N  
ANISOU 5489  NE1 TRP B 330     4162   2553   3101   -475    128   -206       N  
ATOM   5490  CE2 TRP B 330     -32.153 -60.084 -49.658  1.00 28.60           C  
ANISOU 5490  CE2 TRP B 330     4401   3022   3445   -484     73   -247       C  
ATOM   5491  CE3 TRP B 330     -31.394 -58.234 -51.026  1.00 27.70           C  
ANISOU 5491  CE3 TRP B 330     4122   3055   3348   -312    -16   -196       C  
ATOM   5492  CZ2 TRP B 330     -33.293 -60.262 -50.446  1.00 27.26           C  
ANISOU 5492  CZ2 TRP B 330     4198   2931   3230   -610     53   -346       C  
ATOM   5493  CZ3 TRP B 330     -32.528 -58.412 -51.816  1.00 26.15           C  
ANISOU 5493  CZ3 TRP B 330     3905   2928   3105   -408    -46   -285       C  
ATOM   5494  CH2 TRP B 330     -33.464 -59.418 -51.518  1.00 31.43           C  
ANISOU 5494  CH2 TRP B 330     4622   3576   3745   -558    -14   -365       C  
ATOM   5495  N   TYR B 331     -26.284 -57.182 -50.016  1.00 25.75           N  
ANISOU 5495  N   TYR B 331     3825   2782   3178    110     70     30       N  
ATOM   5496  CA  TYR B 331     -25.214 -56.194 -49.998  1.00 27.20           C  
ANISOU 5496  CA  TYR B 331     3910   3051   3373    165     76     63       C  
ATOM   5497  C   TYR B 331     -25.761 -54.773 -49.941  1.00 29.06           C  
ANISOU 5497  C   TYR B 331     4068   3347   3628    100     38     82       C  
ATOM   5498  O   TYR B 331     -26.877 -54.503 -50.388  1.00 26.22           O  
ANISOU 5498  O   TYR B 331     3722   2984   3257     43      2     61       O  
ATOM   5499  CB  TYR B 331     -24.306 -56.359 -51.221  1.00 21.82           C  
ANISOU 5499  CB  TYR B 331     3247   2397   2648    219    116     40       C  
ATOM   5500  CG  TYR B 331     -23.096 -57.209 -50.922  1.00 25.26           C  
ANISOU 5500  CG  TYR B 331     3695   2837   3067    340    157     37       C  
ATOM   5501  CD1 TYR B 331     -22.271 -56.915 -49.831  1.00 26.37           C  
ANISOU 5501  CD1 TYR B 331     3747   3045   3229    402    155     62       C  
ATOM   5502  CD2 TYR B 331     -22.771 -58.295 -51.712  1.00 25.08           C  
ANISOU 5502  CD2 TYR B 331     3773   2761   2995    408    192      1       C  
ATOM   5503  CE1 TYR B 331     -21.148 -57.689 -49.548  1.00 28.22           C  
ANISOU 5503  CE1 TYR B 331     3980   3311   3432    546    181     49       C  
ATOM   5504  CE2 TYR B 331     -21.651 -59.085 -51.435  1.00 30.94           C  
ANISOU 5504  CE2 TYR B 331     4533   3516   3708    557    225     -7       C  
ATOM   5505  CZ  TYR B 331     -20.850 -58.775 -50.353  1.00 26.80           C  
ANISOU 5505  CZ  TYR B 331     3906   3076   3200    634    215     15       C  
ATOM   5506  OH  TYR B 331     -19.739 -59.539 -50.089  1.00 29.36           O  
ANISOU 5506  OH  TYR B 331     4236   3440   3480    810    236     -2       O  
ATOM   5507  N   GLY B 332     -24.963 -53.859 -49.377  1.00 23.26           N  
ANISOU 5507  N   GLY B 332     3254   2673   2911    115     46    114       N  
ATOM   5508  CA  GLY B 332     -25.287 -52.439 -49.435  1.00 22.87           C  
ANISOU 5508  CA  GLY B 332     3168   2660   2860     64     25    133       C  
ATOM   5509  C   GLY B 332     -25.562 -51.951 -50.849  1.00 30.55           C  
ANISOU 5509  C   GLY B 332     4195   3634   3778     46     25    118       C  
ATOM   5510  O   GLY B 332     -25.132 -52.587 -51.821  1.00 26.27           O  
ANISOU 5510  O   GLY B 332     3694   3086   3202     69     56     93       O  
ATOM   5511  N   MET B 333     -26.292 -50.832 -50.975  1.00 26.37           N  
ANISOU 5511  N   MET B 333     3681   3109   3229     20    -11    131       N  
ATOM   5512  CA  MET B 333     -26.655 -50.295 -52.292  1.00 22.32           C  
ANISOU 5512  CA  MET B 333     3244   2591   2644     24    -21    120       C  
ATOM   5513  C   MET B 333     -25.436 -50.034 -53.173  1.00 28.32           C  
ANISOU 5513  C   MET B 333     4041   3361   3357     14     50    124       C  
ATOM   5514  O   MET B 333     -25.532 -50.116 -54.405  1.00 27.09           O  
ANISOU 5514  O   MET B 333     3959   3195   3138     24     57    106       O  
ATOM   5515  CB  MET B 333     -27.446 -48.994 -52.121  1.00 23.79           C  
ANISOU 5515  CB  MET B 333     3461   2776   2801     29    -67    142       C  
ATOM   5516  CG  MET B 333     -28.777 -49.155 -51.397  1.00 23.45           C  
ANISOU 5516  CG  MET B 333     3368   2753   2789     43   -138    123       C  
ATOM   5517  SD  MET B 333     -29.638 -47.573 -51.234  1.00 24.18           S  
ANISOU 5517  SD  MET B 333     3506   2853   2829     93   -193    143       S  
ATOM   5518  CE  MET B 333     -29.886 -47.088 -52.958  1.00 20.99           C  
ANISOU 5518  CE  MET B 333     3231   2441   2304    153   -214    132       C  
ATOM   5519  N   GLU B 334     -24.294 -49.695 -52.563  1.00 23.92           N  
ANISOU 5519  N   GLU B 334     3428   2840   2819    -12    105    138       N  
ATOM   5520  CA  GLU B 334     -23.073 -49.361 -53.294  1.00 24.32           C  
ANISOU 5520  CA  GLU B 334     3488   2931   2820    -46    187    127       C  
ATOM   5521  C   GLU B 334     -22.455 -50.550 -54.022  1.00 23.73           C  
ANISOU 5521  C   GLU B 334     3399   2882   2735      0    224     89       C  
ATOM   5522  O   GLU B 334     -21.627 -50.356 -54.927  1.00 26.42           O  
ANISOU 5522  O   GLU B 334     3761   3261   3019    -25    293     69       O  
ATOM   5523  CB  GLU B 334     -22.031 -48.810 -52.314  1.00 21.16           C  
ANISOU 5523  CB  GLU B 334     2995   2600   2444    -96    233    130       C  
ATOM   5524  CG  GLU B 334     -22.286 -47.383 -51.823  1.00 22.95           C  
ANISOU 5524  CG  GLU B 334     3270   2798   2651   -169    232    161       C  
ATOM   5525  CD  GLU B 334     -23.426 -47.265 -50.818  1.00 25.47           C  
ANISOU 5525  CD  GLU B 334     3584   3071   3023   -133    149    189       C  
ATOM   5526  OE1 GLU B 334     -23.987 -48.284 -50.374  1.00 26.57           O  
ANISOU 5526  OE1 GLU B 334     3671   3205   3217    -73    100    183       O  
ATOM   5527  OE2 GLU B 334     -23.769 -46.127 -50.471  1.00 25.41           O  
ANISOU 5527  OE2 GLU B 334     3636   3026   2992   -169    142    213       O  
ATOM   5528  N   ILE B 335     -22.830 -51.763 -53.643  1.00 24.48           N  
ANISOU 5528  N   ILE B 335     3475   2953   2875     63    189     76       N  
ATOM   5529  CA  ILE B 335     -22.076 -52.973 -53.945  1.00 26.55           C  
ANISOU 5529  CA  ILE B 335     3724   3233   3131    132    227     41       C  
ATOM   5530  C   ILE B 335     -22.874 -53.770 -54.971  1.00 23.42           C  
ANISOU 5530  C   ILE B 335     3430   2767   2702    148    206     16       C  
ATOM   5531  O   ILE B 335     -23.973 -54.257 -54.673  1.00 25.79           O  
ANISOU 5531  O   ILE B 335     3766   3007   3025    140    151     13       O  
ATOM   5532  CB  ILE B 335     -21.793 -53.765 -52.658  1.00 25.78           C  
ANISOU 5532  CB  ILE B 335     3565   3143   3088    197    211     46       C  
ATOM   5533  CG1 ILE B 335     -20.912 -52.902 -51.736  1.00 24.07           C  
ANISOU 5533  CG1 ILE B 335     3233   3023   2890    175    231     58       C  
ATOM   5534  CG2 ILE B 335     -21.138 -55.118 -52.959  1.00 21.43           C  
ANISOU 5534  CG2 ILE B 335     3041   2587   2516    304    243     10       C  
ATOM   5535  CD1 ILE B 335     -20.908 -53.345 -50.248  1.00 29.97           C  
ANISOU 5535  CD1 ILE B 335     3927   3772   3687    229    193     76       C  
ATOM   5536  N   ARG B 336     -22.339 -53.862 -56.194  1.00 24.12           N  
ANISOU 5536  N   ARG B 336     3562   2873   2728    155    256    -11       N  
ATOM   5537  CA  ARG B 336     -22.994 -54.438 -57.363  1.00 22.42           C  
ANISOU 5537  CA  ARG B 336     3450   2605   2463    159    242    -41       C  
ATOM   5538  C   ARG B 336     -22.167 -55.609 -57.886  1.00 27.87           C  
ANISOU 5538  C   ARG B 336     4166   3296   3129    232    299    -83       C  
ATOM   5539  O   ARG B 336     -20.967 -55.704 -57.601  1.00 27.35           O  
ANISOU 5539  O   ARG B 336     4026   3300   3066    283    356    -91       O  
ATOM   5540  CB  ARG B 336     -23.158 -53.408 -58.498  1.00 24.17           C  
ANISOU 5540  CB  ARG B 336     3737   2838   2609    112    250    -34       C  
ATOM   5541  CG  ARG B 336     -23.439 -51.962 -58.077  1.00 27.86           C  
ANISOU 5541  CG  ARG B 336     4198   3314   3072     61    229     11       C  
ATOM   5542  CD  ARG B 336     -24.645 -51.841 -57.146  1.00 29.31           C  
ANISOU 5542  CD  ARG B 336     4357   3471   3310     62    140     28       C  
ATOM   5543  NE  ARG B 336     -25.912 -52.285 -57.732  1.00 26.58           N  
ANISOU 5543  NE  ARG B 336     4063   3101   2933     76     68     -2       N  
ATOM   5544  CZ  ARG B 336     -26.999 -52.533 -57.005  1.00 33.17           C  
ANISOU 5544  CZ  ARG B 336     4857   3936   3810     70     -1    -14       C  
ATOM   5545  NH1 ARG B 336     -26.936 -52.399 -55.681  1.00 24.58           N  
ANISOU 5545  NH1 ARG B 336     3693   2849   2795     59     -5     13       N  
ATOM   5546  NH2 ARG B 336     -28.130 -52.931 -57.586  1.00 27.37           N  
ANISOU 5546  NH2 ARG B 336     4150   3214   3038     67    -62    -61       N  
ATOM   5547  N   PRO B 337     -22.768 -56.517 -58.660  1.00 27.34           N  
ANISOU 5547  N   PRO B 337     4200   3163   3027    243    286   -120       N  
ATOM   5548  CA  PRO B 337     -21.982 -57.638 -59.190  1.00 31.00           C  
ANISOU 5548  CA  PRO B 337     4713   3612   3455    326    345   -162       C  
ATOM   5549  C   PRO B 337     -20.917 -57.129 -60.155  1.00 29.55           C  
ANISOU 5549  C   PRO B 337     4502   3513   3213    338    418   -178       C  
ATOM   5550  O   PRO B 337     -21.137 -56.180 -60.917  1.00 27.33           O  
ANISOU 5550  O   PRO B 337     4243   3253   2888    265    421   -167       O  
ATOM   5551  CB  PRO B 337     -23.027 -58.519 -59.890  1.00 31.95           C  
ANISOU 5551  CB  PRO B 337     4961   3638   3539    296    313   -203       C  
ATOM   5552  CG  PRO B 337     -24.188 -57.604 -60.168  1.00 34.04           C  
ANISOU 5552  CG  PRO B 337     5221   3916   3795    203    243   -191       C  
ATOM   5553  CD  PRO B 337     -24.190 -56.607 -59.041  1.00 30.49           C  
ANISOU 5553  CD  PRO B 337     4666   3509   3409    183    217   -136       C  
ATOM   5554  N   ARG B 338     -19.745 -57.760 -60.104  1.00 27.20           N  
ANISOU 5554  N   ARG B 338     4163   3271   2902    437    482   -209       N  
ATOM   5555  CA  ARG B 338     -18.608 -57.304 -60.902  1.00 30.04           C  
ANISOU 5555  CA  ARG B 338     4465   3744   3204    440    568   -239       C  
ATOM   5556  C   ARG B 338     -18.661 -57.780 -62.360  1.00 30.61           C  
ANISOU 5556  C   ARG B 338     4654   3781   3195    448    607   -280       C  
ATOM   5557  O   ARG B 338     -18.179 -57.076 -63.257  1.00 30.91           O  
ANISOU 5557  O   ARG B 338     4688   3884   3171    391    668   -293       O  
ATOM   5558  CB  ARG B 338     -17.313 -57.764 -60.217  1.00 32.02           C  
ANISOU 5558  CB  ARG B 338     4592   4109   3464    560    616   -270       C  
ATOM   5559  CG  ARG B 338     -16.060 -57.097 -60.729  1.00 32.61           C  
ANISOU 5559  CG  ARG B 338     4547   4355   3488    535    710   -312       C  
ATOM   5560  CD  ARG B 338     -14.847 -57.678 -60.023  1.00 34.04           C  
ANISOU 5560  CD  ARG B 338     4584   4681   3669    683    742   -361       C  
ATOM   5561  NE  ARG B 338     -13.676 -56.827 -60.178  1.00 36.18           N  
ANISOU 5561  NE  ARG B 338     4685   5160   3901    618    828   -410       N  
ATOM   5562  CZ  ARG B 338     -12.425 -57.251 -60.051  1.00 44.10           C  
ANISOU 5562  CZ  ARG B 338     5538   6352   4866    740    882   -486       C  
ATOM   5563  NH1 ARG B 338     -12.185 -58.528 -59.777  1.00 33.99           N  
ANISOU 5563  NH1 ARG B 338     4283   5056   3577    962    855   -512       N  
ATOM   5564  NH2 ARG B 338     -11.416 -56.402 -60.205  1.00 46.20           N  
ANISOU 5564  NH2 ARG B 338     5635   6827   5090    641    968   -544       N  
ATOM   5565  N   LYS B 339     -19.229 -58.949 -62.633  1.00 32.99           N  
ANISOU 5565  N   LYS B 339     5075   3976   3485    505    580   -306       N  
ATOM   5566  CA  LYS B 339     -19.244 -59.471 -64.001  1.00 42.09           C  
ANISOU 5566  CA  LYS B 339     6343   5095   4554    516    618   -354       C  
ATOM   5567  C   LYS B 339     -20.642 -59.872 -64.446  1.00 45.82           C  
ANISOU 5567  C   LYS B 339     6952   5448   5011    449    546   -361       C  
ATOM   5568  O   LYS B 339     -20.964 -59.853 -65.641  1.00 55.41           O  
ANISOU 5568  O   LYS B 339     8255   6647   6151    412    551   -390       O  
ATOM   5569  CB  LYS B 339     -18.318 -60.695 -64.137  1.00 44.66           C  
ANISOU 5569  CB  LYS B 339     6698   5423   4846    668    681   -408       C  
ATOM   5570  CG  LYS B 339     -17.120 -60.737 -63.198  1.00 57.81           C  
ANISOU 5570  CG  LYS B 339     8217   7207   6542    784    719   -413       C  
ATOM   5571  CD  LYS B 339     -15.872 -60.130 -63.829  1.00 65.12           C  
ANISOU 5571  CD  LYS B 339     9017   8311   7416    792    813   -453       C  
ATOM   5572  CE  LYS B 339     -14.630 -60.499 -63.036  1.00 69.02           C  
ANISOU 5572  CE  LYS B 339     9362   8949   7914    948    850   -491       C  
ATOM   5573  NZ  LYS B 339     -13.472 -59.623 -63.359  1.00 69.84           N  
ANISOU 5573  NZ  LYS B 339     9286   9272   7980    900    938   -535       N  
ATOM   5574  N   GLU B 340     -21.448 -60.263 -63.514  1.00 35.40           N  
ANISOU 5574  N   GLU B 340     5644   4056   3750    430    483   -346       N  
ATOM   5575  CA  GLU B 340     -22.793 -60.774 -63.730  1.00 43.31           C  
ANISOU 5575  CA  GLU B 340     6749   4967   4738    352    418   -372       C  
ATOM   5576  C   GLU B 340     -23.756 -59.623 -64.014  1.00 36.92           C  
ANISOU 5576  C   GLU B 340     5900   4206   3923    253    346   -349       C  
ATOM   5577  O   GLU B 340     -23.668 -58.576 -63.368  1.00 36.76           O  
ANISOU 5577  O   GLU B 340     5781   4241   3947    237    326   -295       O  
ATOM   5578  CB  GLU B 340     -23.266 -61.530 -62.486  1.00 42.11           C  
ANISOU 5578  CB  GLU B 340     6618   4733   4647    352    391   -366       C  
ATOM   5579  CG  GLU B 340     -24.596 -62.218 -62.628  1.00 55.13           C  
ANISOU 5579  CG  GLU B 340     8372   6299   6276    246    345   -414       C  
ATOM   5580  CD  GLU B 340     -24.422 -63.679 -62.962  1.00 54.18           C  
ANISOU 5580  CD  GLU B 340     8427   6057   6101    284    399   -472       C  
ATOM   5581  OE1 GLU B 340     -23.417 -64.252 -62.493  1.00 48.27           O  
ANISOU 5581  OE1 GLU B 340     7714   5269   5358    416    456   -457       O  
ATOM   5582  OE2 GLU B 340     -25.269 -64.236 -63.698  1.00 56.77           O  
ANISOU 5582  OE2 GLU B 340     8862   6337   6372    190    385   -537       O  
ATOM   5583  N   PRO B 341     -24.676 -59.777 -64.972  1.00 35.03           N  
ANISOU 5583  N   PRO B 341     5742   3951   3615    196    302   -394       N  
ATOM   5584  CA  PRO B 341     -25.772 -58.806 -65.090  1.00 34.14           C  
ANISOU 5584  CA  PRO B 341     5594   3891   3488    133    212   -381       C  
ATOM   5585  C   PRO B 341     -26.610 -58.794 -63.819  1.00 34.85           C  
ANISOU 5585  C   PRO B 341     5607   3977   3658     87    152   -369       C  
ATOM   5586  O   PRO B 341     -26.894 -59.844 -63.237  1.00 31.79           O  
ANISOU 5586  O   PRO B 341     5250   3526   3303     58    160   -403       O  
ATOM   5587  CB  PRO B 341     -26.580 -59.317 -66.290  1.00 41.95           C  
ANISOU 5587  CB  PRO B 341     6680   4876   4382     94    175   -456       C  
ATOM   5588  CG  PRO B 341     -25.607 -60.138 -67.084  1.00 40.00           C  
ANISOU 5588  CG  PRO B 341     6529   4582   4088    142    265   -487       C  
ATOM   5589  CD  PRO B 341     -24.704 -60.778 -66.055  1.00 39.39           C  
ANISOU 5589  CD  PRO B 341     6423   4453   4088    201    332   -464       C  
ATOM   5590  N   GLU B 342     -27.005 -57.585 -63.395  1.00 30.47           N  
ANISOU 5590  N   GLU B 342     4972   3481   3124     80     98   -321       N  
ATOM   5591  CA  GLU B 342     -27.881 -57.437 -62.235  1.00 29.19           C  
ANISOU 5591  CA  GLU B 342     4728   3334   3028     38     38   -314       C  
ATOM   5592  C   GLU B 342     -29.247 -58.064 -62.477  1.00 33.88           C  
ANISOU 5592  C   GLU B 342     5333   3951   3587    -39    -28   -396       C  
ATOM   5593  O   GLU B 342     -29.902 -58.508 -61.525  1.00 32.95           O  
ANISOU 5593  O   GLU B 342     5172   3827   3522   -102    -46   -418       O  
ATOM   5594  CB  GLU B 342     -28.048 -55.959 -61.875  1.00 29.15           C  
ANISOU 5594  CB  GLU B 342     4656   3387   3033     60     -5   -253       C  
ATOM   5595  CG  GLU B 342     -26.771 -55.272 -61.411  1.00 26.83           C  
ANISOU 5595  CG  GLU B 342     4333   3085   2778     95     65   -183       C  
ATOM   5596  CD  GLU B 342     -27.017 -53.949 -60.706  1.00 31.73           C  
ANISOU 5596  CD  GLU B 342     4900   3737   3421     96     28   -127       C  
ATOM   5597  OE1 GLU B 342     -28.185 -53.641 -60.359  1.00 28.71           O  
ANISOU 5597  OE1 GLU B 342     4486   3383   3040     89    -55   -139       O  
ATOM   5598  OE2 GLU B 342     -26.031 -53.208 -60.500  1.00 32.86           O  
ANISOU 5598  OE2 GLU B 342     5032   3882   3571    101     87    -80       O  
ATOM   5599  N   SER B 343     -29.695 -58.112 -63.735  1.00 34.54           N  
ANISOU 5599  N   SER B 343     5474   4073   3575    -45    -62   -450       N  
ATOM   5600  CA  SER B 343     -30.995 -58.694 -64.052  1.00 38.55           C  
ANISOU 5600  CA  SER B 343     5976   4638   4034   -131   -128   -550       C  
ATOM   5601  C   SER B 343     -31.085 -60.183 -63.706  1.00 39.76           C  
ANISOU 5601  C   SER B 343     6196   4704   4209   -229    -71   -613       C  
ATOM   5602  O   SER B 343     -32.199 -60.720 -63.644  1.00 42.75           O  
ANISOU 5602  O   SER B 343     6553   5130   4560   -343   -110   -704       O  
ATOM   5603  CB  SER B 343     -31.328 -58.455 -65.544  1.00 33.41           C  
ANISOU 5603  CB  SER B 343     5382   4052   3260   -104   -175   -598       C  
ATOM   5604  OG  SER B 343     -30.345 -59.005 -66.411  1.00 38.07           O  
ANISOU 5604  OG  SER B 343     6093   4562   3811    -77    -96   -596       O  
ATOM   5605  N   ASN B 344     -29.964 -60.861 -63.461  1.00 36.77           N  
ANISOU 5605  N   ASN B 344     5902   4202   3865   -186     22   -576       N  
ATOM   5606  CA  ASN B 344     -30.009 -62.256 -63.031  1.00 44.64           C  
ANISOU 5606  CA  ASN B 344     7008   5084   4869   -258     82   -626       C  
ATOM   5607  C   ASN B 344     -30.174 -62.418 -61.521  1.00 43.82           C  
ANISOU 5607  C   ASN B 344     6864   4938   4849   -293     95   -591       C  
ATOM   5608  O   ASN B 344     -30.265 -63.556 -61.045  1.00 38.82           O  
ANISOU 5608  O   ASN B 344     6349   4190   4211   -357    151   -627       O  
ATOM   5609  CB  ASN B 344     -28.740 -63.006 -63.473  1.00 40.43           C  
ANISOU 5609  CB  ASN B 344     6609   4437   4315   -162    174   -609       C  
ATOM   5610  CG  ASN B 344     -28.632 -63.143 -64.990  1.00 47.40           C  
ANISOU 5610  CG  ASN B 344     7569   5340   5102   -149    178   -661       C  
ATOM   5611  OD1 ASN B 344     -29.622 -63.009 -65.714  1.00 47.39           O  
ANISOU 5611  OD1 ASN B 344     7554   5415   5037   -233    113   -728       O  
ATOM   5612  ND2 ASN B 344     -27.424 -63.416 -65.472  1.00 44.87           N  
ANISOU 5612  ND2 ASN B 344     7321   4966   4761    -38    252   -637       N  
ATOM   5613  N   LEU B 345     -30.227 -61.328 -60.761  1.00 31.83           N  
ANISOU 5613  N   LEU B 345     5206   3495   3394   -256     52   -525       N  
ATOM   5614  CA  LEU B 345     -30.143 -61.403 -59.306  1.00 35.85           C  
ANISOU 5614  CA  LEU B 345     5681   3959   3982   -263     72   -478       C  
ATOM   5615  C   LEU B 345     -31.470 -61.048 -58.648  1.00 34.18           C  
ANISOU 5615  C   LEU B 345     5363   3837   3789   -376     11   -516       C  
ATOM   5616  O   LEU B 345     -32.370 -60.478 -59.266  1.00 31.97           O  
ANISOU 5616  O   LEU B 345     5000   3682   3467   -413    -62   -568       O  
ATOM   5617  CB  LEU B 345     -29.052 -60.469 -58.770  1.00 35.47           C  
ANISOU 5617  CB  LEU B 345     5554   3928   3994   -135     82   -376       C  
ATOM   5618  CG  LEU B 345     -27.608 -60.666 -59.234  1.00 47.76           C  
ANISOU 5618  CG  LEU B 345     7167   5440   5538    -14    147   -341       C  
ATOM   5619  CD1 LEU B 345     -26.658 -60.207 -58.137  1.00 39.74           C  
ANISOU 5619  CD1 LEU B 345     6076   4433   4591     72    170   -264       C  
ATOM   5620  CD2 LEU B 345     -27.330 -62.100 -59.623  1.00 51.52           C  
ANISOU 5620  CD2 LEU B 345     7808   5801   5966     -5    209   -392       C  
ATOM   5621  N   VAL B 346     -31.565 -61.368 -57.353  1.00 26.75           N  
ANISOU 5621  N   VAL B 346     4422   2840   2903   -417     40   -493       N  
ATOM   5622  CA  VAL B 346     -32.713 -60.996 -56.534  1.00 31.64           C  
ANISOU 5622  CA  VAL B 346     4927   3550   3547   -518     -4   -524       C  
ATOM   5623  C   VAL B 346     -32.461 -59.615 -55.937  1.00 33.11           C  
ANISOU 5623  C   VAL B 346     4973   3813   3793   -416    -53   -439       C  
ATOM   5624  O   VAL B 346     -31.415 -59.377 -55.318  1.00 28.42           O  
ANISOU 5624  O   VAL B 346     4392   3155   3251   -322    -20   -352       O  
ATOM   5625  CB  VAL B 346     -32.952 -62.042 -55.429  1.00 34.05           C  
ANISOU 5625  CB  VAL B 346     5327   3744   3867   -627     64   -542       C  
ATOM   5626  CG1 VAL B 346     -34.034 -61.562 -54.456  1.00 30.66           C  
ANISOU 5626  CG1 VAL B 346     4761   3419   3467   -728     30   -568       C  
ATOM   5627  CG2 VAL B 346     -33.325 -63.391 -56.052  1.00 35.19           C  
ANISOU 5627  CG2 VAL B 346     5639   3799   3932   -758    121   -639       C  
ATOM   5628  N   ARG B 347     -33.418 -58.701 -56.110  1.00 29.49           N  
ANISOU 5628  N   ARG B 347     4386   3501   3318   -427   -134   -471       N  
ATOM   5629  CA  ARG B 347     -33.229 -57.320 -55.692  1.00 33.26           C  
ANISOU 5629  CA  ARG B 347     4765   4040   3833   -324   -180   -396       C  
ATOM   5630  C   ARG B 347     -34.321 -56.888 -54.723  1.00 28.09           C  
ANISOU 5630  C   ARG B 347     3986   3484   3202   -377   -224   -426       C  
ATOM   5631  O   ARG B 347     -35.451 -57.381 -54.764  1.00 28.96           O  
ANISOU 5631  O   ARG B 347     4046   3681   3276   -488   -245   -527       O  
ATOM   5632  CB  ARG B 347     -33.209 -56.363 -56.900  1.00 33.87           C  
ANISOU 5632  CB  ARG B 347     4832   4191   3845   -229   -239   -390       C  
ATOM   5633  CG  ARG B 347     -34.560 -56.032 -57.514  1.00 33.73           C  
ANISOU 5633  CG  ARG B 347     4735   4328   3753   -246   -330   -480       C  
ATOM   5634  CD  ARG B 347     -34.361 -55.096 -58.722  1.00 37.97           C  
ANISOU 5634  CD  ARG B 347     5312   4905   4209   -124   -382   -457       C  
ATOM   5635  NE  ARG B 347     -35.600 -54.511 -59.231  1.00 40.49           N  
ANISOU 5635  NE  ARG B 347     5552   5391   4443    -80   -489   -530       N  
ATOM   5636  CZ  ARG B 347     -36.228 -53.462 -58.693  1.00 62.33           C  
ANISOU 5636  CZ  ARG B 347     8233   8248   7203      2   -556   -517       C  
ATOM   5637  NH1 ARG B 347     -35.761 -52.863 -57.593  1.00 47.55           N  
ANISOU 5637  NH1 ARG B 347     6347   6309   5411     28   -523   -433       N  
ATOM   5638  NH2 ARG B 347     -37.348 -53.017 -59.253  1.00 70.20           N  
ANISOU 5638  NH2 ARG B 347     9157   9414   8102     69   -660   -597       N  
ATOM   5639  N   SER B 348     -33.968 -55.938 -53.868  1.00 24.64           N  
ANISOU 5639  N   SER B 348     3497   3047   2820   -303   -234   -347       N  
ATOM   5640  CA  SER B 348     -34.940 -55.311 -52.985  1.00 27.19           C  
ANISOU 5640  CA  SER B 348     3698   3472   3159   -321   -279   -368       C  
ATOM   5641  C   SER B 348     -35.922 -54.484 -53.803  1.00 33.94           C  
ANISOU 5641  C   SER B 348     4471   4484   3940   -262   -374   -427       C  
ATOM   5642  O   SER B 348     -35.516 -53.710 -54.676  1.00 25.87           O  
ANISOU 5642  O   SER B 348     3494   3461   2873   -149   -408   -388       O  
ATOM   5643  CB  SER B 348     -34.228 -54.420 -51.970  1.00 23.17           C  
ANISOU 5643  CB  SER B 348     3173   2915   2715   -245   -267   -267       C  
ATOM   5644  OG  SER B 348     -35.179 -53.684 -51.221  1.00 29.38           O  
ANISOU 5644  OG  SER B 348     3849   3806   3509   -240   -316   -288       O  
ATOM   5645  N   MET B 349     -37.216 -54.641 -53.518  1.00 27.80           N  
ANISOU 5645  N   MET B 349     3576   3849   3136   -334   -414   -527       N  
ATOM   5646  CA  MET B 349     -38.260 -53.873 -54.189  1.00 30.78           C  
ANISOU 5646  CA  MET B 349     3852   4415   3430   -253   -517   -600       C  
ATOM   5647  C   MET B 349     -38.723 -52.680 -53.359  1.00 32.63           C  
ANISOU 5647  C   MET B 349     3992   4731   3676   -146   -568   -573       C  
ATOM   5648  O   MET B 349     -39.657 -51.975 -53.763  1.00 35.07           O  
ANISOU 5648  O   MET B 349     4211   5209   3907    -46   -660   -636       O  
ATOM   5649  CB  MET B 349     -39.448 -54.782 -54.525  1.00 31.81           C  
ANISOU 5649  CB  MET B 349     3885   4699   3501   -395   -536   -756       C  
ATOM   5650  CG  MET B 349     -39.077 -55.996 -55.363  1.00 32.48           C  
ANISOU 5650  CG  MET B 349     4082   4697   3560   -511   -483   -796       C  
ATOM   5651  SD  MET B 349     -38.443 -55.545 -56.992  1.00 40.28           S  
ANISOU 5651  SD  MET B 349     5177   5657   4472   -360   -534   -759       S  
ATOM   5652  CE  MET B 349     -39.884 -54.734 -57.685  1.00 45.67           C  
ANISOU 5652  CE  MET B 349     5698   6622   5034   -264   -678   -875       C  
ATOM   5653  N   VAL B 350     -38.067 -52.426 -52.219  1.00 29.01           N  
ANISOU 5653  N   VAL B 350     3560   4158   3303   -151   -512   -482       N  
ATOM   5654  CA  VAL B 350     -38.478 -51.423 -51.244  1.00 31.32           C  
ANISOU 5654  CA  VAL B 350     3776   4510   3616    -75   -543   -459       C  
ATOM   5655  C   VAL B 350     -37.675 -50.153 -51.460  1.00 31.81           C  
ANISOU 5655  C   VAL B 350     3938   4483   3666     85   -563   -351       C  
ATOM   5656  O   VAL B 350     -36.456 -50.204 -51.655  1.00 31.58           O  
ANISOU 5656  O   VAL B 350     4024   4305   3669     79   -507   -266       O  
ATOM   5657  CB  VAL B 350     -38.277 -51.938 -49.803  1.00 37.01           C  
ANISOU 5657  CB  VAL B 350     4474   5160   4426   -191   -466   -432       C  
ATOM   5658  CG1 VAL B 350     -38.558 -50.828 -48.802  1.00 37.90           C  
ANISOU 5658  CG1 VAL B 350     4525   5315   4559   -104   -493   -398       C  
ATOM   5659  CG2 VAL B 350     -39.163 -53.135 -49.537  1.00 38.70           C  
ANISOU 5659  CG2 VAL B 350     4614   5455   4634   -371   -432   -546       C  
ATOM   5660  N   THR B 351     -38.353 -49.005 -51.398  1.00 36.38           N  
ANISOU 5660  N   THR B 351     4480   5156   4188    224   -636   -360       N  
ATOM   5661  CA  THR B 351     -37.701 -47.701 -51.309  1.00 33.14           C  
ANISOU 5661  CA  THR B 351     4186   4645   3759    356   -640   -260       C  
ATOM   5662  C   THR B 351     -38.220 -47.008 -50.056  1.00 39.45           C  
ANISOU 5662  C   THR B 351     4913   5490   4587    397   -653   -258       C  
ATOM   5663  O   THR B 351     -39.363 -46.542 -50.035  1.00 40.07           O  
ANISOU 5663  O   THR B 351     4900   5724   4600    499   -728   -330       O  
ATOM   5664  CB  THR B 351     -37.978 -46.843 -52.543  1.00 39.20           C  
ANISOU 5664  CB  THR B 351     5045   5450   4400    523   -716   -264       C  
ATOM   5665  OG1 THR B 351     -37.515 -47.516 -53.721  1.00 42.26           O  
ANISOU 5665  OG1 THR B 351     5500   5801   4757    479   -702   -272       O  
ATOM   5666  CG2 THR B 351     -37.275 -45.496 -52.413  1.00 43.39           C  
ANISOU 5666  CG2 THR B 351     5740   5847   4899    633   -701   -161       C  
ATOM   5667  N   ALA B 352     -37.396 -46.944 -49.014  1.00 35.62           N  
ANISOU 5667  N   ALA B 352     4460   4886   4190    329   -582   -182       N  
ATOM   5668  CA  ALA B 352     -37.766 -46.187 -47.816  1.00 34.25           C  
ANISOU 5668  CA  ALA B 352     4243   4735   4038    372   -588   -170       C  
ATOM   5669  C   ALA B 352     -37.563 -44.676 -48.021  1.00 46.83           C  
ANISOU 5669  C   ALA B 352     5969   6265   5558    535   -619   -111       C  
ATOM   5670  O   ALA B 352     -37.979 -43.864 -47.190  1.00 49.77           O  
ANISOU 5670  O   ALA B 352     6331   6659   5922    609   -636   -107       O  
ATOM   5671  CB  ALA B 352     -36.977 -46.662 -46.631  1.00 31.26           C  
ANISOU 5671  CB  ALA B 352     3857   4257   3763    245   -507   -117       C  
ATOM   5672  OXT ALA B 352     -36.988 -44.219 -49.019  1.00 47.23           O  
ANISOU 5672  OXT ALA B 352     6164   6235   5548    593   -622    -67       O  
TER    5673      ALA B 352                                                      
HETATM 5674  C1  NAG A 401      18.648 -21.806  -6.562  1.00 31.05           C  
HETATM 5675  C2  NAG A 401      19.991 -21.174  -6.970  1.00 35.61           C  
HETATM 5676  C3  NAG A 401      20.051 -19.708  -6.523  1.00 30.96           C  
HETATM 5677  C4  NAG A 401      18.809 -18.943  -6.963  1.00 32.34           C  
HETATM 5678  C5  NAG A 401      17.533 -19.691  -6.575  1.00 38.40           C  
HETATM 5679  C6  NAG A 401      16.289 -19.060  -7.164  1.00 52.51           C  
HETATM 5680  C7  NAG A 401      21.789 -22.880  -6.993  1.00 42.99           C  
HETATM 5681  C8  NAG A 401      21.418 -23.161  -8.403  1.00 24.13           C  
HETATM 5682  N2  NAG A 401      21.086 -21.924  -6.375  1.00 37.43           N  
HETATM 5683  O3  NAG A 401      21.217 -19.076  -7.046  1.00 29.35           O  
HETATM 5684  O4  NAG A 401      18.793 -17.667  -6.332  1.00 34.17           O  
HETATM 5685  O5  NAG A 401      17.578 -21.037  -7.073  1.00 34.37           O  
HETATM 5686  O6  NAG A 401      15.120 -19.491  -6.482  1.00 63.18           O  
HETATM 5687  O7  NAG A 401      22.703 -23.485  -6.430  1.00 52.48           O  
HETATM 5688  C1  NAG A 402     -42.934 -30.693 -14.367  1.00 74.78           C  
HETATM 5689  C2  NAG A 402     -44.143 -31.627 -14.232  1.00 84.48           C  
HETATM 5690  C3  NAG A 402     -45.167 -31.054 -13.243  1.00 90.46           C  
HETATM 5691  C4  NAG A 402     -44.504 -30.624 -11.938  1.00 89.79           C  
HETATM 5692  C5  NAG A 402     -43.314 -29.718 -12.226  1.00 87.89           C  
HETATM 5693  C6  NAG A 402     -42.541 -29.330 -10.985  1.00 85.87           C  
HETATM 5694  C7  NAG A 402     -44.597 -32.961 -16.252  1.00 69.31           C  
HETATM 5695  C8  NAG A 402     -45.298 -32.994 -17.578  1.00 59.13           C  
HETATM 5696  N2  NAG A 402     -44.758 -31.843 -15.534  1.00 78.02           N  
HETATM 5697  O3  NAG A 402     -46.155 -32.042 -12.971  1.00 93.20           O  
HETATM 5698  O4  NAG A 402     -45.437 -29.923 -11.122  1.00 92.02           O  
HETATM 5699  O5  NAG A 402     -42.398 -30.410 -13.082  1.00 85.84           O  
HETATM 5700  O6  NAG A 402     -41.418 -28.518 -11.303  1.00 80.52           O  
HETATM 5701  O7  NAG A 402     -43.925 -33.906 -15.846  1.00 69.04           O  
HETATM 5702  S   SO4 A 403     -25.301 -11.727 -19.524  1.00124.07           S  
HETATM 5703  O1  SO4 A 403     -23.926 -12.046 -19.897  1.00124.68           O  
HETATM 5704  O2  SO4 A 403     -25.769 -10.569 -20.284  1.00125.46           O  
HETATM 5705  O3  SO4 A 403     -26.139 -12.874 -19.846  1.00128.27           O  
HETATM 5706  O4  SO4 A 403     -25.374 -11.458 -18.087  1.00118.32           O  
HETATM 5707  C1  NAG B 401     -75.027 -57.250 -43.647  1.00103.33           C  
HETATM 5708  C2  NAG B 401     -76.354 -56.476 -43.442  1.00108.56           C  
HETATM 5709  C3  NAG B 401     -77.467 -57.012 -44.352  1.00118.85           C  
HETATM 5710  C4  NAG B 401     -76.993 -57.120 -45.794  1.00122.20           C  
HETATM 5711  C5  NAG B 401     -75.754 -57.995 -45.832  1.00119.67           C  
HETATM 5712  C6  NAG B 401     -75.187 -58.173 -47.222  1.00117.64           C  
HETATM 5713  C7  NAG B 401     -76.956 -55.462 -41.280  1.00 97.48           C  
HETATM 5714  C8  NAG B 401     -76.693 -54.134 -41.928  1.00 93.40           C  
HETATM 5715  N2  NAG B 401     -76.773 -56.540 -42.050  1.00100.96           N  
HETATM 5716  O3  NAG B 401     -78.590 -56.141 -44.279  1.00121.74           O  
HETATM 5717  O4  NAG B 401     -78.009 -57.686 -46.614  1.00125.58           O  
HETATM 5718  O5  NAG B 401     -74.736 -57.365 -45.046  1.00115.36           O  
HETATM 5719  O6  NAG B 401     -74.254 -59.245 -47.265  1.00115.83           O  
HETATM 5720  O7  NAG B 401     -77.315 -55.556 -40.110  1.00101.16           O  
HETATM 5721  C1  NAG B 402     -10.406 -49.459 -37.398  1.00 64.42           C  
HETATM 5722  C2  NAG B 402      -9.256 -49.978 -36.508  1.00 79.07           C  
HETATM 5723  C3  NAG B 402      -8.305 -50.892 -37.297  1.00 85.06           C  
HETATM 5724  C4  NAG B 402      -9.057 -51.925 -38.125  1.00 86.60           C  
HETATM 5725  C5  NAG B 402     -10.112 -51.234 -38.972  1.00 80.25           C  
HETATM 5726  C6  NAG B 402     -10.927 -52.191 -39.816  1.00 75.15           C  
HETATM 5727  C7  NAG B 402      -8.652 -48.412 -34.697  1.00 80.02           C  
HETATM 5728  C8  NAG B 402      -9.621 -49.161 -33.831  1.00 80.93           C  
HETATM 5729  N2  NAG B 402      -8.517 -48.854 -35.952  1.00 81.44           N  
HETATM 5730  O3  NAG B 402      -7.448 -51.560 -36.377  1.00 89.55           O  
HETATM 5731  O4  NAG B 402      -8.155 -52.612 -38.985  1.00 91.58           O  
HETATM 5732  O5  NAG B 402     -11.015 -50.551 -38.097  1.00 73.24           O  
HETATM 5733  O6  NAG B 402     -12.303 -52.194 -39.459  1.00 67.34           O  
HETATM 5734  O7  NAG B 402      -8.016 -47.452 -34.278  1.00 79.84           O  
HETATM 5735  S   SO4 B 403     -27.410 -55.160 -65.976  1.00 36.56           S  
HETATM 5736  O1  SO4 B 403     -27.225 -55.571 -67.374  1.00 39.79           O  
HETATM 5737  O2  SO4 B 403     -27.540 -53.713 -65.874  1.00 34.51           O  
HETATM 5738  O3  SO4 B 403     -26.228 -55.565 -65.224  1.00 29.35           O  
HETATM 5739  O4  SO4 B 403     -28.629 -55.807 -65.475  1.00 33.48           O  
HETATM 5740  S   SO4 B 404     -29.079 -69.340 -62.125  1.00 75.51           S  
HETATM 5741  O1  SO4 B 404     -28.519 -68.234 -62.898  1.00 79.65           O  
HETATM 5742  O2  SO4 B 404     -30.024 -70.094 -62.941  1.00 79.26           O  
HETATM 5743  O3  SO4 B 404     -28.009 -70.235 -61.696  1.00 80.54           O  
HETATM 5744  O4  SO4 B 404     -29.785 -68.802 -60.965  1.00 78.49           O  
HETATM 5745  S   SO4 B 405     -28.504 -41.884 -54.521  1.00133.73           S  
HETATM 5746  O1  SO4 B 405     -29.326 -41.046 -55.389  1.00139.22           O  
HETATM 5747  O2  SO4 B 405     -27.773 -42.860 -55.325  1.00129.01           O  
HETATM 5748  O3  SO4 B 405     -29.371 -42.579 -53.573  1.00135.90           O  
HETATM 5749  O4  SO4 B 405     -27.557 -41.047 -53.788  1.00131.47           O  
HETATM 5750  S   SO4 B 406     -22.899 -43.505 -57.151  1.00 98.71           S  
HETATM 5751  O1  SO4 B 406     -22.074 -42.949 -58.230  1.00100.71           O  
HETATM 5752  O2  SO4 B 406     -23.420 -44.814 -57.546  1.00100.64           O  
HETATM 5753  O3  SO4 B 406     -24.025 -42.605 -56.887  1.00 98.33           O  
HETATM 5754  O4  SO4 B 406     -22.086 -43.666 -55.941  1.00100.26           O  
HETATM 5755  C1  GOL B 407     -60.519 -40.630 -42.442  1.00 46.57           C  
HETATM 5756  O1  GOL B 407     -59.938 -41.809 -42.969  1.00 29.51           O  
HETATM 5757  C2  GOL B 407     -61.141 -39.714 -43.512  1.00 57.57           C  
HETATM 5758  O2  GOL B 407     -60.840 -40.080 -44.843  1.00 36.58           O  
HETATM 5759  C3  GOL B 407     -62.650 -39.600 -43.311  1.00 64.67           C  
HETATM 5760  O3  GOL B 407     -63.289 -39.218 -44.508  1.00 64.60           O  
HETATM 5761  C1  GOL B 408     -38.998 -46.827 -57.311  1.00 93.75           C  
HETATM 5762  O1  GOL B 408     -39.457 -46.211 -58.493  1.00 94.89           O  
HETATM 5763  C2  GOL B 408     -38.517 -45.764 -56.327  1.00 90.32           C  
HETATM 5764  O2  GOL B 408     -37.105 -45.751 -56.288  1.00 88.47           O  
HETATM 5765  C3  GOL B 408     -39.046 -44.395 -56.747  1.00 82.64           C  
HETATM 5766  O3  GOL B 408     -38.662 -43.422 -55.805  1.00 71.85           O  
HETATM 5767  C1  GOL B 409     -54.003 -61.507 -43.692  1.00 67.42           C  
HETATM 5768  O1  GOL B 409     -54.600 -60.241 -43.869  1.00 59.27           O  
HETATM 5769  C2  GOL B 409     -52.524 -61.332 -43.375  1.00 67.58           C  
HETATM 5770  O2  GOL B 409     -52.288 -62.032 -42.180  1.00 68.12           O  
HETATM 5771  C3  GOL B 409     -51.675 -61.911 -44.512  1.00 77.46           C  
HETATM 5772  O3  GOL B 409     -50.499 -61.147 -44.695  1.00 78.20           O  
HETATM 5773  O   HOH A 501      -1.259 -23.534 -17.075  1.00 96.59           O  
HETATM 5774  O   HOH A 502     -27.657  -6.572   4.089  1.00 53.15           O  
HETATM 5775  O   HOH A 503     -29.516 -32.453  -6.727  1.00 69.74           O  
HETATM 5776  O   HOH A 504     -39.007 -25.564  -4.113  1.00 62.83           O  
HETATM 5777  O   HOH A 505     -30.223 -10.259 -16.680  1.00 77.35           O  
HETATM 5778  O   HOH A 506     -15.616 -32.640  -1.055  1.00 60.94           O  
HETATM 5779  O   HOH A 507     -25.827 -15.480 -21.394  1.00 57.09           O  
HETATM 5780  O   HOH A 508     -19.721 -20.696 -25.483  1.00 61.03           O  
HETATM 5781  O   HOH A 509     -23.292 -13.971 -18.641  1.00 72.02           O  
HETATM 5782  O   HOH A 510       0.154 -17.755  -1.309  1.00 59.07           O  
HETATM 5783  O   HOH A 511     -14.541 -54.445  -8.134  1.00 52.37           O  
HETATM 5784  O   HOH A 512     -39.902 -36.221 -15.435  1.00 43.64           O  
HETATM 5785  O   HOH A 513     -37.376 -29.994  -3.190  1.00 65.71           O  
HETATM 5786  O   HOH A 514      10.104 -24.119 -11.434  1.00 72.89           O  
HETATM 5787  O   HOH A 515      -3.992 -23.998 -15.798  1.00137.76           O  
HETATM 5788  O   HOH A 516     -35.492 -46.637 -16.449  1.00107.72           O  
HETATM 5789  O   HOH A 517     -35.536 -47.616 -14.293  1.00 50.16           O  
HETATM 5790  O   HOH A 518     -24.452 -38.096 -14.970  1.00123.49           O  
HETATM 5791  O   HOH A 519     -12.935 -20.368 -18.527  1.00 58.95           O  
HETATM 5792  O   HOH A 520      23.478 -19.715  -6.274  1.00 35.48           O  
HETATM 5793  O   HOH A 521       5.010 -15.643 -17.673  1.00 74.16           O  
HETATM 5794  O   HOH A 522     -29.063 -17.164 -24.179  1.00 50.64           O  
HETATM 5795  O   HOH A 523      12.755 -30.485 -26.415  1.00 51.81           O  
HETATM 5796  O   HOH A 524     -14.170 -32.933 -28.791  1.00 37.11           O  
HETATM 5797  O   HOH A 525     -24.223 -28.632 -29.263  1.00 25.71           O  
HETATM 5798  O   HOH A 526     -41.416 -27.296 -13.490  1.00 57.00           O  
HETATM 5799  O   HOH A 527      -3.745 -23.900  -6.938  1.00 93.41           O  
HETATM 5800  O   HOH A 528      -0.626 -19.336  -6.654  1.00 42.52           O  
HETATM 5801  O   HOH A 529     -17.109 -50.451  -3.397  1.00 67.61           O  
HETATM 5802  O   HOH A 530      15.289 -31.978 -24.069  1.00 63.56           O  
HETATM 5803  O   HOH A 531     -37.435 -36.933 -13.123  1.00 34.33           O  
HETATM 5804  O   HOH A 532     -15.887 -35.679 -19.335  1.00 47.22           O  
HETATM 5805  O   HOH A 533     -21.171 -51.295 -19.958  1.00 26.49           O  
HETATM 5806  O   HOH A 534       5.097 -44.428  -7.094  1.00 44.62           O  
HETATM 5807  O   HOH A 535      -7.651 -43.829 -24.966  1.00 77.02           O  
HETATM 5808  O   HOH A 536      -4.304 -26.844 -11.523  1.00 55.89           O  
HETATM 5809  O   HOH A 537     -20.652 -52.796 -16.473  1.00 29.96           O  
HETATM 5810  O   HOH A 538      11.001 -47.252 -19.813  1.00 72.30           O  
HETATM 5811  O   HOH A 539      -2.533 -23.574 -26.578  1.00 42.97           O  
HETATM 5812  O   HOH A 540       5.637 -30.381 -25.612  1.00 48.00           O  
HETATM 5813  O   HOH A 541     -30.138 -20.334   3.647  1.00 33.80           O  
HETATM 5814  O   HOH A 542     -16.304 -43.546 -16.217  1.00 36.09           O  
HETATM 5815  O   HOH A 543      12.471 -28.244  -5.083  1.00 51.11           O  
HETATM 5816  O   HOH A 544     -20.989 -34.728  -0.642  1.00 50.77           O  
HETATM 5817  O   HOH A 545      12.089 -42.803 -26.853  1.00 66.24           O  
HETATM 5818  O   HOH A 546     -16.047 -44.273  -7.093  1.00 39.42           O  
HETATM 5819  O   HOH A 547      -9.453 -36.929 -26.129  1.00 31.21           O  
HETATM 5820  O   HOH A 548     -16.518 -16.024  -3.076  1.00 46.90           O  
HETATM 5821  O   HOH A 549     -33.048 -26.638   0.938  1.00 41.66           O  
HETATM 5822  O   HOH A 550     -37.850 -46.178 -18.196  1.00 50.30           O  
HETATM 5823  O   HOH A 551       4.746 -39.559 -30.615  1.00 66.34           O  
HETATM 5824  O   HOH A 552     -38.132  -6.540  -6.661  1.00 34.87           O  
HETATM 5825  O   HOH A 553     -35.056 -53.637 -17.697  1.00 39.56           O  
HETATM 5826  O   HOH A 554     -19.058 -25.486 -29.868  1.00 55.40           O  
HETATM 5827  O   HOH A 555     -15.799 -48.817 -24.446  1.00 30.43           O  
HETATM 5828  O   HOH A 556     -31.331 -28.276 -35.435  1.00 42.29           O  
HETATM 5829  O   HOH A 557     -29.288 -40.858 -10.227  1.00 94.39           O  
HETATM 5830  O   HOH A 558     -12.728 -53.182  -5.448  1.00 58.15           O  
HETATM 5831  O   HOH A 559     -21.449 -27.913   5.138  1.00 42.29           O  
HETATM 5832  O   HOH A 560     -39.748 -25.261 -13.244  1.00 44.21           O  
HETATM 5833  O   HOH A 561     -19.521  -9.002   1.161  1.00 54.87           O  
HETATM 5834  O   HOH A 562      18.197 -35.155  -5.637  1.00 45.23           O  
HETATM 5835  O   HOH A 563       0.000 -21.248   0.000  0.50 47.73           O  
HETATM 5836  O   HOH A 564      19.989 -31.917 -14.242  1.00 57.44           O  
HETATM 5837  O   HOH A 565     -14.030 -24.308 -24.535  1.00 32.01           O  
HETATM 5838  O   HOH A 566     -24.688 -24.303 -31.232  1.00 64.51           O  
HETATM 5839  O   HOH A 567     -20.337 -43.272 -15.458  1.00 27.09           O  
HETATM 5840  O   HOH A 568      -5.354 -51.633  -9.009  1.00 44.95           O  
HETATM 5841  O   HOH A 569     -22.883 -45.970  -7.628  1.00 36.48           O  
HETATM 5842  O   HOH A 570      19.836 -28.357  -7.630  1.00 47.02           O  
HETATM 5843  O   HOH A 571     -18.310 -28.749 -33.118  1.00 71.13           O  
HETATM 5844  O   HOH A 572      -5.982 -20.862 -18.464  1.00 41.54           O  
HETATM 5845  O   HOH A 573     -12.872 -36.216 -14.894  1.00 34.11           O  
HETATM 5846  O   HOH A 574     -34.201 -11.136   7.945  1.00 58.69           O  
HETATM 5847  O   HOH A 575     -37.471 -21.702   2.076  1.00 56.29           O  
HETATM 5848  O   HOH A 576     -34.159 -15.376 -16.663  1.00 30.89           O  
HETATM 5849  O   HOH A 577     -21.024 -48.865 -24.630  1.00 32.80           O  
HETATM 5850  O   HOH A 578      11.494 -25.118 -17.335  1.00 44.99           O  
HETATM 5851  O   HOH A 579     -37.040  -5.741 -15.509  1.00 59.18           O  
HETATM 5852  O   HOH A 580     -15.983 -22.191 -27.510  1.00 60.48           O  
HETATM 5853  O   HOH A 581     -44.303 -34.542 -20.748  1.00 59.51           O  
HETATM 5854  O   HOH A 582     -32.927 -11.056 -12.216  1.00 27.80           O  
HETATM 5855  O   HOH A 583     -18.095 -27.837  -1.242  1.00 28.98           O  
HETATM 5856  O   HOH A 584      21.176 -18.954  -9.700  1.00 37.89           O  
HETATM 5857  O   HOH A 585       8.338 -30.957 -27.798  1.00 50.24           O  
HETATM 5858  O   HOH A 586     -17.740 -10.953 -10.686  1.00 83.40           O  
HETATM 5859  O   HOH A 587     -35.317 -29.054 -23.962  1.00 41.77           O  
HETATM 5860  O   HOH A 588      -6.316 -33.759 -31.015  1.00 42.08           O  
HETATM 5861  O   HOH A 589      20.138 -41.020 -17.624  1.00 63.45           O  
HETATM 5862  O   HOH A 590     -37.643 -33.768 -10.744  1.00 49.57           O  
HETATM 5863  O   HOH A 591     -39.860 -52.013 -22.023  1.00 35.35           O  
HETATM 5864  O   HOH A 592     -15.380 -17.148  -5.704  1.00 29.68           O  
HETATM 5865  O   HOH A 593     -36.408 -20.980 -23.310  1.00 67.31           O  
HETATM 5866  O   HOH A 594     -15.659 -46.036 -19.929  1.00 33.22           O  
HETATM 5867  O   HOH A 595      -2.369 -24.333  -9.250  1.00 51.20           O  
HETATM 5868  O   HOH A 596     -42.934  -8.153 -12.547  1.00 49.07           O  
HETATM 5869  O   HOH A 597     -13.958 -18.944 -20.829  1.00 72.70           O  
HETATM 5870  O   HOH A 598     -17.894 -46.230  -7.774  1.00 41.04           O  
HETATM 5871  O   HOH A 599      14.288 -34.340  -5.771  1.00 35.62           O  
HETATM 5872  O   HOH A 600      -9.364 -28.929 -16.128  1.00 24.13           O  
HETATM 5873  O   HOH A 601     -32.372 -19.277 -21.142  1.00 44.37           O  
HETATM 5874  O   HOH A 602     -30.623 -23.125 -26.612  1.00 39.72           O  
HETATM 5875  O   HOH A 603     -20.026 -41.177 -12.682  1.00 28.14           O  
HETATM 5876  O   HOH A 604     -31.573 -15.515 -17.496  1.00 38.65           O  
HETATM 5877  O   HOH A 605      13.686 -36.800 -21.343  1.00 47.25           O  
HETATM 5878  O   HOH A 606     -34.976 -27.085 -20.962  1.00 43.24           O  
HETATM 5879  O   HOH A 607     -24.220 -13.770   1.323  1.00 24.89           O  
HETATM 5880  O   HOH A 608     -41.206 -11.561 -15.334  1.00 53.42           O  
HETATM 5881  O   HOH A 609     -30.723 -39.777  -8.743  1.00 80.73           O  
HETATM 5882  O   HOH A 610     -35.265 -43.469 -13.610  1.00 75.40           O  
HETATM 5883  O   HOH A 611     -20.201 -60.401 -23.445  1.00 35.96           O  
HETATM 5884  O   HOH A 612      -0.742 -32.190 -18.617  1.00 28.38           O  
HETATM 5885  O   HOH A 613     -16.928 -19.833  -0.355  1.00 30.90           O  
HETATM 5886  O   HOH A 614       7.505 -27.246 -25.640  1.00 54.66           O  
HETATM 5887  O   HOH A 615     -18.139 -22.715  -1.809  1.00 30.69           O  
HETATM 5888  O   HOH A 616       0.506 -44.083  -9.266  1.00 50.09           O  
HETATM 5889  O   HOH A 617     -31.111 -22.818 -20.044  1.00 21.30           O  
HETATM 5890  O   HOH A 618      -0.997 -40.141 -28.749  1.00 39.87           O  
HETATM 5891  O   HOH A 619     -40.530 -23.267  -6.012  1.00 58.52           O  
HETATM 5892  O   HOH A 620     -35.738 -24.927   1.001  1.00 41.50           O  
HETATM 5893  O   HOH A 621      12.082 -43.563   1.417  1.00 54.80           O  
HETATM 5894  O   HOH A 622     -31.197  -5.848  -3.335  1.00 47.84           O  
HETATM 5895  O   HOH A 623     -31.812 -12.031   8.575  1.00 34.53           O  
HETATM 5896  O   HOH A 624     -26.178 -20.410   2.884  1.00 29.86           O  
HETATM 5897  O   HOH A 625       2.969 -34.132 -26.814  1.00 54.00           O  
HETATM 5898  O   HOH A 626     -24.948  -7.248 -13.067  1.00 47.04           O  
HETATM 5899  O   HOH A 627     -33.547  -9.225   0.696  1.00 31.16           O  
HETATM 5900  O   HOH A 628      -7.206 -38.569 -19.002  1.00 42.25           O  
HETATM 5901  O   HOH A 629      -0.828 -33.182 -26.194  1.00 31.49           O  
HETATM 5902  O   HOH A 630     -36.916 -17.307   6.805  1.00 39.22           O  
HETATM 5903  O   HOH A 631     -11.510 -36.854 -11.603  1.00 26.42           O  
HETATM 5904  O   HOH A 632       5.477 -35.143 -28.205  1.00 47.99           O  
HETATM 5905  O   HOH A 633     -41.881 -36.780 -26.116  1.00 60.78           O  
HETATM 5906  O   HOH A 634       9.825 -25.996  -4.223  1.00 52.70           O  
HETATM 5907  O   HOH A 635     -17.813 -28.615 -22.775  1.00 22.14           O  
HETATM 5908  O   HOH A 636     -25.592  -7.778   7.280  1.00 41.68           O  
HETATM 5909  O   HOH A 637     -33.227 -30.014 -32.216  1.00 31.41           O  
HETATM 5910  O   HOH A 638     -21.681 -22.312 -22.605  1.00 30.52           O  
HETATM 5911  O   HOH A 639     -12.631 -46.765 -21.691  1.00 36.33           O  
HETATM 5912  O   HOH A 640     -35.282 -52.675 -20.556  1.00 47.25           O  
HETATM 5913  O   HOH A 641     -17.998 -43.252 -14.436  1.00 39.90           O  
HETATM 5914  O   HOH A 642     -18.904 -55.419 -23.120  1.00 31.53           O  
HETATM 5915  O   HOH A 643     -13.281 -37.589  -9.514  1.00 30.78           O  
HETATM 5916  O   HOH A 644      -2.575 -24.826 -11.889  1.00 40.21           O  
HETATM 5917  O   HOH A 645     -17.911 -47.091 -14.259  1.00 38.42           O  
HETATM 5918  O   HOH A 646      -2.863 -31.891 -16.881  1.00 23.81           O  
HETATM 5919  O   HOH A 647     -11.052 -30.440  -8.650  1.00 46.89           O  
HETATM 5920  O   HOH A 648      18.379 -35.208  -8.535  1.00 51.52           O  
HETATM 5921  O   HOH A 649     -40.827 -14.214   2.098  1.00 47.58           O  
HETATM 5922  O   HOH A 650      -9.119 -37.806 -16.934  1.00 54.30           O  
HETATM 5923  O   HOH A 651     -37.913 -31.252 -24.899  1.00 37.43           O  
HETATM 5924  O   HOH A 652       2.419 -47.021 -12.630  1.00 36.12           O  
HETATM 5925  O   HOH A 653     -36.694 -26.108 -18.266  1.00 45.19           O  
HETATM 5926  O   HOH A 654     -34.493 -13.631 -14.359  1.00 31.39           O  
HETATM 5927  O   HOH A 655       8.450 -32.898  -3.737  1.00 36.21           O  
HETATM 5928  O   HOH A 656     -15.382 -40.749  -8.863  1.00 31.95           O  
HETATM 5929  O   HOH A 657       0.894 -34.401 -24.479  1.00 32.90           O  
HETATM 5930  O   HOH A 658     -20.827 -31.728 -25.452  1.00 19.50           O  
HETATM 5931  O   HOH A 659      14.609 -23.278 -11.007  1.00 41.81           O  
HETATM 5932  O   HOH A 660      17.989 -30.599  -0.436  1.00 38.84           O  
HETATM 5933  O   HOH A 661     -28.929  -5.884  -8.152  1.00 96.77           O  
HETATM 5934  O   HOH A 662      14.952 -35.631  -7.993  1.00 33.48           O  
HETATM 5935  O   HOH A 663     -11.300 -38.173 -13.900  1.00 36.22           O  
HETATM 5936  O   HOH A 664     -18.690  -9.275 -12.094  1.00 52.53           O  
HETATM 5937  O   HOH A 665      -3.661 -32.480 -25.343  1.00 24.46           O  
HETATM 5938  O   HOH A 666     -17.294 -15.950 -19.833  1.00 51.81           O  
HETATM 5939  O   HOH A 667      -9.313 -22.670 -18.258  1.00 29.47           O  
HETATM 5940  O   HOH A 668      10.346 -43.166  -3.511  1.00 53.60           O  
HETATM 5941  O   HOH A 669     -24.844 -26.933   1.684  1.00 37.76           O  
HETATM 5942  O   HOH A 670      20.069 -31.170  -3.855  1.00 48.49           O  
HETATM 5943  O   HOH A 671     -11.118 -25.544  -4.959  1.00 49.56           O  
HETATM 5944  O   HOH A 672     -41.980 -20.464 -12.469  1.00 40.03           O  
HETATM 5945  O   HOH A 673     -26.701 -16.202 -27.494  1.00 58.73           O  
HETATM 5946  O   HOH A 674     -12.617 -30.498 -27.977  1.00 36.52           O  
HETATM 5947  O   HOH A 675     -17.748 -29.144 -25.475  1.00 25.94           O  
HETATM 5948  O   HOH A 676     -10.795 -19.934  -7.945  1.00 50.22           O  
HETATM 5949  O   HOH A 677       6.304 -23.014 -21.240  1.00 30.51           O  
HETATM 5950  O   HOH A 678      -6.041 -53.451  -5.432  1.00 50.17           O  
HETATM 5951  O   HOH A 679     -12.908 -35.410 -31.027  1.00 55.65           O  
HETATM 5952  O   HOH A 680     -33.031 -30.284  -8.382  1.00 26.23           O  
HETATM 5953  O   HOH A 681      12.597 -35.180  -3.341  1.00 43.63           O  
HETATM 5954  O   HOH A 682      -8.702 -36.010 -23.754  1.00 27.65           O  
HETATM 5955  O   HOH A 683     -25.302 -56.712 -25.728  1.00 39.67           O  
HETATM 5956  O   HOH A 684     -27.163 -15.215  -6.873  1.00 25.17           O  
HETATM 5957  O   HOH A 685      -3.314 -43.665 -24.224  1.00 53.62           O  
HETATM 5958  O   HOH A 686      14.918 -22.138  -7.858  1.00 51.02           O  
HETATM 5959  O   HOH A 687     -21.761 -26.442 -32.061  1.00 46.90           O  
HETATM 5960  O   HOH A 688     -11.680 -38.629 -28.904  1.00 46.32           O  
HETATM 5961  O   HOH A 689      18.678 -23.949  -9.854  1.00 35.04           O  
HETATM 5962  O   HOH A 690       0.927 -25.303  -2.770  1.00 33.07           O  
HETATM 5963  O   HOH A 691      -4.682 -30.477 -32.454  1.00 41.80           O  
HETATM 5964  O   HOH A 692     -35.725  -5.748  -5.684  1.00 50.38           O  
HETATM 5965  O   HOH A 693     -37.065 -23.976 -12.602  1.00 24.30           O  
HETATM 5966  O   HOH A 694     -36.545 -23.480   3.856  1.00 52.25           O  
HETATM 5967  O   HOH A 695      11.791 -39.759  -3.401  1.00 38.25           O  
HETATM 5968  O   HOH A 696     -28.127 -35.444 -18.566  1.00 22.11           O  
HETATM 5969  O   HOH A 697     -14.178 -33.226  -4.347  1.00 38.13           O  
HETATM 5970  O   HOH A 698     -38.115 -59.937 -14.046  1.00 46.41           O  
HETATM 5971  O   HOH A 699      15.678 -34.860 -22.223  1.00 54.36           O  
HETATM 5972  O   HOH A 700     -10.897 -23.294  -5.153  1.00 55.20           O  
HETATM 5973  O   HOH A 701      -8.170 -42.166  -7.001  1.00 37.88           O  
HETATM 5974  O   HOH A 702      -6.662 -24.221 -10.742  1.00 50.63           O  
HETATM 5975  O   HOH A 703       5.262 -32.177  -1.973  1.00 51.30           O  
HETATM 5976  O   HOH A 704       7.099 -37.166  -2.141  1.00 62.64           O  
HETATM 5977  O   HOH A 705     -27.820  -7.294 -10.019  1.00 39.63           O  
HETATM 5978  O   HOH A 706     -17.639 -17.226   3.525  1.00 43.78           O  
HETATM 5979  O   HOH A 707     -28.670 -28.006   1.235  1.00 44.42           O  
HETATM 5980  O   HOH A 708     -33.379 -10.920   5.133  1.00 38.19           O  
HETATM 5981  O   HOH A 709     -36.563 -29.706  -8.230  1.00 42.41           O  
HETATM 5982  O   HOH A 710     -39.450 -31.836 -11.235  1.00 53.38           O  
HETATM 5983  O   HOH A 711     -31.971 -22.950 -28.905  1.00 69.57           O  
HETATM 5984  O   HOH A 712     -22.423 -30.377  -2.145  1.00 40.73           O  
HETATM 5985  O   HOH A 713     -42.418 -17.390  -6.184  1.00 62.85           O  
HETATM 5986  O   HOH A 714      17.021 -21.737  -9.753  1.00 73.11           O  
HETATM 5987  O   HOH A 715      -4.923 -25.611 -23.981  1.00 26.53           O  
HETATM 5988  O   HOH A 716     -39.350 -19.263  -4.123  1.00 46.08           O  
HETATM 5989  O   HOH A 717     -10.244 -47.931 -20.888  1.00 33.79           O  
HETATM 5990  O   HOH A 718     -17.897 -11.896  -1.298  1.00 36.94           O  
HETATM 5991  O   HOH A 719     -32.791 -61.997 -19.050  1.00 35.48           O  
HETATM 5992  O   HOH A 720       5.896 -42.222  -5.217  1.00 37.37           O  
HETATM 5993  O   HOH A 721     -38.074 -29.025 -10.465  1.00 32.31           O  
HETATM 5994  O   HOH A 722     -43.272 -36.523 -22.743  1.00 57.06           O  
HETATM 5995  O   HOH A 723      -9.361 -41.888 -24.772  1.00 54.72           O  
HETATM 5996  O   HOH A 724     -32.659  -7.002  -6.585  1.00 31.66           O  
HETATM 5997  O   HOH A 725     -24.734 -36.739  -3.000  1.00 52.89           O  
HETATM 5998  O   HOH A 726      -5.093 -25.933  -8.996  1.00 48.64           O  
HETATM 5999  O   HOH A 727     -26.285  -8.979 -16.299  1.00 53.26           O  
HETATM 6000  O   HOH A 728     -38.894 -37.496 -24.417  1.00 26.69           O  
HETATM 6001  O   HOH A 729     -18.073 -13.768 -10.438  1.00 28.37           O  
HETATM 6002  O   HOH A 730     -27.402  -3.953  -3.996  1.00 48.54           O  
HETATM 6003  O   HOH A 731     -12.347 -30.514  -6.217  1.00 46.93           O  
HETATM 6004  O   HOH A 732     -32.626  -7.276   7.160  1.00 47.61           O  
HETATM 6005  O   HOH A 733       9.405 -48.426 -18.215  1.00 70.69           O  
HETATM 6006  O   HOH A 734     -38.224 -24.449 -15.611  1.00 38.17           O  
HETATM 6007  O   HOH A 735      -5.834 -27.085 -13.527  1.00 37.15           O  
HETATM 6008  O   HOH A 736     -11.376 -53.030  -8.063  1.00 45.01           O  
HETATM 6009  O   HOH A 737     -24.927 -18.752 -27.405  1.00 47.08           O  
HETATM 6010  O   HOH A 738       3.922 -27.221 -25.031  1.00 31.17           O  
HETATM 6011  O   HOH A 739       2.892 -27.518  -6.557  1.00 27.51           O  
HETATM 6012  O   HOH A 740      13.622 -25.822  -5.541  1.00 73.23           O  
HETATM 6013  O   HOH A 741      10.244 -36.743  -3.398  1.00 47.39           O  
HETATM 6014  O   HOH A 742     -44.274 -12.293 -11.958  1.00 57.92           O  
HETATM 6015  O   HOH A 743     -33.268 -40.836 -10.731  1.00 50.18           O  
HETATM 6016  O   HOH A 744     -35.895 -30.643 -11.429  1.00 46.49           O  
HETATM 6017  O   HOH A 745     -26.102 -26.599 -31.621  1.00 42.50           O  
HETATM 6018  O   HOH A 746       3.049 -43.345 -18.557  1.00 54.42           O  
HETATM 6019  O   HOH A 747      -6.336 -56.372 -15.940  1.00 48.04           O  
HETATM 6020  O   HOH A 748     -39.152 -58.375 -10.902  1.00 65.50           O  
HETATM 6021  O   HOH A 749      -3.918 -42.375  -8.094  1.00 32.60           O  
HETATM 6022  O   HOH A 750       3.585 -45.110 -21.459  1.00 59.24           O  
HETATM 6023  O   HOH A 751      -9.411 -35.003 -20.030  1.00 33.32           O  
HETATM 6024  O   HOH A 752     -31.150 -12.958 -18.235  1.00 71.59           O  
HETATM 6025  O   HOH A 753     -12.123 -22.682 -19.201  1.00 36.02           O  
HETATM 6026  O   HOH A 754       4.676 -39.833  -3.682  1.00 41.12           O  
HETATM 6027  O   HOH A 755     -12.360 -16.079 -12.715  1.00 31.96           O  
HETATM 6028  O   HOH A 756     -28.031 -22.704 -32.321  1.00 66.17           O  
HETATM 6029  O   HOH A 757       2.848 -14.456 -15.929  1.00 56.23           O  
HETATM 6030  O   HOH A 758     -13.405 -23.688  -2.001  1.00 39.69           O  
HETATM 6031  O   HOH A 759     -18.057 -21.725 -29.126  1.00 62.60           O  
HETATM 6032  O   HOH A 760     -10.785 -54.545 -11.003  1.00 35.14           O  
HETATM 6033  O   HOH A 761     -37.800 -43.236 -17.374  1.00 42.74           O  
HETATM 6034  O   HOH A 762      -0.498 -17.484 -13.867  1.00 36.12           O  
HETATM 6035  O   HOH A 763      -2.522 -39.588  -3.849  1.00 37.34           O  
HETATM 6036  O   HOH A 764     -18.333 -21.380 -21.746  1.00 30.19           O  
HETATM 6037  O   HOH A 765     -20.993 -20.142 -21.182  1.00 39.39           O  
HETATM 6038  O   HOH A 766      -1.780 -31.947 -32.422  1.00 40.24           O  
HETATM 6039  O   HOH A 767     -33.422 -26.474 -24.600  1.00 36.60           O  
HETATM 6040  O   HOH A 768     -14.927 -37.334 -29.484  1.00 57.08           O  
HETATM 6041  O   HOH A 769     -39.550 -12.138   5.112  1.00 52.99           O  
HETATM 6042  O   HOH A 770     -13.590 -43.938  -8.070  1.00 54.67           O  
HETATM 6043  O   HOH A 771      -7.145 -34.050  -5.678  1.00 53.39           O  
HETATM 6044  O   HOH A 772      -3.690 -39.705 -29.427  1.00 47.01           O  
HETATM 6045  O   HOH A 773     -14.878 -31.827 -26.875  1.00 95.24           O  
HETATM 6046  O   HOH A 774     -15.965 -26.124  -1.102  1.00 43.97           O  
HETATM 6047  O   HOH A 775      13.733 -17.017  -5.822  1.00 71.94           O  
HETATM 6048  O   HOH A 776     -13.472 -37.188 -18.857  1.00 27.21           O  
HETATM 6049  O   HOH A 777      20.216 -26.158 -11.969  1.00 59.48           O  
HETATM 6050  O   HOH A 778      17.082 -48.823 -13.311  1.00 69.67           O  
HETATM 6051  O   HOH A 779     -41.602 -17.397 -14.226  1.00 57.25           O  
HETATM 6052  O   HOH A 780       7.544 -43.803  -3.190  1.00 64.39           O  
HETATM 6053  O   HOH A 781     -26.000 -34.386  -4.150  1.00 60.85           O  
HETATM 6054  O   HOH A 782     -21.031  -4.341   3.582  1.00 56.12           O  
HETATM 6055  O   HOH A 783     -31.960 -18.576 -26.296  1.00 58.32           O  
HETATM 6056  O   HOH A 784     -10.047 -30.143 -28.898  1.00 27.27           O  
HETATM 6057  O   HOH A 785     -32.515 -42.966 -16.810  1.00 53.91           O  
HETATM 6058  O   HOH A 786      -6.142 -35.735 -19.675  1.00 40.90           O  
HETATM 6059  O   HOH A 787       2.481 -43.850  -3.295  1.00 62.36           O  
HETATM 6060  O   HOH A 788       0.023 -17.099 -16.984  1.00 41.44           O  
HETATM 6061  O   HOH A 789     -35.106 -43.913 -16.494  1.00 37.92           O  
HETATM 6062  O   HOH A 790       9.268 -35.062 -28.234  1.00 57.16           O  
HETATM 6063  O   HOH A 791       4.838 -19.640  -6.076  1.00 55.67           O  
HETATM 6064  O   HOH A 792     -17.537 -13.312  10.448  1.00 58.49           O  
HETATM 6065  O   HOH A 793     -21.803 -46.239  -3.137  1.00 57.26           O  
HETATM 6066  O   HOH A 794     -17.114 -35.311 -30.545  1.00 27.74           O  
HETATM 6067  O   HOH A 795     -43.035 -15.409  -7.917  1.00 41.23           O  
HETATM 6068  O   HOH A 796       4.035 -23.872 -26.964  1.00 60.22           O  
HETATM 6069  O   HOH A 797      -9.302 -18.760  -9.881  1.00 51.57           O  
HETATM 6070  O   HOH A 798     -37.993 -27.865  -5.259  1.00 35.10           O  
HETATM 6071  O   HOH A 799       1.066 -16.041 -12.255  1.00 46.46           O  
HETATM 6072  O   HOH A 800      -2.517 -20.575  -6.768  1.00 63.00           O  
HETATM 6073  O   HOH A 801      13.671 -18.854  -9.007  1.00 75.87           O  
HETATM 6074  O   HOH A 802     -38.692 -26.349 -16.978  1.00 59.29           O  
HETATM 6075  O   HOH A 803      -7.339 -54.827 -22.886  1.00 62.02           O  
HETATM 6076  O   HOH A 804     -30.393 -59.116 -22.360  1.00 33.39           O  
HETATM 6077  O   HOH A 805      -6.095 -31.568  -3.854  1.00 38.25           O  
HETATM 6078  O   HOH A 806     -16.986 -31.930 -29.246  1.00 29.73           O  
HETATM 6079  O   HOH A 807      12.377 -23.863  -9.525  1.00 37.54           O  
HETATM 6080  O   HOH A 808       1.330 -26.765 -26.774  1.00 34.39           O  
HETATM 6081  O   HOH A 809     -40.531 -33.746 -14.452  1.00 56.53           O  
HETATM 6082  O   HOH A 810     -34.800 -19.693 -21.058  1.00 47.38           O  
HETATM 6083  O   HOH A 811       2.648 -19.103 -23.131  1.00 59.48           O  
HETATM 6084  O   HOH A 812      -5.507 -30.036   0.919  1.00 58.91           O  
HETATM 6085  O   HOH A 813     -39.354 -39.269 -22.566  1.00 28.19           O  
HETATM 6086  O   HOH A 814       4.317 -20.570 -25.128  1.00 40.98           O  
HETATM 6087  O   HOH A 815      15.541 -21.945  -3.996  1.00 39.53           O  
HETATM 6088  O   HOH A 816      -3.656 -24.963  -4.542  1.00 51.91           O  
HETATM 6089  O   HOH A 817      -4.723 -56.280  -6.895  1.00 53.63           O  
HETATM 6090  O   HOH A 818     -11.940 -53.335 -28.492  1.00 59.07           O  
HETATM 6091  O   HOH A 819     -16.891 -15.712   9.290  1.00 61.79           O  
HETATM 6092  O   HOH A 820     -24.694  -2.226   5.166  1.00 63.02           O  
HETATM 6093  O   HOH A 821     -29.496 -34.862  -3.243  1.00 61.70           O  
HETATM 6094  O   HOH A 822     -20.035 -47.185 -15.983  1.00 30.68           O  
HETATM 6095  O   HOH A 823      14.766 -24.562 -20.378  1.00 87.05           O  
HETATM 6096  O   HOH A 824      -6.268 -41.292  -9.004  1.00 28.95           O  
HETATM 6097  O   HOH A 825      -3.995 -34.809 -18.688  1.00 28.58           O  
HETATM 6098  O   HOH A 826     -24.900 -31.624  -1.439  1.00 47.92           O  
HETATM 6099  O   HOH A 827     -35.638  -3.408 -12.649  1.00 58.79           O  
HETATM 6100  O   HOH A 828     -33.887 -61.892 -15.699  1.00 37.22           O  
HETATM 6101  O   HOH A 829      -9.271 -35.557 -28.889  1.00 52.43           O  
HETATM 6102  O   HOH A 830     -24.926  -3.139  -2.878  1.00 57.64           O  
HETATM 6103  O   HOH A 831     -11.776 -23.707   2.715  1.00 61.73           O  
HETATM 6104  O   HOH A 832      17.378 -23.986 -13.743  1.00 61.81           O  
HETATM 6105  O   HOH A 833     -33.440  -3.117 -11.432  1.00 48.46           O  
HETATM 6106  O   HOH A 834     -24.076 -21.062 -29.481  1.00 41.75           O  
HETATM 6107  O   HOH A 835      -0.106 -34.145 -17.291  1.00 48.69           O  
HETATM 6108  O   HOH A 836     -42.580 -33.950 -26.662  1.00 65.25           O  
HETATM 6109  O   HOH A 837     -13.583 -13.253 -12.358  1.00 52.91           O  
HETATM 6110  O   HOH A 838     -13.516 -38.307 -15.565  1.00 69.73           O  
HETATM 6111  O   HOH A 839     -34.852 -10.236   3.172  1.00 37.12           O  
HETATM 6112  O   HOH A 840       3.920 -41.737 -24.110  1.00 45.47           O  
HETATM 6113  O   HOH A 841     -14.535 -54.444 -31.815  1.00 63.27           O  
HETATM 6114  O   HOH A 842      -4.626 -49.407  -7.672  1.00 46.18           O  
HETATM 6115  O   HOH A 843      -1.068 -26.928  -1.923  1.00 34.46           O  
HETATM 6116  O   HOH A 844       7.388 -25.006  -4.943  1.00 49.91           O  
HETATM 6117  O   HOH A 845      -8.776 -46.515 -23.101  1.00 46.17           O  
HETATM 6118  O   HOH A 846       9.739 -22.271 -12.517  1.00 66.08           O  
HETATM 6119  O   HOH A 847     -15.214 -53.617  -5.852  1.00 67.30           O  
HETATM 6120  O   HOH A 848      17.460 -25.979 -14.998  1.00 54.75           O  
HETATM 6121  O   HOH A 849      -2.681 -34.127  -3.774  1.00 64.54           O  
HETATM 6122  O   HOH A 850     -44.759 -28.738  -8.343  1.00 72.21           O  
HETATM 6123  O   HOH A 851       3.640 -42.046 -21.072  1.00 32.11           O  
HETATM 6124  O   HOH A 852       2.392 -18.554  -5.783  1.00 53.48           O  
HETATM 6125  O   HOH A 853     -19.117  -5.787  -1.225  1.00 67.30           O  
HETATM 6126  O   HOH A 854     -39.916 -43.402 -18.670  1.00 76.25           O  
HETATM 6127  O   HOH A 855      21.276 -36.588  -9.124  1.00 48.78           O  
HETATM 6128  O   HOH A 856      12.604 -22.993 -23.045  1.00 52.28           O  
HETATM 6129  O   HOH A 857     -41.067  -6.036  -4.878  1.00 69.77           O  
HETATM 6130  O   HOH A 858       8.716 -47.855 -15.424  1.00 63.35           O  
HETATM 6131  O   HOH A 859      12.663 -18.845  -4.621  1.00 66.89           O  
HETATM 6132  O   HOH A 860     -18.420 -57.165 -27.094  1.00 71.71           O  
HETATM 6133  O   HOH A 861     -18.763 -17.576  10.499  1.00 50.13           O  
HETATM 6134  O   HOH A 862       7.548 -23.156 -23.585  1.00 55.21           O  
HETATM 6135  O   HOH A 863     -22.484  -8.594  -6.263  1.00 57.30           O  
HETATM 6136  O   HOH A 864      14.479 -24.577 -17.972  1.00 66.37           O  
HETATM 6137  O   HOH A 865     -12.794 -42.009  -9.143  1.00 56.31           O  
HETATM 6138  O   HOH A 866     -33.855  -8.115 -18.080  1.00 60.88           O  
HETATM 6139  O   HOH A 867     -27.160 -30.318   0.664  1.00 68.01           O  
HETATM 6140  O   HOH A 868      -6.808 -36.674 -16.278  1.00 58.49           O  
HETATM 6141  O   HOH A 869     -27.605 -20.303   8.458  1.00 51.62           O  
HETATM 6142  O   HOH A 870     -17.108 -52.717  -4.802  1.00 86.30           O  
HETATM 6143  O   HOH A 871      -3.329 -43.355  -5.679  1.00 43.68           O  
HETATM 6144  O   HOH A 872     -32.134 -21.392   7.316  1.00 52.97           O  
HETATM 6145  O   HOH A 873     -11.182 -16.383 -15.167  1.00 50.81           O  
HETATM 6146  O   HOH A 874     -20.118 -37.737  -3.291  1.00 63.86           O  
HETATM 6147  O   HOH A 875     -16.793 -29.014 -27.944  1.00 37.99           O  
HETATM 6148  O   HOH A 876      -3.896 -42.163  -3.694  1.00 63.74           O  
HETATM 6149  O   HOH A 877     -10.310 -25.291  -2.192  1.00 67.82           O  
HETATM 6150  O   HOH A 878     -16.369 -59.996 -29.279  1.00 68.67           O  
HETATM 6151  O   HOH A 879     -46.782 -31.070  -8.372  1.00 65.72           O  
HETATM 6152  O   HOH A 880     -17.372 -44.755 -18.516  1.00 36.27           O  
HETATM 6153  O   HOH A 881     -11.010 -28.879   2.719  1.00 48.48           O  
HETATM 6154  O   HOH A 882      -8.135 -42.126  -4.528  1.00 51.50           O  
HETATM 6155  O   HOH A 883       7.080 -25.077 -24.725  1.00 61.68           O  
HETATM 6156  O   HOH A 884     -44.476 -41.150 -18.594  1.00 69.68           O  
HETATM 6157  O   HOH A 885     -17.577 -36.667  -2.506  1.00 49.70           O  
HETATM 6158  O   HOH A 886       3.094 -28.860  -1.979  1.00 36.85           O  
HETATM 6159  O   HOH A 887      16.111 -19.456  -3.315  1.00 52.68           O  
HETATM 6160  O   HOH A 888     -43.817 -11.564  -7.050  1.00 59.04           O  
HETATM 6161  O   HOH A 889     -42.170 -38.590 -21.898  1.00 62.09           O  
HETATM 6162  O   HOH A 890     -26.576 -27.150 -34.783  1.00 41.18           O  
HETATM 6163  O   HOH A 891     -28.211  -9.528 -18.211  1.00 59.05           O  
HETATM 6164  O   HOH A 892     -35.752 -15.704 -18.956  1.00 54.16           O  
HETATM 6165  O   HOH A 893     -33.567 -27.336 -31.271  1.00 52.14           O  
HETATM 6166  O   HOH A 894     -38.794 -38.152 -14.994  1.00 54.86           O  
HETATM 6167  O   HOH A 895      20.660 -27.697 -10.155  1.00 73.31           O  
HETATM 6168  O   HOH A 896      11.567 -23.228  -6.478  1.00 64.41           O  
HETATM 6169  O   HOH A 897     -32.711  -3.345  -3.224  1.00 51.58           O  
HETATM 6170  O   HOH A 898     -12.620 -55.701  -9.147  1.00 55.78           O  
HETATM 6171  O   HOH A 899      -7.776 -38.178 -31.126  1.00 76.80           O  
HETATM 6172  O   HOH A 900     -33.999  -4.776  -6.668  1.00 61.22           O  
HETATM 6173  O   HOH A 901      -4.563 -20.961 -20.729  1.00 34.84           O  
HETATM 6174  O   HOH A 902     -38.961 -33.777 -26.343  1.00 49.49           O  
HETATM 6175  O   HOH A 903       6.724 -34.147  -0.515  1.00 63.60           O  
HETATM 6176  O   HOH A 904      13.467 -22.390  -5.520  1.00 76.52           O  
HETATM 6177  O   HOH A 905     -11.408 -24.381  -0.141  1.00 64.79           O  
HETATM 6178  O   HOH A 906     -23.086 -10.789 -14.800  1.00 49.74           O  
HETATM 6179  O   HOH A 907     -21.827 -19.872 -29.510  1.00 58.78           O  
HETATM 6180  O   HOH A 908      -5.149 -44.201 -25.955  1.00 53.89           O  
HETATM 6181  O   HOH A 909     -24.682  -7.434  -9.927  1.00 64.96           O  
HETATM 6182  O   HOH A 910     -12.021 -20.920 -21.509  1.00 38.58           O  
HETATM 6183  O   HOH A 911       0.923 -31.863 -28.062  1.00 41.44           O  
HETATM 6184  O   HOH A 912     -21.948 -18.395 -24.608  1.00 61.82           O  
HETATM 6185  O   HOH A 913     -27.156 -25.520   1.568  1.00 36.18           O  
HETATM 6186  O   HOH A 914     -25.562  -6.411 -15.069  1.00106.61           O  
HETATM 6187  O   HOH A 915      -1.205 -51.397  -9.869  1.00 57.98           O  
HETATM 6188  O   HOH A 916     -37.588  -8.303 -17.004  1.00 59.15           O  
HETATM 6189  O   HOH A 917     -20.609 -30.299   0.130  1.00 48.71           O  
HETATM 6190  O   HOH A 918     -15.306 -36.087  -3.035  1.00 65.18           O  
HETATM 6191  O   HOH A 919     -32.493 -10.621 -16.777  1.00 48.42           O  
HETATM 6192  O   HOH A 920       0.642 -49.277  -9.419  1.00 63.33           O  
HETATM 6193  O   HOH A 921     -17.886 -57.633 -24.100  1.00 46.62           O  
HETATM 6194  O   HOH A 922     -19.389 -22.154 -31.327  1.00 59.84           O  
HETATM 6195  O   HOH A 923      -5.432 -51.395  -4.035  1.00 57.14           O  
HETATM 6196  O   HOH A 924      -0.525 -40.212  -2.295  1.00 49.92           O  
HETATM 6197  O   HOH A 925     -23.434 -26.099 -29.547  1.00 46.88           O  
HETATM 6198  O   HOH A 926     -32.269 -11.987 -14.713  1.00 30.90           O  
HETATM 6199  O   HOH A 927      25.193 -21.208  -8.150  1.00 62.83           O  
HETATM 6200  O   HOH A 928     -32.321 -61.257 -21.716  1.00 35.20           O  
HETATM 6201  O   HOH A 929     -37.999 -42.500 -11.956  1.00 69.53           O  
HETATM 6202  O   HOH A 930     -32.727 -24.149 -24.601  1.00 48.29           O  
HETATM 6203  O   HOH A 931     -21.454 -12.898 -17.104  1.00 51.31           O  
HETATM 6204  O   HOH A 932     -27.347 -21.983   4.378  1.00 51.97           O  
HETATM 6205  O   HOH A 933      24.662 -26.378  -4.777  1.00 58.87           O  
HETATM 6206  O   HOH A 934       2.609 -45.878 -10.068  1.00 56.16           O  
HETATM 6207  O   HOH A 935     -33.098 -22.666 -22.020  1.00 40.29           O  
HETATM 6208  O   HOH A 936     -19.779 -45.048 -17.465  1.00 29.21           O  
HETATM 6209  O   HOH A 937       3.012 -26.948  -3.807  1.00 30.41           O  
HETATM 6210  O   HOH A 938     -18.019 -31.274 -33.926  1.00 46.37           O  
HETATM 6211  O   HOH A 939      15.764 -15.213  -6.601  1.00 68.35           O  
HETATM 6212  O   HOH A 940      21.245 -26.119  -8.930  1.00 64.15           O  
HETATM 6213  O   HOH A 941     -33.370 -16.653 -19.718  1.00 56.80           O  
HETATM 6214  O   HOH A 942     -16.461 -17.260  -0.276  1.00 46.26           O  
HETATM 6215  O   HOH A 943     -26.984  -4.093  -6.400  1.00 50.72           O  
HETATM 6216  O   HOH A 944      -2.285 -19.680 -20.769  1.00 38.05           O  
HETATM 6217  O   HOH A 945      -7.727 -18.203 -15.215  1.00 59.26           O  
HETATM 6218  O   HOH A 946     -43.172 -10.784 -13.669  1.00 53.68           O  
HETATM 6219  O   HOH A 947      -9.291 -39.561 -27.121  1.00 33.26           O  
HETATM 6220  O   HOH A 948      10.771 -33.751  -2.309  1.00 62.49           O  
HETATM 6221  O   HOH A 949     -42.358 -22.641 -14.547  1.00 55.72           O  
HETATM 6222  O   HOH A 950       0.000 -28.872   0.000  0.50 50.52           O  
HETATM 6223  O   HOH A 951     -18.820 -10.840   3.068  1.00 38.60           O  
HETATM 6224  O   HOH A 952      19.119 -21.227 -10.831  1.00 75.61           O  
HETATM 6225  O   HOH A 953      -4.211 -53.406  -7.393  1.00 56.84           O  
HETATM 6226  O   HOH A 954     -41.423 -14.457 -16.814  1.00 66.06           O  
HETATM 6227  O   HOH A 955     -11.218 -35.801 -17.581  1.00 42.65           O  
HETATM 6228  O   HOH A 956      10.152 -26.066 -27.137  1.00 69.66           O  
HETATM 6229  O   HOH A 957     -15.760 -23.342  -0.737  1.00 39.69           O  
HETATM 6230  O   HOH A 958     -33.007 -19.916 -28.399  1.00 60.36           O  
HETATM 6231  O   HOH A 959     -25.689  -0.291  -1.572  1.00 61.90           O  
HETATM 6232  O   HOH A 960     -29.136 -21.453   6.400  1.00 46.98           O  
HETATM 6233  O   HOH A 961      13.701 -22.190 -20.373  1.00 37.26           O  
HETATM 6234  O   HOH A 962     -22.795 -22.678 -31.596  1.00 70.66           O  
HETATM 6235  O   HOH A 963     -14.799 -19.572   0.703  1.00 71.77           O  
HETATM 6236  O   HOH A 964     -22.324 -17.815 -27.130  1.00 76.43           O  
HETATM 6237  O   HOH A 965     -34.217 -23.972 -28.223  1.00 58.08           O  
HETATM 6238  O   HOH A 966     -42.109 -42.634 -20.012  1.00 46.05           O  
HETATM 6239  O   HOH A 967     -33.962 -34.140  -8.054  1.00 38.50           O  
HETATM 6240  O   HOH A 968     -32.714 -32.337  -6.502  1.00 43.09           O  
HETATM 6241  O   HOH A 969      -9.214 -30.851   2.024  1.00 52.03           O  
HETATM 6242  O   HOH A 970      14.181 -22.318 -13.220  1.00 81.56           O  
HETATM 6243  O   HOH A 971     -36.030  -8.527   7.379  1.00 54.96           O  
HETATM 6244  O   HOH A 972     -25.123 -29.500   1.368  1.00 61.63           O  
HETATM 6245  O   HOH A 973      -7.535 -39.725 -29.203  1.00 52.41           O  
HETATM 6246  O   HOH A 974      23.951 -31.205  -5.453  1.00 58.66           O  
HETATM 6247  O   HOH A 975     -17.521 -20.700 -24.014  1.00 58.46           O  
HETATM 6248  O   HOH A 976     -29.924  -4.334  -4.873  1.00 73.06           O  
HETATM 6249  O   HOH A 977     -27.504 -24.775   3.966  1.00 48.24           O  
HETATM 6250  O   HOH A 978     -40.977 -23.736 -16.567  1.00 63.58           O  
HETATM 6251  O   HOH A 979      -3.823 -32.581 -34.001  1.00 66.81           O  
HETATM 6252  O   HOH A 980     -38.644 -42.116 -14.792  1.00 50.94           O  
HETATM 6253  O   HOH A 981      -8.340 -20.327 -18.974  1.00 41.23           O  
HETATM 6254  O   HOH A 982     -33.294 -26.580 -34.132  1.00 59.55           O  
HETATM 6255  O   HOH A 983      -7.760 -55.529 -28.222  1.00 71.74           O  
HETATM 6256  O   HOH A 984     -36.018 -32.759  -9.123  1.00 53.46           O  
HETATM 6257  O   HOH A 985     -42.783 -20.042  -5.651  1.00 60.91           O  
HETATM 6258  O   HOH A 986       1.506 -23.674  -0.704  1.00 39.33           O  
HETATM 6259  O   HOH A 987       2.320 -16.123  -3.999  1.00 63.22           O  
HETATM 6260  O   HOH A 988      -4.091 -37.623  -2.813  1.00 54.59           O  
HETATM 6261  O   HOH A 989       3.346 -21.545 -27.406  1.00 51.50           O  
HETATM 6262  O   HOH A 990     -12.615 -17.549  -5.283  1.00 51.52           O  
HETATM 6263  O   HOH A 991      -4.661 -22.308 -11.299  1.00 66.94           O  
HETATM 6264  O   HOH A 992       3.212 -41.524 -29.630  1.00 59.16           O  
HETATM 6265  O   HOH A 993     -14.911 -22.055   1.411  1.00 55.58           O  
HETATM 6266  O   HOH A 994     -16.845 -32.511 -31.943  1.00 54.55           O  
HETATM 6267  O   HOH A 995       3.722 -49.388 -12.693  1.00 57.36           O  
HETATM 6268  O   HOH A 996       0.602 -19.512 -24.818  1.00 47.01           O  
HETATM 6269  O   HOH A 997     -20.930 -17.679 -22.005  1.00 51.81           O  
HETATM 6270  O   HOH A 998      12.316 -20.218 -10.787  1.00 70.68           O  
HETATM 6271  O   HOH A 999       5.189 -25.492  -3.044  1.00 36.34           O  
HETATM 6272  O   HOH A1000      16.616 -15.054  -3.031  1.00 57.53           O  
HETATM 6273  O   HOH A1001     -10.185 -18.256 -17.907  1.00 64.38           O  
HETATM 6274  O   HOH A1002      -3.035 -16.852 -13.516  1.00 53.18           O  
HETATM 6275  O   HOH A1003       1.320 -28.904 -28.265  1.00 49.07           O  
HETATM 6276  O   HOH A1004     -17.034 -12.490   1.991  1.00 52.76           O  
HETATM 6277  O   HOH A1005      15.384 -13.379  -4.872  1.00 60.73           O  
HETATM 6278  O   HOH A1006     -29.399 -26.457   5.715  1.00 66.35           O  
HETATM 6279  O   HOH B 501     -34.972 -53.315 -22.774  1.00 46.40           O  
HETATM 6280  O   HOH B 502      -7.289 -54.126 -40.335  1.00 69.48           O  
HETATM 6281  O   HOH B 503     -40.750 -38.002 -40.866  1.00 57.67           O  
HETATM 6282  O   HOH B 504     -38.995 -45.041 -60.329  1.00115.81           O  
HETATM 6283  O   HOH B 505     -34.159 -37.731 -45.025  1.00 64.22           O  
HETATM 6284  O   HOH B 506     -47.455 -50.418 -40.302  1.00 36.09           O  
HETATM 6285  O   HOH B 507     -26.202 -42.260 -57.374  1.00 61.03           O  
HETATM 6286  O   HOH B 508     -47.398 -58.505 -16.867  1.00 56.49           O  
HETATM 6287  O   HOH B 509     -22.251 -67.395 -60.128  1.00 86.77           O  
HETATM 6288  O   HOH B 510     -76.649 -71.428 -27.909  1.00 68.05           O  
HETATM 6289  O   HOH B 511     -71.668 -63.535 -28.488  1.00 54.92           O  
HETATM 6290  O   HOH B 512     -32.173 -34.054 -40.169  1.00 55.60           O  
HETATM 6291  O   HOH B 513     -32.126 -45.233 -14.416  1.00 66.75           O  
HETATM 6292  O   HOH B 514     -31.680 -47.874 -15.502  1.00 29.82           O  
HETATM 6293  O   HOH B 515     -37.115 -66.122 -28.478  1.00 58.48           O  
HETATM 6294  O   HOH B 516     -65.902 -42.263 -28.305  1.00 86.98           O  
HETATM 6295  O   HOH B 517     -45.736 -41.909 -22.126  1.00 51.90           O  
HETATM 6296  O   HOH B 518     -30.686 -61.447 -67.249  1.00 52.82           O  
HETATM 6297  O   HOH B 519     -20.201 -64.055 -43.379  1.00 43.00           O  
HETATM 6298  O   HOH B 520     -29.412 -34.676 -36.406  1.00 31.66           O  
HETATM 6299  O   HOH B 521     -25.381 -59.195 -29.707  1.00 53.56           O  
HETATM 6300  O   HOH B 522     -39.221 -36.121 -32.101  1.00 40.96           O  
HETATM 6301  O   HOH B 523     -76.299 -63.238 -22.918  1.00 45.79           O  
HETATM 6302  O   HOH B 524     -27.512 -72.608 -62.166  1.00 65.40           O  
HETATM 6303  O   HOH B 525     -22.580 -28.607 -36.008  1.00 41.19           O  
HETATM 6304  O   HOH B 526     -23.601 -61.376 -35.676  1.00 75.34           O  
HETATM 6305  O   HOH B 527     -23.324 -57.732 -36.899  1.00 45.32           O  
HETATM 6306  O   HOH B 528     -40.349 -50.388 -31.316  1.00 41.69           O  
HETATM 6307  O   HOH B 529     -10.400 -50.699 -21.234  1.00 51.55           O  
HETATM 6308  O   HOH B 530     -42.173 -55.395 -38.250  1.00 43.86           O  
HETATM 6309  O   HOH B 531     -43.799 -39.282 -28.483  1.00 32.32           O  
HETATM 6310  O   HOH B 532     -49.178 -58.056 -26.257  1.00 29.36           O  
HETATM 6311  O   HOH B 533     -41.200 -34.581 -36.526  1.00 62.03           O  
HETATM 6312  O   HOH B 534     -49.721 -36.959 -25.169  1.00 45.70           O  
HETATM 6313  O   HOH B 535     -27.723 -63.007 -38.425  1.00 43.44           O  
HETATM 6314  O   HOH B 536     -70.903 -46.925 -34.605  1.00 57.29           O  
HETATM 6315  O   HOH B 537     -44.006 -48.859 -29.264  1.00 55.23           O  
HETATM 6316  O   HOH B 538     -44.524 -42.969 -23.631  1.00 40.00           O  
HETATM 6317  O   HOH B 539     -59.973 -70.198 -29.038  1.00 60.34           O  
HETATM 6318  O   HOH B 540     -32.233 -68.221 -60.656  1.00 49.69           O  
HETATM 6319  O   HOH B 541     -69.713 -57.597 -19.087  1.00 68.26           O  
HETATM 6320  O   HOH B 542     -49.026 -52.364 -41.201  1.00 52.10           O  
HETATM 6321  O   HOH B 543     -21.423 -41.206 -47.238  1.00 43.71           O  
HETATM 6322  O   HOH B 544     -29.259 -57.533 -68.184  1.00 36.41           O  
HETATM 6323  O   HOH B 545     -32.821 -51.057 -24.583  1.00 27.16           O  
HETATM 6324  O   HOH B 546     -65.809 -58.449 -40.266  1.00 46.29           O  
HETATM 6325  O   HOH B 547     -45.895 -46.719 -27.834  1.00 39.69           O  
HETATM 6326  O   HOH B 548     -68.655 -40.446 -33.516  1.00 44.11           O  
HETATM 6327  O   HOH B 549     -48.573 -55.950 -14.834  1.00 57.90           O  
HETATM 6328  O   HOH B 550     -35.497 -31.303 -35.322  1.00 45.00           O  
HETATM 6329  O   HOH B 551     -36.552 -55.658 -61.313  1.00 56.15           O  
HETATM 6330  O   HOH B 552     -24.345 -37.837 -48.499  1.00 44.56           O  
HETATM 6331  O   HOH B 553     -15.903 -52.531 -62.486  1.00 36.63           O  
HETATM 6332  O   HOH B 554     -26.728 -49.673 -60.399  1.00 44.62           O  
HETATM 6333  O   HOH B 555     -11.907 -51.602 -63.381  1.00 64.94           O  
HETATM 6334  O   HOH B 556      -8.878 -40.391 -34.694  1.00 61.17           O  
HETATM 6335  O   HOH B 557     -39.179 -51.434 -58.394  1.00 63.48           O  
HETATM 6336  O   HOH B 558     -68.762 -46.090 -20.026  1.00 65.58           O  
HETATM 6337  O   HOH B 559     -70.089 -59.900 -26.392  1.00 42.63           O  
HETATM 6338  O   HOH B 560     -17.498 -52.581 -20.251  1.00 35.41           O  
HETATM 6339  O   HOH B 561     -46.520 -59.294 -35.073  1.00 58.42           O  
HETATM 6340  O   HOH B 562     -65.790 -39.644 -27.064  1.00 61.23           O  
HETATM 6341  O   HOH B 563     -30.891 -41.659 -51.693  1.00 63.56           O  
HETATM 6342  O   HOH B 564     -21.052 -69.683 -57.349  1.00 49.58           O  
HETATM 6343  O   HOH B 565     -22.266 -56.140 -28.646  1.00 35.59           O  
HETATM 6344  O   HOH B 566     -57.454 -45.135 -52.303  1.00 41.82           O  
HETATM 6345  O   HOH B 567     -36.676 -62.016 -26.921  1.00 85.22           O  
HETATM 6346  O   HOH B 568     -23.418 -65.680 -49.861  1.00 40.55           O  
HETATM 6347  O   HOH B 569     -71.659 -59.356 -33.679  1.00 42.18           O  
HETATM 6348  O   HOH B 570     -27.598 -44.591 -58.304  1.00 44.61           O  
HETATM 6349  O   HOH B 571     -37.054 -58.894 -53.375  1.00 48.33           O  
HETATM 6350  O   HOH B 572     -42.695 -54.463 -48.376  1.00 61.49           O  
HETATM 6351  O   HOH B 573     -59.278 -39.070 -34.881  1.00 44.99           O  
HETATM 6352  O   HOH B 574     -39.371 -49.079 -54.688  1.00 46.09           O  
HETATM 6353  O   HOH B 575     -37.448 -45.721 -31.124  1.00 35.54           O  
HETATM 6354  O   HOH B 576     -39.184 -41.467 -40.021  1.00 43.60           O  
HETATM 6355  O   HOH B 577     -13.560 -44.012 -38.487  1.00 73.96           O  
HETATM 6356  O   HOH B 578     -13.942 -58.127 -50.033  1.00 49.60           O  
HETATM 6357  O   HOH B 579     -53.063 -57.418 -24.511  1.00 58.17           O  
HETATM 6358  O   HOH B 580     -50.103 -42.321 -22.160  1.00 53.69           O  
HETATM 6359  O   HOH B 581     -15.707 -51.803 -31.045  1.00 30.65           O  
HETATM 6360  O   HOH B 582     -35.100 -61.216 -46.946  1.00 33.34           O  
HETATM 6361  O   HOH B 583     -29.412 -62.634 -56.129  1.00 29.78           O  
HETATM 6362  O   HOH B 584     -24.873 -56.607 -68.002  1.00 34.02           O  
HETATM 6363  O   HOH B 585     -48.335 -54.648 -42.310  1.00 53.01           O  
HETATM 6364  O   HOH B 586     -32.135 -46.167  -5.745  1.00 57.82           O  
HETATM 6365  O   HOH B 587     -27.411 -65.124 -49.887  1.00 28.80           O  
HETATM 6366  O   HOH B 588     -23.823 -53.174 -61.968  1.00 28.08           O  
HETATM 6367  O   HOH B 589     -53.357 -55.558 -49.233  1.00 46.46           O  
HETATM 6368  O   HOH B 590     -47.629 -35.145 -40.915  1.00 43.23           O  
HETATM 6369  O   HOH B 591     -11.120 -55.593 -51.980  1.00 55.58           O  
HETATM 6370  O   HOH B 592     -22.360 -42.646 -43.944  1.00 22.84           O  
HETATM 6371  O   HOH B 593     -39.263 -60.121 -35.772  1.00 42.79           O  
HETATM 6372  O   HOH B 594     -12.589 -45.652 -55.621  1.00 45.66           O  
HETATM 6373  O   HOH B 595     -13.632 -49.658 -42.703  1.00 48.50           O  
HETATM 6374  O   HOH B 596     -43.943 -47.835 -38.238  1.00 21.92           O  
HETATM 6375  O   HOH B 597     -52.551 -38.786 -32.143  1.00 32.24           O  
HETATM 6376  O   HOH B 598     -63.804 -66.520 -23.098  1.00 35.29           O  
HETATM 6377  O   HOH B 599     -39.806 -46.371 -29.530  1.00 29.59           O  
HETATM 6378  O   HOH B 600     -65.910 -61.588 -34.073  1.00 40.02           O  
HETATM 6379  O   HOH B 601     -32.295 -51.171 -14.472  1.00 40.21           O  
HETATM 6380  O   HOH B 602     -12.102 -49.525 -40.961  1.00 64.57           O  
HETATM 6381  O   HOH B 603     -23.987 -54.218 -64.666  1.00 30.91           O  
HETATM 6382  O   HOH B 604     -19.487 -44.904 -51.809  1.00 33.92           O  
HETATM 6383  O   HOH B 605     -13.054 -45.580 -14.626  1.00 31.07           O  
HETATM 6384  O   HOH B 606     -31.463 -46.841 -57.451  1.00 46.46           O  
HETATM 6385  O   HOH B 607     -58.691 -56.322 -48.681  1.00 67.34           O  
HETATM 6386  O   HOH B 608     -13.185 -42.861 -56.856  1.00 65.62           O  
HETATM 6387  O   HOH B 609     -45.329 -38.984 -43.066  1.00 48.80           O  
HETATM 6388  O   HOH B 610     -20.923 -48.520 -56.751  1.00 28.13           O  
HETATM 6389  O   HOH B 611     -68.202 -52.062 -44.129  1.00 41.96           O  
HETATM 6390  O   HOH B 612     -44.123 -36.387 -29.892  1.00 63.80           O  
HETATM 6391  O   HOH B 613     -35.485 -51.063 -54.205  1.00 26.73           O  
HETATM 6392  O   HOH B 614     -50.919 -51.342 -42.808  1.00 40.12           O  
HETATM 6393  O   HOH B 615     -20.157 -60.798 -60.910  1.00 31.98           O  
HETATM 6394  O   HOH B 616     -69.609 -62.590 -27.167  1.00 50.27           O  
HETATM 6395  O   HOH B 617     -35.286 -61.357 -19.952  1.00 42.37           O  
HETATM 6396  O   HOH B 618     -42.789 -46.515 -18.593  1.00 37.26           O  
HETATM 6397  O   HOH B 619     -71.271 -64.807 -30.702  1.00 55.06           O  
HETATM 6398  O   HOH B 620     -15.494 -60.220 -39.795  1.00 62.06           O  
HETATM 6399  O   HOH B 621     -27.093 -71.347 -51.864  1.00 48.59           O  
HETATM 6400  O   HOH B 622     -41.675 -53.819 -31.258  1.00 28.81           O  
HETATM 6401  O   HOH B 623     -34.737 -34.231 -39.520  1.00 72.42           O  
HETATM 6402  O   HOH B 624     -73.070 -48.469 -25.304  1.00 62.46           O  
HETATM 6403  O   HOH B 625     -47.328 -45.351 -30.749  1.00 38.12           O  
HETATM 6404  O   HOH B 626     -36.380 -61.851 -50.062  1.00 35.99           O  
HETATM 6405  O   HOH B 627     -54.126 -45.875 -51.545  1.00 38.71           O  
HETATM 6406  O   HOH B 628     -10.853 -46.801 -40.422  1.00 69.28           O  
HETATM 6407  O   HOH B 629     -73.625 -44.975 -31.052  1.00 60.58           O  
HETATM 6408  O   HOH B 630     -50.900 -54.060 -43.634  1.00 64.86           O  
HETATM 6409  O   HOH B 631     -15.142 -64.063 -48.691  1.00 53.30           O  
HETATM 6410  O   HOH B 632     -54.275 -40.734 -31.193  1.00 24.98           O  
HETATM 6411  O   HOH B 633     -10.198 -49.180 -30.097  1.00 64.64           O  
HETATM 6412  O   HOH B 634     -28.169 -73.250 -58.750  1.00 71.22           O  
HETATM 6413  O   HOH B 635     -12.776 -56.736 -45.861  1.00 55.25           O  
HETATM 6414  O   HOH B 636     -57.981 -60.070 -24.196  1.00 44.53           O  
HETATM 6415  O   HOH B 637     -64.963 -68.231 -32.938  1.00 63.44           O  
HETATM 6416  O   HOH B 638     -35.610 -41.290 -37.574  1.00 21.01           O  
HETATM 6417  O   HOH B 639     -36.469 -62.321 -39.658  1.00117.68           O  
HETATM 6418  O   HOH B 640     -67.944 -57.262 -32.609  1.00 25.51           O  
HETATM 6419  O   HOH B 641     -66.987 -44.452 -28.992  1.00 40.02           O  
HETATM 6420  O   HOH B 642     -18.344 -42.423 -39.527  1.00 38.21           O  
HETATM 6421  O   HOH B 643     -26.847 -54.056 -69.613  1.00 25.38           O  
HETATM 6422  O   HOH B 644     -30.984 -65.773 -62.466  1.00 53.34           O  
HETATM 6423  O   HOH B 645     -26.349 -54.645 -53.383  1.00 25.25           O  
HETATM 6424  O   HOH B 646     -47.105 -41.799 -18.264  1.00 56.04           O  
HETATM 6425  O   HOH B 647     -35.083 -62.096 -41.994  1.00 30.55           O  
HETATM 6426  O   HOH B 648     -22.335 -56.195 -63.538  1.00 32.68           O  
HETATM 6427  O   HOH B 649     -36.877 -59.594 -24.876  1.00 41.99           O  
HETATM 6428  O   HOH B 650     -52.547 -46.039 -34.381  1.00 29.47           O  
HETATM 6429  O   HOH B 651     -31.850 -56.863 -60.532  1.00 44.12           O  
HETATM 6430  O   HOH B 652     -50.368 -47.633 -34.911  1.00 22.50           O  
HETATM 6431  O   HOH B 653     -70.916 -56.859 -33.096  1.00 49.03           O  
HETATM 6432  O   HOH B 654     -39.159 -39.567 -42.164  1.00 41.13           O  
HETATM 6433  O   HOH B 655     -23.092 -36.455 -42.427  1.00 41.99           O  
HETATM 6434  O   HOH B 656     -61.786 -55.263 -20.241  1.00 65.14           O  
HETATM 6435  O   HOH B 657     -44.477 -41.470 -29.859  1.00 33.06           O  
HETATM 6436  O   HOH B 658     -36.257 -50.676 -24.168  1.00 47.46           O  
HETATM 6437  O   HOH B 659     -55.335 -63.261 -26.129  1.00 45.40           O  
HETATM 6438  O   HOH B 660     -30.881 -54.387 -64.807  1.00 45.07           O  
HETATM 6439  O   HOH B 661     -10.797 -53.380 -53.387  1.00 51.31           O  
HETATM 6440  O   HOH B 662     -42.348 -58.238 -44.180  1.00 54.52           O  
HETATM 6441  O   HOH B 663     -11.644 -49.769 -47.798  1.00 40.44           O  
HETATM 6442  O   HOH B 664      -9.369 -49.001 -56.525  1.00 59.46           O  
HETATM 6443  O   HOH B 665     -68.735 -67.467 -31.180  1.00 49.35           O  
HETATM 6444  O   HOH B 666     -56.541 -59.675 -42.001  1.00 37.49           O  
HETATM 6445  O   HOH B 667      -5.588 -47.309 -25.832  1.00 45.36           O  
HETATM 6446  O   HOH B 668     -13.727 -57.361 -10.069  1.00 52.26           O  
HETATM 6447  O   HOH B 669